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

NMR study of the cataract-linked P23T mutant of human gammaD-crystallin shows minor changes in hydrophobic patches that reflect its retrograde solubility.

Biochemical and biophysical research communications - 24 Apr 2009

Pande Ajay, Zhang Jianchao, Banerjee Priya R, Puttamadappa Shadakshara S, Shekhtman Alexander, Pande Jayanti

Abstract excerpt

The Pro23 to Thr (P23T) mutation in human gammaD-crystallin (HGD) shows several cataract phenotypes. We found earlier [A. Pande, O. Annunziata, N. Asherie, O. Ogun, G.B. Benedek, J. Pande, Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human gamma D-crystallin, Biochemistry 44 (2005) 2491-2500] that the mutation dramatically lowers the solubility of P23T but the...

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 gamma-Crystallins

Share to Hydrophobic and Hydrophilic Interactions

Share to Magnetic Resonance Spectroscopy

Share to Proline

Share to Solubility

Share to Threonine

Source

Open in PubMed Open full text

Identifiers

PMID: 19275895
DOI: 10.1016/j.bbrc.2009.03.007
PMCID: PMC2707783

Genes

HGD

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

NMR study of the cataract-linked P23T mutant of human gammaD-crystallin shows minor changes in hydrophobic patches that reflect its retrograde solubility.PMID 19275895Read ↗

The structure of the cataract-causing P23T mutant of human gammaD-crystallin exhibits distinctive local conformational and dynamic changes.Semantic proximity Read ↗

Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.Semantic proximity Read ↗

Crystal structure of the cataract-causing P23T γD-crystallin mutant.Semantic proximity Read ↗

The P23T cataract mutation causes loss of solubility of folded gammaD-crystallin.Semantic proximity Read ↗

¹H, ¹³C, and ¹⁵N assignments of wild-type human γS-crystallin and its cataract-related variant γS-G18V.Semantic proximity Read ↗

Cataract-prone variants of γD-crystallin populate a conformation with a partially unfolded N-terminal domain under native conditionsSemantic 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 ↗

High-resolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract.Semantic proximity Read ↗

ATP differentially antagonizes the crowding-induced destabilization of human γS-crystallin and its four cataract-causing mutants.Semantic proximity Read ↗

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

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

Polymorphic protein phase transitions driven by surface anisotropy.Semantic proximity Read ↗

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