Source: ALL
Variant Gene Risk Allele Score vda Association Type Original DB Sentence supporting the association PMID PMID Year
dbSNP: rs1057518802
rs1057518802
SLC19A1 ; COL18A1
T 0.700 GeneticVariation CLINVAR

dbSNP: rs1064796765
rs1064796765
DYNC1H1
A 0.700 GeneticVariation CLINVAR

dbSNP: rs1339616347
rs1339616347
WRN
T 0.700 GeneticVariation CLINVAR

dbSNP: rs1423415130
rs1423415130
XYLT2
A 0.700 GeneticVariation CLINVAR

dbSNP: rs1554781700
rs1554781700
COL5A1
T 0.700 GeneticVariation CLINVAR

dbSNP: rs765919785
rs765919785
COL18A1 ; MIR6815
G 0.700 GeneticVariation CLINVAR

dbSNP: rs1463326176
rs1463326176
CRYGD ; LOC100507443
0.060 GeneticVariation BEFREE Crystal structure of the cataract-causing P23T γD-crystallin mutant. 23670788

2013
dbSNP: rs1463326176
rs1463326176
CRYGD ; LOC100507443
0.060 GeneticVariation BEFREE Benedek, J. Pande, Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human gamma D-crystallin, Biochemistry 44 (2005) 2491-2500] that the mutation dramatically lowers the solubility of P23T but the overall protein fold is maintained. 19275895

2009
dbSNP: rs1463326176
rs1463326176
CRYGD ; LOC100507443
0.060 GeneticVariation BEFREE The present study describes identification of p.Pro23Thr mutation in CRYGD for aculeiform type cataract in an ADCC family of Indian origin. 22669729

2012
dbSNP: rs1463326176
rs1463326176
CRYGD ; LOC100507443
0.060 GeneticVariation BEFREE Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human gamma D-crystallin. 15709761

2005
dbSNP: rs1463326176
rs1463326176
CRYGD ; LOC100507443
0.060 GeneticVariation BEFREE This contact, at the P23T substitution site, relates to a genetic cataract and reveals at a molecular level the origin of the lowered and retrograde solubility of the protein. 31422822

2019
dbSNP: rs1463326176
rs1463326176
CRYGD ; LOC100507443
0.060 GeneticVariation BEFREE 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. 26732753

2016
dbSNP: rs28931605
rs28931605
CRYGD ; LOC100507443
0.060 GeneticVariation BEFREE 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. 26732753

2016
dbSNP: rs28931605
rs28931605
CRYGD ; LOC100507443
0.060 GeneticVariation BEFREE This contact, at the P23T substitution site, relates to a genetic cataract and reveals at a molecular level the origin of the lowered and retrograde solubility of the protein. 31422822

2019
dbSNP: rs28931605
rs28931605
CRYGD ; LOC100507443
0.060 GeneticVariation BEFREE The present study describes identification of p.Pro23Thr mutation in CRYGD for aculeiform type cataract in an ADCC family of Indian origin. 22669729

2012
dbSNP: rs28931605
rs28931605
CRYGD ; LOC100507443
0.060 GeneticVariation BEFREE Crystal structure of the cataract-causing P23T γD-crystallin mutant. 23670788

2013
dbSNP: rs28931605
rs28931605
CRYGD ; LOC100507443
0.060 GeneticVariation BEFREE Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human gamma D-crystallin. 15709761

2005
dbSNP: rs28931605
rs28931605
CRYGD ; LOC100507443
0.060 GeneticVariation BEFREE Benedek, J. Pande, Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human gamma D-crystallin, Biochemistry 44 (2005) 2491-2500] that the mutation dramatically lowers the solubility of P23T but the overall protein fold is maintained. 19275895

2009
dbSNP: rs104894201
rs104894201
CRYAB
0.040 GeneticVariation BEFREE To understand the mechanism of VP1-001, we tested the ability of its enantiomer, ent-VP1-001, to bind and stabilize αB-crystallin (cryAB) in vitro and to produce a similar therapeutic effect in cryAB(R120G) mutant and aged wild-type mice with cataracts. 31369034

2019
dbSNP: rs104894201
rs104894201
CRYAB
0.040 GeneticVariation BEFREE The most promising compound improved lens transparency in the R49C cryAA and R120G cryAB mouse models of hereditary cataract. 26542570

2015
dbSNP: rs104894201
rs104894201
CRYAB
0.040 GeneticVariation BEFREE These data suggest that the cataract and myopathy pathologies in αB-R120G knock-in mice share common mechanisms, including increased insolubility of αB-crystallin and co-aggregation of αB-crystallin with intermediate filament proteins. 21445271

2011
dbSNP: rs104894201
rs104894201
CRYAB
0.040 GeneticVariation BEFREE To investigate the mechanism by which the α-crystallin mutations Cryaa-R49C and Cryab-R120G lead to cataract formation, we determined whether these mutations cause an altered expression of specific transcripts in the lens at an early postnatal age by RNA-seq analysis. 29338044

2018
dbSNP: rs121909596
rs121909596
CRYGD ; LOC100507443
0.030 GeneticVariation BEFREE Interestingly, a mutation of different codon, i.e., p.Arg58His in CRYGD has been reported to be linked with aculeiform cataract in four different families; two from Switzerland, one from Macedonia and in a Mexican family. 22669729

2012
dbSNP: rs121909596
rs121909596
CRYGD ; LOC100507443
0.030 GeneticVariation BEFREE In a nutshell, the increased surface hydrophobicity could be the cause of self-aggregation of mutant R58H leading to aculeiform cataract. 29532225

2018
dbSNP: rs121909596
rs121909596
CRYGD ; LOC100507443
0.030 GeneticVariation BEFREE The R58H mutation described in this Mexican family is identical to that demonstrated previously in three unrelated families with aculeiform cataract, suggesting that this type of cataract has a specific molecular basis represented by the Arg to His change at residue 58 of CRYGD. 16030500

2005