R
Ruoli Bai
Researcher at National Institutes of Health
Publications - 90
Citations - 4093
Ruoli Bai is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Tubulin & Microtubule. The author has an hindex of 32, co-authored 79 publications receiving 3742 citations. Previous affiliations of Ruoli Bai include Leidos & Science Applications International Corporation.
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Halichondrin B and homohalichondrin B, marine natural products binding in the vinca domain of tubulin. Discovery of tubulin-based mechanism of action by analysis of differential cytotoxicity data.
TL;DR: Halichondrin B was compared with other agents which interfere with the binding of vinca alkaloids to tubulin in terms of its effects on tubulin polymerization, inhibition of GTP hydrolysis, inhibited of nucleotide exchange, and stabilization of tubulin, as well as the quantitative assessment of its effect on vincA alkaloid binding and inhibition of cell growth.
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Dolastatin 10, a powerful cytostatic peptide derived from a marine animal: Inhibition of tubulin polymerization mediated through the vinca alkaloid binding domain
TL;DR: Pettit et al. as mentioned in this paper showed that dolastatin 10 inhibited tubulin polymerization and the binding of radiolabeled vinblastine to tubulin.
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Binding of dolastatin 10 to tubulin at a distinct site for peptide antimitotic agents near the exchangeable nucleotide and vinca alkaloid sites.
TL;DR: A tripeptide segment of dolastatin 10 also effectively inhibits tubulin polymerization and GTP hydrolysis and did not significantly inhibit either vincristine binding or nucleotide exchange, nor did it stabilize colchicine binding.
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Synthesis and Biological Evaluation of Dihydrobenzofuran Lignans and Related Compounds as Potential Antitumor Agents that Inhibit Tubulin Polymerization
TL;DR: 2-phenyl-dihydrobenzofuran derivatives constitute a new group of antimitotic and potential antitumor agents that inhibit tubulin polymerization.
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Identification of cysteine 354 of beta-tubulin as part of the binding site for the A ring of colchicine.
Ruoli Bai,Xue-Feng Pei,Olivier Boyé,Zelleka Getahun,Surinder Grover,Joseph Bekisz,N Y Nguyen,Arnold Brossi,Arnold Brossi,Ernest Hamel +9 more
TL;DR: This finding indicates that the C-3 oxygen atom of colchicinoids is within 3 Å of the sulfur atom of the Cys-354 residue, and suggests that the col chicine A ring lies between Cys -354 and CYS-239, based on the known 9 Å distance between these residues.