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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Leslie B. Poole

Department of Biochemistry

Center for Structural Biology

Wake Forest University School of Medicine


United States


Name/email consistency: high



  • Department of Biochemistry, Center for Structural Biology, Wake Forest University School of Medicine, Winston-Salem, United States. 2000 - 2008


  1. Discovering mechanisms of signaling-mediated cysteine oxidation. Poole, L.B., Nelson, K.J. Curr. Opin. Chem. Biol (2008) [Pubmed]
  2. Fluorescent and affinity-based tools to detect cysteine sulfenic acid formation in proteins. Poole, L.B., Klomsiri, C., Knaggs, S.A., Furdui, C.M., Nelson, K.J., Thomas, M.J., Fetrow, J.S., Daniel, L.W., King, S.B. Bioconjug. Chem. (2007) [Pubmed]
  3. Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases. Poole, L.B. Arch. Biochem. Biophys. (2005) [Pubmed]
  4. Synthesis of chemical probes to map sulfenic acid modifications on proteins. Poole, L.B., Zeng, B.B., Knaggs, S.A., Yakubu, M., King, S.B. Bioconjug. Chem. (2005) [Pubmed]
  5. Protein sulfenic acids in redox signaling. Poole, L.B., Karplus, P.A., Claiborne, A. Annu. Rev. Pharmacol. Toxicol. (2004) [Pubmed]
  6. Streptococcus mutans H2O2-forming NADH oxidase is an alkyl hydroperoxide reductase protein. Poole, L.B., Higuchi, M., Shimada, M., Calzi, M.L., Kamio, Y. Free Radic. Biol. Med. (2000) [Pubmed]
  7. 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. Poole, L.B., Godzik, A., Nayeem, A., Schmitt, J.D. Biochemistry (2000) [Pubmed]
  8. AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase. Poole, L.B., Reynolds, C.M., Wood, Z.A., Karplus, P.A., Ellis, H.R., Li Calzi, M. Eur. J. Biochem. (2000) [Pubmed]
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