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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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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.

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

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.
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Tim17p Regulates the Twin Pore Structure and Voltage Gating of the Mitochondrial Protein Import Complex TIM23

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.