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

Structural and functional roles of deamidation of N146 and/or truncation of NH2- or COOH-termini in human αB-crystallin.

Molecular vision - 1 Jan 2011

Asomugha C O, Gupta R, Srivastava O P

Abstract excerpt

PURPOSE: The purpose of the study was to determine the relative effects of deamidation and/or truncation on the structural and functional properties of αB-crystallin. METHODS: Using wild-type (WT) αB-crystallin and the αB deamidated mutant (i.e., αB N146D), we generated NH(2)-terminal domain dele...

Read the complete abstract on PubMed

Topics

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

Share to alpha-Crystallin B Chain
Share to Asparagine
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Insulin

Share to Lens, Crystalline

Share to Molecular Chaperones

Share to Spectrometry, Fluorescence

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Source

Open in PubMed Open full text

Identifiers

PMID: 21976952
PMCID: PMC3185027

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-21976952-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and functional roles of deamidation of N146 and/or truncation of NH2- or COOH-termini in human αB-crystallin.PMID 21976952Read ↗

Structural and functional properties of NH(2)-terminal domain, core domain, and COOH-terminal extension of αA- and αB-crystallins.Semantic proximity Read ↗

Deamidation in human lens betaB2-crystallin destabilizes the dimer.Semantic proximity Read ↗

Truncation of motifs III and IV in human lens betaA3-crystallin destabilizes the structure.Semantic proximity Read ↗

Identification of the Most Impactful Asparagine Residues for γS-Crystallin Aggregation by Deamidation.Semantic proximity Read ↗

Conformational stability of the deamidated and mutated human βB2-crystallin.Semantic proximity Read ↗

Structural and Functional Consequences of Age-Related Isomerization in α-CrystallinsSemantic proximity Read ↗

Deamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin.Semantic proximity Read ↗

Decreasing the homodimer interaction: a common mechanism shared by the deltaG91 mutation and deamidation in betaA3-crystallin.Semantic proximity Read ↗

C-terminal lysine truncation increases thermostability and enhances chaperone-like function of porcine alphaB-crystallin.Semantic proximity Read ↗

Unveiling the structural and functional consequences of the p.D109G pathogenic mutation in human αB-Crystallin responsible for restrictive cardiomyopathy and skeletal myopathy.Semantic proximity Read ↗

UV-A-induced structural and functional changes in human lens deamidated alphaB-crystallin.Semantic proximity Read ↗

Deletion of Specific Conserved Motifs from the N-Terminal Domain of αB-Crystallin Results in the Activation of Chaperone Functions.Semantic proximity Read ↗

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