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D Parsonage

Showing results (21-30 of 31) with videos related to

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Biochemistry|May 30, 1995
Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg 303S S Mande, D Parsonage, A Claiborne, et al.
Biochemistry|October 31, 1995
Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron-reduced enzyme formsE J Crane, D Parsonage, L B Poole, et al.
Journal of Bacteriology|February 29, 2000
The RofA binding site in Streptococcus pyogenes is utilized in multiple transcriptional pathwaysA B Granok, D Parsonage, R P Ross, et al.
The Journal of Biological Chemistry|July 5, 1987
The defective proton-ATPase of uncA mutants of Escherichia coli. Identification by DNA sequencing of residues in the alpha-subunit which are essential for catalysis or normal assemblyM B Maggio, J Pagan, D Parsonage, et al.
Biochemistry|July 21, 1992
Barnase has subsites that give rise to large rate enhancementsA G Day, D Parsonage, S Ebel, et al.
Advances in Protein Chemistry|October 23, 2001
Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulationA Claiborne, T C Mallett, J I Yeh, et al.
Biochemistry|April 18, 1995
An L40C mutation converts the cysteine-sulfenic acid redox center in enterococcal NADH peroxidase to a disulfideH Miller, S S Mande, D Parsonage, et al.
The Journal of Biological Chemistry|May 5, 1987
The defective proton-ATPase of uncD mutants of Escherichia coli. Identification by DNA sequencing of residues in the beta-subunit which are essential for catalysis or normal assemblyD Parsonage, T M Duncan, S Wilke-Mounts, et al.
Biochemistry|November 26, 1999
Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulationA Claiborne, J I Yeh, T C Mallett, et al.
The Journal of Biological Chemistry|May 30, 1997
Cloning and sequencing of two enterococcal glpK genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system-catalyzed phosphorylation of a single histidyl residueV Charrier, E Buckley, D Parsonage, et al.
Pageof 4

Showing results (21-30 of 31) with videos related to

Sort By:
Pageof 4
Biochemistry|May 30, 1995
Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg 303S S Mande, D Parsonage, A Claiborne, et al.
Biochemistry|October 31, 1995
Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron-reduced enzyme formsE J Crane, D Parsonage, L B Poole, et al.
Journal of Bacteriology|February 29, 2000
The RofA binding site in Streptococcus pyogenes is utilized in multiple transcriptional pathwaysA B Granok, D Parsonage, R P Ross, et al.
The Journal of Biological Chemistry|July 5, 1987
The defective proton-ATPase of uncA mutants of Escherichia coli. Identification by DNA sequencing of residues in the alpha-subunit which are essential for catalysis or normal assemblyM B Maggio, J Pagan, D Parsonage, et al.
Biochemistry|July 21, 1992
Barnase has subsites that give rise to large rate enhancementsA G Day, D Parsonage, S Ebel, et al.
Advances in Protein Chemistry|October 23, 2001
Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulationA Claiborne, T C Mallett, J I Yeh, et al.
Biochemistry|April 18, 1995
An L40C mutation converts the cysteine-sulfenic acid redox center in enterococcal NADH peroxidase to a disulfideH Miller, S S Mande, D Parsonage, et al.
The Journal of Biological Chemistry|May 5, 1987
The defective proton-ATPase of uncD mutants of Escherichia coli. Identification by DNA sequencing of residues in the beta-subunit which are essential for catalysis or normal assemblyD Parsonage, T M Duncan, S Wilke-Mounts, et al.
Biochemistry|November 26, 1999
Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulationA Claiborne, J I Yeh, T C Mallett, et al.
The Journal of Biological Chemistry|May 30, 1997
Cloning and sequencing of two enterococcal glpK genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system-catalyzed phosphorylation of a single histidyl residueV Charrier, E Buckley, D Parsonage, et al.
Pageof 4