(Q44532388)

3 December 2017

title

Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90. (English)

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3 December 2017

Harald Wegele

1

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3 December 2017

Paul Muschler

2

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3 December 2017

Melanie Bunck

3

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3 December 2017

Jochen Reinstein

4

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3 December 2017

Johannes Buchner

5

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3 December 2017

language of work or name

English

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publication date

30 July 2003

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Journal of Biological Chemistry

3 December 2017

number of pages

8

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based on heuristic

inferred from page(s)

published in

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3 December 2017

volume

278

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3 December 2017

issue

41

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3 December 2017

page(s)

39303-39310

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Hsp90 & Co. - a holding for folding

3 December 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

Heat-shock protein 90, a chaperone for folding and regulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

Reconstitution of progesterone receptor with heat shock proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

Hsp90 inhibitors as novel cancer chemotherapeutic agents

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

Mechanism of Dimer Formation of the 90‐kDa Heat‐Shock Protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

Coordinated ATP hydrolysis by the Hsp90 dimer

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

GHKL, an emergent ATPase/kinase superfamily

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

The Hsp70 and Hsp60 chaperone machines

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

ATP-binding properties of human Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

Hop modulates Hsp70/Hsp90 interactions in protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

Sti1 Is a Novel Activator of the Ssa Proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M305751200

21 January 2018

Identifiers

DOI

10.1074/JBC.M305751200

1 reference

3 December 2017

1 reference