https://m2.mtmt.hu/ eng 2026-10-23 07:50 JournalArticle 34789190 VALIDATED true * Megosztott szerzőség 0 false 2026-10-09T16:43:02.544+0000 2025-05-17T09:32:34.607+0000 2024-04-15T09:25:05.338+0000 true 10045349 Fekete Rita /api/admin/10045349 Admin Rita Fekete (PTE GYTK admin 5) true 10045349 2025-08-13T07:31:09.569+0000 2025-08-13T07:31:09.569+0000 2024-05-15T07:07:53.259+0000 true 10039043 Milánkovics Róbert /api/admin/10039043 Admin Róbert Milánkovics (PTE ÁOK admin 4) true 10039043 true false true 24 24 /api/publicationtype/24 PublicationType Journal Article 1 true 24 JournalArticle true 10000059 Article true 24 24 /api/publicationtype/24 PublicationType Journal Article 1 true 24 JournalArticle /api/subtype/10000059 Szakcikk SubType Article (Journal Article) 101 true 10000059 true 1 /api/category/1 Category Scientific true 1 Zhao, Jiawei true true /api/journal/3308 REVIEWED NATURE 0028-0836 1476-4687 true false 3308 false 3308 true 0028-0836 1476-4687 Journal FOREIGN 629 8011 474 480 474 7 2024 The µ-opioid receptor (µOR) is an important target for pain management 1 and molecular understanding of drug action on µOR will facilitate the development of better therapeutics. Here we show, using double electron–electron resonance and single-molecule fluorescence resonance energy transfer, how ligand-specific conformational changes of µOR translate into a broad range of intrinsic efficacies at the transducer level. We identify several conformations of the cytoplasmic face of the receptor that interconvert on different timescales, including a pre-activated conformation that is capable of G-protein binding, and a fully activated conformation that markedly reduces GDP affinity within the ternary complex. Interaction of β-arrestin-1 with the μOR core binding site appears less specific and occurs with much lower affinity than binding of G i . Funding 2052998 /api/funding/2052998 (NKFI-137793) Funder: NRDIO false true true 2024 true true true false false GOLD 2026-10-09 true https://doi.org/10.1038/s41586-024-07295-2 45 0 45 40 0 45 45 45 27 45 45 40 40 40 5 0 45 40 45 40 0 1 1 Folyóiratcikk Journal Article 24 45 Könyvrészlet Chapter in Book 25 0 Könyv Book 23 0 Egyéb konferenciaközlemény Conference paper 31 0 Egyéb konferenciakötet Conference proceedings 32 0 Oltalmi formák Protection forms 26 0 Disszertáció Thesis 28 0 Egyéb Miscellaneous 29 0 Alkotás Achievement 22 0 Kutatási adat Research data 33 0 Folyóiratcikk Journal Article 24 0 0 0 Könyvrészlet Chapter in Book 25 0 0 0 Könyv Book 23 0 0 0 Egyéb konferenciaközlemény Conference paper 31 0 0 0 Egyéb konferenciakötet Conference proceedings 32 0 0 0 Oltalmi formák Protection forms 26 0 0 0 Disszertáció Thesis 28 0 0 0 Egyéb Miscellaneous 29 0 0 0 Alkotás Achievement 22 0 0 0 Kutatási adat Research data 33 0 0 0 2024 0 4 3 4 3 2025 0 25 24 25 24 2026 0 16 13 16 13 D1 A false false false false 2024-05-14T07:07:53.008+0000 Szerves és Gyógyszerkémiai Intézet (PTE / GYTK) 1 6 1 12 0 true Language 10002 /api/language/10002 English Angol English true 2 true PersonAuthorship 116189577 /api/authorship/116189577 Zhao, Jiawei 1 0.083333336 true false false Zhao Jiawei true false false AuthorshipType 1 /api/authorshiptype/1 Author 0 true 0 true false true PersonAuthorship 116189578 /api/authorship/116189578 Elgeti, Matthias* ✉ 2 0.083 true false true Elgeti Matthias true false false AuthorshipType 1 /api/authorshiptype/1 Author 0 true 0 true false true PersonAuthorship 116189579 /api/authorship/116189579 O’Brien, Evan S. 3 0.083333336 false false false O’Brien Evan S. true false false AuthorshipType 1 /api/authorshiptype/1 Author 0 true 0 true false true PersonAuthorship 116189580 /api/authorship/116189580 Sár, Cecília P. [Pápayné Sár, Cecília (Szerves kémia), author] Department of Organic and Pharmacological Chemi... (UP / FP) 4 0.083 false false false Author 10006127 /api/author/10006127 Cecília Pápayné Sár (Szerves kémia) Pápayné Sár Cecília true 10006127 true Sár Cecília P. true false false AuthorshipType 1 /api/authorshiptype/1 Author 0 true 0 true false true PersonAuthorship 116189581 /api/authorship/116189581 EI Daibani, Amal 5 0.083333336 false false false EI Daibani Amal true false false AuthorshipType 1 /api/authorshiptype/1 Author 0 true 0 true false true PersonAuthorship 116189582 /api/authorship/116189582 Heng, Jie 6 0.083333336 false false false Heng Jie true false false AuthorshipType 1 /api/authorshiptype/1 Author 0 true 0 true false true PersonAuthorship 116189583 /api/authorship/116189583 Sun, Xiaoou 7 0.083333336 false false false Sun Xiaoou true false false AuthorshipType 1 /api/authorshiptype/1 Author 0 true 0 true false true PersonAuthorship 116189584 /api/authorship/116189584 White, Elizabeth 8 0.083333336 false false false White Elizabeth true false false AuthorshipType 1 /api/authorshiptype/1 Author 0 true 0 true false true PersonAuthorship 116189585 /api/authorship/116189585 Che, Tao 9 0.083333336 false false false Che Tao true false false AuthorshipType 1 /api/authorshiptype/1 Author 0 true 0 true false true PersonAuthorship 116189586 /api/authorship/116189586 Hubbell, Wayne L. 10 0.083333336 false false false Hubbell Wayne L. true false false AuthorshipType 1 /api/authorshiptype/1 Author 0 true 0 true false true PersonAuthorship 116189587 /api/authorship/116189587 Kobilka, Brian K. ✉ 11 0.083 false false true Kobilka Brian K. true false false AuthorshipType 1 /api/authorshiptype/1 Author 0 true 0 true false true PersonAuthorship 116189588 /api/authorship/116189588 Chen, Chunlai ✉ 12 0.083 false true true Chen Chunlai true false false AuthorshipType 1 /api/authorshiptype/1 Author 0 true 0 true false true PublicationIdentifier 26002846 /api/publicationidentifier/26002846 DOI: 10.1038/s41586-024-07295-2 PlainSource 6 /api/publicationsource/6 DOI PublicationSourceType 10001 /api/publicationsourcetype/10001 DOI true true true DOI DOI https://doi.org/@@@ true true 6 true GOLD true IDENTICAL 10.1038/s41586-024-07295-2 https://doi.org/10.1038/s41586-024-07295-2 false true PublicationIdentifier 26209408 /api/publicationidentifier/26209408 WoS: 001201403000020 PlainSource 1 /api/publicationsource/1 WoS PublicationSourceType 10003 /api/publicationsourcetype/10003 Indexelő adatbázis false true true WoS WoS https://www.webofscience.com/wos/woscc/full-record/@@@ true true 1 true IDENTICAL 001201403000020 https://www.webofscience.com/wos/woscc/full-record/001201403000020 false true PublicationIdentifier 26026198 /api/publicationidentifier/26026198 Scopus: 85189967158 PlainSource 3 /api/publicationsource/3 Scopus PublicationSourceType 10003 /api/publicationsourcetype/10003 Indexelő adatbázis false true true Scopus Scopus http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-@@@ true true 3 true IDENTICAL 85189967158 http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85189967158 false true PublicationIdentifier 26026180 /api/publicationidentifier/26026180 PubMed: 38600384 PlainSource 17 /api/publicationsource/17 PubMed PublicationSourceType 10003 /api/publicationsourcetype/10003 Indexelő adatbázis false true true PubMed PubMed http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=@@@&dopt=Abstract true true 17 true IDENTICAL 38600384 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=38600384&dopt=Abstract false true MtaRating 11435135 /api/mtarating/11435135 X. 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Committee on Sociology SZTB Institute 14102 /api/institute/14102 Committee on Sociology HASSELIX SZTB [1901-] 0 false true false Szociológiai Tudományos Bizottság Committee on Sociology true 14102 true true true A nemzetközi true 19065 true SjrRating 11736087 /api/sjrrating/11736087 sjr:D1 (2024) Scopus - Multidisciplinary NATURE 0028-0836 1476-4687 1 0.0 journal RatingType 10002 /api/ratingtype/10002 sjr sjr true true ClassificationExternal 1000 /api/classificationexternal/1000 Scopus - Multidisciplinary true 1000 true D1 DIRECT true true Reference 51912452 /api/reference/51912452 1. Katzung, B. G. Basic & Clinical Pharmacology (LANGE McGraw Hill Medical, 2012). 1 false true Reference 51912453 /api/reference/51912453 2. Bohn, L. M. et al. Enhanced morphine analgesia in mice lacking β-arrestin 2. Science 286, 2495–2498 (1999)., DOI: 10.1126/science.286.5449.2495 2 10.1126/science.286.5449.2495 false true Reference 51912454 /api/reference/51912454 3. Raehal, K. M., Walker, J. K. L. & Bohn, L. M. Morphine side effects in β-arrestin 2 knockout mice. J. Pharmacol. Exp. Ther. 314, 1195–1201 (2005)., DOI: 10.1124/jpet.105.087254 3 10.1124/jpet.105.087254 false true Reference 51912455 /api/reference/51912455 4. DeWire, S. M. et al. A G protein-biased ligand at the μ-opioid receptor is potently analgesic with reduced gastrointestinal and respiratory dysfunction compared with morphine. J. Pharmacol. Exp. Ther. 344, 708–717 (2013)., DOI: 10.1124/jpet.112.201616 4 10.1124/jpet.112.201616 false true Reference 51912456 /api/reference/51912456 5. Manglik, A. et al. Structure-based discovery of opioid analgesics with reduced side effects. Nature 537, 185–190 (2016)., DOI: 10.1038/nature19112 5 10.1038/nature19112 false true Reference 51912457 /api/reference/51912457 6. Váradi, A. et al. Mitragynine/corynantheidine pseudoindoxyls as opioid analgesics with mu agonism and delta antagonism, which do not recruit β-Arrestin-2. J. Med. Chem. 59, 8381–8397 (2016)., DOI: 10.1021/acs.jmedchem.6b00748 6 10.1021/acs.jmedchem.6b00748 false true Reference 51912458 /api/reference/51912458 7. Schmid, C. L. et al. Bias factor and therapeutic window correlate to predict safer opioid analgesics. Cell 171, 1165–1175.e13 (2017)., DOI: 10.1016/j.cell.2017.10.035 7 10.1016/j.cell.2017.10.035 false true Reference 51912459 /api/reference/51912459 8. Lambert, D. & Calo, G. Approval of oliceridine (TRV130) for intravenous use in moderate to severe pain in adults. Br. J. Anaesth. 125, e473–e474 (2020)., DOI: 10.1016/j.bja.2020.09.021 8 10.1016/j.bja.2020.09.021 false true Reference 51912460 /api/reference/51912460 9. Kliewer, A. et al. Phosphorylation-deficient G-protein-biased μ-opioid receptors improve analgesia and diminish tolerance but worsen opioid side effects. Nat. Commun. 10, 367 (2019)., DOI: 10.1038/s41467-018-08162-1 9 10.1038/s41467-018-08162-1 false true Reference 51912461 /api/reference/51912461 10. Kliewer, A. et al. Morphine‐induced respiratory depression is independent of β‐arrestin2 signalling. Br. J. Pharmacol. 177, 2923–2931 (2020)., DOI: 10.1111/bph.15004 10 10.1111/bph.15004 false true Reference 51912462 /api/reference/51912462 11. Bachmutsky, I., Wei, X. P., Durand, A. & Yackle, K. β-arrestin 2 germline knockout does not attenuate opioid respiratory depression. eLife 10, e62552 (2021)., DOI: 10.7554/eLife.62552 11 10.7554/eLife.62552 false true Reference 51912463 /api/reference/51912463 12. Gillis, A. et al. Low intrinsic efficacy for G protein activation can explain the improved side effect profiles of new opioid agonists. Sci. Signal. 13, eaaz3140 (2020)., DOI: 10.1126/scisignal.aaz3140 12 10.1126/scisignal.aaz3140 false true Reference 51912464 /api/reference/51912464 13. Manglik, A. et al. Crystal structure of the µ-opioid receptor bound to a morphinan antagonist. Nature 485, 321–326 (2012)., DOI: 10.1038/nature10954 13 10.1038/nature10954 false true Reference 51912465 /api/reference/51912465 14. Huang, W. et al. Structural insights into µ-opioid receptor activation. Nature 524, 315–321 (2015)., DOI: 10.1038/nature14886 14 10.1038/nature14886 false true Reference 51912466 /api/reference/51912466 15. Koehl, A. et al. Structure of the µ-opioid receptor–Gi protein complex. Nature 558, 547–552 (2018)., DOI: 10.1038/s41586-018-0219-7 15 10.1038/s41586-018-0219-7 false true Reference 51912467 /api/reference/51912467 16. Qu, Q. et al. Insights into distinct signaling profiles of the µOR activated by diverse agonists. Nat. Chem. Biol. 19, 423–430 (2023)., DOI: 10.1038/s41589-022-01208-y 16 10.1038/s41589-022-01208-y false true Reference 51912468 /api/reference/51912468 17. Liu, X. et al. Structural insights into the process of GPCR–G protein complex formation. Cell 177, 1243–1251.e12 (2019)., DOI: 10.1016/j.cell.2019.04.021 17 10.1016/j.cell.2019.04.021 false true Reference 51912469 /api/reference/51912469 18. Weis, W. I. & Kobilka, B. K. The molecular basis of G protein–coupled receptor activation. Annu. Rev. Biochem. 87, 897–919 (2018)., DOI: 10.1146/annurev-biochem-060614-033910 18 10.1146/annurev-biochem-060614-033910 false true Reference 51912470 /api/reference/51912470 19. Okude, J. et al. Identification of a conformational equilibrium that determines the efficacy and functional selectivity of the μ‐opioid receptor. Angew. Chem. Int. Ed. 54, 15771–15776 (2015)., DOI: 10.1002/anie.201508794 19 10.1002/anie.201508794 false true Reference 51912471 /api/reference/51912471 20. Sounier, R. et al. Propagation of conformational changes during μ-opioid receptor activation. Nature 524, 375–378 (2015)., DOI: 10.1038/nature14680 20 10.1038/nature14680 false true Reference 51912472 /api/reference/51912472 21. Hilger, D., Masureel, M. & Kobilka, B. K. Structure and dynamics of GPCR signaling complexes. Nat. Struct. Mol. Biol. 25, 4–12 (2018)., DOI: 10.1038/s41594-017-0011-7 21 10.1038/s41594-017-0011-7 false true Reference 51912473 /api/reference/51912473 22. Hellenkamp, B. et al. Precision and accuracy of single-molecule FRET measurements—a multi-laboratory benchmark study. Nat. Methods 15, 669–676 (2018)., DOI: 10.1038/s41592-018-0085-0 22 10.1038/s41592-018-0085-0 false true Reference 51912474 /api/reference/51912474 23. Ibáñez, L. F., Jeschke, G. & Stoll, S. DeerLab: a comprehensive software package for analyzing dipolar electron paramagnetic resonance spectroscopy data. Magn. Reson. 1, 209–224 (2020)., DOI: 10.5194/mr-1-209-2020 23 10.5194/mr-1-209-2020 false true Reference 51912475 /api/reference/51912475 24. Peter, M. F. et al. Cross-validation of distance measurements in proteins by PELDOR/DEER and single-molecule FRET. Nat. Commun. 13, 4396 (2022)., DOI: 10.1038/s41467-022-31945-6 24 10.1038/s41467-022-31945-6 false true Reference 51912476 /api/reference/51912476 25. Elgeti, M. & Hubbell, W. L. DEER analysis of GPCR conformational heterogeneity. Biomolecules 11, 778 (2021)., DOI: 10.3390/biom11060778 25 10.3390/biom11060778 false true Reference 51912477 /api/reference/51912477 26. Hink, M. A., Visser, N. V., Borst, J. W., van Hoek, A. & Visser, A. J. W. G. Practical use of corrected fluorescence excitation and emission spectra of fluorescent proteins in förster resonance energy transfer (FRET) studies. J. Fluoresc. 13, 185–188 (2003)., DOI: 10.1023/A:1022947411788 26 10.1023/A:1022947411788 false true Reference 51912478 /api/reference/51912478 27. Dror, R. O. et al. Identification of two distinct inactive conformations of the β2-adrenergic receptor reconciles structural and biochemical observations. Proc. Natl Acad. Sci. USA 106, 4689–4694 (2009)., DOI: 10.1073/pnas.0811065106 27 10.1073/pnas.0811065106 false true Reference 51912479 /api/reference/51912479 28. Manglik, A. et al. Structural Insights into the dynamic process of β2-adrenergic receptor signaling. Cell 161, 1101–1111 (2015)., DOI: 10.1016/j.cell.2015.04.043 28 10.1016/j.cell.2015.04.043 false true Reference 51912480 /api/reference/51912480 29. Lerch, M. T. et al. Viewing rare conformations of the β2 adrenergic receptor with pressure-resolved DEER spectroscopy. Proc. Natl Acad. Sci. USA 117, 31824–31831 (2020)., DOI: 10.1073/pnas.2013904117 29 10.1073/pnas.2013904117 false true Reference 51912481 /api/reference/51912481 30. Gregorio, G. G. et al. Single-molecule analysis of ligand efficacy in β2AR–G-protein activation. Nature 547, 68–73 (2017)., DOI: 10.1038/nature22354 30 10.1038/nature22354 false true Reference 51912482 /api/reference/51912482 31. Heng, J. et al. Function and dynamics of the intrinsically disordered carboxyl terminus of β2 adrenergic receptor. Nat. Commun. 14, 2005 (2023)., DOI: 10.1038/s41467-023-37233-1 31 10.1038/s41467-023-37233-1 false true Reference 51912483 /api/reference/51912483 32. Asher, W. B. et al. Single-molecule FRET imaging of GPCR dimers in living cells. Nat. Methods 18, 397–405 (2021)., DOI: 10.1038/s41592-021-01081-y 32 10.1038/s41592-021-01081-y false true Reference 51912484 /api/reference/51912484 33. Asher, W. B. et al. GPCR-mediated β-arrestin activation deconvoluted with single-molecule precision. Cell 185, 1661–1675.e16 (2022)., DOI: 10.1016/j.cell.2022.03.042 33 10.1016/j.cell.2022.03.042 false true Reference 51912485 /api/reference/51912485 34. Han, M.-J. et al. Single-molecule FRET and conformational analysis of beta-arrestin-1 through genetic code expansion and a Se-click reaction. Chem. Sci. 12, 9114–9123 (2021)., DOI: 10.1039/D1SC02653D 34 10.1039/D1SC02653D false true Reference 51912486 /api/reference/51912486 35. Knierim, B., Hofmann, K. P., Ernst, O. P. & Hubbell, W. L. Sequence of late molecular events in the activation of rhodopsin. Proc. Natl Acad. Sci. USA 104, 20290–20295 (2007)., DOI: 10.1073/pnas.0710393104 35 10.1073/pnas.0710393104 false true Reference 51912487 /api/reference/51912487 36. Grushevskyi, E. O. et al. Stepwise activation of a class C GPCR begins with millisecond dimer rearrangement. Proc. Natl Acad. Sci. USA 116, 10150–10155 (2019)., DOI: 10.1073/pnas.1900261116 36 10.1073/pnas.1900261116 false true Reference 51912488 /api/reference/51912488 37. Vilardaga, J.-P. Theme and variations on kinetics of GPCR activation/deactivation. J. Recept. Signal Transduct. Res. 30, 304–312 (2010)., DOI: 10.3109/10799893.2010.509728 37 10.3109/10799893.2010.509728 false true Reference 51912489 /api/reference/51912489 38. Franke, R. R., König, B., Sakmar, T. P., Khorana, H. G. & Hofmann, K. P. Rhodopsin mutants that bind but fail to activate transducin. Science 250, 123–125 (1990)., DOI: 10.1126/science.2218504 38 10.1126/science.2218504 false true Reference 51912490 /api/reference/51912490 39. Du, Y. et al. Assembly of a GPCR–G protein complex. Cell 177, 1232–1242.e11 (2019)., DOI: 10.1016/j.cell.2019.04.022 39 10.1016/j.cell.2019.04.022 false true Reference 51912491 /api/reference/51912491 40. Wingler, L. M. et al. Angiotensin analogs with divergent bias stabilize distinct receptor conformations. Cell 176, 468–478.e11 (2019)., DOI: 10.1016/j.cell.2018.12.005 40 10.1016/j.cell.2018.12.005 false true Reference 51912492 /api/reference/51912492 41. Wang, J., Hua, T. & Liu, Z.-J. Structural features of activated GPCR signaling complexes. Curr. Opin. Struct. Biol. 63, 82–89 (2020)., DOI: 10.1016/j.sbi.2020.04.008 41 10.1016/j.sbi.2020.04.008 false true Reference 51912493 /api/reference/51912493 42. Latorraca, N. R., Venkatakrishnan, A. J. & Dror, R. O. GPCR dynamics: structures in motion. Chem. Rev. 117, 139–155 (2016)., DOI: 10.1021/acs.chemrev.6b00177 42 10.1021/acs.chemrev.6b00177 false true Reference 51912494 /api/reference/51912494 43. Jaakola, V.-P. et al. The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 322, 1211–1217 (2008)., DOI: 10.1126/science.1164772 43 10.1126/science.1164772 false true Reference 51912495 /api/reference/51912495 44. McKinney, S. A., Joo, C. & Ha, T. Analysis of single-molecule FRET trajectories using hidden Markov modeling. Biophys. J. 91, 1941–1951 (2006)., DOI: 10.1529/biophysj.106.082487 44 10.1529/biophysj.106.082487 false true Reference 51912496 /api/reference/51912496 45. Dror, R. O. et al. Structural basis for nucleotide exchange in heterotrimeric G proteins. Science 348, 1361–1365 (2015)., DOI: 10.1126/science.aaa5264 45 10.1126/science.aaa5264 false true Reference 51912497 /api/reference/51912497 46. Elgeti, M. et al. The arrestin-1 finger loop interacts with two distinct conformations of active rhodopsin. J. Biol. Chem. 293, 4403–4410 (2018)., DOI: 10.1074/jbc.M117.817890 46 10.1074/jbc.M117.817890 false true Reference 51912498 /api/reference/51912498 47. Cong, X. et al. Molecular insights into the biased signaling mechanism of the μ-opioid receptor. Mol. Cell 81, 4165–4175.e6 (2021)., DOI: 10.1016/j.molcel.2021.07.033 47 10.1016/j.molcel.2021.07.033 false true Reference 51912499 /api/reference/51912499 48. Daibani, A. E. et al. Molecular mechanism of biased signaling at the kappa opioid receptor. Nat. Commun. 14, 1338 (2023)., DOI: 10.1038/s41467-023-37041-7 48 10.1038/s41467-023-37041-7 false true Reference 51912500 /api/reference/51912500 49. Suomivuori, C.-M. et al. Molecular mechanism of biased signaling in a prototypical G protein-coupled receptor. Science 367, 881–887 (2020)., DOI: 10.1126/science.aaz0326 49 10.1126/science.aaz0326 false true Reference 51912501 /api/reference/51912501 50. Culhane, K. J., Gupte, T. M., Madhugiri, I., Gadgil, C. J. & Sivaramakrishnan, S. Kinetic model of GPCR–G protein interactions reveals allokairic modulation of signaling. Nat. Commun. 13, 1202 (2022)., DOI: 10.1038/s41467-022-28789-5 50 10.1038/s41467-022-28789-5 false true Reference 51912502 /api/reference/51912502 51. Liu, H. & Naismith, J. H. An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol. BMC Biotechnol. 8, 91 (2008)., DOI: 10.1186/1472-6750-8-91 51 10.1186/1472-6750-8-91 false true Reference 51912503 /api/reference/51912503 52. Huang, W. et al. Structure of the neurotensin receptor 1 in complex with β-arrestin 1. Nature 579, 303–308 (2020)., DOI: 10.1038/s41586-020-1953-1 52 10.1038/s41586-020-1953-1 false true Reference 51912504 /api/reference/51912504 53. Hankovszky, H. O., Hideg, K., Sár, P. C., Lovas, M. J. & Jerkovich, G. Synthesis and Dehydrobromination of α-bromo aldehyde and ketone nitroxyl radical spin labels. Synthesis 1990, 59–62 (1990)., DOI: 10.1055/s-1990-26788 53 10.1055/s-1990-26788 false true Reference 51912505 /api/reference/51912505 54. Yang, M. et al. The Conformational Dynamics of Cas9 Governing DNA Cleavage Are Revealed by Single-Molecule FRET. CellReports 22, 372–382 (2018). 54 false true Reference 51912506 /api/reference/51912506 55. Illingworth, J. & Kittler, J. A survey of the Hough transform. Comput. Vis. Graph. Image Process. 44, 87–116 (1988)., DOI: 10.1016/S0734-189X(88)80033-1 55 10.1016/S0734-189X(88)80033-1 false true Reference 51912507 /api/reference/51912507 56. Ha, T. et al. Single-molecule fluorescence spectroscopy of enzyme conformational dynamics and cleavage mechanism. Proc. Natl Acad. Sci. USA 96, 893–898 (1999)., DOI: 10.1073/pnas.96.3.893 56 10.1073/pnas.96.3.893 false true Reference 51912508 /api/reference/51912508 57. Niu, X. et al. Pseudoknot length modulates the folding, conformational dynamics, and robustness of Xrn1 resistance of flaviviral xrRNAs. Nat. Commun. 12, 6417 (2021)., DOI: 10.1038/s41467-021-26616-x 57 10.1038/s41467-021-26616-x false true Reference 51912509 /api/reference/51912509 58. Ibáñez, L. F., Jeschke, G. & Stoll, S. DeerLab: A comprehensive toolbox for analyzing dipolar EPR spectroscopy data. Magn. Reson. 1, 209–224 (2020)., DOI: 10.5194/mr-1-209-2020 58 10.5194/mr-1-209-2020 false true Reference 51912510 /api/reference/51912510 59. Olsen, R. H. J. et al. TRUPATH, an open-source biosensor platform for interrogating the GPCR transducerome. Nat. Chem. Biol. 16, 841–849 (2020)., DOI: 10.1038/s41589-020-0535-8 59 10.1038/s41589-020-0535-8 false true Reference 51912511 /api/reference/51912511 60. Elgeti, M. Ligand efficacy modulates conformational dynamics of the µ-opioid receptor. Zenodo https://doi.org/10.5281/zenodo.10631251 (2024)., DOI: 10.5281/zenodo.10631251 60 10.5281/zenodo.10631251 false true /api/publication/34789190 Zhao Jiawei et al. Ligand efficacy modulates conformational dynamics of the µ-opioid receptor. (2024) NATURE 0028-0836 1476-4687 629 8011 474-480<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" >Zhao Jiawei </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" >Elgeti Matthias^* ✉ </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" >O’Brien Evan S. </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10006127"><a href="/gui2/?type=authors&mode=browse&sel=10006127" target="_blank">Sár Cecília P. (<span class="authorship-author-name">Pápayné Sár Cecília</span> <span class="authorAux-mtmt"> Szerves kémia</span>) </a> </span> <span class="author-affil"><span title="University of Pécs">UP</span>/<span title="Faculty of Pharmacy">FP</span>/Department of Organic and Pharmacological Chemistry</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" >EI Daibani Amal </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" >Heng Jie </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" >Sun Xiaoou </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" >White Elizabeth </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" >Che Tao </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" >Hubbell Wayne L. </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" >Kobilka Brian K. ✉ </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" >Chen Chunlai ✉ </span> </div> </div> <div class="title"><a href="/gui2/?mode=browse&params=publication;34789190" target="_blank">Ligand efficacy modulates conformational dynamics of the µ-opioid receptor</a></div> <div> <span class="journal-title">NATURE</span> <span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/0028-0836">0028-0836</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/1476-4687">1476-4687</a>)</span>: <span class="journal-volume">629</span> <span class="journal-issue">8011</span> <span class="page"> pp 474-480 </span> <span class="year">(2024)</span> </div> <div class="pub-footer"> <span class="language" xmlns="http://www.w3.org/1999/html">Language: English | </span> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.1038/s41586-024-07295-2" target="_blank" href="https://doi.org/10.1038/s41586-024-07295-2"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="001201403000020" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/001201403000020"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85189967158" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85189967158"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="38600384" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=38600384&dopt=Abstract"> PubMed </a> </span> </span> <OnlyViewableByAuthor><div class="ratings"> <div class="journal-subject">Journal subject: Scopus - Multidisciplinary&nbsp;&nbsp;&nbsp;Rank:&nbsp;D1</div> <div class="journal-subject">HAS Section of Earth Sciences (X.) HASSESX&nbsp;&nbsp;&nbsp;A</div> <div class="journal-subject">Committee on Regional Studies HASSELIX RTB [1901-]&nbsp;&nbsp;&nbsp;A nemzetközi</div> <div class="journal-subject">Committee on Sociology HASSELIX SZTB [1901-]&nbsp;&nbsp;&nbsp;A nemzetközi</div> </div></OnlyViewableByAuthor> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="" class="citingPub-count">Citing papers: 45</span> | Independent citation: 40 | Self citation: 5 | Unknown citation: 0 | Number of citations in WoS: 45 | Number of citations in Scopus:&nbsp;27 | WoS/Scopus assigned:&nbsp;45 | Number of citations with DOI:&nbsp;45 </div> <div class="publication-citation"> <a target="_blank" href="/api/publication?cond=citations.related;eq;34789190&sort=publishedYear,desc&sort=title"> Number of cited publications: 1 </a> </div> <div class="mtid"><span class="long-pub-mtid">Publication: 34789190</span> | <span class="status-data status-VALIDATED"> Validated </span> Core Citing | <span class="type-subtype">Journal Article ( Article ) </span> | <span class="pub-category">Scientific</span> | <span class="publication-sourceOfData">kézi felvitel</span> </div> <div class="funder"> (NKFI-137793) Funder: NRDIO </div> <div class="lastModified">Last Modified: 2025.05.17. 11:32 Rita Fekete (PTE GYTK admin 5) </div> <pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Comments</u>: * Megosztott szerzőség</pre> </div></div>