(Q24295270)

English

Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone

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scholarly article

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Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone (English)

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molecular chaperones

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1 reference

GOA release 2020-03-11

Hsp90 family chaperone HSP82 YPL240C

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GOA release 2020-03-11

Hsp90 cochaperone STI1 YOR027W

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GOA release 2020-03-11

author name string

Gregor P Lotz

1

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Hongying Lin

2

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Anja Harst

3

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Wolfgang M J Obermann

4

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language of work or name

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publication date

9 May 2003

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Journal of Biological Chemistry

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278

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19

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17228-35

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Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase

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Steroid receptor interactions with heat shock protein and immunophilin chaperones

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Dynamic activation of endothelial nitric oxide synthase by Hsp90.

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Hsp90 & Co. - a holding for folding

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Hsp90's secrets unfold: new insights from structural and functional studies

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Hsp90: a specialized but essential protein-folding tool

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

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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

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Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine

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

1 reference

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Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

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

1 reference

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ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

1 reference

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Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90

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Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90.

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Functional profiling of the Saccharomyces cerevisiae genome

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Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

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Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation

1 reference

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Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90

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

1 reference

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p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site

1 reference

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21 January 2018

SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212761200

21 January 2018

Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins

1 reference

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In vivo analysis of the Hsp90 cochaperone Sti1 (p60)

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212761200

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The Ydj1 molecular chaperone facilitates formation of active p60v-src in yeast

1 reference

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Heat-shock protein hsp90 governs the activity of pp60v-src kinase

1 reference

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Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212761200

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In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212761200

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212761200

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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

1 reference

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Hop modulates Hsp70/Hsp90 interactions in protein folding

1 reference

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Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

1 reference

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Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release

1 reference

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Regulation of heat shock protein 90 ATPase activity by sequences in the carboxyl terminus

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212761200

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The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212761200

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Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212761200

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A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212761200

7 January 2021

based on heuristic

inferred from DOI database lookup

The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212761200

7 January 2021

based on heuristic

inferred from DOI database lookup

In vitro evidence that hsp90 contains two independent chaperone sites

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212761200

7 January 2021

based on heuristic

inferred from DOI database lookup

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212761200

7 January 2021

based on heuristic

inferred from DOI database lookup

A cyclophilin function in Hsp90-dependent signal transduction

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1074/JBC.M212761200

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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