HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor - Wikidata - awgldk - TriplyDB

HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor

HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor

http://www.wikidata.org/entity/Q28216531

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Optimal functional levels of activation-induced deaminase specifically require the Hsp40 DnaJa1 Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles S100A1 is a novel molecular chaperone and a member of the Hsp70/Hsp90 multichaperone complex A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90 GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.Functions of the Hsp90 chaperone system: lifting client proteins to new heights Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseases The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop Pathways of chaperone-mediated protein folding in the cytosol Characterisation of the Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop)Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling.To fold or not to fold: modulation and consequences of Hsp90 inhibition.Hsp90 and co-chaperones twist the functions of diverse client proteins.Hsp40 chaperones promote degradation of the HERG potassium channel.The multiple facets of drug resistance: one history, different approaches.Temperature differentially affects adenosine triphosphatase activity in Hsc70 orthologs from Antarctic and New Zealand notothenioid fishes Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity The cochaperone SGTA (small glutamine-rich tetratricopeptide repeat-containing protein alpha) demonstrates regulatory specificity for the androgen, glucocorticoid, and progesterone receptors.Efficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatitis B virus reverse transcriptase, an assumed Hsp90 client protein.Independent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1).Regulation of activation-induced deaminase stability and antibody gene diversification by Hsp90.Hsp90: a chaperone for protein folding and gene regulation.Saccharomyces cerevisiae Hsp70 mutations affect [PSI+] prion propagation and cell growth differently and implicate Hsp40 and tetratricopeptide repeat cochaperones in impairment of [PSI+]A highly charged region in the middle domain of plant endoplasmic reticulum (ER)-localized heat-shock protein 90 is required for resistance to tunicamycin or high calcium-induced ER stresses.The ribosomal biogenesis protein Utp21 interacts with Hsp90 and has differing requirements for Hsp90-associated proteins.Hsp70 forms antiparallel dimers stabilized by post-translational modifications to position clients for transfer to Hsp90.Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins The Hsp40 molecular chaperone Ydj1p, along with the protein kinase C pathway, affects cell-wall integrity in the yeast Saccharomyces cerevisiae.Androgen receptor splice variants activate androgen receptor target genes and support aberrant prostate cancer cell growth independent of canonical androgen receptor nuclear localization signal.Functional specificity of co-chaperone interactions with Hsp90 client proteins.Functioning of the Hsp90 machine in chaperoning checkpoint kinase I (Chk1) and the progesterone receptor (PR).Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae.Fluorescent ligand for human progesterone receptor imaging in live cells.Minireview: the intersection of steroid receptors with molecular chaperones: observations and questions Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins.Estrogen regulation of proteins in the rat ventromedial nucleus of the hypothalamus.The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts.Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function.

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P2860

HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor

http://www.wikidata.org/entity/Q28216531

description

2002 nî lūn-bûn

@nan

2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

HSP40 binding is the first ste ...... for the progesterone receptor

@ast

HSP40 binding is the first ste ...... for the progesterone receptor

@en

HSP40 binding is the first ste ...... for the progesterone receptor

@nl

type

label

HSP40 binding is the first ste ...... for the progesterone receptor

@ast

HSP40 binding is the first ste ...... for the progesterone receptor

@en

HSP40 binding is the first ste ...... for the progesterone receptor

@nl

prefLabel

HSP40 binding is the first ste ...... for the progesterone receptor

@ast

HSP40 binding is the first ste ...... for the progesterone receptor

@en

HSP40 binding is the first ste ...... for the progesterone receptor

@nl

P1433

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P2860

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P921

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P356

P1433

Journal of Biological Chemistry

P1476

HSP40 binding is the first ste ...... for the progesterone receptor

@en

P2093

Ahmed Chadli

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

David O Toft

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

M Patricia Hernández

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

P2860

The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system

Kinetics of molecular chaperone action

Human cDNA encoding DnaJ protein homologue

Hop modulates Hsp70/Hsp90 interactions in protein folding

Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery

Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.

Steroid receptor interactions with heat shock protein and immunophilin chaperones

A role for the Hsp40 Ydj1 in repression of basal steroid receptor activity in yeast

Evidence for iterative ratcheting of receptor-bound hsp70 between its ATP and ADP conformations during assembly of glucocorticoid receptor.hsp90 heterocomplexes.

In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins.

P304

11873-81

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P31

scholarly article

P356

10.1074/JBC.M111445200

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P407

P433

14

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P478

277

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

P577

2002-04-05T00:00:00Z

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

P698

11809754

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

P921

molecular chaperones