Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes. (Q38357729)

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31 October 2019

title

Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes (English)

1 reference

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31 October 2019

main subject

Plasmodium falciparum

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1 reference

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31 October 2019

author name string

Gowrishankar Banumathy

series ordinal

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31 October 2019

Varsha Singh

series ordinal

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31 October 2019

Soundara Raghavan Pavithra

series ordinal

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31 October 2019

language of work or name

English

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publication date

12 February 2003

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Journal of Biological Chemistry

31 October 2019

published in

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31 October 2019

volume

278

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31 October 2019

issue

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31 October 2019

page(s)

18336-18345

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A brief illustrated guide to the ultrastructure of Plasmodium falciparum asexual blood stages

31 October 2019

cites work

1 reference

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Induction and localization of Plasmodium falciparum stress proteins related to the heat shock protein 70 family

21 January 2018

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Sequence, transcript characterization and polymorphisms of a Plasmodium falciparum gene belonging to the heat-shock protein (HSP) 90 family

21 January 2018

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Molecular characterization of the heat shock protein 90 gene of the human malaria parasite Plasmodium falciparum.

21 January 2018

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Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells

21 January 2018

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

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In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone

21 January 2018

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Hsp90 as a capacitor for morphological evolution

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Hsp90 as a capacitor of phenotypic variation

21 January 2018

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

21 January 2018

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

21 January 2018

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Evidence for an epigenetic mechanism by which Hsp90 acts as a capacitor for morphological evolution.

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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Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels

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The phosphorylation state of the reticulocyte 90-kDa heat shock protein affects its ability to increase phosphorylation of peptide initiation factor 2 alpha subunit by the heme-sensitive kinase.

21 January 2018

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Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein

21 January 2018

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Possible role for serine/threonine phosphorylation in the regulation of the heteroprotein complex between the hsp90 stress protein and the pp60v-src tyrosine kinase

21 January 2018

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Hsp90 & Co. - a holding for folding

21 January 2018

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hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures

21 January 2018

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Identification of a heat shock-like antigen in P. falciparum, related to the heat shock protein 90 family

21 January 2018

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

21 January 2018

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Sequence of Plasmodium falciparum chromosomes 2, 10, 11 and 14

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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Characterization of the thermotolerant cell. I. Effects on protein synthesis activity and the regulation of heat-shock protein 70 expression

21 January 2018

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Heat shock protein 90 homeostasis controls stage differentiation in Leishmania donovani

21 January 2018

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Hsp-90-associated oncoproteins: multiple targets of geldanamycin and its analogs

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M211309200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12584193%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12584193%20AND%20SRC:MED&resulttype=core&format=json