Properties of the 120,000- and 95,000-dalton actin-binding proteins from Dictyostelium discoideum and their possible functions in assembling the cytoplasmic matrix

@article{Condeelis1984PropertiesOT,
  title={Properties of the 120,000- and 95,000-dalton actin-binding proteins from Dictyostelium discoideum and their possible functions in assembling the cytoplasmic matrix},
  author={J. Condeelis and M. Vahey and J. Carboni and J. Demey and S. Ogihara},
  journal={The Journal of Cell Biology},
  year={1984},
  volume={99},
  pages={119s - 126s}
}
The cell cortex of Dictyostelium amebae contains an actin-rich cytoplasmic matrix. Changes in geometry of this matrix are believed to regulate protrusive activity and motility of the cell cortex. Two actin-binding proteins (120,000 and 95,000 daltons [120K and 95K]) are present in the cell cortex, and their properties, many of which are described here for the first time, suggest that they regulate growth and organization of cortical microfilaments. The 120K protein is a flexible dimer 35 nm in… Expand
A Dictyostelium mutant lacking an F-actin cross-linking protein, the 120-kD gelation factor
Isolation of actin-binding proteins from Dictyostelium discoideum.
The regulation of actin polymerization and cross-linking in Dictyostelium.
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