Bachelor of Science in Chemistry and Doctor of Science (Biochemistry) from the Institute of Chemistry of the University of São Paulo. Performed Postdoctoral training at Stanford University and University of Chile. His main field of investigation is redox biology, developing research lines on protein quality control and cell signaling. Currently, his studies are focused on posttranslational modifications and aggregation of proteins in the endoplasmic reticulum (ER) and their contribution to physio(patho)logical processes of the nervous system. He has contributed to elucidate pathogenic mechanisms of neurodegenerative diseases such as Amyotrophic Lateral Sclerosis and Alzheimer's, working on the characterization of misfolded and aggregated protein species, in addition to cellular responses to ER stress. (Source: Lattes Curriculum)
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The redox folding through disulfide bond formation constitutes an essential step for protein homeostasis (or proteostasis) of the endoplasmic reticulum (ER). The oxidizing environment of the ER lumen thermodynamically favors disulfide bond formation, but the numerous combinations between cysteine residues in a polypeptide chain can generate non-native disulfide bonds. These non-native bon…
Protein disulfide isomerases (PDIs) are enzymes of the endoplasmic reticulum containing thioredoxin domains that catalyze protein folding through the formation of disulfide bonds between cysteine residues. This process, which we refer to as redox folding, is essential for the structural stability of proteins, as well as for the regulation of their functions. Failure in redox folding has b…
The redox folding through disulfide bond formation constitutes an essential step in biogenesis of membrane and secreted proteins trafficking through the endoplasmic reticulum (ER) that confers structural stability while allowing conformational transitions for cellular signaling. This process is tightly regulated to maintain protein homeostasis (or proteostasis) of the ER, being catalyzed …
Intellectual disability (ID) encompasses a broad range of conditions with reduced cognitive capacity and adaptive behaviors. The genetic heterogeneity of these conditions poses a challenge for understanding pathogenic mechanisms and designing therapeutic interventions. Given this complex genetic landscape, functional studies of mutant genes are paramount for unveiling molecular networks a…
A esclerose lateral amiotrófica (ALS) é uma doença neurodegenerativa fatal caracterizada pela perda progressiva dos neurônios motores. Os casos familiares mais conhecidos são devidos à mutações no gene que codifica a enzima superóxido dismutase dependente de cobre e zinco (SOD). A doença conta com modelos animais e celulares sendo adequada para explorar o papel de oxidantes e radicais liv…
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