.png){kind=icon}
.png){kind=icon}
Return
Chaperones in kinase homeostasis and drug discovery
.png){kind=icon}
PRE
AI
DOI：10.1016/j.tips.2026.06.004.png)
.png){kind=icon}
Original request for help.png){kind=icon}
Share.png){kind=icon}
Save
Abstract
En 中文
Kinase homeostasis is shaped by chaperone-directed control of client folding, maturation, and modification. Recent structural studies reveal stepwise heat shock protein 90–cell division cycle 37 remodeling of labile kinase clients. Beyond supporting kinase folding, chaperone assemblies act as platforms for post-translational modification editing and fate determination. Targeting chaperone-dependent kinase homeostasis expands drug discovery beyond catalytic inhibition to interface disruption and bifunctional regulation.
Journal
IF:
19.9
Papers:
3.3K
Citations:
1.5W