Homologous calcium-binding proteins in the activation of skeletal, cardiac, and smooth muscle myosin light chain kinases.

This publication has 29 references indexed in Scilit:

• Evolutionary diversification of structure and function in the family of intracellular calcium-binding proteins
  Journal of Molecular Evolution, 1979
• A new large-scale purification procedure for muscular parvalbumins
  Biochimie, 1979
• Activation of phosphorylase kinase from rabbit skeletal muscle by calmodulin and troponin
  FEBS Letters, 1979
• Magnesium and calcium binding to parvalbumins: evidence for differences between parvalbumins and an explanation of their relaxing function
  Biochemistry, 1979
• Modulator protein as a component of the myosin light chain kinase from chicken gizzard
  Biochemistry, 1978
• Effect of the troponin C‐like protein from bovine brain (brain modulator protein) on the Mg²⁺‐stimulated ATPase of skeletal muscle actomyosin
  FEBS Letters, 1976
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976
• The distribution of parvalbumins in muscle and in other tissues
  FEBS Letters, 1975
• [41] Assay of cyclic AMP-dependent protein kinases
  Published by Elsevier ,1974
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970