M
Maria Luisa Campo
Researcher at University of Extremadura
Publications - 27
Citations - 1591
Maria Luisa Campo is an academic researcher from University of Extremadura. The author has contributed to research in topics: Inner mitochondrial membrane & Mitochondrion. The author has an hindex of 14, co-authored 27 publications receiving 1494 citations. Previous affiliations of Maria Luisa Campo include University at Albany, SUNY & University of Navarra.
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Journal ArticleDOI
Determination of arginase activity in macrophages: a micromethod
TL;DR: A modification of Schimke's method for urea determination as a valuable micromethod for measuring arginase in activated macrophages is proposed and can detect small amounts of urea, in the order of 0.02 mumol.
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Mitochondrial Channel Activity Studied by Patch- Clamping Mitoplasts
TL;DR: This report discusses primarily the 45, 120–150, 350, and 1,000 pS transitions in patch-clamping mitoplasts, which have observed a complex pattern of conductance transitions.
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Arginase I induction during Leishmania major infection mediates the development of disease.
Virginia Iniesta,Jesualdo Carcelén,I. Molano,Pablo M. Peixoto,Eloy Redondo,Pilar Parra,Marina Mangas,Isabel Monroy,Maria Luisa Campo,C.G. Nieto,Inés Corraliza +10 more
TL;DR: Results show that arginase I is induced in both susceptible and resistant mice during the development of the disease, however, in BALB/c-infected tissues, the induction of this protein parallels the time of infection, while in C57BL/6 mice, the enzyme is upregulated only during footpad swelling.
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Arginase I Induction by Modified Lipoproteins in Macrophages: A Peroxisome Proliferator-Activated Receptor-γ/δ-Mediated Effect that Links Lipid Metabolism and Immunity
Alejandro Gallardo-Soler,Carlos Gómez-Nieto,Maria Luisa Campo,Chaitra Marathe,Peter Tontonoz,Antonio Castrillo,Inés Corraliza +6 more
TL;DR: The results strongly suggest that ArgI is a key marker of the alternative program triggered by PPAR in macrophages, and that PPARgamma and -delta ligands promote intracellular amastigote growth in infected macrophage growth, and this effect is dependent on both PPAR expression and Arg activity.
Journal ArticleDOI
Tim17p Regulates the Twin Pore Structure and Voltage Gating of the Mitochondrial Protein Import Complex TIM23
Sonia Martinez-Caballero,Sergey M. Grigoriev,Johannes M. Herrmann,Maria Luisa Campo,Kathleen W. Kinnally +4 more
TL;DR: Although Tim23p is the main structural unit of the pore Tim17p is required for twin pore structure and provides the voltage gate for the TIM23 channel, suggesting that the N terminus is vital for both voltage sensing and protein sorting.