Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.
about
Hsp90: a specialized but essential protein-folding toolHuman butyrate-induced transcript 1 interacts with hepatitis C virus NS5A and regulates viral replicationCofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone systemA proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting proteinCHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substratesCooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signalingHuman Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domainThe architecture of functional modules in the Hsp90 co-chaperone Sti1/HopStructure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p.A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).Hsp90 is regulated by a switch point in the C-terminal domainFunctional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae.PhLP3 modulates CCT-mediated actin and tubulin folding via ternary complexes with substrates.MUC1 oncoprotein is targeted to mitochondria by heregulin-induced activation of c-Src and the molecular chaperone HSP90The aryl hydrocarbon receptor complex and the control of gene expressionMapping the Interactome of a Major Mammalian Endoplasmic Reticulum Heat Shock Protein 90Phenotypic diversity and altered environmental plasticity in Arabidopsis thaliana with reduced Hsp90 levelsIdentification and characterization of Harc, a novel Hsp90-associating relative of Cdc37Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complexA review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.Suppression of heat shock protein 27 using OGX-427 induces endoplasmic reticulum stress and potentiates heat shock protein 90 inhibitors to delay castrate-resistant prostate cancer.Interactions of Exo1p with components of MutLalpha in Saccharomyces cerevisiae.Characterization of the nucleotide-binding capacity and the ATPase activity of the PIP3-binding protein JFC1.Heat shock protein 90β stabilizes focal adhesion kinase and enhances cell migration and invasion in breast cancer cellsCRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90.A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket.Mutations within the hMLH1 and hPMS2 subunits of the human MutLalpha mismatch repair factor affect its ATPase activity, but not its ability to interact with hMutSalpha.Hsp90: chaperoning signal transduction.In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins.Molecular chaperone Hsp90 is important for vaccinia virus growth in cellsRegulation of activation-induced deaminase stability and antibody gene diversification by Hsp90.From the cradle to the grave: molecular chaperones that may choose between folding and degradation.Hsp90: a chaperone for protein folding and gene regulation.The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains.Hsp90 functions in the targeting and outer membrane translocation steps of Tom70-mediated mitochondrial import.The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64A biochemical rationale for the anticancer effects of Hsp90 inhibitors: slow, tight binding inhibition by geldanamycin and its analogues.Mitochondrial protein import and the genesis of steroidogenic mitochondriaGenome-scale co-evolutionary inference identifies functions and clients of bacterial Hsp90
P2860
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P2860
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.
description
2000 nî lūn-bûn
@nan
2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Polypeptide release by Hsp90 i ...... anced by the co-chaperone p23.
@ast
Polypeptide release by Hsp90 i ...... anced by the co-chaperone p23.
@en
type
label
Polypeptide release by Hsp90 i ...... anced by the co-chaperone p23.
@ast
Polypeptide release by Hsp90 i ...... anced by the co-chaperone p23.
@en
prefLabel
Polypeptide release by Hsp90 i ...... anced by the co-chaperone p23.
@ast
Polypeptide release by Hsp90 i ...... anced by the co-chaperone p23.
@en
P2860
P356
P1433
P1476
Polypeptide release by Hsp90 i ...... anced by the co-chaperone p23.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/19.21.5930
P407
P577
2000-11-01T00:00:00Z