ArticleStructure (London, England : 1993)2019
Selection and Characterization of Artificial Proteins Targeting the Tubulin α Subunit.
Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- A coherent structural picture of the interaction of Tau with tubulin provides a link to its aggregation.The Journal of biological chemistry · 2026Review
- Microtubule dynamics and post-translational modifications in cardiovascular diseases: mechanisms and therapeutic implications.Frontiers in cardiovascular medicine · 2026Review
- Cryo-EM structures of the tubulin cofactors reveal the molecular basis of alpha/beta-tubulin biogenesis.Nature communications · 2025Article
- Preparation of Polarity-Marked Microtubules Using a Plus-End Capping DARPin.Bio-protocol · 2024Article
- HURP binding to the vinca domain of β-tubulin accounts for cancer drug resistance.Nature communications · 2024Article
- The minus-end depolymerase KIF2A drives flux-like treadmilling of γTuRC-uncapped microtubules.The Journal of cell biology · 2023Article
- Diverse cytomotive actins and tubulins share a polymerization switch mechanism conferring robust dynamics.Science advances · 2023Article
- Design, synthesis, and characterization of protein origami based on self-assembly of a brick and staple artificial protein pair.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Computational Approaches to the Rational Design of Tubulin-Targeting Agents.Biomolecules · 2023Review
- Structural convergence for tubulin binding of CPAP and vinca domain microtubule inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The molecular biology of tubulinopathies: Understanding the impact of variants on tubulin structure and microtubule regulation.Frontiers in cellular neuroscience · 2022Review
- Comprehensive Analysis of Binding Sites in Tubulin.Angewandte Chemie (International ed. in English) · 2021Article
- Macromolecular interactions in vitro, comparing classical and novel approaches.European biophysics journal : EBJ · 2021Article
- Insight into microtubule nucleation from tubulin-capping proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Microtubules are cytoskeletal filaments of eukaryotic cells made of αβ-tubulin heterodimers. Structural studies of non-microtubular tubulin rely mainly on molecules that prevent its self-assembly and are used as crystallization chaperones. Here we identified artificial proteins from an αRep library that are specific to α-tubulin. Turbidity experiments indicate that these αReps impede microtubule assembly in a dose-dependent manner and total internal reflection fluorescence microscopy further shows that they specifically block growth at the microtubule (-) end. Structural data indicate that they do so by targeting the α-tubulin longitudinal surface. Interestingly, in one of the complexes studied, the α subunit is in a conformation that is intermediate between the ones most commonly observed in X-ray structures of tubulin and those seen in the microtubule, emphasizing the plasticity of tubulin. These α-tubulin-specific αReps broaden the range of tools available for the mechanistic study of microtubule dynamics and its regulation.
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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.