Results 81 to 90 of about 3,296,549 (170)

The redox switch that regulates molecular chaperones

Biomolecular Concepts, 2015
Modification of reactive cysteine residues plays an integral role in redox-regulated reactions. Oxidation of thiolate anions to sulphenic acid can result in disulphide bond formation, or overoxidation to sulphonic acid, representing reversible and ...
Conway Myra E., Lee Christopher
doaj   +1 more source

Emerging roles of molecular chaperones and co-chaperones in selective autophagy: focus on BAG proteins.

, 2011
Macroautophagy is a catabolic process by which the cell degrades cytoplasmic components through the lysosomal machinery. While initially acknowledged as a rather unspecific bulk degradation process, growing lines of evidence indicate the selectivity of ...
CARRA, Serena, Christian Behl, Behl, Christian, Serena Carra, Behl, C., Gamerdinger, M, Gamerdinger, Martin, Martin Gamerdinger   +7 more
core   +1 more source

complementarity of the Ac/N-end rule pathway and the Arg/N-end rule pathway

, 2014
1
황철상
core  

An artificial chaperone serves a dual role in regulating the assembly of peptides through phase separation

Aggregate
In biological systems, molecular assembly primarily relies on the assistance of molecular chaperones. Inspired by nature, strategies like ‘chaperone‐assisted assembly’ and ‘catalyzed assembly’ have been proposed for the sophisticated control of molecular
Wang Li, Yang Zhou, Sheng He, Tianyi Tong, Congsen Wang, Peichen Shi, Suixu Li, Xinchang Wang, Liulin Yang, Xiaoyu Cao, Zhong‐Qun Tian   +10 more
doaj   +1 more source

The known unknowns of the Hsp90 chaperone

eLife
Molecular chaperones are vital proteins that maintain protein homeostasis by assisting in protein folding, activation, degradation, and stress protection. Among them, heat-shock protein 90 (Hsp90) stands out as an essential proteostasis hub in eukaryotes,
Laura-Marie Silbermann, Benjamin Vermeer, Sonja Schmid, Katarzyna Tych   +3 more
doaj   +1 more source

Chaperone dependency during biogenesis does not correlate with chaperone dependency during refolding

Molecular Systems Biology
Many proteins require molecular chaperones to fold into their functional native forms. However, the roles of chaperones during primary biogenesis in vivo can differ from the functions they play during in vitro refolding experiments.
Divya Yadav, İdil I Demiralp, Mark Fakler, Stephen D Fried   +3 more
doaj   +1 more source

Evolvability of Chaperonin Substrate Proteins [PDF]

, 2009
Molecular chaperones ensure that their substrate proteins reach the functional native state, and prevent their aggregation. Recently, an additional function was proposed for molecular chaperones: they serve as buffers (_capacitors_) for evolution by ...
Tobias Maier, Paolo Ribecaa, Luis Serrano, Tobias Maierb, Paolo Ribeca, Emanuele Raineri, Luis Serranob, Emanuele Raineria   +7 more
core  

The role of molecular chaperones in the mechanisms of epileptogenesis. [PDF]

Cell Stress Chaperones, 2023
Davletshin AI, Matveeva AA, Poletaeva II, Evgen'ev MB, Garbuz DG.   +4 more
europepmc   +1 more source

The roles of molecular chaperones in regulating cell metabolism. [PDF]

FEBS Lett, 2023
Binder MJ, Pedley AM.
europepmc   +1 more source

Molecular Chaperones [PDF]

Biophysical Journal, 2008
Marissa V. Powers, Paul Workman
openaire   +2 more sources