Results 171 to 180 of about 33,744 (220)
Upregulated PKM2 Protects Dopaminergic Neurons From Oxidative Damage Through Nrf2 Transactivation in an MPTP-Induced Mouse Model of Parkinson's Disease. [PDF]
CNS Neurosci TherMei M +6 more
europepmc +1 more source
Corrigendum to "Systematic Characterization of Prognostic Values of Peroxiredoxin Family in Gastric Cancer". [PDF]
Biomed Res Inteuropepmc +1 more source
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Biological Chemistry, 2002
Present knowledge on peroxiredoxins is reviewed with special emphasis on catalytic principles, specificities and biological function. Peroxiredoxins are low efficiency peroxidases using thiols as reductants. They appear to be fairly promiscuous with respect to the hydroperoxide substrate; the specificities for the donor substrate vary considerably ...
Birgit, Hofmann +2 more
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Present knowledge on peroxiredoxins is reviewed with special emphasis on catalytic principles, specificities and biological function. Peroxiredoxins are low efficiency peroxidases using thiols as reductants. They appear to be fairly promiscuous with respect to the hydroperoxide substrate; the specificities for the donor substrate vary considerably ...
Birgit, Hofmann +2 more
openaire +2 more sources
Peroxiredoxins in the Lung with Emphasis on Peroxiredoxin VI
2007All six mammalian peroxiredoxins are expressed in the lung. Peroxiredoxin (Prx) VI is the isoform expressed at the highest level and its lung expression exceeds that for other organs. The predominant location of Prx VI is the cytosol and acidic organelles of Clara cells of the conducting airways and type II epithelial cells and macrophages in the ...
Bruno, Schremmer +3 more
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Annual Review of Plant Biology, 2003
Peroxiredoxins (Prxs) are abundant low-efficiency peroxidases located in distinct cell compartments including the chloroplast and mitochondrion. They are grouped into four clans based on their structural and biochemical properties. The catalytic center contains a cysteinyl residue that reduces diverse peroxides and is regenerated via intramolecular or
openaire +2 more sources
Peroxiredoxins (Prxs) are abundant low-efficiency peroxidases located in distinct cell compartments including the chloroplast and mitochondrion. They are grouped into four clans based on their structural and biochemical properties. The catalytic center contains a cysteinyl residue that reduces diverse peroxides and is regenerated via intramolecular or
openaire +2 more sources
Structural Survey of the Peroxiredoxins
2007Peroxiredoxins (Prxs) are ubiquitous proteins that use an active site Cys residue to reduce hydroperoxides. Structural studies since the first Prx structure was determined in 1998 have produced 35 crystal structures of wild type and mutant Prxs with at least one representative structure from each of the five major evolutionary subfamilies of Prxs ...
P Andrew, Karplus, Andrea, Hall
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2007
Some members of the Prx family are up-regulated in cells under stress conditions. Prx I is the major cytoplasmic Prx and is known as a stress-inducible antioxidant enzyme. Various stress agents or conditions activate Prx I gene expression in vitro and in vivo.
Tetsuro, Ishii, Toru, Yanagawa
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Some members of the Prx family are up-regulated in cells under stress conditions. Prx I is the major cytoplasmic Prx and is known as a stress-inducible antioxidant enzyme. Various stress agents or conditions activate Prx I gene expression in vitro and in vivo.
Tetsuro, Ishii, Toru, Yanagawa
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2000
Abstract The peroxiredoxin family is a widely distributed class of enzymes that directly reduce H2O2 and other hydroperoxides, with hydrogen derived from NAD(P)H, by different routes (1). Two highly conserved cysteine residues are revealed by alignment of the peroxiredoxin family members.
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Abstract The peroxiredoxin family is a widely distributed class of enzymes that directly reduce H2O2 and other hydroperoxides, with hydrogen derived from NAD(P)H, by different routes (1). Two highly conserved cysteine residues are revealed by alignment of the peroxiredoxin family members.
openaire +1 more source