Actin polymerization. The mechanism of action of cytochalasin D.

This publication has 33 references indexed in Scilit:

• Cytochalasin B slows but does not prevent monomer addition at the barbed end of the actin filament.
  The Journal of cell biology, 1986
• Lack of nucleotide cleavage on the binding of G-actin-ATP to plasma gelsolin
  FEBS Letters, 1985
• Plasma actin depolymerizing factor has both calcium-dependent and calcium-independent effects on actin
  Biochemistry, 1983
• Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization
  Journal of Muscle Research and Cell Motility, 1983
• Cytochalasin D and platelet gelsolin accelerate actin polymer formation. A model for regulation of the extent of actin polymer formation in vivo
  Biochemistry, 1982
• Mechanism of action of cytochalasin: evidence that it binds to actin filament ends.
  The Journal of cell biology, 1981
• Mechanism of action of cytochalasin B on actin
  Cell, 1980
• Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation.
  The Journal of cell biology, 1980
• Cytochalasin inhibits the rate of elongation of actin filament fragments
  The Journal of cell biology, 1979
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976