Recombinant Human Beta-crystallin A3 (CRYBA1)

1. We identified a de novo in-frame 3-bp deletion in the proband with an autosomal dominant congenital cataract, but not in her parents, in an Iranian family. This mutation has occurred de novo on a paternal gamete during spermatogenesis. The in-silico results predicted the interaction of CRYBA1 protein with the other CRY as well as proteins responsible for eye cell signaling. PMID: 28120589
2. The findings suggest that impaired endolysosomal signaling in ocular astrocytes can cause PFV disease, by adversely affecting the vascular remodeling processes essential to ocular development, including regression of the fetal vasculature. [review] PMID: 26022148
3. association between a frameshift mutation in exon 6 of CRYBA1/A3 and congenital cataracts PMID: 24926697
4. A novel splice site mutation in CRYBA1/A3 is associated with autosomal dominant nuclear cataracts in a Chinese family. PMID: 22665976
5. A splice site mutation (c.215+1G>A) at the first base of intron 3 of the crystallin beta A3/A1 (CRYBA3/A1) gene has been identified in Chinese congenital polymorphic cataract patients. PMID: 22919269
6. ThebetaA3-crystallin and betaB1-crystallin homomers and the betaA3/betaB1-crystallin heteromer all undergo similar five-state folding pathways which include one dimeric and two monomeric intermediates. PMID: 22032798
7. A G-->T splice site mutation of CRYBA1/A3 associated with autosomal dominant suture cataracts in a Chinese family. PMID: 21850182
8. The c.279-281delGAG mutation in CRYBA1 is responsible for the autosomal dominant congenital nuclear cataract disease in this Chinese family. PMID: 21686330
9. A serine-type protease activity of betaA3-crystalllin was responsible for its autodegradation. PMID: 21139689
10. This is the first report of a phenotype of progressive nuclear and cortical cataracts related to the CRYBA3/A1 mutation IVS3+1 G>A. PMID: 21139983
11. Mutations involved in congenital cataracts and deamidation in aged lenses commonly altered protein-protein interaction between human lens betaA3-crystallins. PMID: 20300566
12. This study is the first report relating a mutation of CRYBA1/A3 to posterior polar cataract. PMID: 20142846
13. A deletion mutation in the betaA1/A3 crystallin gene is associated with autosomal dominant congenital nuclear cataract PMID: 14598164
14. comprehensive description of the biophysical consequences of a mutant beta-crystallin protein that is associated with human inherited cataract. PMID: 15016766
15. The DeltaG91 mutation in CRYBA3/A1 is associated with an autosomal dominant congenital nuclear lactescent cataract PMID: 15111599
16. The glutamine residues at the Q180 and the Q85 were substituted with glutamic acid residues by site-directed mutagenesis. These structural changes led to decreased stability during unfolding in urea and increased precipitation during heat denaturation. PMID: 17616172
17. Delta91 mutation arise in a relatively mutation-prone sequence of the CRYBA1 gene. PMID: 17653060
18. Deamidation destabilizes and triggers aggregation of crystallin beta A3. PMID: 18567786
19. mixed betaB1- and betaA3-crystallins associate predominantly into heterotetramers in equilibrium with heterodimers PMID: 18823128
20. deamidation decreased formation of hetero-oligomers between beta-crystallin subunits; excess accumulation of deamidated beta-crystallins in vivo may disrupt normal protein-protein interactions and diminish the stabilizing effects between them PMID: 19190732
21. Results suggest that the N-terminal arm of betaB1-crystallin interacts with betaA3-crystallin during heterooligomerization, and the solubility of betaB1-crystallin and the heterooligomer are dependent on the intact C-terminal domain of betaB1-crystallin. PMID: 19548648

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HGNC: 2394

OMIM: 123610

KEGG: hsa:1411

STRING: 9606.ENSP00000225387

UniGene: Hs.46275