Studies on vinca domain binding drugs were done in great details by a number of workers as it is recognized as a potential target for anticancer drug development. Their structures, properties, mode of action, success and failures as potential anticancer drug have been discussed in short details in this review. Among these drugs rhizoxin and maytansine are competitive inhibitors, and bind at the vinblastine binding site of tubulin where as others are non-competitive inhibitors. Besides binding, these drugs also differ in the extent of GTP hydrolysis, GTP exchange and in the stabilization of colchicine binding site. The toxicity level of these drugs towards the host cells and the extent of efflux of drugs by the P-glycoprotein mediated pump a...
International audienceVinblastine is one of several tubulin-targeting Vinca alkaloids that have been...
Microtubules are high dynamic protein filaments fundamental for cells growth and proliferation. Henc...
Tubulin possesses two distinct binding sites for vinblastine; one of high affinity (Ka = 6.2 X 106M ...
Studies on vinca domain binding drugs were done in great details by a number of workers as it is rec...
Tubulin is the primary target of an ever growing number of natural, semisynthetic and synthetic prod...
Microtubules (MTs) play important and diverse roles in eukaryotic cells. Their function and biophysi...
Microtubules (MTs) play important and diverse roles in eukaryotic cells. Their function and biophysi...
International audienceVinca-domain ligands are compounds that bind to tubulin at its inter-heterodim...
Two independent approaches provide evidence of cysteine residues in the vicinity of the binding site...
53 p.-7 fig.+ 7 p.-1 tab.supl.-6 fig.supl. Saez Calvo, Gonzalo et al.Microtubule-targeting agents (M...
Tubulin targeting agents constitute an important class of anticancer drugs. By acting either as micr...
Tubulin targeting agents constitute an important class of anticancer drugs. By acting either as micr...
Tubulin targeting agents constitute an important class of anticancer drugs. By acting either as micr...
International audienceSome hybrids of vinca alkaloids and phomopsin A, linked by a glycine pattern, ...
173 p.-60 fig.-10 tab.-2 anexos.Nowadays, one of the major public health issues in developed countri...
International audienceVinblastine is one of several tubulin-targeting Vinca alkaloids that have been...
Microtubules are high dynamic protein filaments fundamental for cells growth and proliferation. Henc...
Tubulin possesses two distinct binding sites for vinblastine; one of high affinity (Ka = 6.2 X 106M ...
Studies on vinca domain binding drugs were done in great details by a number of workers as it is rec...
Tubulin is the primary target of an ever growing number of natural, semisynthetic and synthetic prod...
Microtubules (MTs) play important and diverse roles in eukaryotic cells. Their function and biophysi...
Microtubules (MTs) play important and diverse roles in eukaryotic cells. Their function and biophysi...
International audienceVinca-domain ligands are compounds that bind to tubulin at its inter-heterodim...
Two independent approaches provide evidence of cysteine residues in the vicinity of the binding site...
53 p.-7 fig.+ 7 p.-1 tab.supl.-6 fig.supl. Saez Calvo, Gonzalo et al.Microtubule-targeting agents (M...
Tubulin targeting agents constitute an important class of anticancer drugs. By acting either as micr...
Tubulin targeting agents constitute an important class of anticancer drugs. By acting either as micr...
Tubulin targeting agents constitute an important class of anticancer drugs. By acting either as micr...
International audienceSome hybrids of vinca alkaloids and phomopsin A, linked by a glycine pattern, ...
173 p.-60 fig.-10 tab.-2 anexos.Nowadays, one of the major public health issues in developed countri...
International audienceVinblastine is one of several tubulin-targeting Vinca alkaloids that have been...
Microtubules are high dynamic protein filaments fundamental for cells growth and proliferation. Henc...
Tubulin possesses two distinct binding sites for vinblastine; one of high affinity (Ka = 6.2 X 106M ...