Detalhe da pesquisa
1.
The switch from client holding to folding in the Hsp70/Hsp90 chaperone machineries is regulated by a direct interplay between co-chaperones.
Mol Cell
; 82(8): 1543-1556.e6, 2022 04 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-35176233
2.
NudC guides client transfer between the Hsp40/70 and Hsp90 chaperone systems.
Mol Cell
; 82(3): 555-569.e7, 2022 02 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-35063133
3.
Coordinated Conformational Processing of the Tumor Suppressor Protein p53 by the Hsp70 and Hsp90 Chaperone Machineries.
Mol Cell
; 74(4): 816-830.e7, 2019 05 16.
Artigo
em Inglês
| MEDLINE | ID: mdl-31027879
4.
Active unfolding of the glucocorticoid receptor by the Hsp70/Hsp40 chaperone system in single-molecule mechanical experiments.
Proc Natl Acad Sci U S A
; 119(15): e2119076119, 2022 04 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-35377810
5.
Chaperones GroEL/GroES accelerate the refolding of a multidomain protein through modulating on-pathway intermediates.
J Biol Chem
; 289(1): 286-98, 2014 Jan 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-24247249
6.
Functional intermediate in the refolding pathway of a large and multidomain protein malate synthase G.
Biochemistry
; 52(26): 4517-30, 2013 Jul 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-23718231
7.
Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network.
Sci Adv
; 7(51): eabl7295, 2021 Dec 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-34919431
8.
Functional principles and regulation of molecular chaperones.
Adv Protein Chem Struct Biol
; 114: 1-60, 2019.
Artigo
em Inglês
| MEDLINE | ID: mdl-30635079
9.
The structure and oxidation of the eye lens chaperone αA-crystallin.
Nat Struct Mol Biol
; 26(12): 1141-1150, 2019 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-31792453