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International union of pharmacology. XXII. Nomenclature for chemokine receptors.
A widely accepted receptor nomenclature system is described, ratified by the International Union of Pharmacology, that is facilitating clear communication in this area and updating current concepts of the biology and pharmacology of the chemokine system.
The pathogenic basis of malaria
Insight into the complexity of malaria pathogenesis is vital for understanding the disease and will provide a major step towards controlling it.
A family of erythrocyte binding proteins of malaria parasites.
- J. Adams, B. K. Sim, S. A. Dolan, X. Fang, D. Kaslow, L. Miller
- BiologyProceedings of the National Academy of Sciences…
- 1 August 1992
It is proposed that the Duffy binding proteins and the sialic acid binding protein are members of a gene family, separated in evolution, that may indicate the regions where the adhesin function resides.
Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum.
The domain of EBA-175 that binds erythrocytes was identified as region II with the use of truncated portions of E BA-175 expressed on COS cells, and the identification of both the receptor and ligand domains may suggest rational designs for receptor blockade and vaccines.
Switches in expression of plasmodium falciparum var genes correlate with changes in antigenic and cytoadherent phenotypes of infected erythrocytes
The resistance factor to Plasmodium vivax in blacks. The Duffy-blood-group genotype, FyFy.
It is concluded that Duffy determinants (Fya or Fyb or both) on the erythrocyte surface are required for invasion of ery Throcytes by vivax merozoites.
Identification of the erythrocyte binding domains of Plasmodium vivax and Plasmodium knowlesi proteins involved in erythrocyte invasion
The binding domains of these malaria ligands represent potential vaccine candidates and targets for receptor-blockade therapy and indicate conservation of the domain for erythrocyte binding in evolutionarily distant malaria species.
Binding of Plasmodium merozoite proteins RON2 and AMA1 triggers commitment to invasion
- P. Srinivasan, W. Beatty, L. Miller
- BiologyProceedings of the National Academy of Sciences
- 25 July 2011
Results identify the binding of RON2 to the hydrophobic pocket of AMA1 as the step that commits Plasmodium merozoites to RBC invasion and point to RON 2 as a potential vaccine candidate.
Malaria biology and disease pathogenesis: insights for new treatments
The current understanding of the biology of asexual blood-stage parasites and gametocytes and the ability to culture them in vitro lends optimism that high-throughput screenings of large chemical libraries will produce a new generation of antimalarial drugs.