Member database | PANTHER |
PANTHER type | family |
Description Imported from IPR037944
References Imported from IPR037944
1.Divergence of function in the thioredoxin fold suprafamily: evidence for evolution of peroxiredoxins from a thioredoxin-like ancestor. Copley SD, Novak WR, Babbitt PC. Biochemistry 43, 13981-95, (2004). View articlePMID: 15518547
2.Recombinant peroxiredoxin 5 protects against excitotoxic brain lesions in newborn mice. Plaisant F, Clippe A, Vander Stricht D, Knoops B, Gressens P. Free Radic. Biol. Med. 34, 862-72, (2003). View articlePMID: 12654475
3.Human peroxiredoxin 5 is a peroxynitrite reductase. Dubuisson M, Vander Stricht D, Clippe A, Etienne F, Nauser T, Kissner R, Koppenol WH, Rees JF, Knoops B. FEBS Lett. 571, 161-5, (2004). View articlePMID: 15280035
4.Peroxiredoxin Ahp1 acts as a receptor for alkylhydroperoxides to induce disulfide bond formation in the Cad1 transcription factor. Iwai K, Naganuma A, Kuge S. J. Biol. Chem. 285, 10597-604, (2010). View articlePMID: 20145245
5.Distinct functional roles of peroxiredoxin isozymes and glutathione peroxidase from fission yeast, Schizosaccharomyces pombe. Kim JS, Bang MA, Lee S, Chae HZ, Kim K. BMB Rep 43, 170-5, (2010). View articlePMID: 20356456
6.Structure, mechanism and regulation of peroxiredoxins. Wood ZA, Schroder E, Robin Harris J, Poole LB. Trends Biochem. Sci. 28, 32-40, (2003). View articlePMID: 12517450
7.Crystal structure of a dimeric oxidized form of human peroxiredoxin 5. Evrard C, Capron A, Marchand C, Clippe A, Wattiez R, Soumillion P, Knoops B, Declercq JP. J. Mol. Biol. 337, 1079-90, (2004). View articlePMID: 15046979