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Luis E. Rodríguez

Researcher at National University of Colombia

Publications -  47
Citations -  1176

Luis E. Rodríguez is an academic researcher from National University of Colombia. The author has contributed to research in topics: Plasmodium falciparum & Peptide sequence. The author has an hindex of 20, co-authored 47 publications receiving 1151 citations.

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Identification of Plasmodium falciparum MSP-1 peptides able to bind to human red blood cells.

TL;DR: Results show that peptides based on conserved and dimorphic regions of MSP‐1, interact with human red blood cells (RBCs), and showed that the RBC receptors are not sialic acid dependent and appear to be proteic in nature.
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Plasmodium falciparum EBA-175 kDa protein peptides which bind to human red blood cells

TL;DR: Using synthetic peptides and specific receptor-ligand interaction methodology, 6 high-activity binding sequences from the EBA-175 CAMP strain are identified and several of these peptides are located in regions recognized by protective immune clusters of merozoites eluted antibodies.
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Intimate molecular interactions of P. falciparum merozoite proteins involved in invasion of red blood cells and their implications for vaccine design.

TL;DR: The results show that Merozoite Surface Protein-9 (MSP-9) or Acid Basic Repeat Antigen (ABRA) 3679 is superior to other MSPs tested on the basis of its ability to bind to EMTs.
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Plasmodium vivax MSP-1 peptides have high specific binding activity to human reticulocytes.

TL;DR: Interestingly, some high activity binding peptides (HABPs) are located close to the hypothesised 42 and 19kDa fragment cleavage sites for this protein, suggesting that these sequences have an important role in target cell attachment and invasion process by Pv-MSP-1.
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Two MSA 2 peptides that bind to human red blood cells are relevant to Plasmodium falciparum merozoite invasion.

TL;DR: Both of these sequences inhibit in vitro erythrocyte parasite invasion by up to 95% suggesting that they have an important role in the parasite's invasion process.