Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone
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A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting proteinA yeast 2-hybrid analysis of human GTP cyclohydrolase I protein interactionsReview: The HSP90 molecular chaperone-an enigmatic ATPaseMapping the Interactome of a Major Mammalian Endoplasmic Reticulum Heat Shock Protein 90Natural iminosugar (+)-lentiginosine inhibits ATPase and chaperone activity of hsp90The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922A primate specific extra domain in the molecular chaperone Hsp90Medically Relevant Acinetobacter Species Require a Type II Secretion System and Specific Membrane-Associated Chaperones for the Export of Multiple Substrates and Full VirulenceExploring the Functional Complementation between Grp94 and Hsp90Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complexPathways of chaperone-mediated protein folding in the cytosolDifferential modulation of functional dynamics and allosteric interactions in the Hsp90-cochaperone complexes with p23 and Aha1: a computational study.Crystal structure of the toxin Msmeg_6760, the structural homolog of Mycobacterium tuberculosis Rv2035, a novel type II toxin involved in the hypoxic response.A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands.Comprehensive comparative-genomic analysis of type 2 toxin-antitoxin systems and related mobile stress response systems in prokaryotes.To fold or not to fold: modulation and consequences of Hsp90 inhibition.Transcriptomic responses in mouse brain exposed to chronic excess of the neurotransmitter glutamate.Solution structure and function of YndB, an AHSA1 protein from Bacillus subtilisThe Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative DiseasesBiological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis.Δ9-THC increases endogenous AHA1 expression in rat cerebellum and may modulate CB1 receptor function during chronic useAn Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humansHsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway.OS-9 facilitates turnover of nonnative GRP94 marked by hyperglycosylation.Regulation of activation-induced deaminase stability and antibody gene diversification by Hsp90.Hsp70 and Hsp40 functionally interact with soluble mutant huntingtin oligomers in a classic ATP-dependent reaction cycleHsp90: a chaperone for protein folding and gene regulation.Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiaeLow resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis has an elongated shape which allows its interaction with both N- and M-domains of Hsp90.Patterns of gene expression associated with recovery and injury in heat-stressed rats.Hsp90 C-terminal inhibitors exhibit antimigratory activity by disrupting the Hsp90α/Aha1 complex in PC3-MM2 cells.Post-translational modifications of Hsp90 and their contributions to chaperone regulationTranscriptional Response to Acute Thermal Exposure in Juvenile Chinook Salmon Determined by RNAseq.Expression of three topologically distinct membrane proteins elicits unique stress response pathways in the yeast Saccharomyces cerevisiaeGenetically recombinant antibodies: new therapeutics against candidiasis.Lessons from the genome sequence of Neurospora crassa: tracing the path from genomic blueprint to multicellular organism.The Effects of Hsp90α1 Mutations on Myosin Thick Filament OrganizationCharacterizing the role of Hsp90 in production of heat shock proteins in motor neurons reveals a suppressive effect of wild-type Hsf1.Multiple 40-kDa heat-shock protein chaperones function in Tom70-dependent mitochondrial import.
P2860
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P248
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P2860
Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone
description
2003 nî lūn-bûn
@nan
2003 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Aha1 binds to the middle domai ...... ity of the molecular chaperone
@ast
Aha1 binds to the middle domai ...... ity of the molecular chaperone
@en
Aha1 binds to the middle domai ...... ity of the molecular chaperone
@en-gb
Aha1 binds to the middle domai ...... ity of the molecular chaperone
@nl
type
label
Aha1 binds to the middle domai ...... ity of the molecular chaperone
@ast
Aha1 binds to the middle domai ...... ity of the molecular chaperone
@en
Aha1 binds to the middle domai ...... ity of the molecular chaperone
@en-gb
Aha1 binds to the middle domai ...... ity of the molecular chaperone
@nl
prefLabel
Aha1 binds to the middle domai ...... ity of the molecular chaperone
@ast
Aha1 binds to the middle domai ...... ity of the molecular chaperone
@en
Aha1 binds to the middle domai ...... ity of the molecular chaperone
@en-gb
Aha1 binds to the middle domai ...... ity of the molecular chaperone
@nl
P2093
P2860
P3181
P356
P1476
Aha1 binds to the middle domai ...... ity of the molecular chaperone
@en
P2093
Anja Harst
Gregor P Lotz
Hongying Lin
Wolfgang M J Obermann
P2860
P304
P3181
P356
10.1074/JBC.M212761200
P407
P577
2003-05-09T00:00:00Z