(Q34338453)

1 August 2017

title

Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone (English)

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1 August 2017

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Robert M Immormino

1

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1 August 2017

D Eric Dollins

2

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1 August 2017

Paul L Shaffer

3

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1 August 2017

Karen L Soldano

4

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1 August 2017

Melissa A Walker

5

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1 August 2017

Daniel T Gewirth

6

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1 August 2017

language of work or name

English

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publication date

2 August 2004

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Journal of Biological Chemistry

1 August 2017

published in

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1 August 2017

volume

279

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1 August 2017

issue

44

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1 August 2017

page(s)

46162-46171

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Structure, function, and mechanism of the Hsp90 molecular chaperone

1 August 2017

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Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability

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

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

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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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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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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center

21 January 2018

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21 January 2018

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A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors

21 January 2018

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

21 January 2018

1 reference

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

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M405253200

N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle

21 January 2018

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Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M405253200

1 reference

1 August 2017

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