L-arginine availability and arginase activity: Characterization of amino acid permease 3 in Leishmania amazonensis.

Autor: Juliana Ide Aoki, Sandra Marcia Muxel, Ricardo Andrade Zampieri, Stephanie Maia Acuña, Juliane Cristina Ribeiro Fernandes, Rubia Heloisa Vanderlinde, Maria Carmen Oliveira de Pinho Sales, Lucile Maria Floeter-Winter

Publikováno v: PLoS Neglected Tropical Diseases, Vol 11, Iss 10, p e0006025 (2017)

Leishmania uses the amino acid L-arginine as a substrate for arginase, enzyme that produces urea and ornithine, last precursor of polyamine pathway. This pathway is used by the parasite to replicate and it is essential to establish the infection in t

Externí odkaz: https://doaj.org/article/5d276a9c5b0f4bcc82cef116fc506b06

L-arginine availability and arginase activity: Characterization of amino acid permease 3 in Leishmania amazonensis

Autor: Rubia Heloisa Vanderlinde, Sandra Marcia Muxel, Ricardo Andrade Zampieri, Juliana Ide Aoki, Lucile Maria Floeter-Winter, Stephanie Maia Acuña, Maria Carmen Oliveira de Pinho Sales, Juliane Cristina Ribeiro Fernandes

Publikováno v: PLoS Neglected Tropical Diseases, Vol 11, Iss 10, p e0006025 (2017)
PLoS Neglected Tropical Diseases
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP

Background Leishmania uses the amino acid L-arginine as a substrate for arginase, enzyme that produces urea and ornithine, last precursor of polyamine pathway. This pathway is used by the parasite to replicate and it is essential to establish the inf

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3eaea7da2d96bfd7190e587e30f1dffa
http://europepmc.org/articles/PMC5693463?pdf=render