BIOMAT Database Logo BIOMAT Database Logo

Identification of the Ca2+-dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase. 1978

P Cohen, and A Burchell, and J G Foulkes, and P T Cohen, and T C Vanaman, and C Nairn

UI MeSH Term Description Entries
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D010727 Phosphoric Diester Hydrolases A class of enzymes that catalyze the hydrolysis of one of the two ester bonds in a phosphodiester compound. EC 3.1.4. Phosphodiesterase,Phosphodiesterases,Hydrolases, Phosphoric Diester
D010764 Phosphorylase Kinase An enzyme that catalyzes the conversion of ATP and PHOSPHORYLASE B to ADP and PHOSPHORYLASE A. Glycogen Phosphorylase Kinase,Phosphorylase b Kinase,Kinase, Glycogen Phosphorylase,Kinase, Phosphorylase,Kinase, Phosphorylase b,Phosphorylase Kinase, Glycogen,b Kinase, Phosphorylase
D011494 Protein Kinases A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein. Protein Kinase,Kinase, Protein,Kinases, Protein
D002118 Calcium A basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes. Coagulation Factor IV,Factor IV,Blood Coagulation Factor IV,Calcium-40,Calcium 40,Factor IV, Coagulation
D002147 Calmodulin A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels. Calcium-Dependent Activator Protein,Calcium-Dependent Regulator,Bovine Activator Protein,Cyclic AMP-Phosphodiesterase Activator,Phosphodiesterase Activating Factor,Phosphodiesterase Activator Protein,Phosphodiesterase Protein Activator,Regulator, Calcium-Dependent,AMP-Phosphodiesterase Activator, Cyclic,Activating Factor, Phosphodiesterase,Activator Protein, Bovine,Activator Protein, Calcium-Dependent,Activator Protein, Phosphodiesterase,Activator, Cyclic AMP-Phosphodiesterase,Activator, Phosphodiesterase Protein,Calcium Dependent Activator Protein,Calcium Dependent Regulator,Cyclic AMP Phosphodiesterase Activator,Factor, Phosphodiesterase Activating,Protein Activator, Phosphodiesterase,Protein, Bovine Activator,Protein, Calcium-Dependent Activator,Protein, Phosphodiesterase Activator,Regulator, Calcium Dependent
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino

Related Publications

P Cohen, and A Burchell, and J G Foulkes, and P T Cohen, and T C Vanaman, and C Nairn
Identification of Ca2+-binding subunit of myosin light chain kinase from skeletal muscle with modulator protein.
June 1978, FEBS letters,
P Cohen, and A Burchell, and J G Foulkes, and P T Cohen, and T C Vanaman, and C Nairn
Calmodulin as an integral subunit of phosphorylase kinase from rabbit skeletal muscle.
January 1983, Methods in enzymology,
P Cohen, and A Burchell, and J G Foulkes, and P T Cohen, and T C Vanaman, and C Nairn
Phosphorylation of rabbit skeletal muscle phosphorylase kinase by cyclic GMP-dependent protein kinase.
October 1980, FEBS letters,
P Cohen, and A Burchell, and J G Foulkes, and P T Cohen, and T C Vanaman, and C Nairn
Studies of the subunit structure of rabbit skeletal muscle phosphorylase kinase.
February 1973, Biochemistry,
P Cohen, and A Burchell, and J G Foulkes, and P T Cohen, and T C Vanaman, and C Nairn
The activation of rabbit skeletal muscle phosphorylase kinase requires the binding of 3 Ca2+ per delta subunit.
March 1982, Biochemical and biophysical research communications,
P Cohen, and A Burchell, and J G Foulkes, and P T Cohen, and T C Vanaman, and C Nairn
Dephosphorylation and inactivation of phosphorylase kinase: subunit specificity of rabbit skeletal muscle protein phosphatases.
August 1984, Archives of biochemistry and biophysics,
P Cohen, and A Burchell, and J G Foulkes, and P T Cohen, and T C Vanaman, and C Nairn
Autophosphorylation of the alpha subunit of phosphorylase kinase from rabbit skeletal muscle.
August 1987, The Journal of biological chemistry,
P Cohen, and A Burchell, and J G Foulkes, and P T Cohen, and T C Vanaman, and C Nairn
Modulator protein as a Ca2+-dependent activator of rabbit skeletal myosin light-chain kinase. Purification and characterization.
November 1978, Journal of biochemistry,
P Cohen, and A Burchell, and J G Foulkes, and P T Cohen, and T C Vanaman, and C Nairn
Phosphorylase kinase from rabbit skeletal muscle.
January 1983, Methods in enzymology,
P Cohen, and A Burchell, and J G Foulkes, and P T Cohen, and T C Vanaman, and C Nairn
Identification of a calmodulin-dependent glycogen synthase kinase in rabbit skeletal muscle, distinct from phosphorylase kinase.
November 1982, FEBS letters,
Copied contents to your clipboard!