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Full-Text Articles in Medicine and Health Sciences
Proteomic Analysis Of Plasmodium Falciparum Histone Deacetylase 1 Complex Proteins, Jessica A. Engel, Emma L. Norris, Paul Gilson, Jude Przyborski, Addmore Shonhai, Gregory L. Blatch, Tina S. Skinner, Jeffrey Gorman, Madeleine Headlam, Katherine T. Andrews
Proteomic Analysis Of Plasmodium Falciparum Histone Deacetylase 1 Complex Proteins, Jessica A. Engel, Emma L. Norris, Paul Gilson, Jude Przyborski, Addmore Shonhai, Gregory L. Blatch, Tina S. Skinner, Jeffrey Gorman, Madeleine Headlam, Katherine T. Andrews
Health Sciences Papers and Journal Articles
Plasmodium falciparum histone deacetylases (PfHDACs) are an important class of epigenetic regulators that alter protein lysine acetylation, contributing to regulation of gene expression and normal parasite growth and development. PfHDACs are therefore under investigation as drug targets for malaria. Despite this, our understanding of the biological roles of these enzymes is only just beginning to emerge. In higher eukaryotes, HDACs function as part of multi-protein complexes and act on both histone and non-histone substrates. Here, we present a proteomics analysis of PfHDAC1 immunoprecipitates, identifying 26 putative P. falciparum complex proteins in trophozoite-stage asexual intraerythrocytic parasites. The …
Plasmodial Hsp40s: New Avenues For Antimalarial Drug Discovery, M Daniyan, G Blatch
Plasmodial Hsp40s: New Avenues For Antimalarial Drug Discovery, M Daniyan, G Blatch
Medical Papers and Journal Articles
Malaria, an infectious disease caused by Plasmodium spp, is one of the world's most dangerous diseases, accounting for more than half a million deaths yearly. The long years of co-habitation between the parasite and its hosts (human and mosquito), is a testimony to the parasite’s ability to escape the immune system and develop drug resistance mechanisms. Currently, an important search area for improved pharmacotherapy are molecular chaperones of the heat shock protein family, abundant in Plasmodium falciparum and contributing to its continuous survival and development. Thus far, small molecule inhibitor studies on P. falciparum Hsp70s and Hsp90s have indicated that …
The Malarial Exported Pfa0660w Is An Hsp40 Co-Chaperone Of Pfhsp70-X, M Daniyan, A Boshoff, E Prinsloo, E Pesce, G Blatch
The Malarial Exported Pfa0660w Is An Hsp40 Co-Chaperone Of Pfhsp70-X, M Daniyan, A Boshoff, E Prinsloo, E Pesce, G Blatch
Medical Papers and Journal Articles
Plasmodium falciparum, the human pathogen responsible for the most dangerous malaria infection, survives and develops in mature erythrocytes through the export of proteins needed for remodelling of the host cell. Molecular chaperones of the heat shock protein (Hsp) family are prominent members of the exportome, including a number of Hsp40s and a Hsp70. PFA0660w, a type II Hsp40, has been shown to be exported and possibly form a complex with PfHsp70-x in the infected erythrocyte cytosol. However, the chaperone properties of PFA0660w and its interaction with human and parasite Hsp70s are yet to be investigated. Recombinant PFA0660w was found to …