Advances in the structures, mechanisms and targeting of molecular chaperones

Signal Transduction and Targeted Therapy, Journal Year: 2025, Volume and Issue: 10(1)

Published: March 12, 2025

Abstract Molecular chaperones, a class of complex client regulatory systems, play significant roles in the prevention protein misfolding and abnormal aggregation, modulation homeostasis, protection cells from damage under constantly changing environmental conditions. As understanding biological mechanisms molecular chaperones has increased, their link with occurrence progression disease suggested that these proteins are promising targets for therapeutic intervention, drawing intensive interest. Here, we review recent advances determining structures heat shock 90 (HSP90) chaperone system complexes. We also describe features shed light on complicated mechanism operates through interactions various co-chaperones cycles. In addition, how affect diseases by regulating pathogenic been thoroughly analyzed. Furthermore, focus to systematically discuss clinical drug design strategies preclinical stage. Recent studies have identified variety novel targeting systems compounds act different those traditional inhibitors. Therefore, as more developed, will significantly contribute discovery new potential drugs.

Language: Английский

Discovery of new Hsp90–Cdc37 protein–protein interaction inhibitors: in silico screening and optimization of anticancer activity

RSC Advances, Journal Year: 2024, Volume and Issue: 14(39), P. 28347 - 28375

Published: Jan. 1, 2024

The interaction between heat shock protein 90 (Hsp90) and Hsp90 co-chaperone cell-division cycle 37 (Cdc37) is crucial for the folding maturation of several oncogenic proteins, particularly kinases.

Language: Английский