Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. (Q46113733)

19 December 2017

title

Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. (English)

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19 December 2017

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Klaus Richter

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Martin Hessling

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19 December 2017

Johannes Buchner

series ordinal

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19 December 2017

publication date

22 February 2009

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19 December 2017

Nature Structural & Molecular Biology

published in

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19 December 2017

volume

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19 December 2017

issue

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19 December 2017

page(s)

287-293

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19 December 2017

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

cites work

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

21 January 2018

1 reference

Molecular chaperones in the cytosol: from nascent chain to folded protein

21 January 2018

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Hsp90 as a capacitor for morphological evolution

31 March 2020

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HSP90 and the chaperoning of cancer

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Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance

31 March 2020

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The hsp90 molecular chaperone modulates multiple telomerase activities

31 March 2020

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

31 March 2020

1 reference

Molecular chaperones: the busy life of Hsp90.

31 March 2020

1 reference

The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes

31 March 2020

1 reference

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

31 March 2020

1 reference

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

31 March 2020

1 reference

Conserved conformational changes in the ATPase cycle of human Hsp90.

31 March 2020

1 reference

The ATPase cycle of the endoplasmic chaperone Grp94.

31 March 2020

1 reference

The ATPase cycle of the mitochondrial Hsp90 analog Trap1.

31 March 2020

1 reference

GHKL, an emergent ATPase/kinase superfamily

31 March 2020

1 reference

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

31 March 2020

1 reference

Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90.

31 March 2020

1 reference

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

31 March 2020

1 reference

Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones

31 March 2020

1 reference

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

31 March 2020

1 reference

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

31 March 2020

1 reference

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

31 March 2020

1 reference

The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding

31 March 2020

1 reference

The Hsp90 chaperone machinery

31 March 2020

1 reference

Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones

31 March 2020

1 reference

Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle

31 March 2020

1 reference

Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

31 March 2020

1 reference

In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone

31 March 2020

1 reference

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

31 March 2020

1 reference

Intrinsic inhibition of the Hsp90 ATPase activity

31 March 2020

1 reference

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

31 March 2020

1 reference

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

31 March 2020

1 reference

Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform

31 March 2020

1 reference

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

31 March 2020

1 reference

Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile

31 March 2020

1 reference

Steroid receptor interactions with heat shock protein and immunophilin chaperones

31 March 2020

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/19234467

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/19234467

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1038/NSMB.1565

1 reference

19 December 2017

1 reference

19 December 2017