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

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Department of Biochemistry and Molecular Pharmacology

West Virginia University School of Medicine

Morgantown

WV 26506

USA

Name/email consistency: high

Department of Biochemistry and Molecular Pharmacology, West Virginia University School of Medicine, Morgantown, WV 26506, USA. 2002 - 2007
Laboratory of Pharmacology and Chemistry, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, USA. 2000

Bicarbonate and active site zinc modulate the self-peroxidation of bovine copper-zinc superoxide dismutase. Gunther, M.R., Donahue, J.A. Free Radic. Res. (2007) [Pubmed]
Probing the free radicals formed in the metmyoglobin-hydrogen peroxide reaction. Gunther, M.R. Free Radic. Biol. Med. (2004) [Pubmed]
Expression of a familial amyotrophic lateral sclerosis-associated mutant human superoxide dismutase in yeast leads to decreased mitochondrial electron transport. Gunther, M.R., Vangilder, R., Fang, J., Beattie, D.S. Arch. Biochem. Biophys. (2004) [Pubmed]
Tryptophan-14 is the preferred site of DBNBS spin trapping in the self-peroxidation reaction of sperm whale metmyoglobin with a single equivalent of hydrogen peroxide. Gunther, M.R., Tschirret-Guth, R.A., Lardinois, O.M., Ortiz de Montellano, P.R. Chem. Res. Toxicol. (2003) [Pubmed]
Histidinyl radical formation in the self-peroxidation reaction of bovine copper-zinc superoxide dismutase. Gunther, M.R., Peters, J.A., Sivaneri, M.K. J. Biol. Chem. (2002) [Pubmed]
A long-lived tyrosyl radical from the reaction between horse metmyoglobin and hydrogen peroxide. Gunther, M.R., Sturgeon, B.E., Mason, R.P. Free Radic. Biol. Med. (2000) [Pubmed]