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D J Graves

Showing results (11-20 of 136) with videos related to

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Biochemistry|March 26, 1991
Calcineurin-catalyzed reaction with phosphite and phosphate esters of tyrosineH Wang, D J Graves
Biochemistry|May 22, 1973
On the hysteretic response of rabbit skeletal muscle phosphorylase kinaseG Kim, D J Graves
The Journal of Biological Chemistry|July 13, 2001
An inhibitory segment of the catalytic subunit of phosphorylase kinase does not act as a pseudosubstrateC Bartleson, D J Graves
Biochemistry|April 25, 2001
The amino-terminal tail of glycogen phosphorylase is a switch for controlling phosphorylase conformation, activation, and response to ligandsA C Biorn, D J Graves
The Journal of Biological Chemistry|March 10, 1979
Use of an antibody probe to study regulation of glycogen phosphorylase by its NH2-terminal regionA M Janski, D J Graves
The Journal of Biological Chemistry|December 10, 1976
Stimulation of phosphorylase kinase autophosphorylation by peptide analogs of phosphorylaseG M Carlson, D J Graves
The Journal of Biological Chemistry|April 10, 1978
Kinetic mechanism and specificity of the phosphorylase kinase reactionL B Tabatabai, D J Graves
The Journal of Biological Chemistry|May 25, 1982
Rabbit skeletal muscle phosphorylase kinase. Catalytic and regulatory properties of the active alpha gamma delta and gamma delta complexesK F Chan, D J Graves
The Journal of Biological Chemistry|April 5, 1986
Isolation and properties of the active gamma subunit of phosphorylase kinaseS M Kee, D J Graves
Biochemistry|May 8, 1973
Chemistry of the adenosine monophosphate site of rabbit muscle glycogen phosphorylase. I. Hydrophobic nature and affinity labeling of the allosteric siteR A Anderson, D J Graves
Pageof 14

Showing results (11-20 of 136) with videos related to

Sort By:
Pageof 14
Biochemistry|March 26, 1991
Calcineurin-catalyzed reaction with phosphite and phosphate esters of tyrosineH Wang, D J Graves
Biochemistry|May 22, 1973
On the hysteretic response of rabbit skeletal muscle phosphorylase kinaseG Kim, D J Graves
The Journal of Biological Chemistry|July 13, 2001
An inhibitory segment of the catalytic subunit of phosphorylase kinase does not act as a pseudosubstrateC Bartleson, D J Graves
Biochemistry|April 25, 2001
The amino-terminal tail of glycogen phosphorylase is a switch for controlling phosphorylase conformation, activation, and response to ligandsA C Biorn, D J Graves
The Journal of Biological Chemistry|March 10, 1979
Use of an antibody probe to study regulation of glycogen phosphorylase by its NH2-terminal regionA M Janski, D J Graves
The Journal of Biological Chemistry|December 10, 1976
Stimulation of phosphorylase kinase autophosphorylation by peptide analogs of phosphorylaseG M Carlson, D J Graves
The Journal of Biological Chemistry|April 10, 1978
Kinetic mechanism and specificity of the phosphorylase kinase reactionL B Tabatabai, D J Graves
The Journal of Biological Chemistry|May 25, 1982
Rabbit skeletal muscle phosphorylase kinase. Catalytic and regulatory properties of the active alpha gamma delta and gamma delta complexesK F Chan, D J Graves
The Journal of Biological Chemistry|April 5, 1986
Isolation and properties of the active gamma subunit of phosphorylase kinaseS M Kee, D J Graves
Biochemistry|May 8, 1973
Chemistry of the adenosine monophosphate site of rabbit muscle glycogen phosphorylase. I. Hydrophobic nature and affinity labeling of the allosteric siteR A Anderson, D J Graves
Pageof 14