Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases-Reference-Cited by-同舟云学术

Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases

Published:2010-01-21 Issue:6 Volume:107 Page:2449-2454
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

McGowan S.,Oellig C. A.,Birru W. A.,Caradoc-Davies T. T.,Stack C. M.,Lowther J.,Skinner-Adams T.,Mucha A.,Kafarski P.,Grembecka J.,Trenholme K. R.,Buckle A. M.,Gardiner D. L.,Dalton J. P.,Whisstock J. C.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference35 articles.

1. Signs of Drug Resistance Rattle Experts, Trigger Bold Plan

2. Existing antimalarial agents and malaria-treatment strategies

3. ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum

4. Structural basis for the inhibition of the essentialPlasmodium falciparumM1 neutral aminopeptidase

5. Identification of Phosphinate Dipeptide Analog Inhibitors Directed against the Plasmodium falciparum M17 Leucine Aminopeptidase as Lead Antimalarial Compounds

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