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

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

International journal of biological macromolecules - 1 Oct 2017

Zhao Wei-Jie, Xu Jia, Chen Xiang-Jun, Liu Hui-Hui, Yao Ke, Yan Yong-Bin

Abstract excerpt

β/γ-Crystallins, the predominant structural proteins in vertebrate lens with lifelong stability to maintain lens transparency, share a high similarity in their primary sequences and tertiary structures. Four conserved Trp residues have been shown to be important to γ-crystallin structure, stability and protection against UV irradiation, whereas their roles in β-crystallins remain elusive. Herein we found that two...

Read the complete abstract on PubMed

Topics

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

Share to Cataract
Share to Cell Death
Share to Intracellular Space

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

Share to Protein Aggregates

Share to Protein Domains

Share to Protein Stability

Share to Solubility

Share to Ultraviolet Rays

Source

Identifiers

PMID: 28528950
DOI: 10.1016/j.ijbiomac.2017.05.109

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

Effects of cataract-causing mutations W59C and W151C on βB2-crystallin structure, stability and folding.PMID 28528950Read ↗

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

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

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

Characterization of βB2-crystallin tryptophan mutants reveals two different folding states in solution.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 ↗

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

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

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

Cataract-linked mutation R188H promotes βB2-crystallin aggregation and fibrillization during acid denaturation.Semantic proximity Read ↗

Potential role of βB1 crystallin in cataract formation:a systematic review.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 ↗

Increasing susceptibility to oxidative stress by cataract-causing crystallin mutations.Semantic proximity Read ↗

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