The Heat Shock Protein 40 Family of the Malaria Parasite Plasmodium falciparum
Author(s)
Rug, M; Maier, AG;
Details
Publication Year 2011-12,Volume 63,Issue #12,Page 1081-1086
Journal Title
IUBMB LIFE
Publication Type
Journal Article
Abstract
Few diseases have had such a profound influence on human evolution and history as malaria. Despite intense efforts malaria infection continues to be a major killer. The causative agent of malaria, the unicellular eukaryote Plasmodium, displays a fascinating biology in which ubiquitous cellular concepts are modified to serve the particular needs of the malaria parasite. In this review, we explore how Plasmodium utilizes the heat shock protein 40 system, a chaperone system that ensures correct protein folding under normal and stress conditions. We highlight the peculiarities of the Plasmodium system and discuss whether any components of the system might be exploited for intervention strategies against this debilitating disease. (C) 2011 IUBMB IUBMB Life, 63(12): 1081-1086, 2011
Publisher
WILEY-BLACKWELL
Keywords
ERYTHROCYTE SURFACE-ANTIGEN; INFECTED ERYTHROCYTE; HOST ERYTHROCYTE; HSP40 PROTEINS; RESA PROTEIN; CHAPERONE; VIRULENCE; DNAJ; TRANSLOCATION; STABILITY
Publisher's Version
https://doi.org/10.1002/iub.525
Terms of Use/Rights Notice
Refer to copyright notice on published article.


Creation Date: 2011-12-01 12:00:00
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