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1	Material Type: Article	Publisher Correction: Pharmacological targeting of the unfolded protein response for disease intervention Nature chemical biology, 2019-11, Vol.15 (11), p.1129-1129 [Peer Reviewed Journal] Copyright Nature Publishing Group Nov 2019 ;ISSN: 1552-4450 ;EISSN: 1552-4469 ;DOI: 10.1038/s41589-019-0363-x ;PMID: 31439938 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
2	Material Type: Article	Author Correction: Modulating co-translational protein folding by rational design and ribosome engineering Nature communications, 2022-09, Vol.13 (1), p.5441-5441, Article 5441 [Peer Reviewed Journal] The Author(s) 2022. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;The Author(s) 2022 ;ISSN: 2041-1723 ;EISSN: 2041-1723 ;DOI: 10.1038/s41467-022-33270-4 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
3	Material Type: Article	AlphaFold2 fails to predict protein fold switching Protein science, 2022-06, Vol.31 (6), p.e4353-n/a [Peer Reviewed Journal] Published 2022. This article is a U.S. Government work and is in the public domain in the USA. ;2022 The Protein Society ;ISSN: 0961-8368 ;EISSN: 1469-896X ;DOI: 10.1002/pro.4353 ;PMID: 35634782 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
4	Material Type: Article	Abstract 1268 The influence of surface residues on the structure and activity of a salt-dependent halophile enzyme The Journal of biological chemistry, 2024-03, Vol.300 (3) [Peer Reviewed Journal] 2024 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1016/j.jbc.2024.106851 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
5	Material Type: Article	A New Role for the ER Unfolded Protein Response Mediator ATF6 Circulation research, 2017-03, Vol.120 (5), p.759-761 [Peer Reviewed Journal] Copyright Lippincott Williams & Wilkins Ovid Technologies Mar 3, 2017 ;ISSN: 0009-7330 ;EISSN: 1524-4571 ;DOI: 10.1161/CIRCRESAHA.117.310577 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
6	Material Type: Article	Correction: Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response The Journal of cell biology, 2021-04, Vol.220 (4), p.1 [Peer Reviewed Journal] Copyright Rockefeller University Press Apr 2021 ;2021 Schuck et al. 2021 ;ISSN: 0021-9525 ;EISSN: 1540-8140 ;DOI: 10.1083/jcb.20090707402092021c ;PMID: 33600553 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
7	Material Type: Article	Is Protein Folding a Thermodynamically Unfavorable, Active, Energy-Dependent Process? International journal of molecular sciences, 2022-01, Vol.23 (1), p.521 [Peer Reviewed Journal] 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;2022 by the authors. 2022 ;ISSN: 1422-0067 ;ISSN: 1661-6596 ;EISSN: 1422-0067 ;DOI: 10.3390/ijms23010521 ;PMID: 35008947 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
8	Material Type: Article	A Study of a Protein-Folding Machine: Transient Rotation of the Polypeptide Backbone Facilitates Rapid Folding of Protein Domains in All-Atom Molecular Dynamics Simulations International journal of molecular sciences, 2023-06, Vol.24 (12), p.10049 [Peer Reviewed Journal] COPYRIGHT 2023 MDPI AG ;2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;2023 by the authors. 2023 ;ISSN: 1422-0067 ;ISSN: 1661-6596 ;EISSN: 1422-0067 ;DOI: 10.3390/ijms241210049 ;PMID: 37373197 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
9	Material Type: Article	Chris Dobson (1949-2019) Nature chemical biology, 2020-02, Vol.16 (2), p.105-105 [Peer Reviewed Journal] 2020© Springer Nature America, Inc. 2020 ;Springer Nature America, Inc. 2020. ;ISSN: 1552-4450 ;EISSN: 1552-4469 ;DOI: 10.1038/s41589-019-0456-6 ;PMID: 31974526 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
10	Material Type: Article	The TCP1[gamma] subunit of Leishmania donovani forms a biologically active homo-oligomeric complex The FEBS journal, 2015-12, Vol.282 (23), p.4607 [Peer Reviewed Journal] ISSN: 1742-464X ;EISSN: 1742-4658 ;DOI: 10.1111/febs.13521 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
11	Material Type: Article	Modeling protein folding in vivo Biology direct, 2018-07, Vol.13 (1), p.13-13, Article 13 [Peer Reviewed Journal] COPYRIGHT 2018 BioMed Central Ltd. ;COPYRIGHT 2018 BioMed Central Ltd. ;Copyright © 2018. This work is licensed under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and conditions, you may use this content in accordance with the terms of the License. ;The Author(s). 2018 ;ISSN: 1745-6150 ;EISSN: 1745-6150 ;DOI: 10.1186/s13062-018-0217-6 ;PMID: 29980221 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
12	Material Type: Article	Marginally hydrophobic transmembrane [alpha]-helices shaping membrane protein folding Protein science, 2015-07, Vol.24 (7), p.1057 [Peer Reviewed Journal] 2015 The Protein Society ;ISSN: 0961-8368 ;EISSN: 1469-896X ;DOI: 10.1002/pro.2698 ;CODEN: PRCIEI Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
13	Material Type: Article	PiXie Analysis for Monitoring Dynamic Protein Interaction and Folding in a Living Cell Seibutsu Butsuri, 2021, Vol.61(1), pp.036-039 [Peer Reviewed Journal] 2021 by THE BIOPHYSICAL SOCIETY OF JAPAN ;Copyright Japan Science and Technology Agency 2021 ;ISSN: 0582-4052 ;EISSN: 1347-4219 ;DOI: 10.2142/biophys.61.036 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
14	Material Type: Article	Neil J. Bulleid (1960-2023), a virtuoso of protein folding and redox biology info:eu-repo/semantics/OpenAccess ;ISSN: 0261-4189 ;EISSN: 1460-2075 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
15	Material Type: Article	Structure of 3He Scientific reports, 2021-09, Vol.11 (1), p.18903-18903, Article 18903 [Peer Reviewed Journal] The Author(s) 2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;The Author(s) 2021 ;ISSN: 2045-2322 ;EISSN: 2045-2322 ;DOI: 10.1038/s41598-021-98416-8 ;PMID: 34556762 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
16	Material Type: Article	Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress Nature cell biology, 2013-10, Vol.15 (10), p.1231-1243 [Peer Reviewed Journal] COPYRIGHT 2013 Nature Publishing Group ;COPYRIGHT 2013 Nature Publishing Group ;Copyright Nature Publishing Group Oct 2013 ;ISSN: 1465-7392 ;EISSN: 1476-4679 ;DOI: 10.1038/ncb2838 ;PMID: 24036477 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
17	Material Type: Article	Publisher Correction: Examining a Thermodynamic Order Parameter of Protein Folding Scientific reports, 2018-05, Vol.8 (1), p.8269-1, Article 8269 [Peer Reviewed Journal] 2018. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;The Author(s) 2018 ;ISSN: 2045-2322 ;EISSN: 2045-2322 ;DOI: 10.1038/s41598-018-26490-6 ;PMID: 29799017 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
18	Material Type: Article	Cryo-EM structures reveal multiple stages of bacterial outer membrane protein folding Cell, 2022-03, Vol.185 (7), p.1143-1156.e13 [Peer Reviewed Journal] 2022 ;Copyright © 2022. Published by Elsevier Inc. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2022.02.016 ;PMID: 35294859 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
19	Material Type: Article	Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria The Journal of biological chemistry, 2020-07, Vol.295 (30), p.10340-10367 [Peer Reviewed Journal] 2020 © 2020 Horne et al. ;2020 Horne et al. ;2020 Horne et al. 2020 Horne et al. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.REV120.011473 ;PMID: 32499369 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by
20	Material Type: Article	How protein stability and new functions trade off PLoS computational biology, 2008-02, Vol.4 (2), p.e1000002 [Peer Reviewed Journal] COPYRIGHT 2008 Public Library of Science ;Tokuriki et al. 2008 ;2008 Tokuriki 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: Tokuriki N, Stricher F, Serrano L, Tawfik DS (2008) How Protein Stability and New Functions Trade Off. PLoS Comput Biol 4(2): e1000002. doi:10.1371/journal.pcbi.1000002 ;ISSN: 1553-7358 ;ISSN: 1553-734X ;EISSN: 1553-7358 ;DOI: 10.1371/journal.pcbi.1000002 ;PMID: 18463696 Full text available View Online Details Recommendations Reviews Times Cited External Links Citations Cited by

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Results 1 - 20 of 48,562 for All Library Resources

Copyright Nature Publishing Group Nov 2019 ;ISSN: 1552-4450 ;EISSN: 1552-4469 ;DOI: 10.1038/s41589-019-0363-x ;PMID: 31439938

Published 2022. This article is a U.S. Government work and is in the public domain in the USA. ;2022 The Protein Society ;ISSN: 0961-8368 ;EISSN: 1469-896X ;DOI: 10.1002/pro.4353 ;PMID: 35634782

2024 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1016/j.jbc.2024.106851

Copyright Lippincott Williams & Wilkins Ovid Technologies Mar 3, 2017 ;ISSN: 0009-7330 ;EISSN: 1524-4571 ;DOI: 10.1161/CIRCRESAHA.117.310577

Copyright Rockefeller University Press Apr 2021 ;2021 Schuck et al. 2021 ;ISSN: 0021-9525 ;EISSN: 1540-8140 ;DOI: 10.1083/jcb.20090707402092021c ;PMID: 33600553

2020© Springer Nature America, Inc. 2020 ;Springer Nature America, Inc. 2020. ;ISSN: 1552-4450 ;EISSN: 1552-4469 ;DOI: 10.1038/s41589-019-0456-6 ;PMID: 31974526

ISSN: 1742-464X ;EISSN: 1742-4658 ;DOI: 10.1111/febs.13521

2015 The Protein Society ;ISSN: 0961-8368 ;EISSN: 1469-896X ;DOI: 10.1002/pro.2698 ;CODEN: PRCIEI

2021 by THE BIOPHYSICAL SOCIETY OF JAPAN ;Copyright Japan Science and Technology Agency 2021 ;ISSN: 0582-4052 ;EISSN: 1347-4219 ;DOI: 10.2142/biophys.61.036

info:eu-repo/semantics/OpenAccess ;ISSN: 0261-4189 ;EISSN: 1460-2075

COPYRIGHT 2013 Nature Publishing Group ;COPYRIGHT 2013 Nature Publishing Group ;Copyright Nature Publishing Group Oct 2013 ;ISSN: 1465-7392 ;EISSN: 1476-4679 ;DOI: 10.1038/ncb2838 ;PMID: 24036477

2022 ;Copyright © 2022. Published by Elsevier Inc. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2022.02.016 ;PMID: 35294859

2020 © 2020 Horne et al. ;2020 Horne et al. ;2020 Horne et al. 2020 Horne et al. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.REV120.011473 ;PMID: 32499369

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