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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.
Artículo
en Inglés
| 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.
Artículo
en Inglés
| MEDLINE | ID: mdl-35063133
3.
The Co-chaperone Cns1 and the Recruiter Protein Hgh1 Link Hsp90 to Translation Elongation via Chaperoning Elongation Factor 2.
Mol Cell
; 74(1): 73-87.e8, 2019 04 04.
Artículo
en Inglés
| MEDLINE | ID: mdl-30876805
4.
The permanently chaperone-active small heat shock protein Hsp17 from Caenorhabditis elegans exhibits topological separation of its N-terminal regions.
J Biol Chem
; 299(1): 102753, 2023 01.
Artículo
en Inglés
| MEDLINE | ID: mdl-36442512
5.
Deletion of the transcription factors Hsf1, Msn2 and Msn4 in yeast uncovers transcriptional reprogramming in response to proteotoxic stress.
FEBS Lett
; 598(6): 635-657, 2024 Mar.
Artículo
en Inglés
| MEDLINE | ID: mdl-38366111
6.
Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.
Nat Commun
; 12(1): 6697, 2021 11 18.
Artículo
en Inglés
| MEDLINE | ID: mdl-34795272
7.
The Heat Shock Response in Yeast Maintains Protein Homeostasis by Chaperoning and Replenishing Proteins.
Cell Rep
; 29(13): 4593-4607.e8, 2019 12 24.
Artículo
en Inglés
| MEDLINE | ID: mdl-31875563
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