The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins (Q24290709)

GOA release 2020-03-11

Hsp90 protein binding

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GOA release 2020-03-11

author name string

P Connell

1

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C A Ballinger

2

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J Jiang

3

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Y Wu

4

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L J Thompson

5

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J Höhfeld

6

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C Patterson

The function of steroid hormone receptors is inhibited by the hsp90-specific compound geldanamycin

7

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language of work or name

English

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publication date

January 2001

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published in

Nature Cell Biology

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volume

3

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page(s)

93-6

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issue

1

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cites work

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7 January 2021

Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90

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7 January 2021

Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions

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7 January 2021

Molecular chaperones in cellular protein folding

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7 January 2021

Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators

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7 January 2021

Cofactor-induced modulation of the functional specificity of the molecular chaperone Hsc70

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7 January 2021

Posttranslational quality control: folding, refolding, and degrading proteins.

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7 January 2021

The base of the proteasome regulatory particle exhibits chaperone-like activity

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7 January 2021

Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones

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7 January 2021

A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains

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7 January 2021

The cyclosporin A-binding immunophilin CyP-40 and the FK506-binding immunophilin hsp56 bind to a common site on hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor

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7 January 2021

Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor

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7 January 2021

Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation

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7 January 2021

Differential effects of the hsp70-binding protein BAG-1 on glucocorticoid receptor folding by the hsp90-based chaperone machinery

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7 January 2021

A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly.

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7 January 2021

Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae

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7 January 2021

Physical association of ubiquitin ligases and the 26S proteasome

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7 January 2021

The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome

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7 January 2021

Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains

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7 January 2021

Consolidated OpenCitations Corpus – April 2017

Identifiers

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1 reference

Dimensions Publication ID

564493

1027958026

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1013227263

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564493

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference