Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Cataract-related variant R114C increases βA3-crystallin susceptibility to environmental stresses by disrupting the protein senior structure.

International journal of biological macromolecules - 1 Mar 2024

Chen Silong, Guo Jiarui, Xu Wanyue, Song Hang, Xu Jingjie, Luo Chenqi, Yao Ke, Hu Lidan, Chen Xiangjun, Yu Yibo

Abstract excerpt

Congenital cataract is a major cause of childhood blindness worldwide, with crystallin mutations accounting for over 40 % of gene-mutation-related cases. Our research focused on a novel R114C mutation in a Chinese family, resulting in bilateral coronary cataract with blue punctate opacity. Spectroscopic experiments revealed that βA3-R114C significantly altered the senior structure, exhibiting aggregation, and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cataract
Share to Crystallins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mutation

Source

Identifiers

PMID: 38360245
DOI: 10.1016/j.ijbiomac.2024.130191

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cataract-related variant R114C increases βA3-crystallin susceptibility to environmental stresses by disrupting the protein senior structure.PMID 38360245Read ↗

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

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

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

S209W mutation enhance π-π interactions in the fourth Greek-key of βA3/A1-crystallin linking with aggregation formation and stress susceptibility.Semantic proximity Read ↗

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

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

Increasing susceptibility to oxidative stress by cataract-causing crystallin mutations.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-causing mutations S78F and S78P of γD-crystallin decrease protein conformational stability and drive aggregation.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 ↗

⌁Select a neighboring publication to make it the new centre.