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N D Meadow

Showing results (1-10 of 23) with videos related to

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The Journal of Biological Chemistry|December 27, 1996
Rate and equilibrium constants for phosphoryltransfer between active site histidines of Escherichia coli HPr and the signal transducing protein IIIGlcN D Meadow, S Roseman
The Journal of Biological Chemistry|December 10, 1982
Sugar transport by the bacterial phosphotransferase system. Isolation and characterization of a glucose-specific phosphocarrier protein (IIIGlc) from Salmonella typhimuriumN D Meadow, S Roseman
The Journal of Biological Chemistry|October 15, 1986
Phosphate transfer between acetate kinase and enzyme I of the bacterial phosphotransferase systemD K Fox, N D Meadow, S Roseman
The Journal of Biological Chemistry|November 25, 1987
Sugar transport by the bacterial phosphotransferase system. Reconstitution of inducer exclusion in Salmonella typhimurium membrane vesiclesT P Misko, W J Mitchell, N D Meadow, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 1, 1987
II-BGlc, a glucose receptor of the bacterial phosphotransferase system: molecular cloning of ptsG and purification of the receptor from an overproducing strain of Escherichia coliC L Bouma, N D Meadow, E W Stover, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 1, 1982
Molecular cloning of the crr gene and evidence that it is the structural gene for IIIGlc, a phosphocarrier protein of the bacterial phosphotransferase systemN D Meadow, D W Saffen, R P Dottin, et al.
Biochemistry|May 16, 1998
Cation-promoted association of Escherichia coli phosphocarrier protein IIAGlc with regulatory target protein glycerol kinase: substitutions of a Zinc(II) ligand and implications for inducer exclusionD W Pettigrew, N D Meadow, S Roseman, et al.
Protein Science : a Publication of the Protein Society|April 1, 1993
Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniquesJ G Pelton, D A Torchia, N D Meadow, et al.
Biochemistry|June 9, 1992
Structural comparison of phosphorylated and unphosphorylated forms of IIIGlc, a signal-transducing protein from Escherichia coli, using three-dimensional NMR techniquesJ G Pelton, D A Torchia, N D Meadow, et al.
The Journal of Biological Chemistry|October 15, 1986
Limited proteolysis of IIIGlc, a regulatory protein of the phosphoenolpyruvate:glycose phosphotransferase system, by membrane-associated enzymes from Salmonella typhimurium and Escherichia coliN D Meadow, P Coyle, A Komoryia, et al.
Pageof 3

Showing results (1-10 of 23) with videos related to

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Pageof 3
The Journal of Biological Chemistry|December 27, 1996
Rate and equilibrium constants for phosphoryltransfer between active site histidines of Escherichia coli HPr and the signal transducing protein IIIGlcN D Meadow, S Roseman
The Journal of Biological Chemistry|December 10, 1982
Sugar transport by the bacterial phosphotransferase system. Isolation and characterization of a glucose-specific phosphocarrier protein (IIIGlc) from Salmonella typhimuriumN D Meadow, S Roseman
The Journal of Biological Chemistry|October 15, 1986
Phosphate transfer between acetate kinase and enzyme I of the bacterial phosphotransferase systemD K Fox, N D Meadow, S Roseman
The Journal of Biological Chemistry|November 25, 1987
Sugar transport by the bacterial phosphotransferase system. Reconstitution of inducer exclusion in Salmonella typhimurium membrane vesiclesT P Misko, W J Mitchell, N D Meadow, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 1, 1987
II-BGlc, a glucose receptor of the bacterial phosphotransferase system: molecular cloning of ptsG and purification of the receptor from an overproducing strain of Escherichia coliC L Bouma, N D Meadow, E W Stover, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 1, 1982
Molecular cloning of the crr gene and evidence that it is the structural gene for IIIGlc, a phosphocarrier protein of the bacterial phosphotransferase systemN D Meadow, D W Saffen, R P Dottin, et al.
Biochemistry|May 16, 1998
Cation-promoted association of Escherichia coli phosphocarrier protein IIAGlc with regulatory target protein glycerol kinase: substitutions of a Zinc(II) ligand and implications for inducer exclusionD W Pettigrew, N D Meadow, S Roseman, et al.
Protein Science : a Publication of the Protein Society|April 1, 1993
Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniquesJ G Pelton, D A Torchia, N D Meadow, et al.
Biochemistry|June 9, 1992
Structural comparison of phosphorylated and unphosphorylated forms of IIIGlc, a signal-transducing protein from Escherichia coli, using three-dimensional NMR techniquesJ G Pelton, D A Torchia, N D Meadow, et al.
The Journal of Biological Chemistry|October 15, 1986
Limited proteolysis of IIIGlc, a regulatory protein of the phosphoenolpyruvate:glycose phosphotransferase system, by membrane-associated enzymes from Salmonella typhimurium and Escherichia coliN D Meadow, P Coyle, A Komoryia, et al.
Pageof 3