anti-Crystallin, beta A1 (CRYBA1) Antikörper

Human Crystallin, beta A1 (CRYBA1) Interaktionspartner

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.

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]

3. association between a frameshift mutation in exon 6 of CRYBA1/A3 and congenital cataracts

4. Data indicate that alpha-crystallin B chain and beta-crystallin A3-cyrstallins dissociate to the monomers upon racemization of d-aspartic acids (Asp).

5. A novel splice site mutation in CRYBA1/A3 is associated with autosomal dominant nuclear cataracts in a Chinese family.

6. 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.

7. 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.

8. A G-->T splice site mutation of CRYBA1/A3 associated with autosomal dominant suture cataracts in a Chinese family.

9. The c.279-281delGAG mutation in CRYBA1 is responsible for the autosomal dominant congenital nuclear cataract disease in this Chinese family.

10. A serine-type protease activity of betaA3-crystalllin was responsible for its autodegradation.

11. This is the first report of a phenotype of progressive nuclear and cortical cataracts related to the CRYBA3/A1 mutation IVS3+1 G>A.

12. Mutations involved in congenital cataracts and deamidation in aged lenses commonly altered protein-protein interaction between human lens betaA3-crystallins.

13. This study is the first report relating a mutation of CRYBA1/A3 to posterior polar cataract.

14. A deletion mutation in the betaA1/A3 crystallin gene is associated with autosomal dominant congenital nuclear cataract

15. comprehensive description of the biophysical consequences of a mutant beta-crystallin protein that is associated with human inherited cataract.

16. The DeltaG91 mutation in CRYBA3/A1 is associated with an autosomal dominant congenital nuclear lactescent cataract

17. 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.

18. Delta91 mutation arise in a relatively mutation-prone sequence of the CRYBA1 gene.

19. This study confirmed the interactions between a low molecular weight peptide derived from betaA3/A1-crystallin found in aged and cataract lenses and alphaB-crystallin.

20. Deamidation destabilizes and triggers aggregation of crystallin beta A3.

Mouse (Murine) Crystallin, beta A1 (CRYBA1) Interaktionspartner

1. CRYbetaA3/A1-crystallin has a role in preventing nuclear cataract impaired lysosomal cargo clearance and calpain activation

2. Data suggest a mechanism by which betaA3/A1-crystallin regulates lysosomal function by modulating the activity of V-ATPase.

3. Data show that betaA3/A1-crystallin affects the signal transducer and activator of transcription 3 (STAT3) activation in optic nerve astrocytes.

4. loss of CRYBA1 causes lysosomal dysregulation leading to the impairment of both autophagy and phagocytosis

5. p53 can regulate lens differentiation by controlling expression of the differentiation genes coding for the lens crystallins.

6. The thermodynamic consequences of the loss of beta A3-crystallin terminal extensions by in vivo proteolytic processing could increase their tendency to associate and so promote the formation of higher order associates in the aging and cataractous lens.

Cow (Bovine) Crystallin, beta A1 (CRYBA1) Interaktionspartner

1. Results show that both betaB2- and betaA3-crystallin bind calcium with moderate affinity.