The in vivo phosphorylation sites of bovine alpha B-crystallin.
about
HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 ((3D)HSP27)Phosphorylation-induced change of the oligomerization state of alpha B-crystallin.Chaperone function of mutant versions of alpha A- and alpha B-crystallin prepared to pinpoint chaperone binding sites.Identification of in vivo phosphorylation sites of lens proteins from porcine eye lenses by a gel-free phosphoproteomics approachStructure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology.A potential role of crystallin in the vitreous bodies of rats after ischemia-reperfusion injury.Phosphoproteomics characterization of novel phosphorylated sites of lens proteins from normal and cataractous human eye lensesMass spectrometry-based characterization of the vitreous phosphoproteomeAnalysis of the dominant effects mediated by wild type or R120G mutant of αB-crystallin (HspB5) towards Hsp27 (HspB1)Proteomics of old world camelid (Camelus dromedarius): Better understanding the interplay between homeostasis and desert environment.Identification of the posttranslational modifications of bovine lens alpha B-crystallins by mass spectrometry.αA-crystallin and αB-crystallin reside in separate subcellular compartments in the developing ocular lens.Peptide aptamers: tools to negatively or positively modulate HSPB1(27) function.Small heat-shock proteins: important players in regulating cellular proteostasis.Overview of the Lens.HspB5/αB-crystallin increases dendritic complexity and protects the dendritic arbor during heat shock in cultured rat hippocampal neurons.Defined sequence segments of the small heat shock proteins HSP25 and alphaB-crystallin inhibit actin polymerization.The carboxy-terminal lysine of alpha B-crystallin is an amine-donor substrate for tissue transglutaminase.The apparent molecular size of native alpha-crystallin B in non-lenticular tissues.Phosphorylation of alpha-crystallin B in Alexander's disease brain.AlphaB-crystallin in the rat lens is phosphorylated at an early post-natal age.Phosphorylation of alphaB-crystallin in response to various types of stress.Conversion from oligomers to tetramers enhances autophosphorylation by lens alpha A-crystallin. Specificity between alpha A- and alpha B-crystallin subunits.
P2860
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P2860
The in vivo phosphorylation sites of bovine alpha B-crystallin.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
1989年學術文章
@zh
1989年學術文章
@zh-hant
name
The in vivo phosphorylation sites of bovine alpha B-crystallin.
@en
The in vivo phosphorylation sites of bovine alpha B-crystallin.
@nl
type
label
The in vivo phosphorylation sites of bovine alpha B-crystallin.
@en
The in vivo phosphorylation sites of bovine alpha B-crystallin.
@nl
prefLabel
The in vivo phosphorylation sites of bovine alpha B-crystallin.
@en
The in vivo phosphorylation sites of bovine alpha B-crystallin.
@nl
P2093
P2860
P1433
P1476
The in vivo phosphorylation sites of bovine alpha B-crystallin.
@en
P2093
Bloemendal H
Roersma ES
Voorter CE
de Haard-Hoekman WA
de Jong WW
P2860
P356
10.1016/0014-5793(89)81491-7
P407
P577
1989-12-01T00:00:00Z