About: Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70

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scientific article published on 01 June 1996

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в червні 1996 (uk) article scientifique publié en 1996 (fr) im Juni 1996 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xunu de 1996 (ast) scientific article published on 01 June 1996 (en)
publication date	wds:Q71454165-560214D9-701A-4BBE-8013-C636245C25DD
publication date	1996-06-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q71454165-10C7C9F0-459F-4161-90E9-2869772352B7 wds:Q71454165-660E1580-A8C1-442F-9E1B-DF63477B7164 wds:Q71454165-77B15C88-A74B-4BF8-8ACB-D6F12CEAFC94 wds:Q71454165-F30B4B09-D95F-4459-A7FE-998E2B12C1B5
author name string	Chen S Smith DF Rimerman RA Prapapanich V
rdfs:label	Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70 (en) Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70 (nl)
skos:prefLabel	Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70 (en) Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70 (nl)
name	Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70 (en) Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70 (nl)
author	wds:Q71454165-7A4D4619-A13D-4A5F-AAAE-FCABA877BCF4
author	Bent Honoré
title	wds:Q71454165-328E1B11-49F6-40D6-95C2-84E994760E48
title	Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70 (en)
page(s)	wds:Q71454165-848B2A88-41F7-4D84-98F1-973F5B54616C
page(s)	682-693
instance of	wds:Q71454165-CF767D7E-5ACD-4BD8-8999-E6DEC6FA8956
instance of	scholarly article
PubMed ID	wds:Q71454165-2057207D-E0CB-4525-B425-8C9C03093C40
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8776728
PubMed ID	8776728
published in	wds:Q71454165-DBFFE219-7049-4AFA-85D5-48FDF5BE7C71
published in	Molecular Endocrinology
issue	wds:Q71454165-2DCE67D9-30FE-4786-B682-187E8E6FAD10
volume	wds:Q71454165-CBAD7E25-0C5C-42E6-ACD9-8BEA0C66DFF3
issue	6
volume	10
DOI	wds:Q71454165-5DBD0DC1-A65F-48CA-BE5D-41D7FD4BBC1B
DOI	http://dx.doi.org/10.1210/MEND.10.6.8776728
DOI	10.1210/MEND.10.6.8776728
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q71454165
is cites work of	In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90 Regulation of transcription factor Pdr1p function by an Hsp70 protein in Saccharomyces cerevisiae Mammalian protein RAP46: an interaction partner and modulator of 70 kDa heat shock proteins Interference between proteins Hap46 and Hop/p60, which bind to different domains of the molecular chaperone hsp70/hsc70. Molecular markers for predicting response to tamoxifen in breast cancer patients Characterization of a plant homolog of hop, a cochaperone of hsp90. Mutational analysis of the hsp70-interacting protein Hip Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions C-terminal sequences of hsp70 and hsp90 as non-specific anchors for tetratricopeptide repeat (TPR) proteins Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradation Comparison of the carboxy-terminal DP-repeat region in the co-chaperones Hop and Hip. In vivo analysis of the Hsp90 cochaperone Sti1 (p60) Hsp104 interacts with Hsp90 cochaperones in respiring yeast Different combinations of the heat-shock cognate protein 70 (hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors Tetratricopeptide repeat cochaperones in steroid receptor complexes Domain:domain interactions within Hop, the Hsp70/Hsp90 organizing protein, are required for protein stability and structure Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cells Identification of Saccharomyces cerevisiae genes conferring resistance to quinoline ring-containing antimalarial drugs Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability Mutation of Hip's carboxy-terminal region inhibits a transitional stage of progesterone receptor assembly Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae Independent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1). The Chemical Biology of Molecular Chaperones--Implications for Modulation of Proteostasis Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent Loss of Hsp70 in Drosophila is pleiotropic, with effects on thermotolerance, recovery from heat shock and neurodegeneration Heat shock cognate protein 70 chaperone-binding site in the co-chaperone murine stress-inducible protein 1 maps to within three consecutive tetratricopeptide repeat motifs Inhibition of hsp70 by methylene blue affects signaling protein function and ubiquitination and modulates polyglutamine protein degradation Regulation of the Hsp90-binding immunophilin, cyclophilin 40, is mediated by multiple sites for GA-binding protein (GABP). Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions Minireview: the intersection of steroid receptors with molecular chaperones: observations and questions Disruption of the Bcr-Abl/Hsp90 protein complex: a possible mechanism to inhibit Bcr-Abl-positive human leukemic blasts by novobiocin Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104. Structural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA binding Function of cytosolic chaperones in Tom70-mediated mitochondrial import Versatile TPR domains accommodate different modes of target protein recognition and function Cucumber Necrosis Virus Recruits Cellular Heat Shock Protein 70 Homologs at Several Stages of Infection Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70 The HSP90 chaperone machinery. Chaperone receptors: guiding proteins to intracellular compartments Hop/Sti1 - A Two-Faced Cochaperone Involved in Pattern Recognition Receptor Maturation and Viral Infection Quantitative assessment of complex formation of nuclear-receptor accessory proteins Protein cross-linking capillary electrophoresis at increased throughput for a range of protein-protein interactions. Heat Shock Protein 90 Ensures Efficient Mumps Virus Replication by Assisting with Viral Polymerase Complex Formation The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation Maturation of steroid receptors: an example of functional cooperation among molecular chaperones and their associated proteins The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies Sequence analyses reveal that a TPR-DP module, surrounded by recombinable flanking introns, could be at the origin of eukaryotic Hop and Hip TPR-DP domains and prokaryotic GerD proteins Hyperactivity and attention deficits in mice with decreased levels of stress-inducible phosphoprotein 1 (STIP1).

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