The ability of lens alpha crystallin to protect against heat-induced aggregation is age-dependent.
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Alpha B-crystallin expression in mouse NIH 3T3 fibroblasts: glucocorticoid responsiveness and involvement in thermal protectionDifferential gene expression in anatomical compartments of the human eye.The role of Eph receptors in lens function and diseaseRole of αA-crystallin-derived αA66-80 peptide in guinea pig lens crystallin aggregation and insolubilization.αA-crystallin peptide SDRDKFVIFLDVKHF accumulating in aging lens impairs the function of α-crystallin and induces lens protein aggregationChanges in protein profiles of guinea pig sclera during development of form deprivation myopia and recoveryLens proteomics: analysis of rat crystallins when lenses are exposed to dexamethasone.Formation of amyloid fibrils in vitro from partially unfolded intermediates of human gammaC-crystallin.Proteomics analysis of water insoluble-urea soluble crystallins from normal and dexamethasone exposed lens.The twelfth Frederick H. Verhoeff Lecture: gene sharing in the visual system.Identification of histidine residues involved in Zn(2+) binding to αA- and αB-crystallin by chemical modification and MALDI TOF mass spectrometry.Impact of Subunit Composition on the Uptake of α-Crystallin by Lens and RetinaalphaB-crystallin protects retinal tissue during Staphylococcus aureus-induced endophthalmitisThe role thermal physiology plays in species invasion.Identification of the in vivo truncation sites at the C-terminal region of alpha-A crystallin from aged bovine and human lens.Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins.Lens Endogenous Peptide αA66-80 Generates Hydrogen Peroxide and Induces Cell Apoptosis.Insights into the domains required for dimerization and assembly of human alphaB crystallin.Effect of aging on the chaperone-like function of human alpha-crystallin assessed by three methods.The C-terminal region of alpha-crystallin: involvement in protection against heat-induced denaturation.Molecular chaperone properties of the high molecular weight aggregate from aged lens.Maternal loading of a small heat shock protein increases embryo thermal tolerance in Drosophila melanogaster.Effect of Green Tea Polyphenol Epigallocatechin-3-gallate on the Aggregation of αA(66-80) Peptide, a Major Fragment of αA-crystallin Involved in Cataract Development.
P2860
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P2860
The ability of lens alpha crystallin to protect against heat-induced aggregation is age-dependent.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
The ability of lens alpha crys ...... aggregation is age-dependent.
@en
type
label
The ability of lens alpha crys ...... aggregation is age-dependent.
@en
prefLabel
The ability of lens alpha crys ...... aggregation is age-dependent.
@en
P2093
P2860
P1433
P1476
The ability of lens alpha crys ...... aggregation is age-dependent.
@en
P2093
P2860
P304
P356
10.3109/02713689209000754
P577
1992-08-01T00:00:00Z