| Truncation mutations of CRYGD gene in congenital cataracts cause protein aggregation by disrupting the structural stability of gammaD-crystallin. | Truncation mutations of CRYGD gene in congenital cataracts cause protein aggregation by disrupting the structural stability of γD-crystallin.
Lin N, Song H, Zhang Y, Chen F, Xu J, Wu W, Tian Q, Luo C, Yao K, Hu L, Chen X. | 10/2/2024 |
| Effect of Pressure on the Conformational Landscape of Human gammaD-Crystallin from Replica Exchange Molecular Dynamics Simulations. | Effect of Pressure on the Conformational Landscape of Human γD-Crystallin from Replica Exchange Molecular Dynamics Simulations.
Kacirani A, Uralcan B, Domingues TS, Haji-Akbari A. | 08/2/2024 |
| Cataract-causing mutations S78F and S78P of gammaD-crystallin decrease protein conformational stability and drive aggregation. | Cataract-causing mutations S78F and S78P of γD-crystallin decrease protein conformational stability and drive aggregation.
Lin N, Zhang Y, Song X, Xu J, Luo C, Tian Q, Yao K, Wu W, Chen X, Hu L. | 03/20/2024 |
| Congenital coralliform cataract is the predominant consequence of a recurrent mutation in the CRYGD gene. | Congenital coralliform cataract is the predominant consequence of a recurrent mutation in the CRYGD gene.
Wang KJ, Wang JX, Wang JD, Li M, Zhang JS, Mao YY, Wan XH., Free PMC Article | 07/30/2023 |
| Insights to Human gammaD-Crystallin Unfolding by NMR Spectroscopy and Molecular Dynamics Simulations. | Insights to Human γD-Crystallin Unfolding by NMR Spectroscopy and Molecular Dynamics Simulations.
Hsueh SS, Wang SS, Chen SH, Wang CL, Wu WJ, Lin TH., Free PMC Article | 03/19/2022 |
| Surface Exposed Free Cysteine Suppresses Crystallization of Human gammaD-Crystallin. | Surface Exposed Free Cysteine Suppresses Crystallization of Human γD-Crystallin.
Strofaldi A, Khan AR, McManus JJ. | 12/4/2021 |
| Assessing the Structures and Interactions of gammaD-Crystallin Deamidation Variants. | Assessing the Structures and Interactions of γD-Crystallin Deamidation Variants.
Guseman AJ, Whitley MJ, González JJ, Rathi N, Ambarian M, Gronenborn AM., Free PMC Article | 11/27/2021 |
| Increased hydrophobicity of CRYGD p.(Ala159ProfsTer9): Suspected cause of congenital cataracts in a large Chinese family. | Increased hydrophobicity of CRYGD p.(Ala159ProfsTer9): Suspected cause of congenital cataracts in a large Chinese family.
Lin M, Jin Y, Chen X, Sui Y, Li Y, Li H, Ni X, Zhao N, Lu Y, Jiang M., Free PMC Article | 06/26/2021 |
| Cataract-Associated New Mutants S175G/H181Q of betaBeta2-Crystallin and P24S/S31G of gammaD-Crystallin Are Involved in Protein Aggregation by Structural Changes. | Cataract-Associated New Mutants S175G/H181Q of βΒ2-Crystallin and P24S/S31G of γD-Crystallin Are Involved in Protein Aggregation by Structural Changes.
Song IK, Na S, Paek E, Lee KJ., Free PMC Article | 02/27/2021 |
| Temperature-Dependent Interactions Explain Normal and Inverted Solubility in a gammaD-Crystallin Mutant. | Temperature-Dependent Interactions Explain Normal and Inverted Solubility in a γD-Crystallin Mutant.
Khan AR, James S, Quinn MK, Altan I, Charbonneau P, McManus JJ., Free PMC Article | 09/19/2020 |
| Kinetic Stability of Long-Lived Human Lens gamma-Crystallins and Their Isolated Double Greek Key Domains. | Kinetic Stability of Long-Lived Human Lens γ-Crystallins and Their Isolated Double Greek Key Domains.
Mills-Henry IA, Thol SL, Kosinski-Collins MS, Serebryany E, King JA., Free PMC Article | 09/12/2020 |
| The W42R variant assumes a distinct conformation in solution that leaves the Greek key domains of the native fold largely unaltered but lacks the hydrophobic interdomain interface that is key to the stability of wild-type gammaD-crystallin. | 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. | 06/13/2020 |
| a previously unknown oxidoreductase activity in gammaD-crystallin (HgammaD) is found. This activity was assigned to a redox-active internal disulfide bond that is dynamically exchanged among HgammaD molecules. The W42Q variant acts as a disulfide sink, reducing oxidized WT and forming a distinct internal disulfide that kinetically traps the aggregation-prone intermediate. | 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., Free PMC Article | 04/13/2019 |
| At physiological pH, CRYGD forms aggregates that look amorphous and disordered by electron microscopy. Surprisingly, solid-state NMR reveals that these amorphous deposits have a high degree of structural homogeneity at the atomic level and that the aggregated protein retains a native-like conformation, with no evidence for large-scale misfolding. | Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.
Boatz JC, Whitley MJ, Li M, Gronenborn AM, van der Wel PCA., Free PMC Article | 12/22/2018 |
| A molecular dynamics approach to explore the structural characterization of cataract causing mutation R58H on human gammaD crystallin. | A molecular dynamics approach to explore the structural characterization of cataract causing mutation R58H on human γD crystallin.
Karunakaran R, Srikumar PS. | 12/22/2018 |
| This research compared the effects of various glycation modifiers on Hgammad-crystallin aggregation, by treating samples of Hgammad-crystallin with ribose, galactose, or methylglyoxal using several biophysical techniques | Effects of glycation on human γd-crystallin proteins by different glycation-inducing agents.
Li CT, How SC, Chen ME, Lo CH, Chun MC, Chang CK, Chen WA, Wu JW, Wang SS. | 12/22/2018 |
| Study reports the identification of Cys111 as the major residue responsible for disulfide formation in protein dimers as well as for Cu2+-induced aggregation of human gammaD-crystallin. | Reactive cysteine residues in the oxidative dimerization and Cu(2+) induced aggregation of human γD-crystallin: Implications for age-related cataract.
Ramkumar S, Fan X, Wang B, Yang S, Monnier VM., Free PMC Article | 12/22/2018 |
| Using the P23T mutant of gammaD-crystallin, a protein associated with congenital cataract, we have demonstrated that the equilibrium solubility boundary and solution behavior measured using phase diagrams of purified protein solutions is consistent with the assembly of the protein expressed in cell-free expression medium in artificial cells (without fluorescent labelling) and condensates formed in mammalian cells. | Protein self-assembly following in situ expression in artificial and mammalian cells.
Migas UM, Quinn MK, McManus JJ. | 03/17/2018 |
| we identified two heterozygous rare variants in genes that are involved in early cataract development; the novel c.809C>A; p.(Ser270Tyr) in MAF and the c.168C>G; p.(Tyr56 *) variant in CRYGD, previously reported as pathogenic | Segregation of a novel p.(Ser270Tyr) MAF mutation and p.(Tyr56∗) CRYGD variant in a family with dominantly inherited congenital cataracts.
Dudakova L, Stranecky V, Ulmanova O, Hlavova E, Trková M, Vincent AL, Liskova P. | 01/6/2018 |
| Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract. | Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract.
Serebryany E, Takata T, Erickson E, Schafheimer N, Wang Y, King JA., Free PMC Article | 06/10/2017 |
| the mechanism of aggregation of two gammaD-crystallin mutants, W42R and W42Q: the former a congenital cataract mutation | An Internal Disulfide Locks a Misfolded Aggregation-prone Intermediate in Cataract-linked Mutants of Human γD-Crystallin.
Serebryany E, Woodard JC, Adkar BV, Shabab M, King JA, Shakhnovich EI., Free PMC Article | 05/13/2017 |
| Mutational analysis of CRYGD identified a recurrent (p.P24T) mutation in two unrelated families with congenital coralliform cataracts and three novel (p.Q101X, p.E104fsX4 and p.E135X) mutations in three families with congenital nuclear cataracts. | Novel mutations in CRYGD are associated with congenital cataracts in Chinese families.
Yang G, Chen Z, Zhang W, Liu Z, Zhao J., Free PMC Article | 12/17/2016 |
| The nonsense mutation c.471G>A of the CRYGD gene probably underlies the congenital cataract in the pedigree | [A novel pathogenic mutation of CRYGD gene in a congenital cataract family].
Gao M, Huang S, Li J, Zou Y, Xu P, Kang R, Gao Y. | 09/24/2016 |
| Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human gammaD-Crystallin Protein. | Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human γD-Crystallin Protein.
Garcia-Manyes S, Giganti D, Badilla CL, Lezamiz A, Perales-Calvo J, Beedle AE, Fernández JM., Free PMC Article | 07/16/2016 |
| We have identified a novel mutation, c.451_452insGACT, in CRYGD, which is associated with nuclear cataract. This is the first insertion mutation of CRYGD found to cause autosomal dominant congenital cataract. | A Novel Insertion Variant of CRYGD Is Associated with Congenital Nuclear Cataract in a Chinese Family.
Zhuang X, Wang L, Song Z, Xiao W., Free PMC Article | 04/9/2016 |