ArticleEMBO molecular medicine2021
Inhibiting parasite proliferation using a rationally designed anti-tubulin agent.
Article in EMBO molecular medicine, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- Adaptations in Plasmodium tubulin determine distinct microtubule architectures, mechanics and drug susceptibility.Nature communications · 2026Article
- Discovery of Peptide-Based Tubulin Inhibitors Through Structure-Guided Design.Pharmaceutics · 2026Article
- Computational discovery of potential therapeutic agents against brain-eating amoeba (Naegleria fowleri).PloS one · 2025Article
- Synthesis and biological evaluation of orally active anti-Trypanosoma agents.Bioorganic & medicinal chemistry · 2024Article
- Structural Changes, Biological Consequences, and Repurposing of Colchicine Site Ligands.Biomolecules · 2023Article
- The Tubulin Superfamily in Apicomplexan Parasites.Microorganisms · 2023Article
- Watching the release of a photopharmacological drug from tubulin using time-resolved serial crystallography.Nature communications · 2023Article
- Rational Design of a Novel Tubulin Inhibitor with a Unique Mechanism of Action.Angewandte Chemie (International ed. in English) · 2022Article
- Unveiling the Possible Oryzalin-Binding Site in the α-Tubulin ofACS omega · 2022Article
- The microtubule cytoskeleton: An old validated target for novel therapeutic drugs.Frontiers in pharmacology · 2022Review
- Systematic Analysis of Clemastine, a Candidate Apicomplexan Parasite-Selective Tubulin-Targeting Agent.International journal of molecular sciences · 2021Article
- Inhibiting parasite proliferation using a rationally designed anti-tubulin agent.EMBO molecular medicine · 2021Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
Abstract
Infectious diseases caused by apicomplexan parasites remain a global public health threat. The presence of multiple ligand-binding sites in tubulin makes this protein an attractive target for anti-parasite drug discovery. However, despite remarkable successes as anti-cancer agents, the rational development of protozoan parasite-specific tubulin drugs has been hindered by a lack of structural and biochemical information on protozoan tubulins. Here, we present atomic structures for a protozoan tubulin and microtubule and delineate the architectures of apicomplexan tubulin drug-binding sites. Based on this information, we rationally designed the parasite-specific tubulin inhibitor parabulin and show that it inhibits growth of parasites while displaying no effects on human cells. Our work presents for the first time the rational design of a species-specific tubulin drug providing a framework to exploit structural differences between human and protozoa tubulin variants enabling the development of much-needed, novel parasite inhibitors.
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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.