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2000
Volume 15, Issue 12
  • ISSN: 1389-4501
  • E-ISSN: 1873-5592

Abstract

Malaria is a devastating human parasitic disease that receives enhanced attention due to the emergence of resistance to traditional drugs. Thus, the search for new molecular targets is a major goal. PfAM1 is an aminopeptidase from Plasmodium falciparum, William H. Welch 1897, belonging to the M1 family of metalloproteases, which is a promising target of inhibitors to block the intra-erythrocytic stages of the parasite. Since its identification in 1998, many efforts have been done to validate PfAM1 as an appropriate target of antimalarials. The present work is a critical review of the main structural, functional and kinetic characteristics of PfAM1, as well as a summary of the effects of key inhibitors at molecular and cellular levels. The systematization of experimental results should contribute to a better understanding of the properties of PfAM1 as a target of antimalarials and promote research projects focused on the development of PfAM1 inhibitors.

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/content/journals/cdt/10.2174/1389450115666141024115641
2014-11-01
2025-05-22
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