αA- and αB-crystallins interact with caspase-3 and Bax to guard mouse lens development.
about
Human small heat shock proteins: protein interactomes of homo- and hetero-oligomeric complexes: an updateThe specificity of the interaction between αB-crystallin and desmin filaments and its impact on filament aggregation and cell viability.Analysis of the cytoprotective role of α-crystallins in cell survival and implication of the αA-crystallin C-terminal extension domain in preventing Bax-induced apoptosisNovel roles for α-crystallins in retinal function and disease.Study of αB-crystallin expression in Gerbil BCAO model of transient global cerebral ischemia.Antiapoptotic properties of α-crystallin-derived peptide chaperones and characterization of their uptake transporters in human RPE cells.Heat shock factor 1 induces crystallin-αB to protect against cisplatin nephrotoxicity.Loss of the small heat shock protein αA-crystallin does not lead to detectable defects in early zebrafish lens development.One size does not fit all: the oligomeric states of αB crystallin.Identification of proteins that interact with alpha A-crystallin using a human proteome microarray.The small heat shock protein αA-crystallin negatively regulates pancreatic tumorigenesisProtein interactomes of three stress inducible small heat shock proteins: HspB1, HspB5 and HspB8.Therapeutic potential of α-crystallin.Medical implications of understanding the functions of human small heat shock proteins.HspB1, HspB5 and HspB4 in Human Cancers: Potent Oncogenic Role of Some of Their Client Proteins.Differential phosphorylation-based regulation of αB-crystallin chaperone activity for multipass transmembrane proteins.Chaperones: needed for both the good times and the bad times.HSF4 regulates lens fiber cell differentiation by activating p53 and its downstream regulators.The role of αB-crystallin in skeletal and cardiac muscle tissues.Increased expression of small heat shock protein αB-crystallin after intracerebral hemorrhage in adult rats.
P2860
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P2860
αA- and αB-crystallins interact with caspase-3 and Bax to guard mouse lens development.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh-hant
name
αA- and αB-crystallins interact with caspase-3 and Bax to guard mouse lens development.
@en
αA- and αB-crystallins interact with caspase-3 and Bax to guard mouse lens development.
@nl
type
label
αA- and αB-crystallins interact with caspase-3 and Bax to guard mouse lens development.
@en
αA- and αB-crystallins interact with caspase-3 and Bax to guard mouse lens development.
@nl
prefLabel
αA- and αB-crystallins interact with caspase-3 and Bax to guard mouse lens development.
@en
αA- and αB-crystallins interact with caspase-3 and Bax to guard mouse lens development.
@nl
P2093
P1476
αA- and αB-crystallins interact with caspase-3 and Bax to guard mouse lens development
@en
P2093
E Wawrousek
P304
P356
10.2174/156652412798889036
P577
2012-02-01T00:00:00Z