Buscar
Mostrando ítems 1-10 de 203
From Conformation To Interaction: Techniques To Explore The Hsp70/hsp90 Network
(BENTHAM SCIENCE PUBL LTDSHARJAH, 2015)
Structural and functional characterization of the chaperone Hsp70 from sugarcane. Insights into conformational changes during cycling from cross-linking/mass spectrometry assays
(Elsevier B.V., 2014-06-02)
Hsp70 cycles from an ATP-bound state, in which the affinity for unfolded polypeptides is low, to an ADP-bound state, in which the affinity for unfolded polypeptides is high, to assist with cell proteostasis. Such cycling ...
Protein folding assisted by chaperones
(Bentham Science Publ LtdSharjahEmirados Árabes Unidos, 2005)
The Molecular Chaperone Hsp70 Family Members Function by a Bidirectional Heterotrophic Allosteric Mechanism
(BENTHAM SCIENCE PUBL LTD, 2011)
The Hsp70 family is one of the most important and conserved molecular chaperone families. It is well documented that Hsp70 family members assist many cellular processes involving protein quality control, as follows: protein ...
Identification and in silico analysis of the Citrus HSP70 molecular chaperone gene family
(Genetics and Molecular Biology, 2019)
Low resolution structural study of two human HSP40 chaperones in solution - DjA1 from subfamily A and DjB4 from subfamily B have different quaternary structures
(Amer Soc Biochemistry Molecular Biology IncBethesdaEUA, 2005)
ATPase Subdomain IA Is a Mediator of Interdomain Allostery in Hsp70 Molecular Chaperones
(Public Library of Science, 2014-05)
The versatile functions of the heat shock protein 70 (Hsp70) family of molecular chaperones rely on allosteric interactions between their nucleotide-binding and substrate-binding domains, NBD and SBD. Understanding the ...