ArticleProceedings of the National Academy of Sciences of the United States of America1984
erythro-9-[3-(2-Hydroxynonyl)]adenine is an effective inhibitor of cell motility and actin assembly.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1984. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 37 citations in OpenAlex.
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- Effect of a dynein inhibitor on vasopressin action in toad urinary bladder.The Journal of physiology · 1996Article
- Mechanism of centrosome positioning during the wound response in BSC-1 cells.The Journal of cell biology · 1992Article
- Evidence for active interactions between microfilaments and microtubules in myxomycete flagellates.The Journal of cell biology · 1989Article
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- Tension and compression in the cytoskeleton of PC-12 neurites. II: Quantitative measurements.The Journal of cell biology · 1988Article
- Isolation and characterization of dynein ATPase from bull spermatozoa.The Biochemical journal · 1986Article
- Reactivation of organelle movements along the cytoskeletal framework of a giant freshwater ameba.The Journal of cell biology · 1986Article
- Physiological and ultrastructural analysis of elongating mitotic spindles reactivated in vitro.The Journal of cell biology · 1986Article
- Tension and compression in the cytoskeleton of PC 12 neurites.The Journal of cell biology · 1985Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
erythro-9-[3-(2-Hydroxynonyl)]adenine (EHNA) has been reported previously to be an agent that arrests sperm motility by inhibiting the axonemal dynein ATPase activity and has been used to probe the involvement of putative cytoplasmic dyneins in mitosis and intracellular organelle transport. We report here that EHNA profoundly and reversibly affects several actin-dependent processes, both in vivo and in vitro. It induces dramatic changes in actin organization in cultured cells, inhibits cell translocation, blocks actin-dependent cytoplasmic streaming, interferes with actin-dependent gelation of cytoplasmic extracts, and inhibits actin assembly. Just as the cytochalasins, EHNA appears to be a highly effective inhibitor of actin-based motility, whose effects in complex biological systems should be interpreted with caution.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.