ArticleProceedings of the National Academy of Sciences of the United States of America2013
Single-molecule inhibition of human kinesin by adociasulfate-13 and -14 from the sponge Cladocroce aculeata.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Review
- Cholesterol in the cargo membrane amplifies tau inhibition of kinesin-1-based transport.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Chemical and biological diversity of new natural products from marine sponges: a review (2009-2018).Marine life science & technology · 2022Review
- Targeting and extending the eukaryotic druggable genome with natural products: cytoskeletal targets of natural products.Natural product reports · 2020Review
- Profilin choreographs actin and microtubules in cells and cancer.International review of cell and molecular biology · 2020Article
- Biogenetic Relationships of Bioactive Sponge Merotriterpenoids.Marine drugs · 2017Review
- The Effect of Temperature on Microtubule-Based Transport by Cytoplasmic Dynein and Kinesin-1 Motors.Biophysical journal · 2016Article
- Axonal Transport and Neurodegeneration: How Marine Drugs Can Be Used for the Development of Therapeutics.Marine drugs · 2016Review
- Engineered kinesin motor proteins amenable to small-molecule inhibition.Nature communications · 2016Article
- Constructing 3D microtubule networks using holographic optical trapping.Scientific reports · 2015Article
- Cargo transport at microtubule crossings: evidence for prolonged tug-of-war between kinesin motors.Biophysical journal · 2015Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Two merotriterpenoid hydroquinone sulfates designated adociasulfate-13 (1) and adociasulfate-14 (2) were purified from Cladocroce aculeata (Chalinidae) along with adociasulfate-8. All three compounds were found to inhibit microtubule-stimulated ATPase activity of kinesin at 15 µM by blocking both the binding of microtubules and the processive motion of kinesin along microtubules. These findings directly show that substitution of the 5'-sulfate in 1 for a glycolic acid moiety in 2 maintains kinesin inhibition. Nomarski imaging and bead diffusion assays in the presence of adociasulfates showed no signs of either free-floating or bead-bound adociasulfate aggregates. Single-molecule biophysical experiments also suggest that inhibition of kinesin activity does not involve adociasulfate aggregation. Furthermore, both mitotic and nonmitotic kinesins are inhibited by adociasulfates to a significantly different extent. We also report evidence that microtubule binding of nonkinesin microtubule binding domains may be affected by adociasulfates.
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