(Q28143894)

English

The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone

scientific article (publication date: 24 November 2000)

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scholarly article

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The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone (English)

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molecular chaperones

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5

object named as

L M Neckers

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author name string

M G Marcu

1

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A Chadli

2

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I Bouhouche

3

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M Catelli

4

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language of work or name

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publication date

24 November 2000

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Journal of Biological Chemistry

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275

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37181-6

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47

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Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent

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21 January 2018

Steroid receptor interactions with heat shock protein and immunophilin chaperones

1 reference

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p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2.

1 reference

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Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4

1 reference

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Chaperones get in touch: the Hip-Hop connection

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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

1 reference

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Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90.

1 reference

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ATP-binding properties of human Hsp90.

1 reference

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

1 reference

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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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The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003701200

21 January 2018

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

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

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Delimitation of two regions in the 90-kDa heat shock protein (Hsp90) able to interact with the glucocorticosteroid receptor (GR)

1 reference

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The charged region of Hsp90 modulates the function of the N-terminal domain

1 reference

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The interaction between coumarin drugs and DNA gyrase

1 reference

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DNA gyrase: affinity chromatography on novobiocin-Sepharose and catalytic properties

1 reference

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21 January 2018

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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21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003701200

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003701200

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

1 reference

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21 January 2018

The Clp ATPases define a novel class of molecular chaperones

1 reference

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21 January 2018

Identifiers

10.1074/JBC.M003701200

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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