Binding of ATP to heat shock protein 90: evidence for an ATP-binding site in the C-terminal domain (Q28216259)

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6 December 2019

title

Binding of ATP to heat shock protein 90: evidence for an ATP-binding site in the C-terminal domain (English)

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6 December 2019

2

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6 December 2019

author name string

Cyrille Garnier

1

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6 December 2019

Philipp O Tsvetkov

3

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6 December 2019

Pascale Barbier

4

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6 December 2019

Jocelyne Leclerc-Devin

5

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6 December 2019

Jean-Marc Millot

6

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6 December 2019

Claudette Briand

7

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6 December 2019

Alexander A Makarov

8

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6 December 2019

Maria G Catelli

9

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6 December 2019

Vincent Peyrot

10

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6 December 2019

language of work or name

English

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publication date

22 January 2002

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Journal of Biological Chemistry

6 December 2019

published in

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6 December 2019

volume

277

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6 December 2019

page(s)

12208-12214

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6 December 2019

issue

14

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The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins

6 December 2019

cites work

1 reference

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21 January 2018

The heat-shock proteins

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The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review

21 January 2018

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Hsp90 & Co. - a holding for folding

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

21 January 2018

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Radicicol leads to selective depletion of Raf kinase and disrupts K-Ras-activated aberrant signaling pathway

21 January 2018

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Coordinated ATP hydrolysis by the Hsp90 dimer

21 January 2018

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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

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

21 January 2018

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Mechanism of dimer formation of the 90-kDa heat-shock protein

21 January 2018

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Oligomeric forms of the 90-kDa heat shock protein

21 January 2018

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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

21 January 2018

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

21 January 2018

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Phosphorylation and oligomerization states of native pig brain HSP90 studied by mass spectrometry

21 January 2018

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Scanning microcalorimetry in studying temperature-induced changes in proteins.

21 January 2018

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Database of homology-derived protein structures and the structural meaning of sequence alignment

21 January 2018

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Prediction of protein secondary structure at better than 70% accuracy

21 January 2018

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Improved prediction of protein secondary structure by use of sequence profiles and neural networks

21 January 2018

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Combining evolutionary information and neural networks to predict protein secondary structure

21 January 2018

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Conservation and prediction of solvent accessibility in protein families

21 January 2018

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Progress of 1D protein structure prediction at last

21 January 2018

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Improvements in protein secondary structure prediction by an enhanced neural network

21 January 2018

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Regulation of cell magnesium

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

21 January 2018

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

21 January 2018

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Charge Changes in Loop 2 Affect the Thermal Unfolding of the Myosin Motor Domain Bound to F-Actin†

21 January 2018

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