(Q24299657)

2

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Daniel Southworth

3

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Patrick R Griffin

4

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David A Agard

CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates

5

0 references

language of work or name

English

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publication date

19 June 2014

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published in

Cell

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volume

157

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page(s)

1685-97

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issue

7

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cites work

1 reference

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Hsp70 chaperones: cellular functions and molecular mechanism

19 March 2017

1 reference

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Disassembly of transcriptional regulatory complexes by molecular chaperones

19 March 2017

1 reference

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In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

19 March 2017

1 reference

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The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop

19 March 2017

1 reference

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Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition

19 March 2017

1 reference

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Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors

19 March 2017

1 reference

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Structural analysis of substrate binding by the molecular chaperone DnaK

19 March 2017

1 reference

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Accurate determination of local defocus and specimen tilt in electron microscopy

19 March 2017

1 reference

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EMAN: semiautomated software for high-resolution single-particle reconstructions

19 March 2017

1 reference

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SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields

19 March 2017

1 reference

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Chaperoning of glucocorticoid receptors

19 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

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

19 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling

19 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

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

19 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

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

19 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events

19 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

HSP90 at the hub of protein homeostasis: emerging mechanistic insights

19 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Modulation of the Hsp90 chaperone cycle by a stringent client protein

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Time window expansion for HDX analysis of an intrinsically disordered protein

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

HDX workbench: software for the analysis of H/D exchange MS data

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Conformational dynamics of the molecular chaperone Hsp90

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Hormone binding and co-regulator binding to the glucocorticoid receptor are allosterically coupled

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Glucocorticoid signaling in the cell. Expanding clinical implications to complex human behavioral and somatic disorders

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

A conformational switch in the ligand-binding domain regulates the dependence of the glucocorticoid receptor on Hsp90.

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Nuclear receptor structure: implications for function

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Unliganded and hormone-bound glucocorticoid receptors interact with distinct hydrophobic sites in the Hsp90 C-terminal domain

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1.

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Folding and stability of the ligand-binding domain of the glucocorticoid receptor

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Stimulation of the weak ATPase activity of human hsp90 by a client protein

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

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

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

The assembly of progesterone receptor-hsp90 complexes using purified proteins

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

The role of DnaJ-like proteins in glucocorticoid receptor.hsp90 heterocomplex assembly by the reconstituted hsp90.p60.hsp70 foldosome complex.

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70.

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90.

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocket

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Mapping the HSP90 binding region of the glucocorticoid receptor.

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Reduced levels of hsp90 compromise steroid receptor action in vivo

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Mechanics of Hsp70 chaperones enables differential interaction with client proteins.

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones.

29 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.

29 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Continuous recycling: a mechanism for modulatory signal transduction

29 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Reconstitution of the steroid receptor.hsp90 heterocomplex assembly system of rabbit reticulocyte lysate.

29 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4087167

Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes

29 November 2018

1 reference

12 December 2020

Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways

1 reference

12 December 2020

ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates

1 reference

12 December 2020

Multistep mechanism of substrate binding determines chaperone activity of Hsp70

1 reference

12 December 2020

Protein Structure Initiative Material Repository: an open shared public resource of structural genomics plasmids for the biological community

1 reference

Crossref

https://api.crossref.org/works/10.1016%2FJ.CELL.2014.04.038

7 January 2021

inferred from DOI database lookup

Identifiers

DOI

10.1016/J.CELL.2014.04.038

1 reference

419635

419635

1 reference

1 reference

1 reference