Apo-Hsp90 coexists in two open conformational states in solution. (Q41623374)

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1 January 2020

title

Apo-Hsp90 coexists in two open conformational states in solution (English)

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1

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J. Fernando Díaz

6

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1 January 2020

author name string

Emmanuel Giudice

2

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1 January 2020

Jean-Paul Rolland

3

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1 January 2020

Rubén M Buey

4

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1 January 2020

Pascale Barbier

5

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Vincent Peyrot

7

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1 January 2020

Daniel Thomas

8

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Cyrille Garnier

9

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publication date

1 July 2008

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1 January 2020

number of pages

13

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based on heuristic

inferred from page(s)

published in

Biology of the Cell

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volume

100

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issue

7

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page(s)

413-425

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

1 January 2020

cites work

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Hsp90 & Co. - a holding for folding

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Structural intermediates in the assembly of taxoid-induced microtubules and GDP-tubulin double rings: time-resolved X-ray scattering

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The two-state process of the heat shock protein 90 thermal denaturation: effect of calcium and magnesium

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Hydrodynamic properties and quaternary structure of the 90 kDa heat-shock protein: effects of divalent cations.

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The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site

21 January 2018

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The middle domain of Hsp90 acts as a discriminator between different types of client proteins

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Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins

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Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

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Structure and mechanism of the Hsp90 molecular chaperone machinery

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Conformational dynamics of the molecular chaperone Hsp90 in complexes with a co-chaperone and anticancer drugs.

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

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

21 January 2018

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21 January 2018

hsp90: twist and fold.

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Intrinsic inhibition of the Hsp90 ATPase activity

21 January 2018

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Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements

21 January 2018

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

21 January 2018

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Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing

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Structure of an Hsp90-Cdc37-Cdk4 complex.

21 January 2018

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HSP90 and the chaperoning of cancer

21 January 2018

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Biochemical and structural studies of the interaction of Cdc37 with Hsp90.

21 January 2018

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Automated matching of high- and low-resolution structural models

21 January 2018

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21 January 2018

Identifiers

DOI

10.1042/BC20070149

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1 January 2020

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