CRYGS Antibody

1. aberrant modifications in gammaS-crystallin structure might contribute to the lower stability and higher aggregatory potency of the mutated protein, which subsequently resulted in cataracts in the patients PMID: 29857103
2. The Tyr67Asn substitution was predicted to decrease the local hydrophobicity and affect the three-dimensional structure of gammaS-crystallin, and resulted in a portion of mutant protein translocation from the cytoplasm to cell membrane. This observations expand the mutation spectrum of CRYGS and provide further evidence for the genetic basis and molecular mechanism of congenital cataract. PMID: 29964096
3. Cataract-related G18V point mutation affects CRYGS stability and hydration. PMID: 27052457
4. novel mutation (G57W) in CRYGS in this Chinese family is associated with autosomal dominant pulverulent cataract. PMID: 24328668
5. The data suggest that enhanced attractive protein-protein interactions, arising from the deamidation of HGS, promote protein aggregation, thereby leading to increased light scattering and opacity over time. PMID: 26158710
6. The effects of the V41M mutation on the structural changes of gamma S-crystallin were studied. PMID: 24287181
7. The cataract-associated mutant D26G of human gammaS-crystallin is remarkably close to the wild type molecule in structural features, with only a microenvironmental change in the packing around the mutation site. PMID: 23761725
8. replacement of valine in position 42 by the longer and bulkier methionine in human gammaS-crystallin perturbs the compact beta-sheet core packing topology in the N-terminal domain of the molecule PMID: 23284690
9. age-dependent cleavage of gammaS-crystallin generates a peptide that binds to cell membranes PMID: 22995907
10. The degree of deamidation for Gln92 and Gln170 was found to increase from birth to teen-age years and then to remain constant for four decades. PMID: 22593035
11. Molecular dynamics (MD) simulations, circular dichroism (CD), and dynamic light scattering (DLS) measurements were used to investigate the aggregation propensity of the eye-lens protein gammaS-crystallin. PMID: 21244846
12. Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin. PMID: 20621668
13. Deamidation in cataractous lenses is influenced by surface exposure. PMID: 12093281
14. A lens gamma S-crystallin has been identified with an in vivo modification, S-methylation of cysteine residues, that may block intermolecular disulfide bondng and serve as a form of protection against cataract. PMID: 12475213
15. when glutathione becomes bound to gammaS-crystallin, it causes it to bind in turn to the beta-crystallin polypeptides to form a dimer PMID: 14763903
16. report a novel missense mutation, p.V42M, in CRYGS associated with bilateral congenital cataract in a family of Indian origin PMID: 19262743
17. Fast charge transfer quenching is an evolved property of the gamma S-crystallin fold, probably protecting it from ultraviolet-induced photodamage. PMID: 19358562
18. Results confirm the high stability of wild-type HgammaS-crystallin and demonstrates that the G18V mutation destabilizes the protein toward heat and GuHCl-induced unfolding. PMID: 19558189

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HGNC: 2417

OMIM: 116100

KEGG: hsa:1427

STRING: 9606.ENSP00000312099

UniGene: Hs.376209