Partially Folded Aggregation Intermediates of Human γD-, γC- and γS-Crystallin Are Recognized and Bound by Human αB-crystallin Chaperone

Human γ-crystallins are long-lived unusually stable proteins of the eye lens exhibiting duplicated, double Greek key domains. The lens also contains high concentrations of the small heat shock chaperone α-crystallin, which suppresses aggregation of model substrates in vitro. Mature-onset cataract is...

Full description

Saved in:

Bibliographic Details
Main Authors:	Acosta-Sampson, Ligia, King, Jonathan
Format:	Artigo
Language:	Inglês
Published:	2010
Subjects:	Article
Online Access:	https://ncbi.nlm.nih.gov/pmc/articles/PMC3072757/ https://ncbi.nlm.nih.gov/pubmed/20621668 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2010.05.067
Tags:	Add Tag No Tags, Be the first to tag this record!

Partially Folded Aggregation Intermediates of Human γD-, γC- and γS-Crystallin Are Recognized and Bound by Human αB-crystallin Chaperone

Similar Items