Latrunculin alters the actin-monomer subunit interface to prevent polymerization

@article{Morton2000LatrunculinAT,
  title={Latrunculin alters the actin-monomer subunit interface to prevent polymerization},
  author={W. M. Morton and K. Ayscough and P. Mclaughlin},
  journal={Nature Cell Biology},
  year={2000},
  volume={2},
  pages={376-378}
}
atrunculin-A is a drug that is capable of rapidly, reversibly and specifically disrupting the actin cytoskeleton. The efficacy of its action has made it a compound of choice in many cell-biology laboratories, supplanting the classic actin-depolymerizing drug cytochalasin-D. One reason for this is that the mode of action of latrunculin seems to be less complex than that of cytochalasin. Whereas the latter affects the kinetics of actin-filament polymerization at both the barbed and pointed ends… Expand
452 Citations
Tropomodulin 3 Binds to Actin Monomers*
Actin binding proteins: regulation of cytoskeletal microfilaments.
ATPase activity and conformational changes in the regulation of actin.
  • H. Schüler
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 2001
Biomolecular mimicry in the actin cytoskeleton: Mechanisms underlying the cytotoxicity of kabiramide C and related macrolides
  • J. Tanaka, Y. Yan, +4 authors G. Marriott
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 2003
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 16 REFERENCES
Domain motions in actin.
Atomic model of the actin filament
Crystallization of the complex of actin with gelsolin segment 1.
Refinement of macromolecular structures by the maximum-likelihood method.
...
1
2
...