238 related articles for article (PubMed ID: 22394327)
1. Structural and biochemical characterization of the childhood cataract-associated R76S mutant of human γD-crystallin.
Ji F; Jung J; Gronenborn AM
Biochemistry; 2012 Mar; 51(12):2588-96. PubMed ID: 22394327
[TBL] [Abstract][Full Text] [Related]
2. Cataract-linked γD-crystallin mutants have weak affinity to lens chaperones α-crystallins.
Mishra S; Stein RA; McHaourab HS
FEBS Lett; 2012 Feb; 586(4):330-6. PubMed ID: 22289178
[TBL] [Abstract][Full Text] [Related]
3. A novel gammaD-crystallin mutation causes mild changes in protein properties but leads to congenital coralliform cataract.
Zhang LY; Gong B; Tong JP; Fan DS; Chiang SW; Lou D; Lam DS; Yam GH; Pang CP
Mol Vis; 2009 Aug; 15():1521-9. PubMed ID: 19668596
[TBL] [Abstract][Full Text] [Related]
4. Molecular Mechanism of Aggregation of the Cataract-Related γD-Crystallin W42R Variant from Multiscale Atomistic Simulations.
Wong EK; Prytkova V; Freites JA; Butts CT; Tobias DJ
Biochemistry; 2019 Sep; 58(35):3691-3699. PubMed ID: 31393108
[TBL] [Abstract][Full Text] [Related]
5. Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin.
Moreau KL; King J
J Biol Chem; 2009 Nov; 284(48):33285-95. PubMed ID: 19758984
[TBL] [Abstract][Full Text] [Related]
6. Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.
Moreau KL; King JA
PLoS One; 2012; 7(5):e37256. PubMed ID: 22655036
[TBL] [Abstract][Full Text] [Related]
7. Wild-type human γD-crystallin promotes aggregation of its oxidation-mimicking, misfolding-prone W42Q mutant.
Serebryany E; King JA
J Biol Chem; 2015 May; 290(18):11491-503. PubMed ID: 25787081
[TBL] [Abstract][Full Text] [Related]
8. 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]
9. Increased hydrophobicity and decreased backbone flexibility explain the lower solubility of a cataract-linked mutant of γD-crystallin.
Banerjee PR; Puttamadappa SS; Pande A; Shekhtman A; Pande J
J Mol Biol; 2011 Sep; 412(4):647-59. PubMed ID: 21827768
[TBL] [Abstract][Full Text] [Related]
10. GammaD-crystallin associated protein aggregation and lens fiber cell denucleation.
Wang K; Cheng C; Li L; Liu H; Huang Q; Xia CH; Yao K; Sun P; Horwitz J; Gong X
Invest Ophthalmol Vis Sci; 2007 Aug; 48(8):3719-28. PubMed ID: 17652744
[TBL] [Abstract][Full Text] [Related]
11. 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]
12. The P23T cataract mutation causes loss of solubility of folded gammaD-crystallin.
Evans P; Wyatt K; Wistow GJ; Bateman OA; Wallace BA; Slingsby C
J Mol Biol; 2004 Oct; 343(2):435-44. PubMed ID: 15451671
[TBL] [Abstract][Full Text] [Related]
13. ATP differentially antagonizes the crowding-induced destabilization of human γS-crystallin and its four cataract-causing mutants.
He Y; Kang J; Song J
Biochem Biophys Res Commun; 2020 Dec; 533(4):913-918. PubMed ID: 33004175
[TBL] [Abstract][Full Text] [Related]
14. The mutation V42M distorts the compact packing of the human gamma-S-crystallin molecule, resulting in congenital cataract.
Vendra VP; Chandani S; Balasubramanian D
PLoS One; 2012; 7(12):e51401. PubMed ID: 23284690
[TBL] [Abstract][Full Text] [Related]
15. A novel F30S mutation in γS-crystallin causes autosomal dominant congenital nuclear cataract by increasing susceptibility to stresses.
Wang KJ; Liao XY; Lin K; Xi YB; Wang S; Wan XH; Yan YB
Int J Biol Macromol; 2021 Mar; 172():475-482. PubMed ID: 33454329
[TBL] [Abstract][Full Text] [Related]
16. Contributions of aromatic pairs to the folding and stability of long-lived human γD-crystallin.
Kong F; King J
Protein Sci; 2011 Mar; 20(3):513-28. PubMed ID: 21432932
[TBL] [Abstract][Full Text] [Related]
17. Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin chaperone.
Acosta-Sampson L; King J
J Mol Biol; 2010 Aug; 401(1):134-52. PubMed ID: 20621668
[TBL] [Abstract][Full Text] [Related]
18. Assessing the Structures and Interactions of γD-Crystallin Deamidation Variants.
Guseman AJ; Whitley MJ; González JJ; Rathi N; Ambarian M; Gronenborn AM
Structure; 2021 Mar; 29(3):284-291.e3. PubMed ID: 33264606
[TBL] [Abstract][Full Text] [Related]
19. Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.
DiMauro MA; Nandi SK; Raghavan CT; Kar RK; Wang B; Bhunia A; Nagaraj RH; Biswas A
Biochemistry; 2014 Nov; 53(46):7269-82. PubMed ID: 25393041
[TBL] [Abstract][Full Text] [Related]
20. The human W42R γD-crystallin mutant structure provides a link between congenital and age-related cataracts.
Ji F; Jung J; Koharudin LM; Gronenborn AM
J Biol Chem; 2013 Jan; 288(1):99-109. PubMed ID: 23124202
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
