Intrasteric regulation of calmodulin-dependent protein kinases.
Kemp
B E
BE
St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
Barden
J A
JA
Kobe
B
B
House
C
C
Parker
M W
MW
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D029742:Caenorhabditis elegans Proteins; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000502:physiology*; D002148:Calmodulin-Binding Proteins / Q000737:chemistry; D002384:Catalysis; D004789:Enzyme Activation / Q000502:physiology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000737:chemistry; D009219:Myosin-Light-Chain Kinase / Q000145:classification / Q000502:physiology; D010764:Phosphorylase Kinase / Q000502:physiology; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012045:Regulatory Sequences, Nucleic Acid / Q000502:physiology
D029742:Caenorhabditis elegans Proteins; D002148:Calmodulin-Binding Proteins; D009124:Muscle Proteins; C489233:unc-22 protein, C elegans; D010764:Phosphorylase Kinase; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D009219:Myosin-Light-Chain Kinase