1H, 13C and 15N backbone resonance assignments of the dimeric yeast peroxiredoxin YLR109w.

Verdoucq L, Vignols F, Jacquot JP, Chartier Y, Meyer Y.
In vivo characterization of a thioredoxin h target protein defines a new
peroxiredoxin family.
J Biol Chem. 1999 Jul 9;274(28):19714-22.

In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family.

Crystal Structure Of Peroxiredoxin Ahp1 From Saccharomyces Cerevisiae In Oxidized Form

Crystal Structure Of Peroxiredoxin Ahp1 From Saccharomyces Cerevisiae In Reduced Form

Crystal Structure Of Peroxiredoxin Ahp1 From Saccharomyces Cerevisiae In Complex With Thioredoxin Trx2

Crystal Structure Of Ahp1 From Saccharomyces Cerevisiae In Reduced Form

K7_Ahp1p [Saccharomyces cerevisiae Kyokai no. 7]

unnamed protein product [Saccharomyces cerevisiae]

alkyl hydroperoxide reductase [Saccharomyces cerevisiae YJM789]

alkyl hydroperoxide reductase [Saccharomyces cerevisiae RM11-1a]

YLR109Wp-like protein [Saccharomyces cerevisiae AWRI1631]

RecName: Full=Peroxiredoxin type-2; AltName: Full=AHPC1; AltName: Full=Cytoplasmic thiol peroxidase 3; Short=cTPx 3; AltName: F

TPA: Ahp1p [Saccharomyces cerevisiae S288c]

Backbone 1H, 13C, and 15N Chemical Shift Assignment of The Dimer Yeast
Peroxiredoxin YLR109w

The sample was reduced by 5 DTT equvalents.