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

Macromolecular Interaction of Halichondrin B Analogues Eribulin (E7389) and ER-076349 with Tubulin by Analytical Ultracentrifugation

8 Jul 2009

Abstract excerpt

Halichondrin B is an antimitotic drug that inhibits microtubule assembly. To understand the molecular details of its interaction with tubulin, we investigated the binding of two halichondrin B analogues, eribulin (previously, ER-086526, E7389) and ER-076349, to tubulin by quantitative analytical ultracentrifugation. Eribulin is currently undergoing phase III clinical trials for cancer; ER-076349 is a closely...

Read the complete abstract on PubMed

Topics

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

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: 19586046
DOI: 10.1021/bi900776u

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 · 8 closest

Macromolecular Interaction of Halichondrin B Analogues Eribulin (E7389) and ER-076349 with Tubulin by Analytical UltracentrifugationPMID 19586046Read ↗

Eribulin Binds at Microtubule Ends to a Single Site on Tubulin To Suppress Dynamic InstabilitySemantic proximity Read ↗

The primary antimitotic mechanism of action of the synthetic halichondrin E7389 is suppression of microtubule growthSemantic proximity Read ↗

Structural basis for drug resistance conferred by β-tubulin mutations: a molecular modeling study on native and mutated tubulin complexes with epothilone B.Semantic proximity Read ↗

Tubulin-based Structure-affinity Relationships for Antimitotic Vinca AlkaloidsSemantic proximity Read ↗

Hallmarks of Molecular Action of Microtubule Stabilizing AgentsSemantic proximity Read ↗

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

The Coral-Derived Natural Products Eleutherobin and Sarcodictyins A and B: Effects on the Assembly of Purified Tubulin with and without Microtubule-Associated Proteins and Binding at the Polymer Taxoid SiteSemantic proximity Read ↗

Tubulin-Interactive Natural Products as Anticancer AgentsSemantic proximity Read ↗

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