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1.
The endoplasmic reticulum chaperone BiP is a closure-accelerating cochaperone of Grp94.
Proc Natl Acad Sci U S A
; 119(5)2022 02 01.
Article
in English
| MEDLINE | ID: mdl-35078937
2.
Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.
Mol Cell
; 49(3): 464-73, 2013 Feb 07.
Article
in English
| MEDLINE | ID: mdl-23260660
3.
The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation.
J Biol Chem
; 294(16): 6387-6396, 2019 04 19.
Article
in English
| MEDLINE | ID: mdl-30787103
4.
Multimapping confounds ribosome profiling analysis: A case-study of the Hsp90 molecular chaperone.
Proteins
; 88(1): 57-68, 2020 01.
Article
in English
| MEDLINE | ID: mdl-31254414
5.
Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone.
Mol Cell
; 42(1): 96-105, 2011 Apr 08.
Article
in English
| MEDLINE | ID: mdl-21474071
6.
Two-sided block of a dual-topology F- channel.
Proc Natl Acad Sci U S A
; 112(18): 5697-701, 2015 May 05.
Article
in English
| MEDLINE | ID: mdl-25902543
7.
Crowding Activates Heat Shock Protein 90.
J Biol Chem
; 291(12): 6447-55, 2016 Mar 18.
Article
in English
| MEDLINE | ID: mdl-26797120
8.
Conformational dynamics of the molecular chaperone Hsp90.
Q Rev Biophys
; 44(2): 229-55, 2011 May.
Article
in English
| MEDLINE | ID: mdl-21414251
9.
Mechanisms of Protein Quality Control in the Endoplasmic Reticulum by a Coordinated Hsp40-Hsp70-Hsp90 System.
Annu Rev Biophys
; 52: 509-524, 2023 05 09.
Article
in English
| MEDLINE | ID: mdl-37159299
10.
Electrostatics Drive the Molecular Chaperone BiP to Preferentially Bind Oligomerized States of a Client Protein.
J Mol Biol
; 434(13): 167638, 2022 07 15.
Article
in English
| MEDLINE | ID: mdl-35597552
11.
The ER Chaperones BiP and Grp94 Regulate the Formation of Insulin-Like Growth Factor 2 (IGF2) Oligomers.
J Mol Biol
; 433(13): 166963, 2021 06 25.
Article
in English
| MEDLINE | ID: mdl-33811917
12.
Are proteins made from a limited parts list?
Trends Biochem Sci
; 30(2): 73-80, 2005 Feb.
Article
in English
| MEDLINE | ID: mdl-15691652
13.
Hsp90 chaperones have an energetic hot-spot for binding inhibitors.
Protein Sci
; 29(10): 2101-2111, 2020 10.
Article
in English
| MEDLINE | ID: mdl-32812680
14.
Conformational Cycling within the Closed State of Grp94, an Hsp90-Family Chaperone.
J Mol Biol
; 431(17): 3312-3323, 2019 08 09.
Article
in English
| MEDLINE | ID: mdl-31202885
15.
Physical-chemical determinants of turn conformations in globular proteins.
Protein Sci
; 16(8): 1720-7, 2007 Aug.
Article
in English
| MEDLINE | ID: mdl-17656584
16.
The role of introns in repeat protein gene formation.
J Mol Biol
; 360(2): 258-66, 2006 Jul 07.
Article
in English
| MEDLINE | ID: mdl-16781737
17.
Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.
J Mol Biol
; 429(19): 2918-2930, 2017 09 15.
Article
in English
| MEDLINE | ID: mdl-28822683
18.
Molecular mechanism of bacterial Hsp90 pH-dependent ATPase activity.
Protein Sci
; 26(6): 1206-1213, 2017 06.
Article
in English
| MEDLINE | ID: mdl-28383119
19.
5'-N-ethylcarboxamidoadenosine is not a paralog-specific Hsp90 inhibitor.
Protein Sci
; 25(12): 2209-2215, 2016 12.
Article
in English
| MEDLINE | ID: mdl-27667530
20.
An improved experimental system for determining small folding entropy changes resulting from proline to alanine substitutions.
Protein Sci
; 14(9): 2429-35, 2005 Sep.
Article
in English
| MEDLINE | ID: mdl-16131666