Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
about
Hsp90: a specialized but essential protein-folding toolGlucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cyclesS100A1 is a novel molecular chaperone and a member of the Hsp70/Hsp90 multichaperone complexCofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone systemCo-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53.Small glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activityCytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulumSmall Molecule Inhibitors to Disrupt Protein-protein Interactions of Heat Shock Protein 90 Chaperone MachineryChaperone machines for protein folding, unfolding and disaggregationElectrostatic Interactions of Hsp-organizing Protein Tetratricopeptide Domains with Hsp70 and Hsp90: COMPUTATIONAL ANALYSIS AND PROTEIN ENGINEERINGThe architecture of functional modules in the Hsp90 co-chaperone Sti1/HopContribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae.Sti1 is a novel activator of the Ssa proteins.The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes.Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle.The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptorThe Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone systemHSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptorA brain-specific isoform of small glutamine-rich tetratricopeptide repeat-containing protein binds to Hsc70 and the cysteine string proteinFunctional similarity between the chloroplast translocon component, Tic40, and the human co-chaperone, Hsp70-interacting protein (Hip)Degradation of HIF-1alpha under hypoxia combined with induction of Hsp90 polyubiquitination in cancer cells by hypericin: a unique cancer therapyLoss of the histone methyltransferase EZH2 induces resistance to multiple drugs in acute myeloid leukemia.Regulation of stress-inducible phosphoprotein 1 nuclear retention by protein inhibitor of activated STAT PIAS1.Insights into regulation and function of the major stress-induced hsp70 molecular chaperone in vivo: analysis of mice with targeted gene disruption of the hsp70.1 or hsp70.3 gene.Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes.Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling.Stress genes and proteins in the archaea.HIV replication enhances production of free fatty acids, low density lipoproteins and many key proteins involved in lipid metabolism: a proteomics studyAn AlphaScreen-based high-throughput screen to identify inhibitors of Hsp90-cochaperone interaction.To fold or not to fold: modulation and consequences of Hsp90 inhibition.Hsp90 and co-chaperones twist the functions of diverse client proteins.HOP is a monomer: investigation of the oligomeric state of the co-chaperone HOP.The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative DiseasesAn Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humansPolypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 In vivoHsp104 interacts with Hsp90 cochaperones in respiring yeastThe cochaperone SGTA (small glutamine-rich tetratricopeptide repeat-containing protein alpha) demonstrates regulatory specificity for the androgen, glucocorticoid, and progesterone receptors.Chaperones in cell cycle regulation and mitogenic signal transduction: a review.Maturation of steroid receptors: an example of functional cooperation among molecular chaperones and their associated proteins
P2860
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P2860
Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
description
1998 nî lūn-bûn
@nan
1998 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
@ast
Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
@en
Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
@nl
type
label
Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
@ast
Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
@en
Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
@nl
prefLabel
Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
@ast
Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
@en
Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
@nl
P3181
P356
P1476
Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
@en
P2093
P304
P3181
P356
10.1074/JBC.273.52.35194
P407
P577
1998-12-25T00:00:00Z