K-252a, a novel microbial product, inhibits smooth muscle myosin light chain kinase.

This publication has 27 references indexed in Scilit:

• K-252 compounds, novel and potent inhibitors of protein kinase C and cyclic nucleotide-dependent protein kinases
  Biochemical and Biophysical Research Communications, 1986
• Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA
  Biochemistry, 1986
• The modulatory role of myosin light chain phosphorylation in human platelet activation
  Biochemical and Biophysical Research Communications, 1986
• Amino acid sequence of an active fragment of rabbit skeletal muscle myosin light chain kinase
  Biochemistry, 1985
• An aortic spontaneously active phosphatase dephosphorylates myosin and inhibits actin-myosin interaction
  Biochemical and Biophysical Research Communications, 1983
• Ca2+-induced hydrophobic site on calmodulin: Application for purification of calmodulin by phenyl-Sepharose affinity chromatography
  Biochemical and Biophysical Research Communications, 1982
• Lack of tissue specificity of calmodulin: A rapid and high‐yield purification method
  FEBS Letters, 1981
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976
• Myosin light‐chain kinase, a new enzyme from striated muscle
  FEBS Letters, 1974
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970