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.
The IMiD target CRBN determines HSP90 activity toward transmembrane proteins essential in multiple myeloma.
Mol Cell
; 81(6): 1170-1186.e10, 2021 03 18.
Artigo
em Inglês
| MEDLINE | ID: mdl-33571422
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.
Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle.
Nat Commun
; 12(1): 828, 2021 02 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-33547294
5.
Author Correction: A methylated lysine is a switch point for conformational communication in the chaperone Hsp90.
Nat Commun
; 11(1): 3727, 2020 07 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-32694502
6.
Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90.
Nat Commun
; 11(1): 1410, 2020 03 16.
Artigo
em Inglês
| MEDLINE | ID: mdl-32179743
7.
A methylated lysine is a switch point for conformational communication in the chaperone Hsp90.
Nat Commun
; 11(1): 1219, 2020 03 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-32139682
8.
Cytosolic Hsp70 and Hsp40 chaperones enable the biogenesis of mitochondrial ß-barrel proteins.
J Cell Biol
; 217(9): 3091-3108, 2018 09 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-29930205