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Article

The congenital cataract-linked G61C mutation destabilizes γD-crystallin and promotes non-native aggregation.

PloS one - 1 Jan 2011

Zhang Wang, Cai Hong-Chen, Li Fei-Feng, Xi Yi-Bo, Ma Xu, Yan Yong-Bin

Abstract excerpt

γD-crystallin is one of the major structural proteins in human eye lens. The solubility and stability of γD-crystallin play a crucial role in maintaining the optical properties of the lens during the life span of an individual. Previous study has shown that the inherited mutation G61C results in autosomal dominant congenital cataract. In this research, we studied the effects of the G61C mutation on γD-crystallin...

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Source

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Identifiers

PMID: 21655238
DOI: 10.1371/journal.pone.0020564
PMCID: PMC3105094

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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The congenital cataract-linked G61C mutation destabilizes γD-crystallin and promotes non-native aggregation.PMID 21655238Read ↗

Cataract-causing mutations S78F and S78P of γD-crystallin decrease protein conformational stability and drive aggregation.Semantic proximity Read ↗

The cataract-causing mutation G75V promotes γS-crystallin aggregation by modifying and destabilizing the native structure.Semantic proximity Read ↗

Congenital Cataract-Causing Mutation G129C in γC-Crystallin Promotes the Accumulation of Two Distinct Unfolding Intermediates That Form Highly Toxic Aggregates.Semantic proximity Read ↗

A novel cataract-causing mutation Ile82Met of γA crystallin trends to aggregate with unfolding intermediate.Semantic proximity Read ↗

Cataract-causing variant Q70P damages structural stability of βB1-crystallin and increases its tendency to form insoluble aggregates.Semantic proximity Read ↗

Cataract-causing mutations L45P and Y46D impair the thermal stability of γC-crystallin.Semantic proximity Read ↗

A novel cataract-related mutation R10P in γA-crystallin increases susceptibility to thermal shock and ultraviolet radiation of γA-crystallin.Semantic proximity Read ↗

A novel F30S mutation in γS-crystallin causes autosomal dominant congenital nuclear cataract by increasing susceptibility to stresses.Semantic proximity Read ↗

Cataract-causing mutation R48C increases γA-crystallin susceptibility to oxidative stress and ultraviolet radiation.Semantic proximity Read ↗

A novel mutation impairing the tertiary structure and stability of γC-crystallin (CRYGC) leads to cataract formation in humans and zebrafish lens.Semantic proximity Read ↗

Cataract-associated New Mutants S175G/H181Q of βB2-Crystallin and P24S/S31G of γD-Crystallin are Involved in Protein aggregation by Structural ChangesSemantic proximity Read ↗

Effects of cataract-causing mutations W59C and W151C on βB2-crystallin structure, stability and folding.Semantic proximity Read ↗

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