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Article

Effect of cataract-associated mutations in the N-terminal domain of αB-crystallin (HspB5).

Experimental eye research - 1 Aug 2020

Muranova Lydia K, Strelkov Sergei V, Gusev Nikolai B

Abstract excerpt

Physico-chemical properties of three cataract-associated missense mutants of αB-crystallin (HspB5) (R11H, P20S, R56W) were analyzed. The oligomers formed by the R11H mutant were smaller, whereas the oligomers of the P20S and R56W mutants were larger than those of the wild-type protein. The P20S mutant possessed lower thermal stability than the wild-type HspB5 or two other HspB5 mutants. All HspB5 mutants were...

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Identifiers

PMID: 32533979
DOI: 10.1016/j.exer.2020.108091

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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