Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain.

This publication has 31 references indexed in Scilit:

• Amino acid sequence of rabbit skeletal muscle myosin light chain kinase
  Biochemistry, 1986
• Interaction of calmodulin and a calmodulin-binding peptide from myosin light chain kinase: major spectral changes in both occur as the result of complex formation
  Biochemistry, 1985
• Steady‐state kinetics of skeletal muscle myosin light chain kinase indicate a strong down regulation by products
  European Journal of Biochemistry, 1985
• Amino acid sequence of an active fragment of rabbit skeletal muscle myosin light chain kinase
  Biochemistry, 1985
• Phosphorylation site sequence of smooth muscle myosin light chain (M_r = 20 000)
  FEBS Letters, 1984
• Shape and substructure of skeletal muscle myosin light chain kinase
  Biochemistry, 1983
• Skeletal muscle myosin light chain kinase
  FEBS Letters, 1983
• High affinity binding of the mastoparans by calmodulin
  Biochemical and Biophysical Research Communications, 1983
• Conformational transition accompanying the binding of calcium(2+) ion to the protein activator of 3',5'-cyclic adenosine monophosphate phosphodiesterase
  Biochemistry, 1977
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976