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 …

Heat shock protein 90 (Hsp90), an ATP-dependent molecular chaperone, is a highly
conserved and ubiquitously expressed stress protein in eukaryotes. It is responsible for …

Ongoing research into the chaperone systems of malaria parasites, and particularly of
Plasmodium falciparum, suggests that heat shock proteins (Hsps) could potentially be an …

The main agent of human malaria, the protozoa, Plasmodium falciparum is known to infect
liver cells, subsequently invading the host erythrocyte, leading to the manifestation of clinical …

Heat shock proteins act as molecular chaperones, facilitating protein folding in cells of living
organisms. Their role is particularly important in parasites because environmental changes …

The heat shock protein 70 (Hsp70) family of molecular chaperones are crucial for the
survival and pathogenicity of the main agent of malaria, Plasmodium falciparum. Hsp70 is …

Plasmodial heat shock protein 70 (Hsp70) chaperones represent a promising new class of
antimalarial drug targets because of the important roles they play in the survival and …

Background The recent reduction in mortality due to malaria is being threatened by the
appearance of Plasmodium falciparum parasites that are resistant to artemisinin in …

When Springer Nature invited us to consider a second edition of our book Heat Shock
Proteins of Malaria, we were unsure if we could do justice to the book project. The field is …

Malaria continues to exact a great human toll in tropical settings. Antimalarial resistance is
rife and the parasite inexorably develops mechanisms to outwit our best drugs, including the …