(Q34105936)

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A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket

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Europe PubMed Central

PubMed publication ID

31 July 2017

A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket (English)

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

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Csaba Söti

1

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

Attila Rácz

2

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

Péter Csermely

3

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Europe PubMed Central

PubMed publication ID

31 July 2017

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publication date

19 December 2001

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Europe PubMed Central

PubMed publication ID

31 July 2017

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

31 July 2017

277

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Europe PubMed Central

PubMed publication ID

31 July 2017

9

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

7066-7075

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

Steroid receptor interactions with heat shock protein and immunophilin chaperones

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

Hsp90 & Co. - a holding for folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

ATP-binding properties of human Hsp90.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

GHKL, an emergent ATPase/kinase superfamily

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

Domain structures and immunogenic regions of the 90-kDa heat-shock protein (HSP90). Probing with a library of anti-HSP90 monoclonal antibodies and limited proteolysis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

A double-filter method for nitrocellulose-filter binding: application to protein-nucleic acid interactions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

Prediction of protein secondary structure at better than 70% accuracy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

Combining evolutionary information and neural networks to predict protein secondary structure

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone HSP90.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

Modulation of RNA function by aminoglycoside antibiotics

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

Stoichiometry, abundance, and functional significance of the hsp90/hsp70-based multiprotein chaperone machinery in reticulocyte lysate.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

Hsp90 chaperone activity requires the full-length protein and interaction among its multiple domains

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

HSP100/Clp proteins: a common mechanism explains diverse functions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

The ATPase activity of Hsp104, effects of environmental conditions and mutations.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

Subunit interactions influence the biochemical and biological properties of Hsp104

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

Cisplatin and DNA repair in cancer chemotherapy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

Molecular mechanisms involved in cisplatin cytotoxicity.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105568200

21 January 2018

Identifiers

10.1074/JBC.M105568200

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

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