We previously reported a potent tubulin inhibitor CH-2-77. In this study, we optimized the
structure of CH-2-77 by blocking metabolically labile sites and synthesized a series of CH-2 …

The colchicine binding site of tubulin is a promising target for discovering novel antitumor
agents which exert the antiangiogenic effect and are not susceptible to multidrug resistance …

Targeting the colchicine binding site on tubulin is a promising strategy to develop cancer
therapeutics. Herein, we describe our systematic structure–activity relationship studies of …

Due to the three domains of the colchicine-site which is conducive to the combination with
small molecule compounds, colchicine-site on the tubulin has become a common target for …

Polymerization of tubulin dimers to form microtubules is one of the key events in cell
proliferation. The inhibition of this event has long been recognized as a potential treatment …

Tubulin inhibitors that bind to the colchicine site are widely studied anticancer agents. In
continuous our researches, we designed a series of novel indazole derivatives as …

Based on our prior antitumor hits, 32 novel N-alkyl-N-substituted phenylpyridin-2-amine
derivatives were designed, synthesized and evaluated for cytotoxic activity against A549 …

Microtubules (composed of α-and β-tubulin heterodimers) play a pivotal role in mitosis and
cell division, and are regarded as an excellent target for chemotherapeutic agents to treat …

Small molecules that interact with the colchicine binding site in tubulin have demonstrated
therapeutic efficacy in treating cancers. We report the design, syntheses, and antitumor …

We report the design, synthesis, and biological evaluation of heterocyclic-fused pyrimidines
as tubulin polymerization inhibitors targeting the colchicine binding site with significantly …