234 related articles for article (PubMed ID: 30552875)
1. The Structure and Stability of the Disulfide-Linked γS-Crystallin Dimer Provide Insight into Oxidation Products Associated with Lens Cataract Formation.
Thorn DC; Grosas AB; Mabbitt PD; Ray NJ; Jackson CJ; Carver JA
J Mol Biol; 2019 Feb; 431(3):483-497. PubMed ID: 30552875
[TBL] [Abstract][Full Text] [Related]
2. Deamidation of the human eye lens protein γS-crystallin accelerates oxidative aging.
Norton-Baker B; Mehrabi P; Kwok AO; Roskamp KW; Rocha MA; Sprague-Piercy MA; von Stetten D; Miller RJD; Martin RW
Structure; 2022 May; 30(5):763-776.e4. PubMed ID: 35338852
[TBL] [Abstract][Full Text] [Related]
3. The cataract-related S39C variant increases γS-crystallin sensitivity to environmental stress by destroying the intermolecular disulfide cross-links.
Yang X; Xu J; Fu C; Jia Z; Yao K; Chen X
Biochem Biophys Res Commun; 2020 May; 526(2):459-465. PubMed ID: 32234236
[TBL] [Abstract][Full Text] [Related]
4. Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein.
Sprague-Piercy MA; Wong E; Roskamp KW; Fakhoury JN; Freites JA; Tobias DJ; Martin RW
Biochim Biophys Acta Gen Subj; 2020 Mar; 1864(3):129502. PubMed ID: 31812542
[TBL] [Abstract][Full Text] [Related]
5. Reactive cysteine residues in the oxidative dimerization and Cu
Ramkumar S; Fan X; Wang B; Yang S; Monnier VM
Biochim Biophys Acta Mol Basis Dis; 2018 Nov; 1864(11):3595-3604. PubMed ID: 30251679
[TBL] [Abstract][Full Text] [Related]
6. The identification of a reaction site of glutathione mixed-disulphide formation on gammaS-crystallin in human lens.
Craghill J; Cronshaw AD; Harding JJ
Biochem J; 2004 May; 379(Pt 3):595-600. PubMed ID: 14763903
[TBL] [Abstract][Full Text] [Related]
7. Site specific oxidation of amino acid residues in rat lens γ-crystallin induced by low-dose γ-irradiation.
Kim I; Saito T; Fujii N; Kanamoto T; Chatake T; Fujii N
Biochem Biophys Res Commun; 2015 Oct; 466(4):622-8. PubMed ID: 26385181
[TBL] [Abstract][Full Text] [Related]
8. Cumulative deamidations of the major lens protein γS-crystallin increase its aggregation during unfolding and oxidation.
Vetter CJ; Thorn DC; Wheeler SG; Mundorff CC; Halverson KA; Wales TE; Shinde UP; Engen JR; David LL; Carver JA; Lampi KJ
Protein Sci; 2020 Sep; 29(9):1945-1963. PubMed ID: 32697405
[TBL] [Abstract][Full Text] [Related]
9. Cataract-causing G18V eliminates the antagonization by ATP against the crowding-induced destabilization of human γS-crystallin.
He Y; Kang J; Song J
Biochem Biophys Res Commun; 2020 Sep; 530(3):554-560. PubMed ID: 32753316
[TBL] [Abstract][Full Text] [Related]
10. Human γS-Crystallin-Copper Binding Helps Buffer against Aggregation Caused by Oxidative Damage.
Roskamp KW; Azim S; Kassier G; Norton-Baker B; Sprague-Piercy MA; Miller RJD; Martin RW
Biochemistry; 2020 Jun; 59(25):2371-2385. PubMed ID: 32510933
[TBL] [Abstract][Full Text] [Related]
11. Deamidation of N76 in human γS-crystallin promotes dimer formation.
Ray NJ; Hall D; Carver JA
Biochim Biophys Acta; 2016 Jan; 1860(1 Pt B):315-24. PubMed ID: 26318015
[TBL] [Abstract][Full Text] [Related]
12. Evidence of Highly Conserved β-Crystallin Disulfidome that Can be Mimicked by In Vitro Oxidation in Age-related Human Cataract and Glutathione Depleted Mouse Lens.
Fan X; Zhou S; Wang B; Hom G; Guo M; Li B; Yang J; Vaysburg D; Monnier VM
Mol Cell Proteomics; 2015 Dec; 14(12):3211-23. PubMed ID: 26453637
[TBL] [Abstract][Full Text] [Related]
13. Dynamic disulfide exchange in a crystallin protein in the human eye lens promotes cataract-associated aggregation.
Serebryany E; Yu S; Trauger SA; Budnik B; Shakhnovich EI
J Biol Chem; 2018 Nov; 293(46):17997-18009. PubMed ID: 30242128
[TBL] [Abstract][Full Text] [Related]
14. Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin.
Kingsley CN; Brubaker WD; Markovic S; Diehl A; Brindley AJ; Oschkinat H; Martin RW
Structure; 2013 Dec; 21(12):2221-7. PubMed ID: 24183572
[TBL] [Abstract][Full Text] [Related]
15. ATP antagonizes the crowding-induced destabilization of the human eye-lens protein γS-crystallin.
He Y; Kang J; Song J
Biochem Biophys Res Commun; 2020 Jun; 526(4):1112-1117. PubMed ID: 32307080
[TBL] [Abstract][Full Text] [Related]
16. Altered Protein Dynamics and Increased Aggregation of Human γS-Crystallin Due to Cataract-Associated Deamidations.
Forsythe HM; Vetter CJ; Jara KA; Reardon PN; David LL; Barbar EJ; Lampi KJ
Biochemistry; 2019 Oct; 58(40):4112-4124. PubMed ID: 31490062
[TBL] [Abstract][Full Text] [Related]
17. γ-Crystallin redox-detox in the lens.
Quinlan RA; Hogg PJ
J Biol Chem; 2018 Nov; 293(46):18010-18011. PubMed ID: 30446601
[TBL] [Abstract][Full Text] [Related]
18. The G18V CRYGS mutation associated with human cataracts increases gammaS-crystallin sensitivity to thermal and chemical stress.
Ma Z; Piszczek G; Wingfield PT; Sergeev YV; Hejtmancik JF
Biochemistry; 2009 Aug; 48(30):7334-41. PubMed ID: 19558189
[TBL] [Abstract][Full Text] [Related]
19. EGCG prevents tryptophan oxidation of cataractous ocular lens human γ-crystallin in presence of H2O2.
Chaudhury S; Ghosh I; Saha G; Dasgupta S
Int J Biol Macromol; 2015; 77():287-92. PubMed ID: 25841365
[TBL] [Abstract][Full Text] [Related]
20. Structural studies on the individual domains of human γS-crystallin and its G57W mutant unfolds mechanistic insights into childhood cataracts.
Bari KJ; Sharma S; Chary KVR
Biochem Biophys Res Commun; 2019 Sep; 517(3):499-506. PubMed ID: 31371024
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]