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Results:
1-11
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Results: 11
Authors:
Ritz, D
Lim, J
Reynolds, CM
Poole, LB
Beckwith, J
Citation: D. Ritz et al., Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion, SCIENCE, 294(5540), 2001, pp. 158-160
Authors:
Baker, LMS
Raudonikiene, A
Hoffman, PS
Poole, LB
Citation: Lms. Baker et al., Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: Genetic and kinetic characterization, J BACT, 183(6), 2001, pp. 1961-1973
Authors:
Wood, ZA
Poole, LB
Karplus, PA
Citation: Za. Wood et al., Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis, BIOCHEM, 40(13), 2001, pp. 3900-3911
Authors:
Reynolds, CM
Poole, LB
Citation: Cm. Reynolds et Lb. Poole, Activity of one of two engineered heterodimers of AhpF, the NADH : peroxiredoxin oxidoreductase from Salmonella typhimurium, reveals intrasubunit electron transfer between domains, BIOCHEM, 40(13), 2001, pp. 3912-3919
Authors:
Yamamoto, Y
Higuchi, M
Poole, LB
Kamio, Y
Citation: Y. Yamamoto et al., Identification of a new gene responsible for the oxygen tolerance in aerobic life of Streptococcus mutans, BIOS BIOT B, 64(5), 2000, pp. 1106-1109
Authors:
Poole, LB
Higuchi, M
Shimada, M
Li Calzi, M
Kamio, Y
Citation: Lb. Poole et al., Streptococcus mutans H2O2-forming NADH oxidase is an alkyl hydroperoxide reductase protein, FREE RAD B, 28(1), 2000, pp. 108-120
Authors:
Yamamoto, Y
Higuchi, M
Poole, LB
Kamio, Y
Citation: Y. Yamamoto et al., Role of the dpr product in oxygen tolerance in Streptococcus mutans, J BACT, 182(13), 2000, pp. 3740-3747
Authors:
Poole, LB
Reynolds, CM
Wood, ZA
Karplus, PA
Ellis, HR
Calzi, ML
Citation: Lb. Poole et al., AhpF and other NADH : peroxiredoxin oxidoreductases, homologues of low M-rthioredoxin reductase, EUR J BIOCH, 267(20), 2000, pp. 6126-6133
Authors:
Reynolds, CM
Poole, LB
Citation: Cm. Reynolds et Lb. Poole, Attachment of the N-terminal domain of Salmonella typhimurium AhpF to Escherichia coli thioredoxin reductase confers AhpC reductase activity but doesnot affect thioredoxin reductase activity, BIOCHEM, 39(30), 2000, pp. 8859-8869
Authors:
Poole, LB
Godzik, A
Nayeem, A
Schmitt, JD
Citation: Lb. Poole et al., AhpF can be dissected into two functional units: Tandem repeats of two thioredoxin-like folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like C-terminus to AhpC, BIOCHEM, 39(22), 2000, pp. 6602-6615
Authors:
Higuchi, M
Yamamoto, Y
Poole, LB
Shimada, M
Sato, Y
Takahashi, N
Kamio, Y
Citation: M. Higuchi et al., Functions of two types of NADH oxidases in energy metabolism and oxidativestress of Streptococcus mutans, J BACT, 181(19), 1999, pp. 5940-5947
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