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Proceedings of the National Academy of Sciences of the United States of America|March 15, 2000
Design and properties of human D-amino acid oxidase with covalently attached flavinA A Raibekas, K Fukui, V MasseyBiochemistry|October 10, 2001
Studies of the mechanism of phenol hydroxylase: mutants Tyr289Phe, Asp54Asn, and Arg281MetD Xu, D P Ballou, V MasseyBiochemistry|September 12, 2001
Mechanistic studies of cyclohexanone monooxygenase: chemical properties of intermediates involved in catalysisD Sheng, D P Ballou, V MasseyThe Journal of Biological Chemistry|March 18, 1994
Lactate monooxygenase. III. Additive contributions of active site residues to catalytic efficiency and stabilization of an anionic transition stateU Müh, C H Williams, V MasseyBiochemistry|March 24, 1987
Identification of methionine-110 as the residue covalently modified in the electrophilic inactivation of D-amino-acid oxidase by O-(2,4-dinitrophenyl) hydroxylamineC D'Silva, C H Williams, V MasseyAnalytical Biochemistry|September 1, 1989
Determination of the dead time of a stopped-flow fluorometerP Brissette, D P Ballou, V MasseyThe Journal of Biological Chemistry|November 10, 1979
Covalent adducts of lactate oxidase. Photochemical formation and structure identificationS Ghisla, V Massey, Y S ChoongThe Journal of Biological Chemistry|September 10, 1979
Properties of flavins where the 8-methyl group is replaced by mercapto- residuesE G Moore, S Ghisla, V MasseyThe Journal of Biological Chemistry|October 10, 1979
8-Mercaptoflavins as active site probes of flavoenzymesV Massey, S Ghisla, E G MooreThe Journal of Biological Chemistry|December 25, 1992
p-Hydroxyphenylacetate-3-hydroxylase. A two-protein component enzymeU Arunachalam, V Massey, C S VaidyanathanPageof 28