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- W2922388086 endingPage "331" @default.
- W2922388086 startingPage "310" @default.
- W2922388086 abstract "Microtubules are a protein which is made of α- and β-heterodimer. It is one of the main components of the cell which play a vital role in cell division especially in G2/M-phase. It exists in equilibrium dynamic of polymerization and depolymerization of α- and β-heterodimer. It is one of the best targets for developing anti-cancer drugs. Various natural occurring molecules are well known for their anti-tubulin effect such as vinca, paclitaxel, combretastatin, colchicine etc. These microtubule-targeted drugs are acted through two processes (i) inhibiting depolymerization of tubulin (tubulin stabilizing agents) and (ii) inhibiting polymerization of tubulin (tubulin destabilizing agents). Now days, various binding domains have been explore through which these molecules are binding to tubulin but the three major binding domain of tubulin are taxol, vinca and colchicine binding domain. The present article mainly focus on the classification of various naturally occurring compounds on the basis of their inhibition processes (depolymerization and polymerization) and the site of interaction (targets taxol, vinca and colchicine binding domain) which has been hitherto reported. By placing all the naturally occurring taxol, vinca and colchicine binding site analogues at one place makes a better understanding of the tubulin interactions with known natural tubulin binders that would helps in the discovery of new and potent natural, semi-synthetic and synthetic analogues for treating cancer." @default.
- W2922388086 created "2019-03-22" @default.
- W2922388086 creator A5054723639 @default.
- W2922388086 creator A5064704034 @default.
- W2922388086 creator A5084229883 @default.
- W2922388086 creator A5091578726 @default.
- W2922388086 date "2019-06-01" @default.
- W2922388086 modified "2023-10-11" @default.
- W2922388086 title "Anti-tubulin agents of natural origin: Targeting taxol, vinca, and colchicine binding domains" @default.
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