ArticleProceedings of the National Academy of Sciences of the United States of America1999
Selective, covalent modification of beta-tubulin residue Cys-239 by T138067, an antitumor agent with in vivo efficacy against multidrug-resistant tumors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
33 citing papers in PubMed, 162 citations in OpenAlex.
- Phase 2 study of T138067-sodium in patients with malignant glioma: Trial of the National Cancer Institute of Canada Clinical Trials Group.Neuro-oncology · 2005Trial
- Review
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- A Multipronged Approach Establishes Covalent Modification of β-Tubulin as the Mode of Action of Benzamide Anti-cancer Toxins.Journal of medicinal chemistry · 2020Article
- Allocolchicinoids bearing a Michael acceptor fragment for possible irreversible binding of tubulin.RSC medicinal chemistry · 2020Article
- Covalent modification of Cys-239 in β-tubulin by small molecules as a strategy to promote tubulin heterodimer degradation.The Journal of biological chemistry · 2019Article
- The compound millepachine and its derivatives inhibit tubulin polymerization by irreversibly binding to the colchicine-binding site in β-tubulin.The Journal of biological chemistry · 2018Article
- Novel Natural Product- and Privileged Scaffold-Based Tubulin Inhibitors Targeting the Colchicine Binding Site.Molecules (Basel, Switzerland) · 2016Review
- Signal transducer and activator of transcription 3 (STAT3) inhibitor, S3I-201, acts as a potent and non-selective alkylating agent.Oncotarget · 2016Article
- Stabilizing versus destabilizing the microtubules: a double-edge sword for an effective cancer treatment option?Analytical cellular pathology (Amsterdam) · 2015Review
- Design, synthesis, and biological evaluation of stable colchicine binding site tubulin inhibitors as potential anticancer agents.Journal of medicinal chemistry · 2014Article
- Design, synthesis, and biological evaluation of (E)-N-aryl-2-arylethenesulfonamide analogues as potent and orally bioavailable microtubule-targeted anticancer agents.Journal of medicinal chemistry · 2013Article
- Synthesis and antiproliferative activities of ottelione a analogues.ACS medicinal chemistry letters · 2012Article
- An overview of tubulin inhibitors that interact with the colchicine binding site.Pharmaceutical research · 2012Review
- Identification and mechanistic studies of a novel ubiquitin E1 inhibitor.Journal of biomolecular screening · 2012Article
- Cyclostreptin derivatives specifically target cellular tubulin and further map the paclitaxel site.Biochemistry · 2012Article
- The molecular basis that unifies the metabolism, cellular uptake and chemopreventive activities of dietary isothiocyanates.Carcinogenesis · 2012Review
- Allyl isothiocyanate arrests cancer cells in mitosis, and mitotic arrest in turn leads to apoptosis via Bcl-2 protein phosphorylation.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
13 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microtubules are linear polymers of alpha- and beta-tubulin heterodimers and are the major constituents of mitotic spindles, which are essential for the separation of chromosomes during mitosis. Here we describe a synthetic compound, 2-fluoro-1-methoxy-4-pentafluorophenylsulfonamidobenzene (T138067), which covalently and selectively modifies the beta1, beta2, and beta4 isotypes of beta-tubulin at a conserved cysteine residue, thereby disrupting microtubule polymerization. Cells exposed to T138067 become altered in shape, indicating a collapse of the cytoskeleton, and show an increase in chromosomal ploidy. Subsequently, these cells undergo apoptosis. Furthermore, T138067 exhibits cytotoxicity against tumor cell lines that exhibit substantial resistance to vinblastine, paclitaxel, doxorubicin, and actinomycin D. T138067 is also equally efficacious in inhibiting the growth of sensitive and multidrug-resistant human tumor xenografts in athymic nude mice. These observations suggest that T138067 may be clinically useful for the treatment of multidrug-resistant tumors.
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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.