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

Truncation mutations of CRYGD gene in congenital cataracts cause protein aggregation by disrupting the structural stability of γD-crystallin.

International journal of biological macromolecules - 1 Oct 2024

Lin Ningqin, Song Hang, Zhang Ying, Chen Fanrui, Xu Jingjie, Wu Wei, Tian Qing, Luo Chenqi, Yao Ke, Hu Lidan, Chen Xiangjun

Abstract excerpt

Congenital cataracts, a prevalent cause of blindness in children, are associated with protein aggregation. γD-crystallin, essential for sustaining lens transparency, exists as a monomer and exhibits excellent structural stability. In our cohort, we identified a nonsense mutation (c.451_452insGACT, p.Y151X) in the CRYGD gene. To explore the effect of truncation mutations on the structure of γD-crystallin, we...

Read the complete abstract on PubMed

Topics

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

Share to Cataract
Share to gamma-Crystallins

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

Share to Molecular Dynamics Simulation

Share to Protein Aggregates

Share to Protein Aggregation, Pathological

Share to Protein Folding

Share to Protein Stability

Share to Solubility

Source

Identifiers

PMID: 39084439
DOI: 10.1016/j.ijbiomac.2024.134292

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

Truncation mutations of CRYGD gene in congenital cataracts cause protein aggregation by disrupting the structural stability of γD-crystallin.PMID 39084439Read ↗

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

The Y46D Mutation Destabilizes Dense Packing of the Second Greek Key Pair of Human γC-Crystallin Causing Congenital Nuclear Cataracts.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 ↗

Structural integrity of the Greek key motif in βγ-crystallins is vital for central eye lens transparency.Semantic proximity Read ↗

The importance of the fourth Greek key motif of human γD-crystallin in maintaining lens transparency-the tale told by the tail.Semantic proximity Read ↗

Human γS-Crystallin Mutation F10_Y11delinsLN in the First Greek Key Pair Destabilizes and Impairs Tight Packing Causing Cortical Lamellar Cataract.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 ↗

Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin.Semantic proximity Read ↗

βB2 W151R mutant is prone to degradation, aggregation and exposes the hydrophobic side chains in the fourth Greek Key motif.Semantic proximity Read ↗

βA4-Crystallin Mutations Disrupt Structural Stability and Crystallin Interactions in Congenital Cataract Pathogenesis.Semantic proximity Read ↗

The importance of the last strand at the C-terminus in βB2-crystallin stability and assembly.Semantic proximity Read ↗

Aggregation of γ-crystallins associated with human cataracts via domain swapping at the C-terminal β-strandsSemantic proximity Read ↗

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