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The results suggest that the N-terminal domain of CRYAA is required during in vitro complex formation with filensin (zeige BFSP1 ELISA Kits) and phakinin (zeige BFSP2 ELISA Kits).
CRYAA polymorphism is a genetic marker of inter-individual differences in the risk of nuclear ARC (zeige NOL3 ELISA Kits).
Results demonstrated that CRYAA rs7278468 and CRYAB (zeige CRYAB ELISA Kits) rs370803064/rs387907338 are correlated with the risk and clinicopathological features of children suffering from congenital cataract.
These mutations revealed a range of detrimental effects on the structure, stability and functional properties of aA-Cry (zeige CRY2 ELISA Kits) which all together can explain the pathomechanisms underlying development of the associated congenital cataract disorders
The study demonstrates that residues 70-88 in CRYAA act as a primary substrate binding site and account for the bulk of the total chaperone activity.
The T allele of rs7278468 in the crystallin alpha A promoter is associated with age-related cataract through increasing binding of KLF-10 and thus decreasing crystallin alpha A transcription.
The evidence presented suggests that the methylation of the CpG sites of the CRYAA promotor directly affect Sp1 (zeige PSG1 ELISA Kits) binding, leading to down expression of CRYAA in human lens epithelial cells.
The p.R21Q mutation of CRYAA is the most likely cause of paediatric cataract in this family.
these results suggest that individuals carrying the alphaA-Crystallin R12C mutation are at an increased risk to develop early-onset cataract under condition of oxidative stress
alphaA-crystallin membrane insertion is oligomer-size dependent
Collectively, these studies show that FGF signaling up-regulates expression of alphaA-crystallin both directly and indirectly via up-regulation of c-Maf (zeige MAF ELISA Kits).
Knockout of alphaA-crystallin inhibited pathologic neovascularization through the VEGF (zeige VEGFA ELISA Kits) and VEGFR2 (zeige KDR ELISA Kits) signaling pathways both in vitro and in vivo.
p53 (zeige TP53 ELISA Kits) can regulate lens differentiation by controlling expression of the differentiation genes coding for the lens crystallins.
Alpha A crystallin is a moonlighting protein that functions as a heat shock protein as well as a lens crystalline.
alphaA-crystallin may protect against geographic atrophy.
alphaA and alphaB regulate caspase-3 (zeige CASP3 ELISA Kits) and Bax (zeige BAX ELISA Kits) in vitro and in vivo to regulate lens differentiation.
these findings show that mutation of alphaA-crystallin induces activation of the UPR during cataract formation.
Hydroimidazolone modification of human alphaA-crystallin: Effect on the chaperone function and protein refolding ability.
Methionine oxidation of alpha-crystallin in combination with loss of MsrA (zeige MSR1 ELISA Kits) repair causes loss of alpha-crystallin chaperone function.
mouse lens epithelial cell progression through the cell cycle is significantly affected by expression of alphaA and alphaB-crystallin (zeige CRYAB ELISA Kits)
For moderate O-GlcNAcylation on bovine crystalline alpha, the preferred amino acids were Pro > Ala > Gly at position -2, Ala > Thr (zeige TRH ELISA Kits) >Val > Lys (zeige LYZ ELISA Kits) > Pro at position -1, and Ala > Gly > Arg > Glu (zeige DCTN1 ELISA Kits) at position +2.
Alpha-crystallin, in the presence of the sorbitol dehydrogenase (SDH (zeige SORD ELISA Kits)) pyridine cofactor NAD(H), can exert a remarkable chaperone action by favoring the recovery of the enzyme activity from chemically denaturated SDH (zeige SDS ELISA Kits) up to 77%.
Conserved triad in alphaA-crystallin contributes to stability of higher order oligomers but is not essential for formation of tetramers.
Mass spectrometry analysis and a database search identified carbamylated proteins originating from alphaA-crystallin, betaB2- and gammaS-(betaS)-crystallins.
The ontogeny and localization of the alphaA-crystallin and betaB1-crystallin (zeige CRYBB1 ELISA Kits) during embryonic lens development and regeneration indicated a different development program, although they have identical origins, the ectoderm.
The normal development observed in alphaA-crystallin deficient zebrafish embryos may reflect similarly non-essential roles for this protein in the early stages of both zebrafish and mammalian lens development.
Fndings establish that the C-terminal extension of alphaA crystallin can be either 3D domain swapped or non-3D domain swapped.
alphaA-crystallin (HSPB4) is expressed during development.
Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families\; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone\; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits\; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed\; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Defects in this gene cause autosomal dominant congenital cataract (ADCC).
alpha-crystallin A chain
, crystallin, alpha-1
, heat shock protein beta-4
, human alphaA-crystallin (CRYA1)
, crystallin, alpha 1
, lens opacity 18
, alpha A crystallin
, alpha-A-crystallin protein
, alpha-crystallin A chain-like
, Crystallin, alpha polypeptide A
, crystallin, alpha A
, Alpha-crystallin A chain