(Q33840745)

29 July 2017

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title

Structure and in vivo function of Hsp90. (English)

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29 July 2017

author

Chrisostomos Prodromou

series ordinal

2

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29 July 2017

Pearl LH

1

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29 July 2017

publication date

1 February 2000

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Current Opinion in Structural Biology

29 July 2017

published in

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29 July 2017

volume

10

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29 July 2017

issue

1

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29 July 2017

page(s)

46-51

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The hsp90-based Chaperone System: Involvement in Signal Transduction from a Variety of Hormone and Growth Factor Receptors

29 July 2017

cites work

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7 January 2021

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

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7 January 2021

The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation

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7 January 2021

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

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7 January 2021

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

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7 January 2021

The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes

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7 January 2021

A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone

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7 January 2021

Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin

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7 January 2021

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

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7 January 2021

Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis

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7 January 2021

Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair

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7 January 2021

Structure of CheA, a signal-transducing histidine kinase

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7 January 2021

Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies

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7 January 2021

A model for the mechanism of strand passage by DNA gyrase

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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

The assembly of progesterone receptor-hsp90 complexes using purified proteins

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7 January 2021

The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions

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7 January 2021

Identification of conserved residues required for the binding of a tetratricopeptide repeat domain to heat shock protein 90.

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7 January 2021

The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90.

1 reference

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7 January 2021

Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants

1 reference

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7 January 2021

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

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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

Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cells

1 reference

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7 January 2021

CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90.

1 reference

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7 January 2021

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900047-0

7 January 2021

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

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900047-0

7 January 2021

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

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7 January 2021

Hop modulates Hsp70/Hsp90 interactions in protein folding

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

The Peptidyl-prolyl Isomerase Domain of the CyP-40 Cyclophilin Homolog Cpr7 Is Not Required to Support Growth or Glucocorticoid Receptor Activity in Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900047-0

7 January 2021

Studies with Purified Chaperones Advance the Understanding of the Mechanism of Glucocorticoid Receptor-hsp90 Heterocomplex Assembly

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900047-0

7 January 2021

A conserved proline in the hsp90 binding region of the glucocorticoid receptor is required for hsp90 heterocomplex stabilization and receptor signaling

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900047-0

7 January 2021

Binding of hsp90 to the Glucocorticoid Receptor Requires a Specific 7-Amino Acid Sequence at the Amino Terminus of the Hormone-binding Domain

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Modular Folding and Evidence for Phosphorylation-induced Stabilization of an hsp90-dependent Kinase

1 reference

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7 January 2021

Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900047-0

7 January 2021

Dynamic activation of endothelial nitric oxide synthase by Hsp90.

1 reference

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7 January 2021

Functional requirement of p23 and Hsp90 in telomerase complexes

1 reference

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7 January 2021

Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900047-0

7 January 2021

HSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes

1 reference

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7 January 2021

Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response

1 reference

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7 January 2021

Hsp90 as a capacitor for morphological evolution

1 reference

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7 January 2021

Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation

1 reference

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7 January 2021

Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900047-0

7 January 2021

Radicicol Leads to Selective Depletion of Raf Kinase and Disrupts K-Ras-activated Aberrant Signaling Pathway

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900047-0

7 January 2021

The Physical Association of Multiple Molecular Chaperone Proteins with Mutant p53 Is Altered by Geldanamycin, an hsp90-Binding Agent

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900047-0

7 January 2021

Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900047-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900047-0

7 January 2021

10.1016/S0959-440X(99)00047-0

Identifiers

DOI

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release_pegvxv2l5zaghchq7be5y7rg6m

29 July 2017

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/pegvxv2l5zaghchq7be5y7rg6m

24 November 2022

mapped directly with Wikidata item

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