Plasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shock

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Botha, Melissa, Chiang, Annette, Needham, Patrick, Stephens, Linda L, Hoppe, Heinrich, Kulzer, Simone, Przyborski, Jude M, Lingelbach, Klaus, Wipf, Peter, Brodsky, Jeffrey, Shonhai, Addmore and Blatch, Gregory ORCID: 0000-0003-0778-8577 (2011) Plasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shock. Cell Stress & Chaperones, 16 (4). pp. 389-401. ISSN 1355-8145

Abstract

Plasmodium falciparum causes cerebral malaria in humans, and nearly all malaria deaths result from infection by this species. Observations suggest that heat shock proteins play a key role in the management of toxicity conferred by drugs to the parasite, and may augment drug resistance. In addition to their role within the parasite, growing evidence suggests that parasite heat shock proteins are involved in the trafficking of parasite-encoded proteins to the erythrocyte surface, thus playing a key role in the pathogenesis of P. falciparum malaria.

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Item type	Article
URI	https://vuir.vu.edu.au/id/eprint/9015
DOI	10.1007/s12192-010-0250-6
Official URL	http://link.springer.com/article/10.1007%2Fs12192-...
Subjects	Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences Historical > FOR Classification > 0601 Biochemistry and Cell Biology Historical > SEO Classification > 970111 Expanding Knowledge in the Medical and Health Sciences
Keywords	ResPubID23311, heat shock protein 70 (Hsp70), heat shock protein 40 (Hsp40), suppressed protein aggregation, Plasmodium falciparum (malaria), immunofluorescence microscopy, ATP hydrolytic rates, molecular chaperone
Citations in Scopus	49 - View on Scopus
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