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

AlphaB-crystallin modified by methylglyoxal prevents fibrillization of α-synuclein A53T.

Archives of biochemistry and biophysics - 1 Jun 2026

Barinova K V, Medvedeva M V, Serebryakova M V, Kurochkina L P, Muronetz V I, Schmalhausen E V

Abstract excerpt

AlphaB-crystallin is a small heat shock protein that is found in the eye lens, retina, heart, brain, skin, and skeletal muscle. Mutations of αB-crystallin lead to the development of cataracts, human muscle and heart disorders. The role of non-enzymatic glycation of αB-crystallin in the development of pathological processes has been little studied. The aim of this study was to evaluate the influence of enhanced...

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 alpha-Synuclein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Amyloid

Share to Mutation

Share to Protein Aggregates

Share to Pyruvaldehyde

Share to Recombinant Proteins

Source

Identifiers

PMID: 41831819
DOI: 10.1016/j.abb.2026.110791

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

AlphaB-crystallin modified by methylglyoxal prevents fibrillization of α-synuclein A53T.PMID 41831819Read ↗

Hydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimics.Semantic proximity Read ↗

Protein Aggregation and Cataract: Role of Age-Related Modifications and Mutations in α-Crystallins.Semantic proximity Read ↗

Trimethylamine N-oxide alleviates the severe aggregation and ER stress caused by G98R alphaA-crystallin.Semantic proximity Read ↗

Regulation of αA- and αB-crystallins via phosphorylation in cellular homeostasis.Semantic proximity Read ↗

Molecular mechanisms of α-crystallinopathy and its therapeutic strategy.Semantic proximity Read ↗

Myopathy-associated G154S mutation causes important changes in the conformational stability, amyloidogenic properties, and chaperone-like activity of human αB-crystallin.Semantic proximity Read ↗

Protective role of antioxidant compounds against peroxynitrite-mediated modification of R54C mutant αA-crystallin.Semantic proximity Read ↗

The effect of small molecules in modulating the chaperone activity of alphaB-crystallin against ordered and disordered protein aggregation.Semantic proximity Read ↗

Emerging Role for αB-Crystallin as a Therapeutic Agent: Pros and ConsSemantic proximity Read ↗

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

Genetic Code Expansion and Enzymatic Modifications as Accessible Methods for Studying Site-Specific Post-Translational Modifications of Alpha-Synuclein and TauSemantic proximity Read ↗

Glycated alpha-synuclein assemblies cause distinct Parkinson’s disease pathogenesis in miceSemantic proximity Read ↗

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