A copy of this work was available on the public web and has been preserved in the Wayback Machine. The capture dates from 2017; you can also visit the original URL.
The file type is application/pdf
.
Effect of a Single AGE Modification on the Structure and Chaperone Activity of Human αB-Crystallin†
2007
Biochemistry
During aging, human lens proteins undergo several post-translational modifications, one of which is glycation. This process leads to the formation of advanced glycation end products (AGEs) which accumulate with time possibly leading to the formation of cataract. RB-Crystallin, a predominant protein in the lens, is a member of the small heat shock proteins (sHSPs) which are a ubiquitous class of molecular chaperones that interact with partially denatured proteins to prevent aggregation. This
doi:10.1021/bi701326b
pmid:18027913
fatcat:fhtntvqk25c3pde7dh36luifvy