Intrasteric regulation of calmodulin-dependent protein kinases

Adv Pharmacol. 1996:36:221-49. doi: 10.1016/s1054-3589(08)60584-0.
No abstract available

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Caenorhabditis elegans Proteins
  • Calcium-Calmodulin-Dependent Protein Kinases / physiology*
  • Calmodulin-Binding Proteins / chemistry
  • Catalysis
  • Enzyme Activation / physiology
  • Models, Molecular
  • Molecular Sequence Data
  • Muscle Proteins / chemistry
  • Myosin-Light-Chain Kinase / classification
  • Myosin-Light-Chain Kinase / physiology
  • Phosphorylase Kinase / physiology
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Regulatory Sequences, Nucleic Acid / physiology

Substances

  • Caenorhabditis elegans Proteins
  • Calmodulin-Binding Proteins
  • Muscle Proteins
  • unc-22 protein, C elegans
  • Phosphorylase Kinase
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Myosin-Light-Chain Kinase