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Scripps Institution of Oceanography, UC San DiegoCA, United States
Institute of Organic Chemistry and Macromolecular Chemistry, Cluster of Excellence 'Balance of the Microverse', Friedrich-Schiller-University Jena, Germany
Institute of Enzymology, Research Centre of Natural Sciences, Eötvös Loránd Research Network, Budapest, Hungary
Institute of Cancer Research, Medical University of Vienna, Austria
Max F. Perutz Laboratories, Department of Medical Biochemistry, Medical University Vienna, Austria
Export Date: 7 April 2021
CODEN: FEBLA
Correspondence Address: Hamdoun, A.; Scripps Institution of Oceanography, United States; email: ahamdoun@ucsd.edu
Correspondence Address: Hellmich, U.A.; Institute of Organic Chemistry and Macromolecular Chemistry, Germany; email: ute.hellmich@uni-jena.de
Correspondence Address: Szakacs, G.; Institute of Enzymology, Hungary; email: gergely-szakacs@meduniwien.ac.at
Correspondence Address: Szakacs, G.; Institute of Cancer Research, Austria; email: gergely-szakacs@meduniwien.ac.at
Scripps Institution of Oceanography, UC San DiegoCA, United States
Institute of Organic Chemistry and Macromolecular Chemistry, Cluster of Excellence 'Balance of the Microverse', Friedrich-Schiller-University Jena, Germany
Institute of Enzymology, Research Centre of Natural Sciences, Eötvös Loránd Research Network, Budapest, Hungary
Institute of Cancer Research, Medical University of Vienna, Austria
Max F. Perutz Laboratories, Department of Medical Biochemistry, Medical University Vienna, Austria
Export Date: 13 August 2021
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Correspondence Address: Hamdoun, A.; Scripps Institution of Oceanography, United States; email: ahamdoun@ucsd.edu
Correspondence Address: Hellmich, U.A.; Institute of Organic Chemistry and Macromolecular Chemistry, Germany; email: ute.hellmich@uni-jena.de
Correspondence Address: Szakacs, G.; Institute of Enzymology, Hungary; email: gergely-szakacs@meduniwien.ac.at
Correspondence Address: Szakacs, G.; Institute of Cancer Research, Austria; email: gergely-szakacs@meduniwien.ac.at
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Hamdoun, A. ✉ </span> <span class="author-type"> </span> ; <span class="author-name" > Hellmich, U.A. ✉ </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10001932"> <a href="/gui2/?type=authors&mode=browse&sel=10001932" target="_blank">Szakacs, G. ✉</a> </span> <span class="author-type"> </span> ; <span class="author-name" > Kuchler, K. </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;31953886" mtid="31953886" target="_blank">The incredible diversity of structures and functions of ABC transporters</a></div> <div class="pub-info"> <span class="journal-title">FEBS LETTERS</span> <span class="journal-volume">595</span> : <span class="journal-issue">6</span> <span class="page"> pp. 671-674. , 4 p. </span> <span class="year">(2021)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1002/1873-3468.14061" target="_blank" href="https://doi.org/10.1002/1873-3468.14061"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000631255800001" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000631255800001"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85102805249" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85102805249"> Scopus </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:31953886 </span> <span class="status-holder"><span class="status-data status-VALIDATED"> Egyeztetett </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Hozzászólás, helyreigazítás ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 3</span> | Független: 3 | Függő: 0 | Nem jelölt: 0 | WoS jelölt: 1 | Scopus jelölt: 3 | WoS/Scopus jelölt: 3 | DOI jelölt: 3 </div> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;31953886" target="_blank">The incredible diversity of structures and functions of ABC transporters</a></div> <div> <span class="journal-title">FEBS LETTERS</span>
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<div class="lastModified">Utolsó módosítás: 2021.10.07. 12:53 MTMT API (MTMT API user, admin)
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Scripps Institution of Oceanography, UC San DiegoCA, United States
Institute of Organic Chemistry and Macromolecular Chemistry, Cluster of Excellence 'Balance of the Microverse', Friedrich-Schiller-University Jena, Germany
Institute of Enzymology, Research Centre of Natural Sciences, Eötvös Loránd Research Network, Budapest, Hungary
...</pre>
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Atomic-level structural insight on the human ABCG2 membrane protein, a pharmacologically important transporter, has been recently revealed by several key papers. In spite of the wealth of structural data, the pathway of transmembrane movement for the large variety of structurally different ABCG2 substrates and the physiological lipid regulation of the transporter has not been elucidated. The complex molecular dynamics simulations presented here may provide a breakthrough in understanding the steps of the substrate transport process and its regulation by cholesterol. Our analysis revealed drug binding cavities other than the central binding site and delineated a putative dynamic transport pathway for substrates with variable structures. We found that membrane cholesterol accelerated drug transport by promoting the closure of cytoplasmic protein regions. Since ABCG2 is present in all major biological barriers and drug-metabolizing organs, influences the pharmacokinetics of numerous clinically applied drugs, and plays a key role in uric acid extrusion, this information may significantly promote a reliable prediction of clinically important substrate characteristics and drug-drug interactions. © 2020, The Author(s).
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" mtid="10078334"> <a href="/gui2/?type=authors&mode=browse&sel=10078334" target="_blank">Nagy, T.</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10094506"> <a href="/gui2/?type=authors&mode=browse&sel=10094506" target="_blank">Tóth, Á.</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10027670"> <a href="/gui2/?type=authors&mode=browse&sel=10027670" target="_blank">Telbisz, Á.</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="1241938"> <a href="/gui2/?type=authors&mode=browse&sel=1241938" target="_blank">Sarkadi, B.</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10010378"> <a href="/gui2/?type=authors&mode=browse&sel=10010378" target="_blank">Tordai, H.</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10002439"> <a href="/gui2/?type=authors&mode=browse&sel=10002439" target="_blank">Tordai, A.</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10015687"> <a href="/gui2/?type=authors&mode=browse&sel=10015687" target="_blank">Hegedűs, T. ✉</a> </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;31623716" mtid="31623716" target="_blank">The transport pathway in the ABCG2 protein and its regulation revealed by molecular dynamics simulations</a></div> <div class="pub-info"> <span class="journal-title">CELLULAR AND MOLECULAR LIFE SCIENCES</span> <span class="journal-volume">78</span> : <span class="journal-issue">5</span> <span class="page"> pp. 2329-2339. , 11 p. </span> <span class="year">(2021)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.1007/s00018-020-03651-3" target="_blank" href="https://doi.org/10.1007/s00018-020-03651-3"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000573028400001" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000573028400001"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85091466123" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85091466123"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="32979053" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=32979053&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="deleted-record">Zárolt</span> <span class="short-pub-mtid"> Közlemény:31623716 </span> <span class="status-holder"><span class="status-data status-VALIDATED"> Egyeztetett </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 11</span> | Független: 9 | Függő: 2 | Nem jelölt: 0 | WoS jelölt: 11 | Scopus jelölt: 11 | WoS/Scopus jelölt: 11 | DOI jelölt: 11 </div> </div> </div> </div><div class="JournalArticle Publication long-list"> <div class="authors"> <img title="Forrásközlemény" style="float: left" src="/frontend/resources/grid/publication-core-icon.png"> <img title="Idézőközlemény" style="float: left" src="/frontend/resources/grid/publication-citation-icon.png"> <div class="autype autype0"> <span class="author-name" mtid="10078334"><a href="/gui2/?type=authors&mode=browse&sel=10078334" target="_blank">Nagy T. (<span class="authorship-author-name">Nagy Tamás</span> <span class="authorAux-mtmt"> bioinformatika</span>) </a> </span> <span class="author-affil"><span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Intézet">I</span>/Biofizikai és Sugárbiológiai Intézet</span> ; <span class="author-name" mtid="10094506"><a href="/gui2/?type=authors&mode=browse&sel=10094506" target="_blank">Tóth Á. (<span class="authorship-author-name">Tóth Ágota</span> <span class="authorAux-mtmt"> biofizika</span>) </a> </span> ; <span class="author-name" mtid="10027670"><a href="/gui2/?type=authors&mode=browse&sel=10027670" target="_blank">Telbisz Á. (<span class="authorship-author-name">Telbisz Ágnes Mária</span> <span class="authorAux-mtmt"> Biomembrán</span>) </a> </span> <span class="author-affil"><span title="Természettudományi Kutatóközpont">TTK</span>/Enzimológiai Intézet</span> ; <span class="author-name" mtid="1241938"><a href="/gui2/?type=authors&mode=browse&sel=1241938" target="_blank">Sarkadi B. (<span class="authorship-author-name">Sarkadi Balázs</span> <span class="authorAux-mtmt"> biofizika</span>) </a> </span> <span class="author-affil"><span title="Természettudományi Kutatóközpont">TTK</span>/Enzimológiai Intézet; <span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Intézet">I</span>/Biofizikai és Sugárbiológiai Intézet</span> ; <span class="author-name" mtid="10010378"><a href="/gui2/?type=authors&mode=browse&sel=10010378" target="_blank">Tordai H. 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(<span class="authorship-author-name">Tordai Attila</span> <span class="authorAux-mtmt"> Orvostudomány</span>) </a> </span> <span class="author-affil"><span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Klinikum">K</span>/Transzfúziológiai Tanszék</span> ; <span class="author-name" mtid="10015687"><a href="/gui2/?type=authors&mode=browse&sel=10015687" target="_blank">Hegedűs T. ✉ (<span class="authorship-author-name">Hegedűs Tamás</span> <span class="authorAux-mtmt"> bioinformatika, biofizika</span>) </a> </span> <span class="author-affil"><span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Intézet">I</span>/Biofizikai és Sugárbiológiai Intézet</span> </div> </div> <div class="title"><a href="/gui2/?mode=browse¶ms=publication;31623716" target="_blank">The transport pathway in the ABCG2 protein and its regulation revealed by molecular dynamics simulations</a></div> <div> <span class="journal-title">CELLULAR AND MOLECULAR LIFE SCIENCES</span> <span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/1420-682X">1420-682X</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/1420-9071">1420-9071</a>)</span>: <span class="journal-volume">78</span> <span class="journal-issue">5</span> <span class="page"> pp 2329-2339 </span> <span class="year">(2021)</span> </div> <div class="pub-footer"> <span class="language" xmlns="http://www.w3.org/1999/html">Nyelv: Angol | </span> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.1007/s00018-020-03651-3" target="_blank" href="https://doi.org/10.1007/s00018-020-03651-3"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000573028400001" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000573028400001"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85091466123" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85091466123"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="32979053" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=32979053&dopt=Abstract"> PubMed </a> </span> </span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 11</span> | Független: 9 | Függő: 2 | Nem jelölt: 0 | WoS jelölt: 11 | Scopus jelölt: 11 | WoS/Scopus jelölt: 11 | DOI jelölt: 11 </div> <div class="publication-citation"> <a target="_blank" href="/api/publication?cond=citations.related;eq;31623716&sort=publishedYear,desc&sort=title"> Idézett közlemények száma: 11 </a> </div> <div class="mtid"><span class="long-pub-mtid">Közlemény: 31623716</span> | <span class="status-data status-VALIDATED"> Egyeztetett </span> Forrás Idéző | <span class="type-subtype">Folyóiratcikk ( Szakcikk ) </span> | <span class="pub-category">Tudományos</span> | <span class="publication-sourceOfData">Scopus</span> </div> <div class="funder"> (Open access funding provided by Semmelweis University), (K127961) Támogató: NKFIH, (Semmelweis Science and Innovation Fund) </div> <div class="lastModified">Utolsó módosítás: 2024.03.18. 14:24 Tóth Ágota (biofizika) </div> <div class="lockedBy">Ideiglenesen zárolva 2022.07.08. 12:16 Boros Annamária (MTMT Központi admin) </div> </div></div>
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Funding Agency and Grant Number: Semmelweis Egyetem [Sci_Innov18] Funding Source: Medline; Cystic Fibrosis Foundation (US) [HEGEDU18I0] Funding Source: Medline; Nemzeti Kutatasi, Fejlesztesi es Innovacios Hivatal (HU) [K127961, K111678] Funding Source: Medline
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Export Date: 31 August 2021
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Correspondence Address: Hegedűs, T.; Department of Biophysics and Radiation Biology, Hungary; email: hegedus@hegelab.org
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" mtid="10062898"> <a href="/gui2/?type=authors&mode=browse&sel=10062898" target="_blank">Farkas, Bianka</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10010378"> <a href="/gui2/?type=authors&mode=browse&sel=10010378" target="_blank">Tordai, Hedvig</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10029020"> <a href="/gui2/?type=authors&mode=browse&sel=10029020" target="_blank">Padányi, Rita</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10002439"> <a href="/gui2/?type=authors&mode=browse&sel=10002439" target="_blank">Tordai, Attila</a> </span> <span class="author-type"> </span> ; <span class="author-name" > Gera, János </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10017319"> <a href="/gui2/?type=authors&mode=browse&sel=10017319" target="_blank">Paragi, Gábor</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10015687"> <a href="/gui2/?type=authors&mode=browse&sel=10015687" target="_blank">Hegedűs, Tamás ✉</a> </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;30745347" mtid="30745347" target="_blank">Discovering the chloride pathway in the CFTR channel</a></div> <div class="pub-info"> <span class="journal-title">CELLULAR AND MOLECULAR LIFE SCIENCES</span> <span class="journal-volume">77</span> : <span class="journal-issue">4</span> <span class="page"> pp. 765-778. , 12 p. </span> <span class="year">(2020)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.1007/s00018-019-03211-4" target="_blank" href="https://doi.org/10.1007/s00018-019-03211-4"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000519371800014" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000519371800014"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85069529571" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85069529571"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="31327045" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=31327045&dopt=Abstract"> PubMed </a> </span> <span class="id identifier oa_GREEN" title=" Green "> <a style="color:blue" title="17150" target="_blank" href="http://publicatio.bibl.u-szeged.hu/17150"> SZTE Publicatio </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="deleted-record">Zárolt</span> <span class="short-pub-mtid"> Közlemény:30745347 </span> <span class="status-holder"><span class="status-data status-VALIDATED"> Egyeztetett </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 12</span> | Független: 10 | Függő: 2 | Nem jelölt: 0 | WoS jelölt: 12 | Scopus jelölt: 11 | WoS/Scopus jelölt: 12 | DOI jelölt: 12 </div> </div> </div> </div><div class="JournalArticle Publication long-list">
<div class="authors">
<img title="Forrásközlemény" style="float: left" src="/frontend/resources/grid/publication-core-icon.png">
<img title="Idézőközlemény" style="float: left" src="/frontend/resources/grid/publication-citation-icon.png">
<div class="autype autype0"> <span class="author-name" mtid="10062898"><a
href="/gui2/?type=authors&mode=browse&sel=10062898" target="_blank">Farkas Bianka
(<span class="authorship-author-name">Farkas Bianka Vivien</span>
<span class="authorAux-mtmt"> Biológia tudományág, bioinformatika</span>)
</a>
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<span class="author-affil"><span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Intézet">I</span>/Biofizikai és Sugárbiológiai Intézet; <span title="Pázmány Péter Katolikus Egyetem">PPKE</span>/<span title="Információs Technológiai és Bionikai Kar">ITK</span>/Roska Tamás Műszaki és Természettudományi Doktori Iskola</span>
;
<span class="author-name" mtid="10010378"><a
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(<span class="authorship-author-name">Tordai Hedvig</span>
<span class="authorAux-mtmt"> molekuláris biológia</span>)
</a>
</span>
<span class="author-affil"><span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Intézet">I</span>/Biofizikai és Sugárbiológiai Intézet</span>
;
<span class="author-name" mtid="10029020"><a
href="/gui2/?type=authors&mode=browse&sel=10029020" target="_blank">Padányi Rita
(<span class="authorship-author-name">Padányi Rita</span>
<span class="authorAux-mtmt"> Molekuláris biológia</span>)
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Funding Agency and Grant Number: Semmelweis Egyetem [Sci_Innov18] Funding Source: Medline; Cystic Fibrosis Foundation (US) [HEGEDU18I0] Funding Source: Medline; Nemzeti Kutatasi, Fejlesztesi es Innovacios Hivatal (HU) [K127961, K111678] Funding Source: Medline
Cited By :2
Export Date: 31 August 2021
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Funding Agency and Grant Number: National Research, Development and Innovation Office [K 127961, K 128123]
Funding text: This work has been supported by National Research, Development and Innovation Office (grant numbers: K 127961 to TH and K 128123 to LH. The authors thank M~at~e Homolya for his help in graphics.
Institute of Enzymology, Research Centre for Natural Sciences, Budapest, Hungary
Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary
Cited By :6
Export Date: 2 June 2021
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Correspondence Address: Sarkadi, B.; Institute of Enzymology, Hungary; email: sarkadi@biomembrane.hu
Correspondence Address: Sarkadi, B.; Department of Biophysics and Radiation Biology, Hungary; email: sarkadi@biomembrane.hu
Funding Agency and Grant Number: National Research, Development and Innovation OfficeNational Research, Development & Innovation Office (NRDIO) - Hungary [K 127961, K 128123]
Funding text: This work has been supported by National Research, Development and Innovation Office (grant numbers: K 127961 to TH and K 128123 to LH. The authors thank M~at~e Homolya for his help in graphics.
Institute of Enzymology, Research Centre for Natural Sciences, Budapest, Hungary
Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary
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Correspondence Address: Sarkadi, B.; Institute of Enzymology, Hungary; email: sarkadi@biomembrane.hu
Correspondence Address: Sarkadi, B.; Department of Biophysics and Radiation Biology, Hungary; email: sarkadi@biomembrane.hu
Institute of Enzymology, Research Centre for Natural Sciences, Budapest, Hungary
Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary
Cited By :7
Export Date: 31 August 2021
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Correspondence Address: Sarkadi, B.; Institute of Enzymology, Hungary; email: sarkadi@biomembrane.hu
Correspondence Address: Sarkadi, B.; Department of Biophysics and Radiation Biology, Hungary; email: sarkadi@biomembrane.hu
Institute of Enzymology, Research Centre for Natural Sciences, Budapest, Hungary
Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary
Cited By :7
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CODEN: FEBLA
Correspondence Address: Sarkadi, B.; Institute of Enzymology, Hungary; email: sarkadi@biomembrane.hu
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The ABCG2 protein has a key role in the transport of a wide range of structurally dissimilar endo- and xenobiotics in the human body, especially in the tissue barriers and the metabolizing or secreting organs. The human ABCG2 gene harbors a high number of polymorphisms and mutations, which may significantly modulate its expression and function. Recent high-resolution structural data, complemented with molecular dynamic simulations, may significantly help to understand intramolecular movements and substrate handling, as well as the effects of mutations on the membrane transporter function of ABCG2. As reviewed here, structural alterations may result not only in direct alterations in drug binding and transporter activity, but also in improper folding or problems in the carefully regulated process of trafficking, including vesicular transport, endocytosis, recycling, and degradation. Here, we also review the clinical importance of altered ABCG2 expression and function in general drug metabolism, cancer multidrug resistance, and impaired uric acid excretion, leading to gout.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" mtid="1241938"> <a href="/gui2/?type=authors&mode=browse&sel=1241938" target="_blank">Sarkadi, Balázs ✉</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10010446"> <a href="/gui2/?type=authors&mode=browse&sel=10010446" target="_blank">Homolya, László</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10015687"> <a href="/gui2/?type=authors&mode=browse&sel=10015687" target="_blank">Hegedűs, Tamás</a> </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;31634543" mtid="31634543" target="_blank">The ABCG2/BCRP transporter and its variants - from structure to pathology</a></div> <div class="pub-info"> <span class="journal-title">FEBS LETTERS</span> <span class="journal-volume">594</span> : <span class="journal-issue">23</span> <span class="page"> pp. 4012-4034. , 23 p. </span> <span class="year">(2020)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1002/1873-3468.13947" target="_blank" href="https://doi.org/10.1002/1873-3468.13947"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000577742800001" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000577742800001"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85092567283" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85092567283"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="33015850" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=33015850&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="deleted-record">Zárolt</span> <span class="short-pub-mtid"> Közlemény:31634543 </span> <span class="status-holder"><span class="status-data status-VALIDATED"> Egyeztetett </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Összefoglaló cikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 34</span> | Független: 29 | Függő: 5 | Nem jelölt: 0 | WoS jelölt: 33 | Scopus jelölt: 34 | WoS/Scopus jelölt: 34 | DOI jelölt: 34 </div> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;31634543" target="_blank">The ABCG2/BCRP transporter and its variants - from structure to pathology</a></div> <div> <span class="journal-title">FEBS LETTERS</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Funding Agency and Grant Number: National Research, Development and Innovation Office [K 127961, K 128123]
Funding text: This work has been supported by National Research, Development and Innovation Office (grant numbers: K 127961 to TH and K 128123 to LH. The authors thank M~at~e Homolya for his help in graphics.
Institute of Enzymology, Research Centre for Natural Sciences, Budape...</pre>
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Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Germany
Department of Pharmacology and Toxicology, University of Alabama at BirminghamAL, United States
Department of Life Sciences, Imperial College London, London South Kensington, United Kingdom
Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot, United Kingdom
Structural Genomics Consortium, University of Oxford, United Kingdom
Skaggs School of Pharmacy and Pharmaceutical Sciences and Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA, United States
State Key Laboratory of Membrane Biology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, Beijing, China
Peking-Tsinghua Center for Life Sciences, Peking University, Beijing, China
Institut Pasteur, Paris Cedex 15, France
Division of Cancer Epidemiology and Genetics, National Cancer Institute, NIH, Gaithersburg, MD, United States
Department of Biochemistry and Molecular Biology, Faculty of Medicine, Life Sciences Institute, University of British Columbia, Vancouver, BC, Canada
Department of Cell Biology and Department of Microbiology, New York University School of MedicineNY, United States
Faculty of Biology, Medicine and Health, The University of Manchester, United Kingdom
Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA, United States
Department of Biology, Southern University of Science and Technology, Shenzhen, China
Institute for Integrative Biology of the Cell (I2BC), Université Paris-Sud, Orsay, France
National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, United States
Institute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Japan
Department of Pathology, University of Cambridge, United Kingdom
Structural Biology, Genentech Inc., South San Francisco, CA, United States
Division of Integrative Bioscience and Biotechnology, POSTECH, Pohang, South Korea
Department of Biochemistry, The Bruce and Ruth Rappaport Faculty of Medicine, The Technion-Israel Institute of Technology, Haifa, Israel
Institut für Zytobiologie, Philipps-Universität Marburg, Germany
Department of Plant and Microbial Biology, University Zurich, Switzerland
International Research Centre for Environmental Membrane Biology, Foshan University, Foshan, China
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan
Department of Molecular Biosciences, Northwestern University, Evanston, IL, United States
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Netherlands
Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, United States
Institute of Enzymology, Research Center for Natural Sciences (RCNS), Budapest, Hungary
Institute of Biochemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany
Department of Biology/Microbial Physiology, Humboldt-University of Berlin, Germany
Institute of Biology, Westlake Institute for Advanced Study, School of Life Sciences, Westlake University, Hangzhou, China
Department of Chemical Physiology and Biochemistry, Oregon Health & Science University, Portland, OR, United States
Department of Biochemistry, Center for Biophysics and Quantitative Biology, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-ChampaignIL, United States
Department of Biological Sciences and Centre for Molecular Simulation, University of CalgaryAB, Canada
Institute for Integrated Cell-Material Sciences (WPI-iCeMS), KUIAS, Kyoto University, Japan
Department of Molecular Biology, Princeton UniversityNJ, United States
National Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China
Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO, United States
Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA, United States
Export Date: 17 November 2020
CODEN: FEBLA
Correspondence Address: Thomas, C.; Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Institute of Biochemistry, Biocenter, Goethe University FrankfurtGermany; email: c.thomas@em.uni-frankfurt.de
Funding details: Canada Research Chairs
Funding details: Wellcome Trust, WT, LI 415/5, 101828/Z/13/Z
Funding details: National Institutes of Health, NIH, MR/N000994/1
Funding details: Medical Research Council, MRC, MR/N020103/1
Funding details: Deutsche Forschungsgemeinschaft, DFG, SFB 807, TA157/12‐1
Funding text 1: K.B. acknowledges support by a grant of the Medical Research Council (MR/N020103/1). M.D. is supported in part by the Intramural Program of the NIH. V.K. acknowledges support by the Medical Research Council (MR/N000994/1) and Wellcome Trust (101828/Z/13/Z). R.L. acknowledges generous financial support from German Research Foundation (LI 415/5). D.P.T. is supported in part by the Canada Research Chairs program. This work was supported by the German Research Foundation (SFB 807 and TA157/12‐1 (Reinhart Koselleck Award Program) to R.T.).
Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Germany
Department of Pharmacology and Toxicology, University of Alabama at BirminghamAL, United States
Department of Life Sciences, Imperial College London, London South Kensington, United Kingdom
Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot, United Kingdom
Structural Genomics Consortium, University of Oxford, United Kingdom
Skaggs School of Pharmacy and Pharmaceutical Sciences and Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA, United States
State Key Laboratory of Membrane Biology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, Beijing, China
Peking-Tsinghua Center for Life Sciences, Peking University, Beijing, China
Institut Pasteur, Paris Cedex 15, France
Division of Cancer Epidemiology and Genetics, National Cancer Institute, NIH, Gaithersburg, MD, United States
Department of Biochemistry and Molecular Biology, Faculty of Medicine, Life Sciences Institute, University of British Columbia, Vancouver, BC, Canada
Department of Cell Biology and Department of Microbiology, New York University School of MedicineNY, United States
Faculty of Biology, Medicine and Health, The University of Manchester, United Kingdom
Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA, United States
Department of Biology, Southern University of Science and Technology, Shenzhen, China
Institute for Integrative Biology of the Cell (I2BC), Université Paris-Sud, Orsay, France
National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, United States
Institute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Japan
Department of Pathology, University of Cambridge, United Kingdom
Structural Biology, Genentech Inc., South San Francisco, CA, United States
Division of Integrative Bioscience and Biotechnology, POSTECH, Pohang, South Korea
Department of Biochemistry, The Bruce and Ruth Rappaport Faculty of Medicine, The Technion-Israel Institute of Technology, Haifa, Israel
Institut für Zytobiologie, Philipps-Universität Marburg, Germany
Department of Plant and Microbial Biology, University Zurich, Switzerland
International Research Centre for Environmental Membrane Biology, Foshan University, Foshan, China
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan
Department of Molecular Biosciences, Northwestern University, Evanston, IL, United States
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Netherlands
Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, United States
Institute of Enzymology, Research Center for Natural Sciences (RCNS), Budapest, Hungary
Institute of Biochemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany
Department of Biology/Microbial Physiology, Humboldt-University of Berlin, Germany
Institute of Biology, Westlake Institute for Advanced Study, School of Life Sciences, Westlake University, Hangzhou, China
Department of Chemical Physiology and Biochemistry, Oregon Health & Science University, Portland, OR, United States
Department of Biochemistry, Center for Biophysics and Quantitative Biology, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-ChampaignIL, United States
Department of Biological Sciences and Centre for Molecular Simulation, University of CalgaryAB, Canada
Institute for Integrated Cell-Material Sciences (WPI-iCeMS), KUIAS, Kyoto University, Japan
Department of Molecular Biology, Princeton UniversityNJ, United States
National Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China
Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO, United States
Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA, United States
Cited By :3
Export Date: 5 February 2021
CODEN: FEBLA
Correspondence Address: Thomas, C.; Institute of Biochemistry, Germany; email: c.thomas@em.uni-frankfurt.de
Correspondence Address: Tampé, R.; Institute of Biochemistry, Germany; email: tampe@em.uni-frankfurt.de
Funding details: Canada Research Chairs
Funding details: Wellcome Trust, WT, LI 415/5, 101828/Z/13/Z
Funding details: National Institutes of Health, NIH, MR/N000994/1
Funding details: Medical Research Council, MRC, MR/N020103/1
Funding details: Deutsche Forschungsgemeinschaft, DFG, SFB 807, TA157/12‐1
Funding text 1: K.B. acknowledges support by a grant of the Medical Research Council (MR/N020103/1). M.D. is supported in part by the Intramural Program of the NIH. V.K. acknowledges support by the Medical Research Council (MR/N000994/1) and Wellcome Trust (101828/Z/13/Z). R.L. acknowledges generous financial support from German Research Foundation (LI 415/5). D.P.T. is supported in part by the Canada Research Chairs program. This work was supported by the German Research Foundation (SFB 807 and TA157/12‐1 (Reinhart Koselleck Award Program) to R.T.).
Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Germany
Department of Pharmacology and Toxicology, University of Alabama at BirminghamAL, United States
Department of Life Sciences, Imperial College London, London South Kensington, United Kingdom
Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot, United Kingdom
Structural Genomics Consortium, University of Oxford, United Kingdom
Skaggs School of Pharmacy and Pharmaceutical Sciences and Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA, United States
State Key Laboratory of Membrane Biology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, Beijing, China
Peking-Tsinghua Center for Life Sciences, Peking University, Beijing, China
Institut Pasteur, Paris Cedex 15, France
Division of Cancer Epidemiology and Genetics, National Cancer Institute, NIH, Gaithersburg, MD, United States
Department of Biochemistry and Molecular Biology, Faculty of Medicine, Life Sciences Institute, University of British Columbia, Vancouver, BC, Canada
Department of Cell Biology and Department of Microbiology, New York University School of MedicineNY, United States
Faculty of Biology, Medicine and Health, The University of Manchester, United Kingdom
Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA, United States
Department of Biology, Southern University of Science and Technology, Shenzhen, China
Institute for Integrative Biology of the Cell (I2BC), Université Paris-Sud, Orsay, France
National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, United States
Institute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Japan
Department of Pathology, University of Cambridge, United Kingdom
Structural Biology, Genentech Inc., South San Francisco, CA, United States
Division of Integrative Bioscience and Biotechnology, POSTECH, Pohang, South Korea
Department of Biochemistry, The Bruce and Ruth Rappaport Faculty of Medicine, The Technion-Israel Institute of Technology, Haifa, Israel
Institut für Zytobiologie, Philipps-Universität Marburg, Germany
Department of Plant and Microbial Biology, University Zurich, Switzerland
International Research Centre for Environmental Membrane Biology, Foshan University, Foshan, China
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan
Department of Molecular Biosciences, Northwestern University, Evanston, IL, United States
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Netherlands
Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, United States
Institute of Enzymology, Research Center for Natural Sciences (RCNS), Budapest, Hungary
Institute of Biochemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany
Department of Biology/Microbial Physiology, Humboldt-University of Berlin, Germany
Institute of Biology, Westlake Institute for Advanced Study, School of Life Sciences, Westlake University, Hangzhou, China
Department of Chemical Physiology and Biochemistry, Oregon Health & Science University, Portland, OR, United States
Department of Biochemistry, Center for Biophysics and Quantitative Biology, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-ChampaignIL, United States
Department of Biological Sciences and Centre for Molecular Simulation, University of CalgaryAB, Canada
Institute for Integrated Cell-Material Sciences (WPI-iCeMS), KUIAS, Kyoto University, Japan
Department of Molecular Biology, Princeton UniversityNJ, United States
National Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China
Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO, United States
Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA, United States
Cited By :10
Export Date: 1 April 2021
CODEN: FEBLA
Correspondence Address: Thomas, C.; Institute of Biochemistry, Germany; email: c.thomas@em.uni-frankfurt.de
Correspondence Address: Tampé, R.; Institute of Biochemistry, Germany; email: tampe@em.uni-frankfurt.de
Funding details: National Institutes of Health, NIH, MR/N000994/1
Funding details: Wellcome Trust, WT, 101828/Z/13/Z, LI 415/5
Funding details: Medical Research Council, MRC, MR/N020103/1
Funding details: Deutsche Forschungsgemeinschaft, DFG, SFB 807, TA157/12‐1
Funding details: Canada Research Chairs
Funding text 1: K.B. acknowledges support by a grant of the Medical Research Council (MR/N020103/1). M.D. is supported in part by the Intramural Program of the NIH. V.K. acknowledges support by the Medical Research Council (MR/N000994/1) and Wellcome Trust (101828/Z/13/Z). R.L. acknowledges generous financial support from German Research Foundation (LI 415/5). D.P.T. is supported in part by the Canada Research Chairs program. This work was supported by the German Research Foundation (SFB 807 and TA157/12‐1 (Reinhart Koselleck Award Program) to R.T.).
Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Germany
Department of Pharmacology and Toxicology, University of Alabama at BirminghamAL, United States
Department of Life Sciences, Imperial College London, London South Kensington, United Kingdom
Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot, United Kingdom
Structural Genomics Consortium, University of Oxford, United Kingdom
Skaggs School of Pharmacy and Pharmaceutical Sciences and Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA, United States
State Key Laboratory of Membrane Biology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, Beijing, China
Peking-Tsinghua Center for Life Sciences, Peking University, Beijing, China
Institut Pasteur, Paris Cedex 15, France
Division of Cancer Epidemiology and Genetics, National Cancer Institute, NIH, Gaithersburg, MD, United States
Department of Biochemistry and Molecular Biology, Faculty of Medicine, Life Sciences Institute, University of British Columbia, Vancouver, BC, Canada
Department of Cell Biology and Department of Microbiology, New York University School of MedicineNY, United States
Faculty of Biology, Medicine and Health, The University of Manchester, United Kingdom
Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA, United States
Department of Biology, Southern University of Science and Technology, Shenzhen, China
Institute for Integrative Biology of the Cell (I2BC), Université Paris-Sud, Orsay, France
National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, United States
Institute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Japan
Department of Pathology, University of Cambridge, United Kingdom
Structural Biology, Genentech Inc., South San Francisco, CA, United States
Division of Integrative Bioscience and Biotechnology, POSTECH, Pohang, South Korea
Department of Biochemistry, The Bruce and Ruth Rappaport Faculty of Medicine, The Technion-Israel Institute of Technology, Haifa, Israel
Institut für Zytobiologie, Philipps-Universität Marburg, Germany
Department of Plant and Microbial Biology, University Zurich, Switzerland
International Research Centre for Environmental Membrane Biology, Foshan University, Foshan, China
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan
Department of Molecular Biosciences, Northwestern University, Evanston, IL, United States
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Netherlands
Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, United States
Institute of Enzymology, Research Center for Natural Sciences (RCNS), Budapest, Hungary
Institute of Biochemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany
Department of Biology/Microbial Physiology, Humboldt-University of Berlin, Germany
Institute of Biology, Westlake Institute for Advanced Study, School of Life Sciences, Westlake University, Hangzhou, China
Department of Chemical Physiology and Biochemistry, Oregon Health & Science University, Portland, OR, United States
Department of Biochemistry, Center for Biophysics and Quantitative Biology, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-ChampaignIL, United States
Department of Biological Sciences and Centre for Molecular Simulation, University of CalgaryAB, Canada
Institute for Integrated Cell-Material Sciences (WPI-iCeMS), KUIAS, Kyoto University, Japan
Department of Molecular Biology, Princeton UniversityNJ, United States
National Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China
Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO, United States
Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA, United States
Cited By :10
Export Date: 3 May 2021
CODEN: FEBLA
Correspondence Address: Thomas, C.; Institute of Biochemistry, Germany; email: c.thomas@em.uni-frankfurt.de
Correspondence Address: Tampé, R.; Institute of Biochemistry, Germany; email: tampe@em.uni-frankfurt.de
Funding details: National Institutes of Health, NIH, MR/N000994/1
Funding details: Wellcome Trust, WT, 101828/Z/13/Z, LI 415/5
Funding details: Medical Research Council, MRC, MR/N020103/1
Funding details: Deutsche Forschungsgemeinschaft, DFG, SFB 807, TA157/12‐1
Funding details: Canada Research Chairs
Funding text 1: K.B. acknowledges support by a grant of the Medical Research Council (MR/N020103/1). M.D. is supported in part by the Intramural Program of the NIH. V.K. acknowledges support by the Medical Research Council (MR/N000994/1) and Wellcome Trust (101828/Z/13/Z). R.L. acknowledges generous financial support from German Research Foundation (LI 415/5). D.P.T. is supported in part by the Canada Research Chairs program. This work was supported by the German Research Foundation (SFB 807 and TA157/12‐1 (Reinhart Koselleck Award Program) to R.T.).
Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Germany
Department of Pharmacology and Toxicology, University of Alabama at BirminghamAL, United States
Department of Life Sciences, Imperial College London, London South Kensington, United Kingdom
Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot, United Kingdom
Structural Genomics Consortium, University of Oxford, United Kingdom
Skaggs School of Pharmacy and Pharmaceutical Sciences and Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA, United States
State Key Laboratory of Membrane Biology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, Beijing, China
Peking-Tsinghua Center for Life Sciences, Peking University, Beijing, China
Institut Pasteur, Paris Cedex 15, France
Division of Cancer Epidemiology and Genetics, National Cancer Institute, NIH, Gaithersburg, MD, United States
Department of Biochemistry and Molecular Biology, Faculty of Medicine, Life Sciences Institute, University of British Columbia, Vancouver, BC, Canada
Department of Cell Biology and Department of Microbiology, New York University School of MedicineNY, United States
Faculty of Biology, Medicine and Health, The University of Manchester, United Kingdom
Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA, United States
Department of Biology, Southern University of Science and Technology, Shenzhen, China
Institute for Integrative Biology of the Cell (I2BC), Université Paris-Sud, Orsay, France
National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, United States
Institute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Japan
Department of Pathology, University of Cambridge, United Kingdom
Structural Biology, Genentech Inc., South San Francisco, CA, United States
Division of Integrative Bioscience and Biotechnology, POSTECH, Pohang, South Korea
Department of Biochemistry, The Bruce and Ruth Rappaport Faculty of Medicine, The Technion-Israel Institute of Technology, Haifa, Israel
Institut für Zytobiologie, Philipps-Universität Marburg, Germany
Department of Plant and Microbial Biology, University Zurich, Switzerland
International Research Centre for Environmental Membrane Biology, Foshan University, Foshan, China
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan
Department of Molecular Biosciences, Northwestern University, Evanston, IL, United States
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Netherlands
Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, United States
Institute of Enzymology, Research Center for Natural Sciences (RCNS), Budapest, Hungary
Institute of Biochemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany
Department of Biology/Microbial Physiology, Humboldt-University of Berlin, Germany
Institute of Biology, Westlake Institute for Advanced Study, School of Life Sciences, Westlake University, Hangzhou, China
Department of Chemical Physiology and Biochemistry, Oregon Health & Science University, Portland, OR, United States
Department of Biochemistry, Center for Biophysics and Quantitative Biology, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-ChampaignIL, United States
Department of Biological Sciences and Centre for Molecular Simulation, University of CalgaryAB, Canada
Institute for Integrated Cell-Material Sciences (WPI-iCeMS), KUIAS, Kyoto University, Japan
Department of Molecular Biology, Princeton UniversityNJ, United States
National Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China
Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO, United States
Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA, United States
Cited By :20
Export Date: 30 July 2021
CODEN: FEBLA
Correspondence Address: Thomas, C.; Institute of Biochemistry, Germany; email: c.thomas@em.uni-frankfurt.de
Correspondence Address: Tampé, R.; Institute of Biochemistry, Germany; email: tampe@em.uni-frankfurt.de
Chemicals/CAS: ATP-Binding Cassette Transporters
Funding details: National Institutes of Health, NIH, MR/N000994/1
Funding details: Wellcome Trust, WT, 101828/Z/13/Z, LI 415/5
Funding details: Medical Research Council, MRC, MR/N020103/1
Funding details: Deutsche Forschungsgemeinschaft, DFG, SFB 807, TA157/12‐1
Funding details: Canada Research Chairs
Funding text 1: K.B. acknowledges support by a grant of the Medical Research Council (MR/N020103/1). M.D. is supported in part by the Intramural Program of the NIH. V.K. acknowledges support by the Medical Research Council (MR/N000994/1) and Wellcome Trust (101828/Z/13/Z). R.L. acknowledges generous financial support from German Research Foundation (LI 415/5). D.P.T. is supported in part by the Canada Research Chairs program. This work was supported by the German Research Foundation (SFB 807 and TA157/12‐1 (Reinhart Koselleck Award Program) to R.T.).
Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Germany
Department of Pharmacology and Toxicology, University of Alabama at BirminghamAL, United States
Department of Life Sciences, Imperial College London, London South Kensington, United Kingdom
Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot, United Kingdom
Structural Genomics Consortium, University of Oxford, United Kingdom
Skaggs School of Pharmacy and Pharmaceutical Sciences and Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA, United States
State Key Laboratory of Membrane Biology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, Beijing, China
Peking-Tsinghua Center for Life Sciences, Peking University, Beijing, China
Institut Pasteur, Paris Cedex 15, France
Division of Cancer Epidemiology and Genetics, National Cancer Institute, NIH, Gaithersburg, MD, United States
Department of Biochemistry and Molecular Biology, Faculty of Medicine, Life Sciences Institute, University of British Columbia, Vancouver, BC, Canada
Department of Cell Biology and Department of Microbiology, New York University School of MedicineNY, United States
Faculty of Biology, Medicine and Health, The University of Manchester, United Kingdom
Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA, United States
Department of Biology, Southern University of Science and Technology, Shenzhen, China
Institute for Integrative Biology of the Cell (I2BC), Université Paris-Sud, Orsay, France
National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, United States
Institute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Japan
Department of Pathology, University of Cambridge, United Kingdom
Structural Biology, Genentech Inc., South San Francisco, CA, United States
Division of Integrative Bioscience and Biotechnology, POSTECH, Pohang, South Korea
Department of Biochemistry, The Bruce and Ruth Rappaport Faculty of Medicine, The Technion-Israel Institute of Technology, Haifa, Israel
Institut für Zytobiologie, Philipps-Universität Marburg, Germany
Department of Plant and Microbial Biology, University Zurich, Switzerland
International Research Centre for Environmental Membrane Biology, Foshan University, Foshan, China
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan
Department of Molecular Biosciences, Northwestern University, Evanston, IL, United States
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Netherlands
Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, United States
Institute of Enzymology, Research Center for Natural Sciences (RCNS), Budapest, Hungary
Institute of Biochemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany
Department of Biology/Microbial Physiology, Humboldt-University of Berlin, Germany
Institute of Biology, Westlake Institute for Advanced Study, School of Life Sciences, Westlake University, Hangzhou, China
Department of Chemical Physiology and Biochemistry, Oregon Health & Science University, Portland, OR, United States
Department of Biochemistry, Center for Biophysics and Quantitative Biology, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-ChampaignIL, United States
Department of Biological Sciences and Centre for Molecular Simulation, University of CalgaryAB, Canada
Institute for Integrated Cell-Material Sciences (WPI-iCeMS), KUIAS, Kyoto University, Japan
Department of Molecular Biology, Princeton UniversityNJ, United States
National Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China
Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO, United States
Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA, United States
Cited By :23
Export Date: 14 September 2021
CODEN: FEBLA
Correspondence Address: Thomas, C.; Institute of Biochemistry, Germany; email: c.thomas@em.uni-frankfurt.de
Correspondence Address: Tampé, R.; Institute of Biochemistry, Germany; email: tampe@em.uni-frankfurt.de
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Members of the ATP-binding cassette (ABC) transporter superfamily translocate a broad spectrum of chemically diverse substrates. While their eponymous ATP-binding cassette in the nucleotide-binding domains (NBDs) is highly conserved, their transmembrane domains (TMDs) forming the translocation pathway exhibit distinct folds and topologies, suggesting that during evolution the ancient motor domains were combined with different transmembrane mechanical systems to orchestrate a variety of cellular processes. In recent years, it has become increasingly evident that the distinct TMD folds are best suited to categorize the multitude of ABC transporters. We therefore propose a new ABC transporter classification that is based on structural homology in the TMDs. © 2020 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Thomas, C. ✉ </span> <span class="author-type"> </span> ; <span class="author-name" > Aller, S.G. </span> <span class="author-type"> </span> ; <span class="author-name" > Beis, K. </span> <span class="author-type"> </span> ; <span class="author-name" > Carpenter, E.P. </span> <span class="author-type"> </span> ; <span class="author-name" > Chang, G. </span> <span class="author-type"> </span> ; <span class="author-name" > Chen, L. </span> <span class="author-type"> </span> ; <span class="author-name" > Dassa, E. </span> <span class="author-type"> </span> ; <span class="author-name" > Dean, M. </span> <span class="author-type"> </span> ; <span class="author-name" > Duong, Van Hoa F. </span> <span class="author-type"> </span> ; <span class="author-name" > Ekiert, D. </span> <span class="author-type"> </span> et al. </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;31664473" mtid="31664473" target="_blank">Structural and functional diversity calls for a new classification of ABC transporters</a></div> <div class="pub-info"> <span class="journal-title">FEBS LETTERS</span> <span class="journal-volume">594</span> : <span class="journal-issue">23</span> <span class="page"> pp. 3767-3775. , 9 p. </span> <span class="year">(2020)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1002/1873-3468.13935" target="_blank" href="https://doi.org/10.1002/1873-3468.13935"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000583296400001" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000583296400001"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85093960508" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85093960508"> Scopus </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:31664473 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Sokszerzős vagy csoportos szerzőségű szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 141</span> | Független: 101 | Függő: 40 | Nem jelölt: 0 | WoS jelölt: 132 | Scopus jelölt: 136 | WoS/Scopus jelölt: 140 | DOI jelölt: 141 </div> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div><a target="_blank" href="/api/publication/31664473?labelLang=hun">Összes szerző</a></div>
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;31664473" target="_blank">Structural and functional diversity calls for a new classification of ABC transporters</a></div> <div> <span class="journal-title">FEBS LETTERS</span>
<span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/0014-5793">0014-5793</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/1873-3468">1873-3468</a>)</span>:
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pp 3767-3775
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<span class="language" xmlns="http://www.w3.org/1999/html">Nyelv:
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<span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 141</span>
| Független: 101
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Idézett közlemények száma: 3
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<div class="mtid"><span class="long-pub-mtid">Közlemény: 31664473</span>
| <span class="status-data status-APPROVED"> Nyilvános
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Forrás Idéző
| <span class="type-subtype">Folyóiratcikk
( Sokszerzős vagy csoportos szerzőségű szakcikk
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| <span class="pub-category">Tudományos</span>
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<div class="lastModified">Utolsó módosítás: 2020.12.22. 14:00 Sonnevend Kinga (SE_AOK_Adm5_Élet_kutcsop, admin)
</div>
<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Germany
Department of Pharmacology and Toxicology, University of Alabama at BirminghamAL, United States
Department of Life Sciences, Imperial College London, London South Kensington, United Kingdom
Rutherford Appleton Laboratory, Research Complex at Harwell,...</pre>
</div></div>
JournalArticle
30387986
ADMIN_APPROVED
true
Department of Medical Biochemistry, Semmelweis UniversityBudapest, Hungary
MTA-SE Ion Channel Research GroupBudapest, Hungary
Department of Neuroscience, Physiology and Pharmacology, University College London, London, United Kingdom
Laboratory of Cardiac/Membrane Physiology, The Rockefeller University, New York, NY, United States
Cited By :24
Export Date: 2 July 2020
CODEN: PHREA
Chemicals/CAS: adenosine triphosphate, 15237-44-2, 56-65-5, 987-65-5; cyclic AMP dependent protein kinase; cystic fibrosis transmembrane conductance regulator, 126880-72-6; Adenosine Triphosphate; Anions; Cystic Fibrosis Transmembrane Conductance Regulator
Funding details: Cystic Fibrosis Trust, CF
Funding text 1: Supported by Cystic Fibrosis Trust Project no. SRC 005 and Sparks Grant reference no. 15UCL04 (to P. Vergani), and Hungarian Academy of Sciences Lendület Grant LP2017–14/2017 and Cystic Fibrosis Foundation Research Grant CSANAD17G0 (to L. Csanády).
Department of Medical Biochemistry, Semmelweis UniversityBudapest, Hungary
MTA-SE Ion Channel Research GroupBudapest, Hungary
Department of Neuroscience, Physiology and Pharmacology, University College London, London, United Kingdom
Laboratory of Cardiac/Membrane Physiology, The Rockefeller University, New York, NY, United States
Cited By :60
Export Date: 11 August 2021
CODEN: PHREA
Funding Agency and Grant Number: Cystic Fibrosis Trust [SRC 005]; Sparks Grant [15UCL04]; Hungarian Academy of Sciences Lendulet Grant [LP2017-14/2017]; Cystic Fibrosis Foundation Research Grant [CSANAD17G0]
Funding text: Supported by Cystic Fibrosis Trust Project no. SRC 005 and Sparks Grant reference no. 15UCL04 (to P. Vergani), and Hungarian Academy of Sciences Lendulet Grant LP2017-14/2017 and Cystic Fibrosis Foundation Research Grant CSANAD17G0 (to L. Csanady).
Department of Medical Biochemistry, Semmelweis UniversityBudapest, Hungary
MTA-SE Ion Channel Research GroupBudapest, Hungary
Department of Neuroscience, Physiology and Pharmacology, University College London, London, United Kingdom
Laboratory of Cardiac/Membrane Physiology, The Rockefeller University, New York, NY, United States
Cited By :60
Export Date: 30 August 2021
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Department of Medical Biochemistry, Semmelweis UniversityBudapest, Hungary
MTA-SE Ion Channel Research GroupBudapest, Hungary
Department of Neuroscience, Physiology and Pharmacology, University College London, London, United Kingdom
Laboratory of Cardiac/Membrane Physiology, The Rockefeller University, New York, NY, United States
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The cystic fibrosis transmembrane conductance regulator (CFTR) belongs to the ATP binding cassette (ABC) transporter superfamily but functions as an anion channel crucial for salt and water transport across epithelial cells. CFTR dysfunction, because of mutations, causes cystic fibrosis (CF). The anion-selective pore of the CFTR protein is formed by its two transmembrane domains (TMDs) and regulated by its cytosolic domains: two nucleotide binding domains (NBDs) and a regulatory (R) domain. Channel activation requires phosphorylation of the R domain by cAMP-dependent protein kinase (PKA), and pore opening and closing (gating) of phosphorylated channels is driven by ATP binding and hydrolysis at the NBDs. This review summarizes available information on structure and mechanism of the CFTR protein, with a particular focus on atomic-level insight gained from recent cryo-electron microscopic structures and on the molecular mechanisms of channel gating and its regulation. The pharmacological mechanisms of small molecules targeting CFTR's ion channel function, aimed at treating patients suffering from CF and other diseases, are briefly discussed.
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Medical Biochemistry, Semmelweis UniversityBudapest, Hungary
MTA-SE Ion Channel Research GroupBudapest, Hungary
Department of Neuroscience, Physiology and Pharmacology, University College London, London, United Kingdom
Laboratory of Cardiac/Membrane Physiology, The Rockefeller University, New York, NY, United ...</pre>
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Correspondence Address: Chen, J.; Laboratory of Membrane Biophysics and Biology, 1230 York Avenue, United States
Chemicals/CAS: adenosine triphosphatase, 37289-25-1, 9000-83-3; adenosine triphosphate, 15237-44-2, 56-65-5, 987-65-5; arginine, 1119-34-2, 15595-35-4, 7004-12-8, 74-79-3; cyclic AMP dependent protein kinase; cysteine, 4371-52-2, 52-89-1, 52-90-4; cystic fibrosis transmembrane conductance regulator, 126880-72-6; lysine, 56-87-1, 6899-06-5, 70-54-2; multidrug resistance associated protein 1; proline, 147-85-3, 7005-20-1; protein, 67254-75-5; serine, 56-45-1, 6898-95-9; Adenosine Triphosphate; CFTR protein, human; CFTR protein, zebrafish; Cystic Fibrosis Transmembrane Conductance Regulator; Zebrafish Proteins
Funding details: LP2012-39/2012
Funding details: Howard Hughes Medical Institute, HHMI
Funding details: Cystic Fibrosis Foundation, CFF, CSANAD15G0
Funding details: Rockefeller University
Funding text 1: We thank Eric Gouaux for the expression vector, Mark Ebrahim and Johanna Sotiris at the Rockefeller Evelyn Gruss Lipper Cryo-Electron Microscopy Resource Center for assistance in data collection, and Sarah McCarry for editing this manuscript. This work is supported by the Rockefeller University (to J.C. and D.C.G), the Howard Hughes Medical Institute (to J.C.), and MTA-Momentum (LP2012-39/2012) and Cystic Fibrosis Foundation (CSANAD15G0) grants (to L.C.).
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The cystic fibrosis transmembrane conductance regulator (CFTR) is an ATP-binding cassette (ABC) transporter that uniquely functions as an ion channel. Here, we present a 3.9 Å structure of dephosphorylated human CFTR without nucleotides, determined by electron cryomicroscopy (cryo-EM). Close resemblance of this human CFTR structure to zebrafish CFTR under identical conditions reinforces its relevance for understanding CFTR function. The human CFTR structure reveals a previously unresolved helix belonging to the R domain docked inside the intracellular vestibule, precluding channel opening. By analyzing the sigmoid time course of CFTR current activation, we propose that PKA phosphorylation of the R domain is enabled by its infrequent spontaneous disengagement, which also explains residual ATPase and gating activity of dephosphorylated CFTR. From comparison with MRP1, a feature distinguishing CFTR from all other ABC transporters is the helix-loop transition in transmembrane helix 8, which likely forms the structural basis for CFTR's channel function. © 2017 Elsevier Inc.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Liu, F </span> <span class="author-type"> </span> ; <span class="author-name" > Zhang, Z </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10015499"> <a href="/gui2/?type=authors&mode=browse&sel=10015499" target="_blank">Csanády, L</a> </span> <span class="author-type"> </span> ; <span class="author-name" > Gadsby, DC </span> <span class="author-type"> </span> ; <span class="author-name" > Chen, J ✉ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;3210856" mtid="3210856" target="_blank">Molecular Structure of the Human CFTR Ion Channel</a></div> <div class="pub-info"> <span class="journal-title">CELL</span> <span class="journal-volume">169</span> : <span class="journal-issue">1</span> <span class="page"> pp. 85-95.e8. </span> <span class="year">(2017)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_NONE" title=" Nincs "> <a style="color:blue" title="10.1016/j.cell.2017.02.024" target="_blank" href="https://doi.org/10.1016/j.cell.2017.02.024"> DOI </a> </span> <span class="id identifier oa_CLOSED" title=" Zárt "> <a style="color:black" title="85753" target="_blank" href="http://real.mtak.hu/85753"> REAL </a> </span> <span class="id identifier oa_GREEN" title=" Green "> <a style="color:blue" title="6535" target="_blank" href="https://repo.lib.semmelweis.hu/handle/123456789/6535"> SE Repozitórium </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000397090000010" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000397090000010"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85016073190" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85016073190"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="28340353" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=28340353&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:3210856 </span> <span class="status-holder"><span class="status-data status-VALIDATED"> Egyeztetett </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 332</span> | Független: 314 | Függő: 18 | Nem jelölt: 0 | WoS jelölt: 324 | Scopus jelölt: 317 | WoS/Scopus jelölt: 332 | DOI jelölt: 330 </div> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;3210856" target="_blank">Molecular Structure of the Human CFTR Ion Channel</a></div> <div> <span class="journal-title">CELL</span>
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<div class="lastModified">Utolsó módosítás: 2021.05.14. 10:41 xBökönyi Zita (INAKTÍV_SE_AOK_OBI_Admin5_BZ, admin)
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :244
Export Date: 9 March 2022
CODEN: CELLB
Correspondence Address: Chen, J.; Laboratory of Membrane Biophysics and Biology, 1230 York Avenue, United States
Chemicals/CAS: adenosine triphosphatase, 37289-25-1, 9000-83-3; adenosine triphosphate, 15237-44-2, 56-65-5, 987-65-5; arginine, 1119-3...</pre>
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ABCG2/BCRP is a membrane protein, involved in xenobiotic and endobiotic transport in key pharmacological barriers and drug metabolizing organs, in the protection of stem cells, and in multidrug resistance of cancer. Pharmacogenetic studies implicated the role of ABCG2 in response to widely used medicines and anticancer agents, as well as in gout. Its Q141K variant exhibits decreased functional expression thus increased drug accumulation and decreased urate secretion. Still, there has been no reliable molecular model available for this protein, as the published structures of other ABC transporters could not be properly fitted to the ABCG2 topology and experimental data. The recently published high resolution structure of a close homologue, the ABCG5-ABCG8 heterodimer, revealed a new ABC transporter fold, unique for ABCG proteins. Here we present a structural model of the ABCG2 homodimer based on this fold and detail the experimental results supporting this model. In order to describe the effect of mutations on structure and dynamics, and characterize substrate recognition and cholesterol regulation we performed molecular dynamics simulations using full length ABCG2 protein embedded in a membrane bilayer and in silico docking simulations. Our results show that in the Q141K variant the introduced positive charge diminishes the interaction between the nucleotide binding and transmembrane domains and the R482G variation alters the orientation of transmembrane helices. Moreover, the R482 position, which plays a role the substrate specificity of the transporter, is located in one of the substrate binding pockets identified by the in silico docking calculations. In summary, the ABCG2 model and in silico simulations presented here may have significant impact on understanding drug distribution and toxicity, as well as drug development against cancer chemotherapy resistance or gout. © 2016 László et al.This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > László, L </span> <span class="author-type"> </span> ; <span class="author-name" mtid="1241938"> <a href="/gui2/?type=authors&mode=browse&sel=1241938" target="_blank">Sarkadi, B</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10015687"> <a href="/gui2/?type=authors&mode=browse&sel=10015687" target="_blank">Hegedüs, T ✉</a> </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;3135666" mtid="3135666" target="_blank">Jump into a new fold-A homology based model for the ABCG2/BCRP multidrug transporter</a></div> <div class="pub-info"> <span class="journal-title">PLOS ONE</span> <span class="journal-volume">11</span> : <span class="journal-issue">10</span> <span class="page"> Paper: e0164426 </span> <span class="year">(2016)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.1371/journal.pone.0164426" target="_blank" href="https://doi.org/10.1371/journal.pone.0164426"> DOI </a> </span> <span class="id identifier oa_GREEN" title=" Green "> <a style="color:black" title="42291" target="_blank" href="http://real.mtak.hu/42291"> REAL </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000385507000032" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000385507000032"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84992161913" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84992161913"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:black" title="27741279" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=27741279&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="deleted-record">Zárolt</span> <span class="short-pub-mtid"> Közlemény:3135666 </span> <span class="status-holder"><span class="status-data status-VALIDATED"> Egyeztetett </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 43</span> | Független: 36 | Függő: 7 | Nem jelölt: 0 | WoS jelölt: 43 | Scopus jelölt: 42 | WoS/Scopus jelölt: 43 | DOI jelölt: 43 </div> </div> </div> </div><div class="JournalArticle Publication long-list"> <div class="authors"> <img title="Forrásközlemény" style="float: left" src="/frontend/resources/grid/publication-core-icon.png"> <img title="Idézőközlemény" style="float: left" src="/frontend/resources/grid/publication-citation-icon.png"> <div class="autype autype0"> <span class="author-name" >László L </span> ; <span class="author-name" mtid="1241938"><a href="/gui2/?type=authors&mode=browse&sel=1241938" target="_blank">Sarkadi B (<span class="authorship-author-name">Sarkadi Balázs</span> <span class="authorAux-mtmt"> biofizika</span>) </a> </span> <span class="author-affil"><span title="MTA Természettudományi Kutatóközpont">MTA TTK</span>/Enzimológiai Intézet</span> ; <span class="author-name" mtid="10015687"><a href="/gui2/?type=authors&mode=browse&sel=10015687" target="_blank">Hegedüs T ✉ (<span class="authorship-author-name">Hegedűs Tamás</span> <span class="authorAux-mtmt"> bioinformatika, biofizika</span>) </a> </span> <span class="author-affil"><span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Intézet">I</span>/Biofizikai és Sugárbiológiai Intézet; <span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Intézet">I</span>/<span title="Biofizikai és Sugárbiológiai Intézet">BSI</span>/MTA-SE Molekuláris Biofizikai Kutatócsoport</span> </div> </div> <div class="title"><a href="/gui2/?mode=browse¶ms=publication;3135666" target="_blank">Jump into a new fold-A homology based model for the ABCG2/BCRP multidrug transporter</a></div> <div> <span class="journal-title">PLOS ONE</span> <span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/1932-6203">1932-6203</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/1932-6203">1932-6203</a>)</span>: <span class="journal-volume">11</span> <span class="journal-issue">10</span> <span class="page"> Paper e0164426. </span> <span class="year">(2016)</span> </div> <div class="pub-footer"> <span class="language" xmlns="http://www.w3.org/1999/html">Nyelv: Angol | </span> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.1371/journal.pone.0164426" target="_blank" href="https://doi.org/10.1371/journal.pone.0164426"> DOI </a> </span> <span class="id identifier oa_GREEN" title=" Green "> <a style="color:black" title="42291" target="_blank" href="http://real.mtak.hu/42291"> REAL </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000385507000032" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000385507000032"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84992161913" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84992161913"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:black" title="27741279" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=27741279&dopt=Abstract"> PubMed </a> </span> </span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 43</span> | Független: 36 | Függő: 7 | Nem jelölt: 0 | WoS jelölt: 43 | Scopus jelölt: 42 | WoS/Scopus jelölt: 43 | DOI jelölt: 43 </div> <div class="publication-citation"> <a target="_blank" href="/api/publication?cond=citations.related;eq;3135666&sort=publishedYear,desc&sort=title"> Idézett közlemények száma: 20 </a> </div> <div class="mtid"><span class="long-pub-mtid">Közlemény: 3135666</span> | <span class="status-data status-VALIDATED"> Egyeztetett </span> <span class="oldId">Régi azonosító: 3135666</span> | Forrás Idéző | <span class="type-subtype">Folyóiratcikk ( Szakcikk ) </span> | <span class="pub-category">Tudományos</span> | <span class="publication-sourceOfData">Scopus</span> </div> <div class="lastModified">Utolsó módosítás: 2021.05.12. 13:03 Csajbók Edit (SE_KK_Admin5_CSE, admin) </div> <div class="lockedBy">Ideiglenesen zárolva 2022.07.08. 12:16 Boros Annamária (MTMT Központi admin) </div> </div></div>
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Department of Physiology, United States
Department of Biochemistry, United States
GRASP, McGill University, Montréal, QC H3G 1Y6, Canada
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States
Marsico Lung Institute, School of Medicine, University of North Carolina, Chapel Hill, NC 27514, United States
School of Physiology and Pharmacology, University of Bristol, Bristol, BS8 1TD, United Kingdom
Department of Cell Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, United States
Department of Cellular, Developmental, and Integrative Biology, University of Alabama, Birmingham, AL 35294, United States
Department of Anatomy, Physiology and Genetics and Center for Medical Proteomics, Uniformed Services University of Health Sciences, Bethesda, MD 20814, United States
KMcKusick-Nathans Institute of Genetic Medicine, School of Medicine, Johns Hopkins University, Baltimore, MD 21205, United States
Scripps Research Institute, Department of Chemical Physiology, Skaggs Institute of Chemical Physiology, San Diego, CA 92037, United States
Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239, United States
Department of Pediatrics, Emory University School of Medicine, Atlanta, GA 30322, United States
Cited By :224
Export Date: 10 August 2021
CODEN: MBCEE
Correspondence Address: Lukacs, G.L.; GRASP, Canada; email: gergely.lukacs@mcgill.ca
Department of Physiology, United States
Department of Biochemistry, United States
GRASP, McGill University, Montréal, QC H3G 1Y6, Canada
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States
Marsico Lung Institute, School of Medicine, University of North Carolina, Chapel Hill, NC 27514, United States
School of Physiology and Pharmacology, University of Bristol, Bristol, BS8 1TD, United Kingdom
Department of Cell Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, United States
Department of Cellular, Developmental, and Integrative Biology, University of Alabama, Birmingham, AL 35294, United States
Department of Anatomy, Physiology and Genetics and Center for Medical Proteomics, Uniformed Services University of Health Sciences, Bethesda, MD 20814, United States
KMcKusick-Nathans Institute of Genetic Medicine, School of Medicine, Johns Hopkins University, Baltimore, MD 21205, United States
Scripps Research Institute, Department of Chemical Physiology, Skaggs Institute of Chemical Physiology, San Diego, CA 92037, United States
Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239, United States
Department of Pediatrics, Emory University School of Medicine, Atlanta, GA 30322, United States
Cited By :225
Export Date: 11 August 2021
CODEN: MBCEE
Correspondence Address: Lukacs, G.L.; GRASP, Canada; email: gergely.lukacs@mcgill.ca
Funding Agency and Grant Number: National Institutes of Health (NIH)United States Department of Health & Human ServicesNational Institutes of Health (NIH) - USA [NO1-HL28187, IAA-A-HL-14-007.001, R01 DK, CFF CUTT13A1, CUTTXX0, R01-DK068196, P30-DK072506, CFFT FRIZZE05X0]; Cystic Fibrosis Foundation (CFF) [NIH DK51870, TRDRP23RT-0012, HL095524]; CFFT [SHEPPA14XX0, BROD-SK13XX0, NIH GM75061]; Cystic Fibrosis Trust; CFF Research Development Program, CFFT [SORSCH05XXO, SORSCH14XXO]; CF Canada [CFFT Lukacs13XXO, NIH DK075302]; Canadian Institutes of Health ResearchCanadian Institutes of Health Research (CIHR); CF Canada Studentship; Canada Research ChairNatural Resources CanadaCanadian Forest ServiceCanada Research Chairs; Cystic Fibrosis Trust [SRC005] Funding Source: researchfish; NATIONAL HEART, LUNG, AND BLOOD INSTITUTEUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Heart Lung & Blood Institute (NHLBI) [R01HL095524] Funding Source: NIH RePORTER; NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Diabetes & Digestive & Kidney Diseases (NIDDK) [P30DK072482, R01DK068196, R01DK044003, R01DK075302, R01DK051870, P30DK079307, P30DK072506] Funding Source: NIH RePORTER; NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [R01GM056981, R01GM067785, R01GM075061] Funding Source: NIH RePORTER
Funding text: We thank the members of the CFTR Folding Consortium, the CFTR Theratype Group, C. M. Penland, and K. Tuggle (Cystic Fibrosis Foundation, Bethesda, MD) for their valuable support. The work described here was supported by the following institutions and grants: National Institutes of Health (NIH) NO1-HL28187 and IAA-A-HL-14-007.001 to H.B.P.; Cystic Fibrosis Foundation (CFF), NIH DK51870, TRDRP23RT-0012, and HL095524 to W.E.B.; NIH R01 DK, CFF CUTT13A1, and CUTTXX0 to G.R.C.; CFFT SHEPPA14XX0 and Cystic Fibrosis Trust to D.N.S.; NIH R01-DK068196, P30-DK072506, and CFFT FRIZZE05X0 to R.A.F.; NIH RO1 GM56981 and CFFT CYR13XX0 to D.M.C.; the CFF Research Development Program, CFFT SORSCH05XXO, and SORSCH14XXO to E.J.S.; CFFT BROD-SK13XX0 and NIH GM75061 to J.L.B.; CF Canada, CFFT Lukacs13XXO, NIH DK075302, and Canadian Institutes of Health Research to G.L.L. R.G.A. was supported by CF Canada Studentship; G.L.L. is a recipient of a Canada Research Chair.
Department of Physiology, United States
Department of Biochemistry, United States
GRASP, McGill University, Montréal, QC H3G 1Y6, Canada
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States
Marsico Lung Institute, School of Medicine, University of North Carolina, Chapel Hill, NC 27514, United States
School of Physiology and Pharmacology, University of Bristol, Bristol, BS8 1TD, United Kingdom
Department of Cell Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, United States
Department of Cellular, Developmental, and Integrative Biology, University of Alabama, Birmingham, AL 35294, United States
Department of Anatomy, Physiology and Genetics and Center for Medical Proteomics, Uniformed Services University of Health Sciences, Bethesda, MD 20814, United States
KMcKusick-Nathans Institute of Genetic Medicine, School of Medicine, Johns Hopkins University, Baltimore, MD 21205, United States
Scripps Research Institute, Department of Chemical Physiology, Skaggs Institute of Chemical Physiology, San Diego, CA 92037, United States
Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239, United States
Department of Pediatrics, Emory University School of Medicine, Atlanta, GA 30322, United States
Cited By :226
Export Date: 28 August 2021
CODEN: MBCEE
Correspondence Address: Lukacs, G.L.; GRASP, Canada; email: gergely.lukacs@mcgill.ca
Funding Agency and Grant Number: National Institutes of Health (NIH)United States Department of Health & Human ServicesNational Institutes of Health (NIH) - USA [NO1-HL28187, IAA-A-HL-14-007.001, R01 DK, CFF CUTT13A1, CUTTXX0, R01-DK068196, P30-DK072506, CFFT FRIZZE05X0]; Cystic Fibrosis Foundation (CFF) [NIH DK51870, TRDRP23RT-0012, HL095524]; CFFT [SHEPPA14XX0, BROD-SK13XX0, NIH GM75061]; Cystic Fibrosis Trust; CFF Research Development Program, CFFT [SORSCH05XXO, SORSCH14XXO]; CF Canada [CFFT Lukacs13XXO, NIH DK075302]; Canadian Institutes of Health ResearchCanadian Institutes of Health Research (CIHR); CF Canada Studentship; Canada Research ChairNatural Resources CanadaCanadian Forest ServiceCanada Research Chairs; Cystic Fibrosis Trust [SRC005] Funding Source: researchfish; NATIONAL HEART, LUNG, AND BLOOD INSTITUTEUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Heart Lung & Blood Institute (NHLBI) [R01HL095524] Funding Source: NIH RePORTER; NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Diabetes & Digestive & Kidney Diseases (NIDDK) [P30DK079307, P30DK072506, R01DK044003, R01DK068196, R01DK051870, R01DK075302, P30DK072482] Funding Source: NIH RePORTER; NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [R01GM067785, R01GM075061, R01GM056981] Funding Source: NIH RePORTER
Funding text: We thank the members of the CFTR Folding Consortium, the CFTR Theratype Group, C. M. Penland, and K. Tuggle (Cystic Fibrosis Foundation, Bethesda, MD) for their valuable support. The work described here was supported by the following institutions and grants: National Institutes of Health (NIH) NO1-HL28187 and IAA-A-HL-14-007.001 to H.B.P.; Cystic Fibrosis Foundation (CFF), NIH DK51870, TRDRP23RT-0012, and HL095524 to W.E.B.; NIH R01 DK, CFF CUTT13A1, and CUTTXX0 to G.R.C.; CFFT SHEPPA14XX0 and Cystic Fibrosis Trust to D.N.S.; NIH R01-DK068196, P30-DK072506, and CFFT FRIZZE05X0 to R.A.F.; NIH RO1 GM56981 and CFFT CYR13XX0 to D.M.C.; the CFF Research Development Program, CFFT SORSCH05XXO, and SORSCH14XXO to E.J.S.; CFFT BROD-SK13XX0 and NIH GM75061 to J.L.B.; CF Canada, CFFT Lukacs13XXO, NIH DK075302, and Canadian Institutes of Health Research to G.L.L. R.G.A. was supported by CF Canada Studentship; G.L.L. is a recipient of a Canada Research Chair.
Department of Physiology, United States
Department of Biochemistry, United States
GRASP, McGill University, Montréal, QC H3G 1Y6, Canada
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States
Marsico Lung Institute, School of Medicine, University of North Carolina, Chapel Hill, NC 27514, United States
School of Physiology and Pharmacology, University of Bristol, Bristol, BS8 1TD, United Kingdom
Department of Cell Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, United States
Department of Cellular, Developmental, and Integrative Biology, University of Alabama, Birmingham, AL 35294, United States
Department of Anatomy, Physiology and Genetics and Center for Medical Proteomics, Uniformed Services University of Health Sciences, Bethesda, MD 20814, United States
KMcKusick-Nathans Institute of Genetic Medicine, School of Medicine, Johns Hopkins University, Baltimore, MD 21205, United States
Scripps Research Institute, Department of Chemical Physiology, Skaggs Institute of Chemical Physiology, San Diego, CA 92037, United States
Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239, United States
Department of Pediatrics, Emory University School of Medicine, Atlanta, GA 30322, United States
Cited By :226
Export Date: 29 August 2021
CODEN: MBCEE
Correspondence Address: Lukacs, G.L.; GRASP, Canada; email: gergely.lukacs@mcgill.ca
Department of Physiology, United States
Department of Biochemistry, United States
GRASP, McGill University, Montréal, QC H3G 1Y6, Canada
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States
Marsico Lung Institute, School of Medicine, University of North Carolina, Chapel Hill, NC 27514, United States
School of Physiology and Pharmacology, University of Bristol, Bristol, BS8 1TD, United Kingdom
Department of Cell Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, United States
Department of Cellular, Developmental, and Integrative Biology, University of Alabama, Birmingham, AL 35294, United States
Department of Anatomy, Physiology and Genetics and Center for Medical Proteomics, Uniformed Services University of Health Sciences, Bethesda, MD 20814, United States
KMcKusick-Nathans Institute of Genetic Medicine, School of Medicine, Johns Hopkins University, Baltimore, MD 21205, United States
Scripps Research Institute, Department of Chemical Physiology, Skaggs Institute of Chemical Physiology, San Diego, CA 92037, United States
Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239, United States
Department of Pediatrics, Emory University School of Medicine, Atlanta, GA 30322, United States
Cited By :226
Export Date: 30 August 2021
CODEN: MBCEE
Correspondence Address: Lukacs, G.L.; GRASP, Canada; email: gergely.lukacs@mcgill.ca
Department of Physiology, United States
Department of Biochemistry, United States
GRASP, McGill University, Montréal, QC H3G 1Y6, Canada
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States
Marsico Lung Institute, School of Medicine, University of North Carolina, Chapel Hill, NC 27514, United States
School of Physiology and Pharmacology, University of Bristol, Bristol, BS8 1TD, United Kingdom
Department of Cell Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, United States
Department of Cellular, Developmental, and Integrative Biology, University of Alabama, Birmingham, AL 35294, United States
Department of Anatomy, Physiology and Genetics and Center for Medical Proteomics, Uniformed Services University of Health Sciences, Bethesda, MD 20814, United States
KMcKusick-Nathans Institute of Genetic Medicine, School of Medicine, Johns Hopkins University, Baltimore, MD 21205, United States
Scripps Research Institute, Department of Chemical Physiology, Skaggs Institute of Chemical Physiology, San Diego, CA 92037, United States
Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239, United States
Department of Pediatrics, Emory University School of Medicine, Atlanta, GA 30322, United States
Cited By :226
Export Date: 31 August 2021
CODEN: MBCEE
Correspondence Address: Lukacs, G.L.; GRASP, Canada; email: gergely.lukacs@mcgill.ca
Department of Physiology, United States
Department of Biochemistry, United States
GRASP, McGill University, Montréal, QC H3G 1Y6, Canada
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States
Marsico Lung Institute, School of Medicine, University of North Carolina, Chapel Hill, NC 27514, United States
School of Physiology and Pharmacology, University of Bristol, Bristol, BS8 1TD, United Kingdom
Department of Cell Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, United States
Department of Cellular, Developmental, and Integrative Biology, University of Alabama, Birmingham, AL 35294, United States
Department of Anatomy, Physiology and Genetics and Center for Medical Proteomics, Uniformed Services University of Health Sciences, Bethesda, MD 20814, United States
KMcKusick-Nathans Institute of Genetic Medicine, School of Medicine, Johns Hopkins University, Baltimore, MD 21205, United States
Scripps Research Institute, Department of Chemical Physiology, Skaggs Institute of Chemical Physiology, San Diego, CA 92037, United States
Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239, United States
Department of Pediatrics, Emory University School of Medicine, Atlanta, GA 30322, United States
Cited By :226
Export Date: 1 September 2021
CODEN: MBCEE
Correspondence Address: Lukacs, G.L.; GRASP, Canada; email: gergely.lukacs@mcgill.ca
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Veit, Gudio </span> <span class="author-type"> </span> ; <span class="author-name" > Avramescu, Radu G </span> <span class="author-type"> </span> ; <span class="author-name" > Chiang, Annette N </span> <span class="author-type"> </span> ; <span class="author-name" > Houck, Scott A </span> <span class="author-type"> </span> ; <span class="author-name" > Cai, Zhiwei </span> <span class="author-type"> </span> ; <span class="author-name" > Peters, Kathryn W </span> <span class="author-type"> </span> ; <span class="author-name" > Hong, Jeong S </span> <span class="author-type"> </span> ; <span class="author-name" > Pollard, Harvey B </span> <span class="author-type"> </span> ; <span class="author-name" > Guggino, William B </span> <span class="author-type"> </span> ; <span class="author-name" > Balch, William E </span> <span class="author-type"> </span> et al. </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;25803207" mtid="25803207" target="_blank">From CFTR biology toward combinatorial pharmacotherapy: expanded classification of cystic fibrosis mutations</a></div> <div class="pub-info"> <span class="journal-title">MOLECULAR BIOLOGY OF THE CELL</span> <span class="journal-volume">27</span> : <span class="journal-issue">3</span> <span class="page"> pp. 424-433. , 10 p. </span> <span class="year">(2016)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1091/mbc.E14-04-0935" target="_blank" href="https://doi.org/10.1091/mbc.E14-04-0935"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000369127200002" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000369127200002"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84956613592" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84956613592"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="26823392" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=26823392&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:25803207 </span> <span class="status-holder"><span class="status-data status-VALIDATED"> Egyeztetett </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 364</span> | Független: 308 | Függő: 56 | Nem jelölt: 0 | WoS jelölt: 359 | Scopus jelölt: 321 | WoS/Scopus jelölt: 364 | DOI jelölt: 352 (Nem nyilvános: 2) </div> </div> </div> </div><div class="JournalArticle Publication long-list">
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<span class="authorAux-mtmt"> cisztásfibrózis, membrán fehérjék</span>)
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;25803207" target="_blank">From CFTR biology toward combinatorial pharmacotherapy: expanded classification of cystic fibrosis mutations</a></div> <div> <span class="journal-title">MOLECULAR BIOLOGY OF THE CELL</span>
<span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/1059-1524">1059-1524</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/1939-4586">1939-4586</a>)</span>:
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<span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 364</span>
| Független: 308
| Függő: 56
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<div class="mtid"><span class="long-pub-mtid">Közlemény: 25803207</span>
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<div class="lastModified">Utolsó módosítás: 2021.08.10. 13:13 Csajbók Edit (SE_KK_Admin5_CSE, admin)
</div>
<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
Department of Physiology, United States
Department of Biochemistry, United States
GRASP, McGill University, Montréal, QC H3G 1Y6, Canada
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States ...</pre>
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" mtid="10050230"> <a href="/gui2/?type=authors&mode=browse&sel=10050230" target="_blank">Dobson, L</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10054035"> <a href="/gui2/?type=authors&mode=browse&sel=10054035" target="_blank">Reményi, I</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10000061"> <a href="/gui2/?type=authors&mode=browse&sel=10000061" target="_blank">Tusnády, GE ✉</a> </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;2918485" mtid="2918485" target="_blank">CCTOP: a Consensus Constrained TOPology prediction web server.</a></div> <div class="pub-info"> <span class="journal-title">NUCLEIC ACIDS RESEARCH</span> <span class="journal-volume">43</span> : <span class="journal-issue">W1</span> <span class="page"> pp. W408-W412. </span> <span class="year">(2015)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.1093/nar/gkv451" target="_blank" href="https://doi.org/10.1093/nar/gkv451"> DOI </a> </span> <span class="id identifier oa_GREEN" title=" Green "> <a style="color:black" title="26004" target="_blank" href="http://real.mtak.hu/26004"> REAL </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000359772700064" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000359772700064"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84979853667" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84979853667"> Scopus </a> </span> <span class="id identifier oa_GREEN" title=" Green "> <a style="color:black" title="25943549" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=25943549&dopt=Abstract"> PubMed </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:black" title="http://nar.oxfordjournals.org/content/early/2015/05/04/nar.gkv451.full" target="_blank" href="http://nar.oxfordjournals.org/content/early/2015/05/04/nar.gkv451.full"> Teljes dokumentum </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:2918485 </span> <span class="status-holder"><span class="status-data status-VALIDATED"> Egyeztetett </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 274</span> | Független: 254 | Függő: 20 | Nem jelölt: 0 | WoS jelölt: 255 | Scopus jelölt: 260 | WoS/Scopus jelölt: 272 | DOI jelölt: 271 </div> </div> </div> </div><div class="JournalArticle Publication long-list"> <div class="authors"> <img title="Forrásközlemény" style="float: left" src="/frontend/resources/grid/publication-core-icon.png"> <img title="Idézőközlemény" style="float: left" src="/frontend/resources/grid/publication-citation-icon.png"> <div class="autype autype0"> <span class="author-name" mtid="10050230"><a href="/gui2/?type=authors&mode=browse&sel=10050230" target="_blank">Dobson L (<span class="authorship-author-name">Dobson László</span> <span class="authorAux-mtmt"> Bioinformatika</span>) </a> </span> <span class="author-affil"><span title="MTA Természettudományi Kutatóközpont">MTA TTK</span>/Enzimológiai Intézet</span> ; <span class="author-name" mtid="10054035"><a href="/gui2/?type=authors&mode=browse&sel=10054035" target="_blank">Reményi I (<span class="authorship-author-name">Reményi István</span> <span class="authorAux-mtmt"> Informatika</span>) </a> </span> ; <span class="author-name" mtid="10000061"><a href="/gui2/?type=authors&mode=browse&sel=10000061" target="_blank">Tusnády GE ✉ (<span class="authorship-author-name">Tusnády Gábor</span> <span class="authorAux-mtmt"> Bioinformatika</span>) </a> </span> </div> </div> <div class="title"><a href="/gui2/?mode=browse¶ms=publication;2918485" target="_blank">CCTOP: a Consensus Constrained TOPology prediction web server.</a></div> <div> <span class="journal-title">NUCLEIC ACIDS RESEARCH</span> <span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/0305-1048">0305-1048</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/1362-4962">1362-4962</a>)</span>: <span class="journal-volume">43</span> <span class="journal-issue">W1</span> <span class="page"> pp W408-W412 </span> <span class="year">(2015)</span> </div> <div class="pub-footer"> <span class="language" xmlns="http://www.w3.org/1999/html">Nyelv: Angol | </span> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.1093/nar/gkv451" target="_blank" href="https://doi.org/10.1093/nar/gkv451"> DOI </a> </span> <span class="id identifier oa_GREEN" title=" Green "> <a style="color:black" title="26004" target="_blank" href="http://real.mtak.hu/26004"> REAL </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000359772700064" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000359772700064"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84979853667" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84979853667"> Scopus </a> </span> <span class="id identifier oa_GREEN" title=" Green "> <a style="color:black" title="25943549" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=25943549&dopt=Abstract"> PubMed </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:black" title="http://nar.oxfordjournals.org/content/early/2015/05/04/nar.gkv451.full" target="_blank" href="http://nar.oxfordjournals.org/content/early/2015/05/04/nar.gkv451.full"> Teljes dokumentum </a> </span> </span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 274</span> | Független: 254 | Függő: 20 | Nem jelölt: 0 | WoS jelölt: 255 | Scopus jelölt: 260 | WoS/Scopus jelölt: 272 | DOI jelölt: 271 </div> <div class="publication-citation"> <a target="_blank" href="/api/publication?cond=citations.related;eq;2918485&sort=publishedYear,desc&sort=title"> Idézett közlemények száma: 13 </a> </div> <div class="mtid"><span class="long-pub-mtid">Közlemény: 2918485</span> | <span class="status-data status-VALIDATED"> Egyeztetett </span> <span class="oldId">Régi azonosító: 2918485</span> | Forrás Idéző | <span class="type-subtype">Folyóiratcikk ( Szakcikk ) </span> | <span class="pub-category">Tudományos</span> | <span class="publication-sourceOfData">kézi felvitel</span> </div> <div class="funder"> (K104586) Támogató: OTKA, (‘Momentum’ Program of the Hungarian Academy of Science) </div> <div class="notDuplums"><a target="_blank" href="/api/publication/2918485/notduplums">1 Nem duplumnak jelölés</a> </div> <div class="lastModified">Utolsó módosítás: 2024.02.12. 08:37 Molnár-Taga Márta (SE 4-es admin) </div> </div></div>
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Export Date: 29 September 2023
Correspondence Address: Tusnády, G.E.; 'Momentum' Membrane Protein Bioinformatics Research Group, PO Box 7, Hungary; email: tusnady.gabor@ttk.mta.hu
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The human transmembrane proteome
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Background: Transmembrane proteins have important roles in cells, as they are involved in energy production, signal transduction, cell-cell interaction, cell-cell communication and more. In human cells, they are frequently targets for pharmaceuticals; therefore, knowledge about their properties and structure is crucial. Topology of transmembrane proteins provide a low resolution structural information, which can be a starting point for either laboratory experiments or modelling their 3D structures. Results: Here, we present a database of the human α-helical transmembrane proteome, including the predicted and/or experimentally established topology of each transmembrane protein, together with the reliability of the prediction. In order to distinguish transmembrane proteins in the proteome as well as for topology prediction, we used a newly developed consensus method (CCTOP) that incorporates recent state of the art methods, with tested accuracies on a novel human benchmark protein set. CCTOP utilizes all available structure and topology data as well as bioinformatical evidences for topology prediction in a probabilistic framework provided by the hidden Markov model. This method shows the highest accuracy (98.5 % for discrinimating between transmembrane and non-transmembrane proteins and 84 % for per protein topology prediction) among the dozen tested topology prediction methods. Analysis of the human proteome with the CCTOP indicates that it contains 4998 (26 %) transmembrane proteins. Besides predicting topology, reliability of the predictions is estimated as well, and it is demonstrated that the per protein prediction accuracies of more than 60 % of the predictions are over 98 % on the benchmark sets and most probably on the predicted human transmembrane proteome too. Conclusions: Here, we present the most accurate prediction of the human transmembrane proteome together with the experimental topology data. These data, as well as various statistics about the human transmembrane proteins and their topologies can be downloaded from and can be visualized at the website of the human transmembrane proteome (http://htp.enzim.hu). Reviewers: This article was reviewed by Dr. Sandor Pongor, Dr. Michael Galperin and Dr. Pascale Gaudet (nominated by Dr Michael Galperin). © 2015 Dobson et al.; licensee BioMed Central.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" mtid="10050230"> <a href="/gui2/?type=authors&mode=browse&sel=10050230" target="_blank">Dobson, L</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10054035"> <a href="/gui2/?type=authors&mode=browse&sel=10054035" target="_blank">Reményi, I</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10000061"> <a href="/gui2/?type=authors&mode=browse&sel=10000061" target="_blank">Tusnády, GE</a> </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;2905250" mtid="2905250" target="_blank">The human transmembrane proteome</a></div> <div class="pub-info"> <span class="journal-title">BIOLOGY DIRECT</span> <span class="journal-volume">10</span> <span class="page"> Paper: 31 , 18 p. </span> <span class="year">(2015)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.1186/s13062-015-0061-x" target="_blank" href="https://doi.org/10.1186/s13062-015-0061-x"> DOI </a> </span> <span class="id identifier oa_GREEN" title=" Green "> <a style="color:black" title="24606" target="_blank" href="http://real.mtak.hu/24606"> REAL </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000355161200001" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000355161200001"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84929920413" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84929920413"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:black" title="26018427" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=26018427&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:2905250 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 85</span> | Független: 65 | Függő: 20 | Nem jelölt: 0 | WoS jelölt: 76 | Scopus jelölt: 80 | WoS/Scopus jelölt: 82 | DOI jelölt: 83 </div> </div> </div> </div><div class="JournalArticle Publication long-list">
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<span class="author-name" mtid="10000061"><a
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<span class="authorAux-mtmt"> Bioinformatika</span>)
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;2905250" target="_blank">The human transmembrane proteome</a></div> <div> <span class="journal-title">BIOLOGY DIRECT</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :74
Export Date: 29 September 2023
Correspondence Address: Tusnády, G.E.; 'Momentum' Membrane Protein Bioinformatics Research Group, PO Box 7, Hungary; email: tusnady.gabor@ttk.mta.hu</pre>
</div></div>
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Lendület Membrane Protein Bioinformatics Research Group, Institute of Enzymology, MTA RCNS, PO Box 7, H-1518 Budapest, Hungary
Protein Structure Research Group, Institute of Enzymology, MTA RCNS, PO Box 7, H-1518 Budapest, Hungary
Cited By :199
Export Date: 29 September 2023
CODEN: NARHA
Correspondence Address: Tusnády, G.E.; Lendület Membrane Protein Bioinformatics Research Group, PO Box 7, H-1518 Budapest, Hungary; email: tusnady.gabor@ttk.mta.hu
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Lendület Membrane Protein Bioinformatics Research Group, Institute of Enzymology, MTA RCNS, PO Box 7, H-1518 Budapest, Hungary
Protein Structure Research Group, Institute of Enzymology, MTA RCNS, PO Box 7, H-1518 Budapest, Hungary
Cited By :199
Export Date: 29 September 2023
CODEN: NARHA
...</pre>
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Serohijos AW and Hegedus T authors contributed equally to this
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Funding Agency and Grant Number: Cystic Fibrosis FoundationItalian Cystic Fibrosis Research Foundation [DOKHOL07I0]; NIHUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USA [DK051870]; AHA Predoctoral FellowshipAmerican Heart Association [0715215U]; NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Diabetes & Digestive & Kidney Diseases (NIDDK) [R01DK051870] Funding Source: NIH RePORTER
Funding text: This work is partially supported by Cystic Fibrosis Foundation grant DOKHOL07I0 (to NVD) and by the NIH grant DK051870 (to JRR). AWRS is supported by an AHA Predoctoral Fellowship, 0715215U.
Department of Physics and Astronomy, University of North Carolina Chapel Hill, Chapel Hill, NC, United States
Department of Biochemistry and Biophysics, University of North Carolina Chapel Hill, Chapel Hill, NC, United States
Cystic Fibrosis Research Center, University of North Carolina Chapel Hill, Chapel Hill, NC, United States
Cited By :33
Export Date: 31 August 2021
Correspondence Address: Serohijos, A. W. R.; Department of Physics and Astronomy, , Chapel Hill, NC, United States
Department of Physics and Astronomy, University of North Carolina Chapel Hill, Chapel Hill, NC, United States
Department of Biochemistry and Biophysics, University of North Carolina Chapel Hill, Chapel Hill, NC, United States
Cystic Fibrosis Research Center, University of North Carolina Chapel Hill, Chapel Hill, NC, United States
Cited By :33
Export Date: 2 September 2021
Correspondence Address: Serohijos, A. W. R.; Department of Physics and Astronomy, , Chapel Hill, NC, United States
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The absence of a functional ATP Binding Cassette (ABC) protein called the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) from apical membranes of epithelial cells is responsible for cystic fibrosis (CF). Over 90% of CF patients carry at least one mutant allele with deletion of phenylalanine at position 508 located in the N-terminal nucleotide binding domain (NBD1). Biochemical and cell biological studies show that the DeltaF508 mutant exhibits inefficient biosynthetic maturation and susceptibility to degradation probably due to misfolding of NBD1 and the resultant misassembly of other domains. However, little is known about the direct effect of the Phe508 deletion on the NBD1 folding, which is essential for rational design strategies of cystic fibrosis treatment. Here we show that the deletion of Phe508 alters the folding dynamics and kinetics of NBD1, thus possibly affecting the assembly of the complete CFTR. Using molecular dynamics simulations, we find that meta-stable intermediate states appearing on wild type and mutant folding pathways are populated differently and that their kinetic accessibilities are distinct. The structural basis of the increased misfolding propensity of the DeltaF508 NBD1 mutant is the perturbation of interactions in residue pairs Q493/P574 and F575/F578 found in loop S7-H6. As a proof-of-principle that the S7-H6 loop conformation can modulate the folding kinetics of NBD1, we virtually design rescue mutations in the identified critical interactions to force the S7-H6 loop into the wild type conformation. Two redesigned NBD1-DeltaF508 variants exhibited significantly higher folding probabilities than the original NBD1-DeltaF508, thereby partially rescuing folding ability of the NBD1-DeltaF508 mutant. We propose that these observed defects in folding kinetics of mutant NBD1 may also be modulated by structures separate from the 508 site. The identified structural determinants of increased misfolding propensity of NBD1-DeltaF508 are essential information in correcting this pathogenic mutant.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Serohijos, AW </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10015687"> <a href="/gui2/?type=authors&mode=browse&sel=10015687" target="_blank">Hegedus, T<sup>*</sup></a> </span> <span class="author-type"> </span> ; <span class="author-name" > Riordan, JR </span> <span class="author-type"> </span> ; <span class="author-name" > Dokholyan, NV ✉ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;1506345" mtid="1506345" target="_blank">Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding.</a></div> <div class="pub-info"> <span class="journal-title">PLOS COMPUTATIONAL BIOLOGY</span> <span class="journal-volume">4</span> : <span class="journal-issue">2</span> <span class="page"> p. e1000008 </span> <span class="year">(2008)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.1371/journal.pcbi.1000008" target="_blank" href="https://doi.org/10.1371/journal.pcbi.1000008"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000269692800011" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000269692800011"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="40149102264" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-40149102264"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="18463704" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=18463704&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="deleted-record">Zárolt</span> <span class="short-pub-mtid"> Közlemény:1506345 </span> <span class="status-holder"><span class="status-data status-VALIDATED"> Egyeztetett </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 46</span> | Független: 37 | Függő: 9 | Nem jelölt: 0 | WoS jelölt: 39 | Scopus jelölt: 40 | WoS/Scopus jelölt: 41 | DOI jelölt: 39 </div> </div> </div> </div><div class="JournalArticle Publication long-list">
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<span class="author-name" mtid="10015687"><a
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<span class="authorAux-mtmt"> bioinformatika, biofizika</span>)
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<span class="author-affil"><span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Intézet">I</span>/<span title="Biofizikai és Sugárbiológiai Intézet">BSI</span>/MTA-OGYK Membránbiológiai Kutatócsoport</span>
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<span class="author-name" >Riordan JR
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<span class="author-name" >Dokholyan NV ✉
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;1506345" target="_blank">Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding.</a></div> <div> <span class="journal-title">PLOS COMPUTATIONAL BIOLOGY</span>
<span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/1553-734X">1553-734X</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/1553-7358">1553-7358</a>)</span>:
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<div class="lastModified">Utolsó módosítás: 2017.07.11. 11:54 Csajbók Edit (SE_KK_Admin5_CSE, admin)
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<div class="lockedBy">Ideiglenesen zárolva 2022.07.08. 12:16 Boros Annamária (MTMT Központi admin)
</div>
<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Serohijos AW and Hegedus T authors contributed equally to this
work.
Funding Agency and Grant Number: Cystic Fibrosis FoundationItalian Cystic Fibrosis Research Foundation [DOKHOL07I0]; NIHUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USA [DK051870]; AHA Predoctoral FellowshipAmerican Heart Association [0715215U]; NATIONAL INSTITUTE OF DIABETES AND DI...</pre>
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Correspondence Address: Sarkadi, B.; Natl. Inst. of Haematology/Immunol., , H-1113 Budapest, Hungary; email: B.Sarkadi@ohvi.hu
Chemicals/CAS: ATP-Binding Cassette Transporters; Multidrug Resistance-Associated Proteins; P-Glycoprotein; Recombinant Fusion Proteins
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The human multidrug resistance protein (MRP1) contributes to drug resistance in cancer cells. In addition to an MDR1-like core, MRP1 contains an N-terminal membrane-bound (TMD0) region and a cytoplasmic linker (L0), both characteristic of several members of the MRP family. In order to study the role of the TMD0 and L0 regions, we constructed various truncated and mutated MRP1, and chimeric MRP1-MDR1 molecules, which were expressed in insect (Sf9) and polarized mammalian (MDCKII) cells. The function of the various proteins was examined in isolated membrane vesicles by measuring the transport of leukotriene C4 and other glutathione conjugates, and by vanadate-dependent nucleotide occlusion. Cellular localization, and glutathione-conjugate and drug transport, were also studied in MDCKII cells. We found that chimeric proteins consisting of N-terminal fragments of MRP1 fused to the N terminus of MDR1 preserved the transport, nucleotide occlusion and apical membrane routing of wild-type MDR1. As shown before, MRP1 without TMD0L0 (ΔMRP1), was non-functional and localized intracellularly, so we investigated the coexpression of ΔMRP1 with the isolated L0 region. Coexpression yielded a functional MRP1 molecule in Sf9 cells and routing to the lateral membrane in MDCKII cells. Interestingly, the L0 peptide was found to be associated with membranes in Sf9 cells and could only be solubilized by urea or detergent. A 10-amino-acid deletion in a predicted amphipathic region of L0 abolished its attachment to the membrane and eliminated MRP1 transport function, but did not affect membrane routing. Taken together, these experiments suggest that the L0 region forms a distinct domain within MRP1, which interacts with hydrophobic membrane regions and with the core region of MRP1.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" mtid="10010374"> <a href="/gui2/?type=authors&mode=browse&sel=10010374" target="_blank">Bakos, E</a> </span> <span class="author-type"> </span> ; <span class="author-name" > Evers, R<sup>*</sup> </span> <span class="author-type"> </span> ; <span class="author-name" > Calenda, G </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10000061"> <a href="/gui2/?type=authors&mode=browse&sel=10000061" target="_blank">Tusnady, GE</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10001932"> <a href="/gui2/?type=authors&mode=browse&sel=10001932" target="_blank">Szakács, G</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10000030"> <a href="/gui2/?type=authors&mode=browse&sel=10000030" target="_blank">Varadi, A</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="1241938"> <a href="/gui2/?type=authors&mode=browse&sel=1241938" target="_blank">Sarkadi, B</a> </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;151391" mtid="151391" target="_blank">Characterization of the amino-terminal regions in the human multidrug resistance protein (MRP1)</a></div> <div class="pub-info"> <span class="journal-title">JOURNAL OF CELL SCIENCE</span> <span class="journal-volume">113</span> : <span class="journal-issue">24</span> <span class="page"> pp. 4451-4461. , 11 p. </span> <span class="year">(2000)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000166325600010" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000166325600010"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="0034502842" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-0034502842"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="11082039" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11082039&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:151391 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 103</span> | Független: 93 | Függő: 10 | Nem jelölt: 0 | WoS jelölt: 97 | Scopus jelölt: 103 | WoS/Scopus jelölt: 103 | DOI jelölt: 99 </div> </div> </div> </div><div class="JournalArticle Publication long-list">
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<span class="authorAux-mtmt"> biofizika</span>)
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;151391" target="_blank">Characterization of the amino-terminal regions in the human multidrug resistance protein (MRP1)</a></div> <div> <span class="journal-title">JOURNAL OF CELL SCIENCE</span>
<span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/0021-9533">0021-9533</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/1477-9137">1477-9137</a>)</span>:
<span class="journal-volume">113</span> <span class="journal-issue">24</span>
<span class="page">
pp 4451-4461
</span> <span class="year">(2000)</span>
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| <span class="publication-sourceOfData">kézi felvitel</span>
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<div class="lastModified">Utolsó módosítás: 2022.05.03. 10:34 Pécsi Éva (MTMT Közp 3, admin)
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :100
Export Date: 10 February 2023
CODEN: JNCSA
Correspondence Address: Sarkadi, B.; Natl. Inst. of Haematology/Immunol., , H-1113 Budapest, Hungary; email: B.Sarkadi@ohvi.hu
Chemicals/CAS: ATP-Binding Cassette Transporters; Multidrug Resistance-Associated Proteins; P-Glycoprotein; Recombina...</pre>
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