ArticleBiomolecular NMR assignments2018
Solution NMR assignment of the C-terminal domain of human chTOG.
Article in Biomolecular NMR assignments, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 8 citations in OpenAlex.
- Molecular insight into microtubule nucleation by the XMAP215/γ-TuRC module.Nature communications · 2026Article
- Structural characterization and inhibition of the interaction between ch-TOG and TACC3.The Journal of cell biology · 2025Article
- Mechanism of how the universal module XMAP215 γ-TuRC nucleates microtubules.bioRxiv : the preprint server for biology · 2024Article
- TACC3-ch-TOG interaction regulates spindle microtubule assembly by controlling centrosomal recruitment of γ-TuRC.Bioscience reports · 2023Article
- How Microtubules Build the Spindle Branch by Branch.Annual review of cell and developmental biology · 2022Review
- Solution NMR Structure of Titin N2A Region Ig Domain I83 and Its Interaction with Metal Ions.Journal of molecular biology · 2021Article
- Development of a Potential Yeast-Based Vaccine Platform forFrontiers in immunology · 2021Article
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4 authors at 2 institutions in 1 country.
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Abstract
The microtubule regulatory protein colonic and hepatic tumor overexpressed gene (chTOG), also known as cytoskeleleton associated protein 5 (CKAP5) plays an important role in organizing the cytoskeleton and in particular in the assembly of k-fibres in mitosis. Recently, we dissected the hitherto poorly understood C-terminus of this protein by discovering two new domains-a cryptic TOG domain (TOG6) and a smaller, helical domain at the very C-terminus. It was shown that the C-terminal domain is important for the interaction with the TACC domain in TACC3 during the assembly of k-fibres in a ternary complex that also includes clathrin. Here we now present the solution NMR assignment of the chTOG C-terminal domain which confirms our earlier prediction that it is mainly made of α-helices. However, the appearance of the
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