CRYGD Antibody

1. 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. PMID: 28474685
2. A molecular dynamics approach to explore the structural characterization of cataract causing mutation R58H on human gammaD crystallin. PMID: 29532225
3. 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 PMID: 29949747
4. 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. PMID: 30251679
5. 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. PMID: 28401204
6. 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 PMID: 28849415
7. Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract. PMID: 26991007
8. the mechanism of aggregation of two gammaD-crystallin mutants, W42R and W42Q: the former a congenital cataract mutation PMID: 27417136
9. 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. PMID: 26732753
10. The nonsense mutation c.471G>A of the CRYGD gene probably underlies the congenital cataract in the pedigree PMID: 27455011
11. Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human gammaD-Crystallin Protein. PMID: 26703476
12. 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. PMID: 26147294
13. We have used trio-based exome sequencing to uncover a recurrent missense mutation in CRYGD and two novel missense mutations in GJA8 associated with autosomal dominant cataract in three nuclear families. PMID: 25403472
14. Created are three double mutants of human gamma D-crystallin for which the phase diagrams for singly mutated proteins can be used to predict the behavior of the double mutants. PMID: 25613833
15. oxidation-mimicking W42Q mutant of gammad-crystallin formed non-native polymers starting from a native-like state under physiological conditions PMID: 25787081
16. Shared epitopes and smoking were associated with the production of anti-CCP antibodies and rheumatoid factors of IgM and IgA isotypes, which again were associated with erosive disease at presentation only in smokers. PMID: 25205362
17. The presence of anti-CCP antibodies was a reliable serologic marker in rheumatoid arthritis diagnosis and was associated with cigarette smoking. PMID: 24366391
18. These results indicated that the single lysine residue at the second position (K2) is acetylated at an early age and that the amount of K2-acetylated gamma D-crystallin increased with age. PMID: 25393041
19. Results show that thermal denaturation of gammaD-crystallin results in sheet-like aggregates that contain cross-linked oligomers of the protein. PMID: 24415662
20. This study identified a novel congenital nuclear and posterior polar cataract phenotype caused by the recurrent mutation p. R140X in CRYGD. PMID: 24465161
21. Presentation and discussion of the first crystal structure of the P23T mutant at 2.5 A resolution. PMID: 23670788
22. Outcome from protein formulation characterization supports the hypothesis that the gammaD-crystallin it is able to recover and improve the mechanical properties of chemical damaged hair. PMID: 23651449
23. study establishes that UV-B irradiation of gammaD-Crystallin leads to structurally specific modifications and precipitation via two mechanisms: amorphous aggregates and amyloid fibers PMID: 23957864
24. The missense P24T mutation in CRYGD was responsible for the coralliform cataract afflicting a four-generation Chinese family. PMID: 24103489
25. Mass spectrometry identifies residues 80-163 as the amyloid core, which spans most of the C-terminal domain, the linker, and a small portion of the N-terminal domain. PMID: 23082813
26. human W42R gammaD-crystallin mutant structure provides a link between congenital and age-related cataracts PMID: 23124202
27. A missense mutation in CRYGD linked with autosomal dominant congenital cataract of aculeiform type. PMID: 22669729
28. study of effects of G61C mutation on gammaD-crystallin structure, stability and aggregation; results suggest the decrease in protein stability followed by aggregation-prone property may be the major cause in hereditary cataract induced by the G61C mutation PMID: 21655238
29. The mutations in CRYGD were shown to cause changes in protein surface polarity, hydrophobicity, and spatial structure, contributing to protein deposition and cataract formation. PMID: 18041179
30. neither structural nor stability changes in the protein are responsible for the R76S gammaD-crystallin variant's association with cataract PMID: 22394327
31. Upon acid-induced amyloid fibril formation, the C-terminal domain forms amyloid beta-sheets, the N-terminal domain becomes extremely disordered but lies near to the beta-sheets. Fibril nucleation & extension occur only in the C-terminal domain. PMID: 22328156
32. The heterozygous 109C to A CRYGD missense mutation is associated with a distinct crystalline cataract in two US Caucasian pedigrees. PMID: 22219628
33. mutants and possibly age-damaged gammaD-crystallin can escape quality control by lens chaperones rationalizing the observation that they nucleate protein aggregation and lead to cataract PMID: 22289178
34. A novel substitution has been found in CRYGD in a Brazilian family with congenital cataract in which there is no segregation with the disease, indicating that it is probably not a disease-causing mutation. PMID: 21866214
35. CRYGD gene mutation co-segregated with all autosomal dominant congenital nuclear cataract affected individuals and was not observed in either unaffected family members or in 200 normal unrelated individuals. PMID: 21031598
36. Identification of the residues in the P23T mutant that give rise to novel hydrophobic surfaces, and regions of the protein backbone where fluctuations in different timescales are restricted, which explains how lens opacity could result from this mutation. PMID: 21827768
37. A novel mutation in gammaD-crystallin associated with autosomal dominant congenital cataract in a Chinese family. PMID: 21527994
38. P24T mutation of gammaD-crystallin (CRYGD) was responsible for two Chinese pedigrees with congenital coralliform cataracts. CRYGD and coralliform cataracts are highly related, and P24T may be a hot-point mutation for this disorder. PMID: 21552497
39. Data show that only substitutions of the second Greek key pair of each crystallin domain slowed refolding, and suggest that the second Greek keys may provide nucleation sites during the folding of the double-Greek-key crystallin domains. PMID: 21432932
40. S130P point mutations of gammaD crystallin was the most resistant to aggregation, indicating a decrease of its intrinsic aggregation propensity. PMID: 21184609
41. The conformational features and aggregation properties of the mutant protein E107A human gammaD-crystallin (HGDC), associated with congenital nuclear cataract, were analyzed. PMID: 21197114
42. Family having anterior polar coronary cataract that co-segregates with novel allele R77S of CRYGD in all affected members. PMID: 20508808
43. This work thus provides direct evidence of the dominant role played by net hydrophobic and anisotropic protein-protein interactions in the aggregation of the P23T cataract-associated gammaD-crystallin. PMID: 20553008
44. Findings indicate that Glu135 and Arg142 of gammaD-crystallin are crucial for stabilizing its hydrophobic domain interface in native conformation, and disruption of charges on the gammaD-crystallin surface may lead to unfolding and subsequent aggregat'n. PMID: 19937657
45. Data show that during thermal denaturation, the mutant proteins exhibited lowered thermal stability compared with WT. PMID: 19758984
46. This the first report of a mutation in the Gamma-D crystallin gene (CRYGD) resulting in autosomal dominant congenital cerulean cataracts. PMID: 12676897
47. This study has identified an eighth type of cataract morphology associated with CRYGD and suggests that a CRYGD mutation may underlie the historically important "coralliform" cataract first reported in 1895. PMID: 15041957
48. It appearS to be caused by a missense mutation in the CRYGD gene, further supporting the notion that alterations to CRYG play an important factor in human cataract formation. PMID: 15064679
49. These results suggest that insolubility, rather than loss of stability, is the primary basis for human gammaD-crystallin P23T mutation-derived congenital cataracts. PMID: 15451671
50. The cataract-causing mutation proline23 to threonine does not exhibit any significant structural change relative to the native protein. However, in marked contrast to the native protein, the mutant shows a dramatically lowered solubility. PMID: 15709761

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HGNC: 2411

OMIM: 115700

KEGG: hsa:1421

STRING: 9606.ENSP00000264376

UniGene: Hs.546247