CV Lattes
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Secretaria da Saúde (São Paulo - Estado). Hospital das Clínicas da Faculdade de Medicina da USP (HCFMUSP). Instituto do Coração Professor Euryclides de Jesus Zerbini (INCOR) (Institutional affiliation for the last research proposal) Birthplace: Portugal
Ph.D. from Cardiology program at Universidade de São Paulo, USP (2018) Master's at Patologias Humanas from Aix-Marseille Université (2011)., Brasil. Has experience in Biochemistry, focusing on Metabolism and Bioenergetics, acting on the following subjects: fluorescence, map-tau, cell, tubulin and interaction, PDI, NADPH oxydase, Ras, Redox cell signaling. (Source: Lattes Curriculum)
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Redox processes emerged as major regulatory mechanisms of cell signaling and strongly regulate (patho)physiological processes, but several fundamental underlying mechanisms remain unclear, including in particular the associated subcellular compartmentalization. This remains a fundamental problem in cell biology, essential to clarify the implications of redox processes in health and diseas…
Understanding the mechanisms whereby the endoplasmic reticulum chaperone PDI (protein disulfide isomerase) converges with Nox NADPH oxidase enzymatic complex(es) is the central goal of our Thematic Project. In this direction, the observation that in tumor cells with high constitutive Nox1 expression and a K-Ras mutation there occurs a deregulation of PDI-Nox1 interaction indicates an inte…
Understanding molecular pathways involved in the redox regulation of endoplasmic reticulum-plasma membrane contacts (ER-PM) is an important goal for clarifying several aspects of the ER-related pathophysiology of Nox NADPH oxidases and, in particular, the interplay between PDIA1 and Noxes. Our group has previously described that PDIA1 is a major upstream regulator of Nox family, which are…
Protein Disulfide Isomerase (PDI) is a dithiol/disulfide oxidoreductase chaperone mainly from endoplasmic reticulum (ER), where it assists redox protein folding. Recent works indicate PDI involvement in redox cell signaling, bearing a close functional and physical interaction with the NADPH oxidase complex, the main cellular source of signaling oxidants. In Vascular smooth muscle cells (V…
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