Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Docking Study of Ligands into the Colchicine Binding Site of Tubulin

1 Dec 2004

Abstract excerpt

Cancer is a major cause of mortality in developed countries, following only cardiovascular diseases. Death of cancerous cells can be achieved by stopping mitosis and the antimitotic class of drugs formed by the spindle poisons can be used for this purpose. Their role is to disorganize the mitotic spindle by targeting its main constituent, the microtubules, themselves made of heterodimers of alpha and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to 14-3-3 protein interactions
Share to Cancer Treatment and Pharmacology
Share to Microtubule and mitosis dynamics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 15662957
DOI: 10.1080/14756360412331280545

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Docking Study of Ligands into the Colchicine Binding Site of TubulinPMID 15662957Read ↗

Recent advances in research of colchicine binding site inhibitors and their interaction modes with tubulin.Semantic proximity Read ↗

Antiproliferative Activity and Molecular Docking of Novel Double-Modified Colchicine DerivativesSemantic proximity Read ↗

Discovery of Small Molecule Inhibitors that Interact with γ‐TubulinSemantic proximity Read ↗

Design and Biological Evaluation of Novel Tubulin Inhibitors as Antimitotic Agents Using a Pharmacophore Binding Model with TubulinSemantic proximity Read ↗

Mechanisms of Tubulin Binding Ligands to Target Cancer Cells: Updates on their Therapeutic Potential and Clinical TrialsSemantic proximity Read ↗

Discovery of new quinolines as potent colchicine binding site inhibitors: design, synthesis, docking studies, and anti-proliferative evaluationSemantic proximity Read ↗

PM534, an Optimized Target-Protein Interaction Strategy through the Colchicine Site of TubulinSemantic proximity Read ↗

Differential colchicine-binding across eukaryotic families: the role of highly conserved Pro268beta and Ala248beta residues in animal tubulin.Semantic proximity Read ↗

Microtubulin Binding Sites as Target for Developing Anticancer AgentsSemantic proximity Read ↗

Structure-Based Pharmacophore Design and Virtual Screening for Novel Tubulin Inhibitors with Potential Anticancer ActivitySemantic proximity Read ↗

Microtubules and Cell Division: Potential Pharmacological Targets in Cancer TherapySemantic proximity Read ↗

Computational Approaches to the Rational Design of Tubulin-Targeting AgentsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.