Departamento de Genética e Biologia Evolutiva,
Instituto de Biociências,
Departamento de Genética e Biologia Evolutiva, Instituto de Biociências
I attended the University of Sao Paulo (Bacharel Degree in Biology, 1987; Ph.D. in 1992, under the guidance of Dr. Ohara Augusto) and performed an interchanged program in the Eppley Institute - Nebraska, in collaboration with Dr. Ercole Cavalieri. I was a NIH Postdoctoral Fellow, in collaboration with Dr. Stadtman from 1992 to 1996. I was Professor at State University of Campinas (Brazil) from 1996 to 1997. I am currently Full Professor at Biosciences Institute –University of Sao Paulo (Brazil). I received a prize from the Governor of Sao Paulo State for participation in the Xylella fastidiosa Genome Project (2000). I was head of Department of Genetics and Evolutionary Biology –2013-2017. I am member of the SfRBM council (since 2013).
My research interests are on thiol-based proteins with emphasis in peroxiredoxin enzymes, using the yeast Saccharomyces cerevisiae as a model organism. The response to oxidative stress is also studied in bacteria, with emphasis in Xylella fastidiosa (bacterial plant pathogen) and Pseudomonas aeruginosa. We are characterizing biochemically and structurally a new class of antioxidant enzymes: Ohr (“Organic Hydroperoxide Resistance protein) that are potential targets for drug development. We pursue the structural and functional relationships of Cys-based proteins, employing multiple approaches.
Thiol enzymes protecting mitochondria against oxidative damage.
Methods in enzymology , 2002 | Pubmed ID: 11885279
H(2)O(2) generation in Saccharomyces cerevisiae respiratory pet mutants: effect of cytochrome c.
Free radical biology & medicine Jul, 2003 | Pubmed ID: 12853074
Glutathione and thioredoxin peroxidases mediate susceptibility of yeast mitochondria to Ca(2+)-induced damage.
Archives of biochemistry and biophysics May, 2004 | Pubmed ID: 15081889
Heat stress promotes mitochondrial instability and oxidative responses in yeast deficient in thiazole biosynthesis.
Research in microbiology Apr, 2006 | Pubmed ID: 16171982
Structural insights into enzyme-substrate interaction and characterization of enzymatic intermediates of organic hydroperoxide resistance protein from Xylella fastidiosa.
Journal of molecular biology Jun, 2006 | Pubmed ID: 16631787
Reactive cysteine in proteins: protein folding, antioxidant defense, redox signaling and more.
Comparative biochemistry and physiology. Toxicology & pharmacology : CBP Jul-Aug, 2007 | Pubmed ID: 17045551
Dihydrolipoyl dehydrogenase as a source of reactive oxygen species inhibited by caloric restriction and involved in Saccharomyces cerevisiae aging.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology Jan, 2007 | Pubmed ID: 17110466
Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C.
Proceedings of the National Academy of Sciences of the United States of America Mar, 2007 | Pubmed ID: 17360337
Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome.
The FEBS journal Jun, 2008 | Pubmed ID: 18435761
Superoxide dismutase 1-mediated production of ethanol- and DNA-derived radicals in yeasts challenged with hydrogen peroxide: molecular insights into the genome instability of peroxiredoxin-null strains.
The Journal of biological chemistry Feb, 2009 | Pubmed ID: 19106092
Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase.
The Journal of biological chemistry Jul, 2010 | Pubmed ID: 20463026
Catalytic properties of thioredoxin immobilized on superparamagnetic nanoparticles.
Journal of inorganic biochemistry May, 2011 | Pubmed ID: 21470550
The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process.
BMC microbiology Dec, 2011 | Pubmed ID: 22204397
Redox control of 20S proteasome gating.
Antioxidants & redox signaling Jun, 2012 | Pubmed ID: 22229461
Analysis of the organic hydroperoxide response of Chromobacterium violaceum reveals that OhrR is a cys-based redox sensor regulated by thioredoxin.
PloS one , 2012 | Pubmed ID: 23071722
The essential gene YMR134W from Saccharomyces cerevisiae is important for appropriate mitochondrial iron utilization and the ergosterol biosynthetic pathway.
FEBS letters Sep, 2013 | Pubmed ID: 23892078
Redox regulation of the proteasome via S-glutathionylation.
Redox biology Dec, 2013 | Pubmed ID: 24396728
20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: implications for the degradation of oxidized proteins.
Archives of biochemistry and biophysics Sep, 2014 | Pubmed ID: 24813691
How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily.
The Journal of biological chemistry Mar, 2015 | Pubmed ID: 25666622
The Roles of Peroxiredoxin and Thioredoxin in Hydrogen Peroxide Sensing and in Signal Transduction.
Molecules and cells Jan, 2016 | Pubmed ID: 26813662
Catalytic Thr or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms.
Scientific reports 09, 2016 | Pubmed ID: 27629822
Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite.
Proceedings of the National Academy of Sciences of the United States of America 01, 2017 | Pubmed ID: 28028230
Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2.
The Journal of biological chemistry 05, 2017 | Pubmed ID: 28348082
Functional and evolutionary characterization of Ohr proteins in eukaryotes reveals many active homologs among pathogenic fungi.
Redox biology 08, 2017 | Pubmed ID: 28391181
Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments.
The Journal of biological chemistry 10, 2017 | Pubmed ID: 28821623
Effects of mild running on substantia nigra during early neurodegeneration.
Journal of sports sciences Jun, 2018 | Pubmed ID: 28895489
Structural insights on the efficient catalysis of hydroperoxide reduction by Ohr: Crystallographic and molecular dynamics approaches.
PloS one , 2018 | Pubmed ID: 29782551
Analyses of the three 1-Cys Peroxiredoxins from Aspergillus fumigatus reveal that cytosolic Prx1 is central to HO metabolism and virulence.
Scientific reports 08, 2018 | Pubmed ID: 30120327
Mild Exercise Differently Affects Proteostasis and Oxidative Stress on Motor Areas During Neurodegeneration: A Comparative Study of Three Treadmill Running Protocols.
Neurotoxicity research Feb, 2019 | Pubmed ID: 30276717
Rapid peroxynitrite reduction by human peroxiredoxin 3: Implications for the fate of oxidants in mitochondria.
Free radical biology & medicine 01, 2019 | Pubmed ID: 30391677
Global analysis of erythroid cells redox status reveals the involvement of Prdx1 and Prdx2 in the severity of beta thalassemia.
PloS one , 2018 | Pubmed ID: 30521599
Non-Mammalian Prdx6 Enzymes (Proteins with 1-Cys Prdx Mechanism) Display PLA₂ Activity Similar to the Human Orthologue.
Antioxidants (Basel, Switzerland) Mar, 2019 | Pubmed ID: 30832204
Mutations of Cys and Ser residues in the α5-subunit of the 20S proteasome from Saccharomyces cerevisiae affects gating and chronological lifespan.
Archives of biochemistry and biophysics 05, 2019 | Pubmed ID: 30940569
The bicarbonate/carbon dioxide pair increases hydrogen peroxide-mediated hyperoxidation of human peroxiredoxin 1.
The Journal of biological chemistry 09, 2019 | Pubmed ID: 31366734
The Peroxidatic Thiol of Peroxiredoxin 1 is Nitrosated by Nitrosoglutathione but Coordinates to the Dinitrosyl Iron Complex of Glutathione.
Antioxidants (Basel, Switzerland) Mar, 2020 | Pubmed ID: 32218363
Reduction of sulfenic acids by ascorbate in proteins, connecting thiol-dependent to alternative redox pathways.
Free radical biology & medicine 08, 2020 | Pubmed ID: 32615144
Molecular Structure and Functional Analysis of Pyocin S8 from Pseudomonas aeruginosa Reveals the Essential Requirement of a Glutamate Residue in the H-N-H Motif for DNase Activity.
Journal of bacteriology 10, 2020 | Pubmed ID: 32817098
Oxidative Modification of Proteins: From Damage to Catalysis, Signaling, and Beyond.
Antioxidants & redox signaling Apr, 2021 | Pubmed ID: 33726509
Relevance of peroxiredoxins in pathogenic microorganisms.
Applied microbiology and biotechnology Jul, 2021 | Pubmed ID: 34258640
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