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Cited by 822

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Inhibition of actin polymerization by latrunculin A

Coué, Martine, Brenner, Stephen L., Spector, Ilan, Korn, Edward D.·1987·FEBS Letters

Abstract

Latrunculin A, a toxin purified from the red sea sponge Latrunculia magnifica, was found previously to induce striking reversible changes in the morphology of mammalian cells in culture and to disrupt the organization of their microfilaments. We now provide evidence that latrunculin A affects the polymerization of pureactin in vitro in a manner consistent with the formation of a 1:1 molar complex between latrunculin A and G‐actin. The equilibrium dissociation constant (K d) for the reaction in vitro is about 0.2 μM whereas the effects of the drug on cultured cells are detectable at concentrations in the medium of 0.1–1 μM.

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Metadata

Authors
Coué, M., Brenner, S. L., Spector, I., & Korn, E. D.
Venue
FEBS Letters
Publisher
Wiley
Published
1987-03-23
Volume
213
Issue
2
Pages
316-318
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W1984210761
Cited by
822
References
1
FWCI
0.49
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Inhibition of actin polymerization by latrunculin A. https://app.cochat.ai/papers/10.1016/0014-5793(87)81513-2
The paper
Coué, M., Brenner, S. L., Spector, I., & Korn, E. D. (1987). Inhibition of actin polymerization by latrunculin A. FEBS Letters. https://doi.org/10.1016/0014-5793(87)81513-2

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.