about
Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite.Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments.Structural insights on the efficient catalysis of hydroperoxide reduction by Ohr: Crystallographic and molecular dynamics approaches.Analyses of the three 1-Cys Peroxiredoxins from Aspergillus fumigatus reveal that cytosolic Prx1 is central to HO metabolism and virulenceNon-Mammalian Prdx6 Enzymes (Proteins with 1-Cys Prdx Mechanism) Display PLA₂ Activity Similar to the Human OrthologueExpression of human HSP27 in yeast extends replicative lifespan and uncovers a hormetic responseThe Peroxidatic Thiol of Peroxiredoxin 1 is Nitrosated by Nitrosoglutathione but Coordinates to the Dinitrosyl Iron Complex of GlutathioneThe bicarbonate/carbon dioxide pair increases hydrogen peroxide-mediated hyperoxidation of human peroxiredoxin 1Thiol Peroxidases as Major Regulators of Intracellular Levels of Peroxynitrite in Live Saccharomyces cerevisiae Cells
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description
researcher
@en
name
Luis E S Netto
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type
label
Luis E S Netto
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prefLabel
Luis E S Netto
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P31
P496
0000-0002-4250-9177