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Article

Asp 58 modulates lens αA-crystallin oligomer formation and chaperone function.

The FEBS journal - 1 Jun 2018

Takata Takumi, Nakamura-Hirota Tooru, Inoue Rintaro, Morishima Ken, Sato Nobuhiro, Sugiyama Masaaki, Fujii Noriko

Abstract excerpt

Senile cataract onset is caused by insolubilization of lens proteins. The lens crystallin protein family correctly orders the formation of homo- or hetero-oligomers in lens fiber cells. Because lens fiber cells do not divide, covalent post-translational modifications, such as isomerization of aspartate residues, accumulate with aging. Although many isomerization sites of αA-crystallin have been reported, their...

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Share to Aspartic Acid
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Lens, Crystalline

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Source

Identifiers

PMID: 29676852
DOI: 10.1111/febs.14475

Provenance

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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