The dynamic triage interplay of Hsp90 with its chaperone cycle and client binding
Abstract Hsp90, a crucial molecular chaperone, regulates diverse client proteins, impacting both normal biology and disease. Central to its function is its conformational plasticity, driven by ATPase activity and client interactions. However, comprehensive insights into Hsp90’s dynamic molecular tra...
Saved in:
| Main Authors: | Xiaozhan Qu, Simin Wang, Shuo Zhao, Chanjuan Wan, Weiya Xu, Chengdong Huang |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2024-12-01
|
| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-024-55026-y |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
The known unknowns of the Hsp90 chaperone
by: Laura-Marie Silbermann, et al.
Published: (2024-12-01) -
The DnaJ-Hsp70-Hsp90 co-chaperon networks in scallops under toxic Alexandrium dinoflagellates exposure
by: Moli Li, et al.
Published: (2025-01-01) -
Structural dynamics of RAF1-HSP90-CDC37 and HSP90 complexes reveal asymmetric client interactions and key structural elements
by: Lorenzo I. Finci, et al.
Published: (2024-03-01) -
Identification and expression analysis of the heat shock proteins Hsp70, Hsp90, and Hsp90b in Litopenaeus vannamei under low-temperature stress
by: Min Peng, et al.
Published: (2025-03-01) -
Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle.
by: Rebecca Mercier, et al.
Published: (2023-05-01)