{ "labelLang" : "hun", "responseDate" : "2024-03-28 14:35", "content" : { "otype" : "JournalArticle", "mtid" : 23197053, "status" : "ADMIN_APPROVED", "published" : true, "comment" : "N1 : Chemicals/CASalpha 1 antitrypsin, 9041-92-3; Recombinant Proteins; Solvents; alpha 1-Antitrypsin", "unhandledTickets" : 0, "oldTimestamp" : "2018-10-01T21:48:54.000+0000", "deleted" : false, "oldId" : 13197053, "lastRefresh" : "2023-01-25T13:57:56.534+0000", "lastModified" : "2018-10-01T21:48:54.000+0000", "created" : "2013-07-09T13:34:16.000+0000", "creator" : { "otype" : "Author", "mtid" : 10000346, "link" : "/api/author/10000346", "label" : "Závodszky Péter (Molekuláris immunológia, biokémia)", "familyName" : "Závodszky", "givenName" : "Péter", "published" : true, "oldId" : 10000346, "snippet" : true }, "lastDuplumSearch" : "2023-01-25T13:56:37.723+0000", "adminApproved" : "2014-03-03T14:24:28.000+0000", "adminApprover" : { "otype" : "Admin", "mtid" : 10016863, "link" : "/api/admin/10016863", "label" : "Áts József (ELTE - INAKTÍV, admin)", "familyName" : "Áts", "givenName" : "József", "published" : true, "oldId" : 10016863, "snippet" : true }, "core" : false, "citation" : true, "publicationPending" : false, "type" : { "otype" : "PublicationType", "mtid" : 24, "link" : "/api/publicationtype/24", "label" : "Folyóiratcikk", "code" : 24, "otypeName" : "JournalArticle", "listPosition" : 1, "published" : true, "oldId" : 24, "snippet" : true }, "languages" : [ { "otype" : "Language", "mtid" : 10002, "link" : "/api/language/10002", "label" : "Angol", "name" : "Angol", "nameEng" : "English", "published" : true, "oldId" : 2, "snippet" : true } ], "firstAuthor" : "Stocks, BB", "authorships" : [ { "otype" : "PersonAuthorship", "mtid" : 29417648, "link" : "/api/authorship/29417648", "label" : "Stocks, BB", "listPosition" : 1, "share" : 0.0, "first" : true, "last" : false, "familyName" : "Stocks", "givenName" : "BB", "authorTyped" : true, "editorTyped" : false, "otherTyped" : false, "type" : { "otype" : "AuthorshipType", "mtid" : 1, "link" : "/api/authorshiptype/1", "label" : "Szerző", "code" : 0, "published" : true, "oldId" : 0, "snippet" : true }, "published" : false, "oldId" : 45262138, "snippet" : true }, { "otype" : "PersonAuthorship", "mtid" : 29417649, "link" : "/api/authorship/29417649", "label" : "Sarkar, A", "listPosition" : 2, "share" : 0.0, "first" : false, "last" : false, "familyName" : "Sarkar", "givenName" : "A", "authorTyped" : true, "editorTyped" : false, "otherTyped" : false, "type" : { "otype" : "AuthorshipType", "mtid" : 1, "link" : "/api/authorshiptype/1", "label" : "Szerző", "code" : 0, "published" : true, "oldId" : 0, "snippet" : true }, "published" : false, "oldId" : 45262137, "snippet" : true }, { "otype" : "PersonAuthorship", "mtid" : 29417650, "link" : "/api/authorship/29417650", "label" : "Wintrode, PL", "listPosition" : 3, "share" : 0.0, "first" : false, "last" : false, "familyName" : "Wintrode", "givenName" : "PL", "authorTyped" : true, "editorTyped" : false, "otherTyped" : false, "type" : { "otype" : "AuthorshipType", "mtid" : 1, "link" : "/api/authorshiptype/1", "label" : "Szerző", "code" : 0, "published" : true, "oldId" : 0, "snippet" : true }, "published" : false, "oldId" : 45262136, "snippet" : true }, { "otype" : "PersonAuthorship", "mtid" : 29417651, "link" : "/api/authorship/29417651", "label" : "Konermann, L", "listPosition" : 4, "share" : 0.0, "first" : false, "last" : true, "familyName" : "Konermann", "givenName" : "L", "authorTyped" : true, "editorTyped" : false, "otherTyped" : false, "type" : { "otype" : "AuthorshipType", "mtid" : 1, "link" : "/api/authorshiptype/1", "label" : "Szerző", "code" : 0, "published" : true, "oldId" : 0, "snippet" : true }, "published" : false, "oldId" : 45262135, "snippet" : true } ], "title" : "Early hydrophobic collapse of α1-antitrypsin facilitates formation of a metastable state: Insights from oxidative labeling and mass spectrometry", "identifiers" : [ { "otype" : "PublicationIdentifier", "mtid" : 6385755, "link" : "/api/publicationidentifier/6385755", "label" : "DOI: 10.1016/j.jmb.2012.08.019", "source" : { "otype" : "PlainSource", "mtid" : 6, "link" : "/api/publicationsource/6", "label" : "DOI", "type" : { "otype" : "PublicationSourceType", "mtid" : 10001, "link" : "/api/publicationsourcetype/10001", "label" : "DOI", "mayHaveOa" : true, "published" : true, "snippet" : true }, "name" : "DOI", "nameEng" : "DOI", "linkPattern" : "https://doi.org/@@@", "publiclyVisible" : true, "published" : true, "oldId" : 6, "snippet" : true }, "validState" : "IDENTICAL", "idValue" : "10.1016/j.jmb.2012.08.019", "realUrl" : "https://doi.org/10.1016/j.jmb.2012.08.019", "published" : false, "oldId" : 3469252, "snippet" : true }, { "otype" : "PublicationIdentifier", "mtid" : 18447670, "link" : "/api/publicationidentifier/18447670", "label" : "WoS: 000310666400011", "source" : { "otype" : "PlainSource", "mtid" : 1, "link" : "/api/publicationsource/1", "label" : "WoS", "type" : { "otype" : "PublicationSourceType", "mtid" : 10003, "link" : "/api/publicationsourcetype/10003", "label" : "Indexelő adatbázis", "mayHaveOa" : false, "published" : true, "snippet" : true }, "name" : "WoS", "nameEng" : "WoS", "linkPattern" : "https://www.webofscience.com/wos/woscc/full-record/WOS:@@@", "publiclyVisible" : true, "published" : true, "oldId" : 1, "snippet" : true }, "validState" : "IDENTICAL", "idValue" : "000310666400011", "realUrl" : "https://www.webofscience.com/wos/woscc/full-record/WOS:000310666400011", "published" : false, "snippet" : true }, { "otype" : "PublicationIdentifier", "mtid" : 6385754, "link" : "/api/publicationidentifier/6385754", "label" : "Scopus: 84867578111", "source" : { "otype" : "PlainSource", "mtid" : 3, "link" : "/api/publicationsource/3", "label" : "Scopus", "type" : { "otype" : "PublicationSourceType", "mtid" : 10003, "link" : "/api/publicationsourcetype/10003", "label" : "Indexelő adatbázis", "mayHaveOa" : false, "published" : true, "snippet" : true }, "name" : "Scopus", "linkPattern" : "http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-@@@", "publiclyVisible" : true, "published" : true, "oldId" : 3, "snippet" : true }, "validState" : "IDENTICAL", "idValue" : "84867578111", "realUrl" : "http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84867578111", "published" : false, "oldId" : 3469251, "snippet" : true }, { "otype" : "PublicationIdentifier", "mtid" : 6385756, "link" : "/api/publicationidentifier/6385756", "label" : "PubMed: 22940366", "source" : { "otype" : "PlainSource", "mtid" : 17, "link" : "/api/publicationsource/17", "label" : "PubMed", "type" : { "otype" : "PublicationSourceType", "mtid" : 10003, "link" : "/api/publicationsourcetype/10003", "label" : "Indexelő adatbázis", "mayHaveOa" : false, "published" : true, "snippet" : true }, "name" : "PubMed", "nameEng" : "PubMed", "linkPattern" : "http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=@@@&dopt=Abstract", "publiclyVisible" : true, "published" : true, "oldId" : 17, "snippet" : true }, "validState" : "IDENTICAL", "idValue" : "22940366", "realUrl" : "http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=22940366&dopt=Abstract", "published" : false, "oldId" : 3469253, "snippet" : true } ], "journal" : { "otype" : "Journal", "mtid" : 10015785, "link" : "/api/journal/10015785", "label" : "JOURNAL OF MOLECULAR BIOLOGY 0022-2836 1089-8638", "pIssn" : "0022-2836", "eIssn" : "1089-8638", "reviewType" : "REVIEWED", "noIF" : false, "sciIndexed" : true, "scopusIndexed" : true, "lang" : "FOREIGN", "hungarian" : false, "published" : true, "oldId" : 10015785, "snippet" : true }, "volume" : "423", "issue" : "5", "firstPage" : "789", "lastPage" : "799", "firstPageOrInternalIdForSort" : "789", "pageLength" : 11, "publishedYear" : 2012, "digital" : null, "printed" : null, "sourceYear" : 2013, "packet" : "504599", "foreignEdition" : true, "foreignLanguage" : true, "fullPublication" : false, "conferencePublication" : null, "nationalOrigin" : null, "missingAuthor" : false, "oaType" : "NONE", "oaCheckDate" : "2023-01-25", "oaFree" : false, "citationCount" : 0, "citationCountUnpublished" : 0, "citationCountWoOther" : 0, "independentCitCountWoOther" : 0, "doiCitationCount" : 0, "wosCitationCount" : 0, "scopusCitationCount" : 0, "independentCitationCount" : 0, "unhandledCitationCount" : 0, "citingPubCount" : 0, "independentCitingPubCount" : 0, "unhandledCitingPubCount" : 0, "citedPubCount" : 1, "citedCount" : 1, "referenceList" : "De Los Rios, M.A., Muralidhara, B.K., Wildes, D., Sosnick, T.R., Marqusee, S., Wittung-Stafshede, P., On the precision of experimentally determined protein folding rates and Φ-values (2006) Protein Sci., 15, pp. 553-563; \n\nBanachewicz, W., Religa, T.L., Schaeffer, R.D., Daggett, V., Fersht, A.R., Malleability of folding intermediates in the homeodomain superfamily (2011) Proc. Natl Acad. Sci. USA, 108, pp. 5596-5601; \n\nBrockwell, D.J., Radford, S.E., Intermediates: Ubiquitous species on folding energy landscapes? (2007) Current Opinion in Structural Biology, 17 (1), pp. 30-37. , DOI 10.1016/j.sbi.2007.01.003, PII S0959440X07000048, Foldinf and Binding / Protein-Nucleic Interactions; \n\nSanchez, I.E., Kiefhaber, T., Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding (2003) Journal of Molecular Biology, 325 (2), pp. 367-376. , DOI 10.1016/S0022-2836(02)01230-5; \n\nUzawa, T., Nishimura, C., Akiyama, S., Ishimori, K., Takahashi, S., Dyson, H.J., Wright, P.E., Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR (2008) Proc. Natl Acad. Sci. USA, 105, pp. 13859-13864; \n\nAnfinsen, C.B., Principles that govern the folding of protein chains (1973) Science, 181, pp. 223-230; \n\nDill, K.A., Chan, H.S., From levinthal to pathways to funnels (1997) Nature Structural Biology, 4 (1), pp. 10-19. , DOI 10.1038/nsb0197-10; \n\nOnuchic, J.N., Wolynes, P.G., Luthey-Schulten, Z., Socci, N.D., Toward an outline of the topography of a realistic protein-folding funnel (1995) Proc. Natl Acad. Sci. USA, 92, pp. 3626-3630; \n\nXu, Y., Mayne, L., Englander, S.W., Evidence for an unfolding and refolding pathway in cytochrome c (1998) Nature Structural Biology, 5 (9), pp. 774-778. , DOI 10.1038/1810; \n\nLindorff-Larsen, K., Piana, S., Dror, R.O., Shaw, D.E., How fast-folding proteins fold (2011) Science, 334, pp. 517-520; \n\nDinner, A.R., Karplus, M., A metastable state in folding simulations of a protein model (1998) Nature Structural Biology, 5 (3), pp. 236-241. , DOI 10.1038/nsb0398-236; \n\nBaker, D., Metastable states and folding free energy barriers (1998) Nature Structural Biology, 5 (12), pp. 1021-1024. , DOI 10.1038/4130; \n\nGettins, P.G.W., Serpin structure, mechanism, and function (2002) Chem. Rev., 102, pp. 4751-4803; \n\nYamasaki, M., Sendall, T.J., Pearce, M.C., Whisstock, J.C., Huntington, J.A., Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer (2011) EMBO Rep., 12, pp. 1011-1018; \n\nNyon, M.P., Segu, L., Cabrita, L.D., Levy, G.R., Kirkpatrick, J., Roussel, B.D., Structural dynamics associated with intermediate formation in an archetypal conformational disease (2012) Structure, 20, pp. 504-512; \n\nEkeowa, U.I., Freeke, J., Miranda, E., Gooptu, B., Bush, M.F., Perez, J., Defining the mechanism of polymerization in the serpinopathies (2010) Proc. Natl Acad. Sci. USA, 107, pp. 17146-17151; \n\nKrishnan, B., Gierasch, L.M., Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization (2011) Nat. Struct. Mol. Biol., 18, pp. 222-226; \n\nElliott, P.R., Pie, X.Y., Dafforn, T.R., Lomas, D.A., Topography of a 2.0 Å structure of α1-antitrypsin reveals targets for rational drug design to prevent conformational disease (2000) Protein Science, 9 (7), pp. 1274-1281; \n\nIm, H., Woo, M.-S., Hwang, K.Y., Yu, M.-H., Interactions causing the kinetic trap in serpin protein folding (2002) Journal of Biological Chemistry, 277 (48), pp. 46347-46354. , DOI 10.1074/jbc.M207682200; \n\nHuntington, J.A., Read, R.J., Carrell, R.W., Structure of a serpin-protease complex shows inhibition by deformation (2000) Nature, 407, pp. 923-926; \n\nLomas, D.A., Elliott, P.R., Chang, W.-S.W., Wardell, M.R., Carrell, R.W., Preparation and characterization of latent α1- antitrypsin (1995) J. Biol. Chem., 270, pp. 5282-5288; \n\nDolmer, K., Gettins, P.G.W., How the serpin α1-proteinase inhibitor folds (2012) J. Biol. Chem., 287, pp. 12425-12432; \n\nKaslik, G., Kardos, J., Szabo, E., Szilagyi, L., Zavodszky, P., Westler, W.M., Markley, J.L., Graf, L., Effects of serpin binding on the target proteinase: Global stabilization, localized increased structural flexibility, and conserved hydrogen bonding at the active site (1997) Biochemistry, 36 (18), pp. 5455-5464. , DOI 10.1021/bi962931m; \n\nWhisstock, J.C., Bottomley, S.P., Molecular gymnastics: Serpin structure, folding and misfolding (2006) Current Opinion in Structural Biology, 16 (6), pp. 761-768. , DOI 10.1016/j.sbi.2006.10.005, PII S0959440X06001771, Catalysis and Regulation / Proteins; \n\nJames, E.L., Whisstock, J.C., Gore, M.G., Bottomley, S.P., Probing the unfolding pathway of α1-antitrypsin (1999) J. Biol. Chem., 274, pp. 9482-9488; \n\nTew, D.J., Bottomley, S.P., Probing the equilibrium denaturation of the serpin α1- antitrypsin with single tryptophan mutants; Evidence for structure in the urea unfolded state (2001) Journal of Molecular Biology, 313 (5), pp. 1161-1169. , DOI 10.1006/jmbi.2001.5104; \n\nTsutsui, Y., Wintrode, P.L., Cooperative Unfolding of a Metastable Serpin to a Molten Globule Suggests a Link Between Functional and Folding Energy Landscapes (2007) Journal of Molecular Biology, 371 (1), pp. 245-255. , DOI 10.1016/j.jmb.2007.05.039, PII S0022283607006754; \n\nBottomley, S.P., The folding pathway of α1-antitrypsin: Avoiding the unavoidable (2010) Proc. Am. Thorac. Soc., 7, pp. 404-407; \n\nFersht, A.R., (1999) Structure and Mechanism in Protein Science, , W. H. Freeman & Co. New York; \n\nTsutsui, Y., Dela Cruz, R.G., Wintrode, P.L., The folding mechanism of the metastable serpin α1- antitrypsin (2012) Proc. Natl Acad. Sci. USA, 109, pp. 4467-4472; \n\nKim, D., Yu, M.-H., Folding pathway of human α1-antitrypsin: Characterization of an intermediate that is active but prone to aggregation (1996) Biochemical and Biophysical Research Communications, 226 (2), pp. 378-384. , DOI 10.1006/bbrc.1996.1364; \n\nBrandts, J.F., Brennan, M., Lin, L.N., Unfolding and refolding occur much faster for a proline-free protein than for most proline-containing proteins (1977) Proceedings of the National Academy of Sciences of the United States of America, 74 (10), pp. 4178-4181; \n\nIvankov, D.N., Garbuzynskiy, S.O., Alm, E., Plaxco, K.W., Baker, D., Finkelstein, A.V., Contact order revisited: Influence of protein size on the folding rate (2003) Protein Science, 12 (9), pp. 2057-2062. , DOI 10.1110/ps.0302503; \n\nWang, L., Chance, M.R., Structural mass spectrometry of proteins using hydroxyl radical based protein footprinting (2011) Anal. Chem., 83, pp. 7234-7241; \n\nSmedley, J.G., Sharp, J.S., Kuhn, J.F., Tomer, K.B., Probing the pH-dependent prepore to pore transition of Bacillus anthracis protective antigen with differential oxidative protein footprinting (2008) Biochemistry, 47, pp. 10694-10704; \n\nHambly, D.M., Gross, M.L., Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale (2005) Journal of the American Society for Mass Spectrometry, 16 (12), pp. 2057-2063. , DOI 10.1016/j.jasms.2005.09.008, PII S1044030505008159; \n\nGau, B.C., Sharp, J.S., Rempel, D.L., Gross, M.L., Fast photochemical oxidation of protein footprints faster than protein unfolding (2009) Anal. Chem., 81, pp. 6563-6571; \n\nChen, J., Rempel, D.L., Gross, M.L., Temperature jump and fast photochemical oxidation probe submillisecond protein folding (2010) J. Am. Chem. Soc., 132, pp. 15502-15504; \n\nStocks, B.B., Rezvanpour, A., Shaw, G.S., Konermann, L., Temporal development of protein structure during S100A11 folding and dimerization probed by oxidative labeling and mass spectrometry (2011) J. Mol. Biol., 409, pp. 669-679; \n\nChetty, P.S., Mayne, L., Lund-Katz, S., Stranz, D.D., Englander, S.W., Phillips, M.C., Helical structure and stability in human apolipoprotein A-I by hydrogen exchange and mass spectrometry (2009) Proc. Natl Acad. Sci. USA, 106, pp. 19005-19010; \n\nHaran, G., How, when and why proteins collapse: The relation to folding (2012) Curr. Opin. Struct. Biol., 22, pp. 14-20; \n\nZheng, X., Wintrode, P.L., Chance, M.R., Complementary structural mass spectrometry techniques reveal local dynamics in functionally important regions of a metastable serpin (2008) Structure, 16, pp. 38-51; \n\nChiti, F., Dobson, C.M., Protein misfolding, functional amyloid, and human disease (2006) Annual Review of Biochemistry, 75, pp. 333-366. , DOI 10.1146/annurev.biochem.75.101304.123901; \n\nSadqi, M., Lapidus, L.J., Munoz, V., How fast is protein hydrophobic collapse (2003) Proceedings of the National Academy of Sciences of the United States of America, 100 (21), pp. 12117-12122. , DOI 10.1073/pnas.2033863100; \n\nGettins, P.G.W., The F-helix of serpins plays an essential, active role in the proteinase inhibition mechanism (2002) FEBS Letters, 523 (1-3), pp. 2-6. , DOI 10.1016/S0014-5793(02)02924-1, PII S0014579302029241; \n\nOnda, M., Nakatani, K., Takehara, S., Nishiyama, M., Takahashi, N., Hirose, M., Cleaved serpin refolds into the relaxed state via a stressed conformer (2008) J. Biol. Chem., 283, pp. 17568-17578; \n\nTsutsui, Y., Liu, L., Gershenson, A., Wintrode, P.L., The conformational dynamics of a metastable serpin studied by hydrogen exchange and mass spectrometry (2006) Biochemistry, 45 (21), pp. 6561-6569. , DOI 10.1021/bi060431f; \n\nKonermann, L., Stocks, B.B., Czarny, T., Laminar flow effects during laser-induced oxidative labeling for protein structural studies by mass spectrometry (2010) Anal. Chem., 82, pp. 6667-6674; \n\nDevlin, G.L., Chow, M.K.M., Howlett, G.J., Bottomley, S.P., Acid denaturation of α1-antitrypsin: Characterization of a novel mechanism of serpin polymerization (2002) Journal of Molecular Biology, 324 (4), pp. 859-870. , DOI 10.1016/S0022-2836(02)01088-4; \n\nXu, G., Kiselar, J., He, Q., Chance, M.R., Secondary reactions and strategies to improve quantitative protein footprinting (2005) Analytical Chemistry, 77 (10), pp. 3029-3037. , DOI 10.1021/ac048282z; \n\nHambly, D.M., Gross, M.L., Cold chemical oxidation of proteins (2009) Anal. Chem., 81, pp. 7235-7242; \n\nSmith, A.M., Jahn, T.R., Ashcroft, A.E., Radford, S.E., Direct Observation of Oligomeric Species formed in the Early Stages of Amyloid Fibril Formation using Electrospray Ionisation Mass Spectrometry (2006) Journal of Molecular Biology, 364 (1), pp. 9-19. , DOI 10.1016/j.jmb.2006.08.081, PII S0022283606011399; \n\nBendall, S.C., Hughes, C., Campbell, J.J., Stewart, M.H., Pittock, P., Liu, S., An enhanced mass spectrometry approach reveals human embryonic stem cell growth factors in culture (2009) Mol. Cell. Proteomics, 8, pp. 421-432; \n\nLacerda, C.M.R., Xin, L., Rogers, I., Reardon, K.F., Analysis of iTRAQ data using Mascot and Peaks quantification algorithms (2008) Briefings in Functional Genomics and Proteomics, 7 (2), pp. 119-126. , DOI 10.1093/bfgp/eln017, Special Issue: Outlook and Tools to Maximize Proteomics Information; \n\nStocks, B.B., Konermann, L., Structural characterization of short-lived protein unfolding intermediates by laser-induced oxidative labeling and mass spectrometry (2009) Anal. Chem., 81, pp. 20-27", "hasCitationDuplums" : false, "userChangeableUntil" : "2014-03-03T14:24:28.000+0000", "publishDate" : "2013-07-09T13:38:10.000+0000", "directInstitutesForSort" : "", "ownerAuthorCount" : 3, "ownerInstituteCount" : 19, "directInstituteCount" : 0, "authorCount" : 4, "contributorCount" : 0, "hasQualityFactor" : false, "link" : "/api/publication/23197053", "label" : "Stocks BB et al. Early hydrophobic collapse of α1-antitrypsin facilitates formation of a metastable state: Insights from oxidative labeling and mass spectrometry. (2012) JOURNAL OF MOLECULAR BIOLOGY 0022-2836 1089-8638 423 5 789-799", "template" : "