(Q46930510)

26 December 2017

title

Intrinsic inhibition of the Hsp90 ATPase activity (English)

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26 December 2017

Franz Hagn

3

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Klaus Richter

object named as

Klaus Richter

1

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author name string

Sandra Moser

2

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26 December 2017

Rainer Friedrich

4

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26 December 2017

Otmar Hainzl

5

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26 December 2017

Markus Heller

6

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26 December 2017

Sandra Schlee

7

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26 December 2017

Horst Kessler

8

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26 December 2017

Jochen Reinstein

9

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26 December 2017

Johannes Buchner

10

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26 December 2017

language of work or name

English

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publication date

6 February 2006

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26 December 2017

Journal of Biological Chemistry

published in

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26 December 2017

volume

281

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26 December 2017

issue

16

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26 December 2017

page(s)

11301-11311

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26 December 2017

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

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1 reference

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Coordinated ATP hydrolysis by the Hsp90 dimer

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Structure and functional relationships of Hsp90.

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

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

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

21 January 2018

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The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo

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Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.

21 January 2018

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

21 January 2018

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Stimulation of the weak ATPase activity of human hsp90 by a client protein

21 January 2018

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

21 January 2018

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The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle

21 January 2018

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GHKL, an emergent ATPase/kinase superfamily

21 January 2018

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

21 January 2018

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

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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Crystal structure of an N-terminal fragment of the DNA gyrase B protein.

21 January 2018

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Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change

21 January 2018

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

21 January 2018

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

21 January 2018

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Automated backbone assignment of labeled proteins using the threshold accepting algorithm.

21 January 2018

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Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

21 January 2018

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FAST-Modelfree: a program for rapid automated analysis of solution NMR spin-relaxation data

21 January 2018

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21 January 2018

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Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network.

21 January 2018

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The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs.

21 January 2018

1 reference

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Energetics by NMR: site-specific binding in a positively cooperative system

21 January 2018

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

21 January 2018

1 reference

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NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510142200

Backbone resonance assignments of the 25kD N-terminal ATPase domain from the Hsp90 chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510142200

The high-resolution crystal structure of a 24-kDa gyrase B fragment from E. coli complexed with one of the most potent coumarin inhibitors, clorobiocin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510142200

Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510142200

Heat-shock protein hsp90 governs the activity of pp60v-src kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510142200

Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510142200

The influence of ATP and p23 on the conformation of hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510142200

Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510142200

Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510142200

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.M510142200

The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510142200

Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510142200

21 January 2018

Identifiers

DOI

10.1074/JBC.M510142200

1 reference

26 December 2017

PubMed ID

16461354

1 reference

26 December 2017