Structure of the ATP-binding domain of Plasmodium falciparum Hsp90 (Q27663523)

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Language	Label	Description	Also known as
English	Structure of the ATP-binding domain of Plasmodium falciparum Hsp90	scientific article

Statements

instance of

scholarly article

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title

Structure of the ATP-binding domain of Plasmodium falciparum Hsp90 (English)

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main subject

Plasmodium falciparum

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author

Kevin D Corbett

object named as

Kevin D Corbett

series ordinal

1

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James M. Berger

series ordinal

2

object named as

James M Berger

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language of work or name

English

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publication date

October 2010

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published in

Proteins

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volume

78

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issue

13

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page(s)

2738-44

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cites work

The heat shock protein 90 of Plasmodium falciparum and antimalarial activity of its inhibitor, geldanamycin

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PubMed Central

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20 March 2017

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

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20 March 2017

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

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PubMed Central

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20 March 2017

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

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20 March 2017

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

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20 March 2017

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

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20 March 2017

Protein production by auto-induction in high density shaking cultures

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20 March 2017

Coot: model-building tools for molecular graphics

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20 March 2017

Likelihood-enhanced fast rotation functions

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PubMed Central

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20 March 2017

Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused

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20 March 2017

Multiple alignment of DNA sequences with MAFFT

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7 April 2017

Structure and mechanism of the Hsp90 molecular chaperone machinery

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7 April 2017

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

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7 April 2017

Targeting HSP90 for cancer therapy

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29 September 2017

Systems analysis of chaperone networks in the malarial parasite Plasmodium falciparum

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29 September 2017

Chaperoning a cellular upheaval in malaria: heat shock proteins in Plasmodium falciparum.

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29 September 2017

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

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29 September 2017

Inhibitors of the HSP90 molecular chaperone: current status

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29 September 2017

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

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29 September 2017

Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes.

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29 September 2017

GHKL, an emergent ATPase/kinase superfamily

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29 September 2017

The complementation of yeast with human or Plasmodium falciparum Hsp90 confers differential inhibitor sensitivities.

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PubMed Central

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retrieved

27 November 2018

Processing of X-ray diffraction data collected in oscillation mode

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/20635416

retrieved

12 December 2020

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Identifiers

DOI

10.1002/PROT.22799

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PMC publication ID

2927708

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PubMed publication ID

20635416

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ResearchGate publication ID

45200986

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