Elucidation of the Hsp90 C-terminal inhibitor binding site (Q28236934)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21548602%20AND%20SRC:MED&resulttype=core&format=json

30 January 2020

title

Elucidation of the Hsp90 C-terminal inhibitor binding site (English)

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30 January 2020

8

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30 January 2020

9

Brian S J Blagg

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30 January 2020

author name string

Robert L Matts

1

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30 January 2020

Anshuman Dixit

2

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30 January 2020

Laura B Peterson

3

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30 January 2020

Liang Sun

4

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30 January 2020

Sudhakar Voruganti

5

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30 January 2020

Palgunan Kalyanaraman

6

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30 January 2020

Steve D Hartson

7

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30 January 2020

language of work or name

English

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publication date

17 May 2011

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30 January 2020

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30 January 2020

volume

6

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30 January 2020

page(s)

800-807

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30 January 2020

issue

8

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Hsp90 is regulated by a switch point in the C-terminal domain

30 January 2020

cites work

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Clustal W and Clustal X version 2.0

20 March 2017

1 reference

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Scalable molecular dynamics with NAMD

20 March 2017

1 reference

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Crystal structures of Escherichia coli topoisomerase IV ParE subunit (24 and 43 kilodaltons): a single residue dictates differences in novobiocin potency against topoisomerase IV and DNA gyrase

20 March 2017

1 reference

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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

20 March 2017

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20 March 2017

The Hallmarks of Cancer

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

20 March 2017

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The entropic penalty of ordered water accounts for weaker binding of the antibiotic novobiocin to a resistant mutant of DNA gyrase: a thermodynamic and crystallographic study

20 March 2017

1 reference

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

20 March 2017

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Comparative protein modelling by satisfaction of spatial restraints

20 March 2017

1 reference

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Fragmentation reactions of multiply-protonated peptides and implications for sequencing by tandem mass spectrometry with low-energy collision-induced dissociation

20 March 2017

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Basic local alignment search tool

20 March 2017

1 reference

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Structure and mechanism of the Hsp90 molecular chaperone machinery

20 March 2017

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

7 April 2017

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Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle

7 April 2017

1 reference

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Hsp90 inhibition: elimination of shock and stress

29 September 2017

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Heat shock protein 90: inhibitors in clinical trials.

29 September 2017

1 reference

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KU135, a novel novobiocin-derived C-terminal inhibitor of the 90-kDa heat shock protein, exerts potent antiproliferative effects in human leukemic cells

29 September 2017

1 reference

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Characterization of a novel novobiocin analogue as a putative C-terminal inhibitor of heat shock protein 90 in prostate cancer cells

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3164513

Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3164513

Protein targets of reactive metabolites of thiobenzamide in rat liver in vivo

29 September 2017

1 reference

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Development of novobiocin analogues that manifest anti-proliferative activity against several cancer cell lines

29 September 2017

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The Hsp90 molecular chaperone: an open and shut case for treatment

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3164513

Hsp90: a novel target for the disruption of multiple signaling cascades

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3164513

High-throughput assay for the identification of Hsp90 inhibitors based on Hsp90-dependent refolding of firefly luciferase

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3164513

Inhibitors of the HSP90 molecular chaperone: attacking the master regulator in cancer

29 September 2017

1 reference

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Hsp90 inhibitors identified from a library of novobiocin analogues

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3164513

Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3164513

Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3164513

Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90.

2 June 2018

1 reference

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Conserved conformational changes in the ATPase cycle of human Hsp90.

2 June 2018

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3164513

Apo-Hsp90 coexists in two open conformational states in solution.

2 June 2018

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3164513

Modulation of chaperone function and cochaperone interaction by novobiocin in the C-terminal domain of Hsp90: evidence that coumarin antibiotics disrupt Hsp90 dimerization

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3164513

Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions

27 November 2018

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3164513

Structural models and binding site prediction of the C-terminal domain of human Hsp90: a new target for anticancer drugs

27 November 2018

1 reference

12 December 2020

Exploring the binding site of C-terminal hsp90 inhibitors

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12 December 2020

Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins

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12 December 2020

Syntheses of photolabile novobiocin analogues

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12 December 2020

Molybdate inhibits hsp90, induces structural changes in its C-terminal domain, and alters its interactions with substrates

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12 December 2020

Synthesis and evaluation of coumermycin A1 analogues that inhibit the Hsp90 protein folding machinery

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12 December 2020

Identifiers

DOI

10.1021/CB200052X

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30 January 2020

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30 January 2020

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