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J S Nishimura

Showing results (1-10 of 41) with videos related to

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Advances in Enzymology and Related Areas of Molecular Biology|January 1, 1986
Succinyl-CoA synthetase structure-function relationships and other considerationsJ S Nishimura
Biochimica Et Biophysica Acta|July 15, 1970
The inactivation and dissociation of Escherichia coli succinyl-CoA synthetase by sulfhydryl reagentsF Grinnell, J S Nishimura
The Journal of Biological Chemistry|August 10, 1984
Adenosine 5'-O-(3-thio)triphosphate, a substrate and potent inhibitor of Escherichia coli succinyl-CoA synthetase. Additional evidence for a cooperative alternating-sites mechanismJ S Nishimura, T Mitchell
The Journal of Biological Chemistry|February 25, 1984
Escherichia coli succinyl coenzyme A synthetase. Inhibition of ATP-stimulated succinate----succinyl coenzyme A exchange at low succinyl coenzyme A concentrations by an ADP trapJ S Nishimura, T Mitchell
The Journal of Biological Chemistry|February 25, 1985
Reaction of substrates with 35S-thiophosphorylated succinyl-CoA synthetase of pig heart. Similarities to the case of the Escherichia coli enzymeJ S Nishimura, T Mitchell
The Journal of Biological Chemistry|November 25, 1980
Affinity chromatography and affinity labeling of rat liver succinyl-CoA synthetaseD J Ball, J S Nishimura
The Journal of Biological Chemistry|November 5, 1991
Site-directed mutagenesis of Escherichia coli succinyl-CoA synthetase. Histidine 142 alpha is a facilitative catalytic residueG X Luo, J S Nishimura
The Journal of Biological Chemistry|May 15, 1992
Adenosine 5'-tetraphosphate is synthesized by the histidine alpha 142----asparagine mutant of Escherichia coli succinyl-CoA synthetaseG X Luo, J S Nishimura
Journal of Bacteriology|December 1, 1972
Phenoxazinone synthetase from Streptomyces antibioticus: multiple activities of the enzymeE E Golub, J S Nishimura
The Journal of Biological Chemistry|July 25, 1975
Escherichia coli succinic thiolinase. Stoichiometry of phosphorylation and coenzyme A bindingC M Bowman, J S Nishimura
Pageof 5

Showing results (1-10 of 41) with videos related to

Sort By:
Pageof 5
Advances in Enzymology and Related Areas of Molecular Biology|January 1, 1986
Succinyl-CoA synthetase structure-function relationships and other considerationsJ S Nishimura
Biochimica Et Biophysica Acta|July 15, 1970
The inactivation and dissociation of Escherichia coli succinyl-CoA synthetase by sulfhydryl reagentsF Grinnell, J S Nishimura
The Journal of Biological Chemistry|August 10, 1984
Adenosine 5'-O-(3-thio)triphosphate, a substrate and potent inhibitor of Escherichia coli succinyl-CoA synthetase. Additional evidence for a cooperative alternating-sites mechanismJ S Nishimura, T Mitchell
The Journal of Biological Chemistry|February 25, 1984
Escherichia coli succinyl coenzyme A synthetase. Inhibition of ATP-stimulated succinate----succinyl coenzyme A exchange at low succinyl coenzyme A concentrations by an ADP trapJ S Nishimura, T Mitchell
The Journal of Biological Chemistry|February 25, 1985
Reaction of substrates with 35S-thiophosphorylated succinyl-CoA synthetase of pig heart. Similarities to the case of the Escherichia coli enzymeJ S Nishimura, T Mitchell
The Journal of Biological Chemistry|November 25, 1980
Affinity chromatography and affinity labeling of rat liver succinyl-CoA synthetaseD J Ball, J S Nishimura
The Journal of Biological Chemistry|November 5, 1991
Site-directed mutagenesis of Escherichia coli succinyl-CoA synthetase. Histidine 142 alpha is a facilitative catalytic residueG X Luo, J S Nishimura
The Journal of Biological Chemistry|May 15, 1992
Adenosine 5'-tetraphosphate is synthesized by the histidine alpha 142----asparagine mutant of Escherichia coli succinyl-CoA synthetaseG X Luo, J S Nishimura
Journal of Bacteriology|December 1, 1972
Phenoxazinone synthetase from Streptomyces antibioticus: multiple activities of the enzymeE E Golub, J S Nishimura
The Journal of Biological Chemistry|July 25, 1975
Escherichia coli succinic thiolinase. Stoichiometry of phosphorylation and coenzyme A bindingC M Bowman, J S Nishimura
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