A mathematical model for protein-induced lipid vesicle leakage: Interaction of the intermediate filament protein vimentin and its isolated N-terminus with phosphatidylinositol vesicles

This publication has 18 references indexed in Scilit:

• Specific interaction of the intermediate filament protein vimentin and its isolated N-terminus with negatively charged phospholipids as determined by vesicle aggregation, fusion, and leakage measurements
  Biochemistry, 1990
• Phosphorylation in vitro of vimentin by protein kinases A and C is restricted to the head domain
  European Journal of Biochemistry, 1989
• Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure
  Biochemistry, 1989
• Cyclic AMP‐dependent protein kinase‐induced vimentin filament disassembly involves modification of the N‐terminal domain of intermediate filament subunits
  FEBS Letters, 1988
• Protein-Chemical Identification of the Major Cleavage Sites of the Ca^2⊕Proteinase on Murine Vimentin, the Mesenchymal Intermediate Filament Protein
  Biological Chemistry Hoppe-Seyler, 1986
• Site specificity in vimentin-membrane interactions: intermediate filament subunits associate with the plasma membrane via their head domains.
  The Journal of cell biology, 1985
• The binding of vimentin to human erythrocyte membranes: a model system for the study of intermediate filament-membrane interactions.
  The Journal of cell biology, 1985
• Amino acid sequence characterization of mammalian vimentin, the mesenchymal intermediate filament protein
  FEBS Letters, 1983
• Proteinchemical characterization of three structurally distinct domains along the protofilament unit of desmin 10 nm filaments
  Cell, 1982
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976