Hop modulates Hsp70/Hsp90 interactions in protein folding - Wikidata - awgldk - TriplyDB

Hop modulates Hsp70/Hsp90 interactions in protein folding

Hop modulates Hsp70/Hsp90 interactions in protein folding

http://www.wikidata.org/entity/Q28260829

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In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein Hsp90: a specialized but essential protein-folding tool Human cyclophilin 40 is a heat shock protein that exhibits altered intracellular localization following heat shock Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70 Small glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activity A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity Anatomy of RISC: how do small RNAs and chaperones activate Argonaute proteins?The 'active life' of Hsp90 complexes The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p.Sti1 is a novel activator of the Ssa proteins.Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1.Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes.Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones.Mechanistic Asymmetry in Hsp90 Dimers Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cells Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system Nucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assembly HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor Allostery in the Hsp70 chaperone proteins The regulatory mechanism of Hsp90alpha secretion and its function in tumor malignancy Functional similarity between the chloroplast translocon component, Tic40, and the human co-chaperone, Hsp70-interacting protein (Hip)Identification and characterization of Harc, a novel Hsp90-associating relative of Cdc37 Characterisation of the Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop)Bacterial lipopolysaccharide induces expression of the stress response genes hop and H411.Transthiocarbamoylation of proteins by thiolated isothiocyanates.Loggerhead sea turtle embryos (Caretta caretta) regulate expression of stress response and developmental genes when exposed to a biologically realistic heat stress.The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90.To fold or not to fold: modulation and consequences of Hsp90 inhibition.The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans Identification of a novel inducible cytosolic Hsp70 gene in Chinese shrimp Fenneropenaeus chinensis and comparison of its expression with the cognate Hsc70 under different stresses.Transposons, environmental changes, and heritable induced phenotypic variability.

P2860

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P2860

Hop modulates Hsp70/Hsp90 interactions in protein folding

http://www.wikidata.org/entity/Q28260829

description

1998 nî lūn-bûn

@nan

1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի փետրվարին 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 modulates Hsp70/Hsp90 interactions in protein folding

@ast

Hop modulates Hsp70/Hsp90 interactions in protein folding

@en

Hop modulates Hsp70/Hsp90 interactions in protein folding

@nl

type

label

Hop modulates Hsp70/Hsp90 interactions in protein folding

@ast

Hop modulates Hsp70/Hsp90 interactions in protein folding

@en

Hop modulates Hsp70/Hsp90 interactions in protein folding

@nl

prefLabel

Hop modulates Hsp70/Hsp90 interactions in protein folding

@ast

Hop modulates Hsp70/Hsp90 interactions in protein folding

@en

Hop modulates Hsp70/Hsp90 interactions in protein folding

@nl

P1433

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P1476

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P2860

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P1433

Journal of Biological Chemistry

P1476

Hop modulates Hsp70/Hsp90 interactions in protein folding

@en

P2093

B D Johnson

http://www.w3.org/2001/XMLSchema#string

D O Toft

http://www.w3.org/2001/XMLSchema#string

R J Schumacher

http://www.w3.org/2001/XMLSchema#string

P2860

Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes

A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

Cooperation of the molecular chaperone Ydj1 with specific Hsp70 homologs to suppress protein aggregation.

In vivo analysis of the Hsp90 cochaperone Sti1 (p60)

Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation

Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate

P304

3679-3686

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P31

scholarly article

P3181

3580262

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P356

10.1074/JBC.273.6.3679

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P407

P433

6

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P478

273

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P577

1998-02-01T00:00:00Z

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P698

9452498

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P921

protein folding