The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange
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BAG5 protects against mitochondrial oxidative damage through regulating PINK1 degradationThe nucleotide exchange factors of Hsp70 molecular chaperonesBiochemical and structural studies on the high affinity of Hsp70 for ADPStructural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factorStructural insight into plant programmed cell death mediated by BAG proteins in Arabidopsis thalianaStructure and function of Hip, an attenuator of the Hsp70 chaperone cycleExploiting Protein Conformational Change to Optimize Adenosine-Derived Inhibitors of HSP70.Allostery in the Hsp70 chaperone proteinsHSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.A fragment-based approach applied to a highly flexible target: Insights and challenges towards the inhibition of HSP70 isoforms.Ubiquitinylation of α-synuclein by carboxyl terminus Hsp70-interacting protein (CHIP) is regulated by Bcl-2-associated athanogene 5 (BAG5).Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperonesA role for an Hsp70 nucleotide exchange factor in the regulation of synaptic vesicle endocytosis.BAG5 Interacts with DJ-1 and Inhibits the Neuroprotective Effects of DJ-1 to Combat Mitochondrial Oxidative Damage.Selective suppression of microglial activation by paeoniflorin attenuates morphine tolerance.Non-canonical Interactions between Heat Shock Cognate Protein 70 (Hsc70) and Bcl2-associated Anthanogene (BAG) Co-Chaperones Are Important for Client Release.Chaperone-Based Therapies for Disease Modification in Parkinson's Disease.A novel mutant p53 binding partner BAG5 stabilizes mutant p53 and promotes mutant p53 GOFs in tumorigenesis.In silico characterisation, homology modelling and structure-based functional annotation of blunt snout bream (Megalobrama amblycephala) Hsp70 and Hsc70 proteins.A cell-permeable hairpin peptide inhibits hepatitis C viral nonstructural protein 5A-mediated translation and virus productionGRP78 Interacting Partner Bag5 Responds to ER Stress and Protects Cardiomyocytes From ER Stress-Induced Apoptosis.
P2860
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P2860
The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
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2010年学术文章
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2010年学术文章
@zh-cn
2010年学术文章
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2010年学术文章
@zh-my
2010年学术文章
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2010年學術文章
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name
The C-terminal BAG domain of B ...... ng domain for ADP-ATP exchange
@ast
The C-terminal BAG domain of B ...... ng domain for ADP-ATP exchange
@en
The C-terminal BAG domain of B ...... ng domain for ADP-ATP exchange
@nl
type
label
The C-terminal BAG domain of B ...... ng domain for ADP-ATP exchange
@ast
The C-terminal BAG domain of B ...... ng domain for ADP-ATP exchange
@en
The C-terminal BAG domain of B ...... ng domain for ADP-ATP exchange
@nl
prefLabel
The C-terminal BAG domain of B ...... ng domain for ADP-ATP exchange
@ast
The C-terminal BAG domain of B ...... ng domain for ADP-ATP exchange
@en
The C-terminal BAG domain of B ...... ng domain for ADP-ATP exchange
@nl
P2093
P50
P3181
P1433
P1476
The C-terminal BAG domain of B ...... ng domain for ADP-ATP exchange
@en
P2093
Akihiko Arakawa
Fumiaki Hayashi
Meiri Shida
Noboru Ohsawa
Noriko Handa
P304
P3181
P356
10.1016/J.STR.2010.01.004
P577
2010-03-10T00:00:00Z