Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 330

The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.

Eribulin Binds at Microtubule Ends to a Single Site on Tubulin To Suppress Dynamic Instability

Open access
Smith, Jennifer A., Wilson, Leslie, Azarenko, Olga, Zhu, Xiaojie, Lewis, Bryan M., Littlefield, Bruce A., Jordan, Mary Ann·2010·Biochemistry
DOI 10.1021/bi901810u
Open this paper in CoChat — free account

Abstract

Eribulin mesylate (E7389), a synthetic analogue of the marine natural product halichondrin B, is in phase III clinical trials for the treatment of cancer. Eribulin targets microtubules, suppressing dynamic instability at microtubule plus ends through an inhibition of microtubule growth with little or no effect on shortening [Jordan, M. A., et al. (2005) Mol. Cancer Ther. 4, 1086-1095]. Using [(3)H]eribulin, we found that eribulin binds soluble tubulin at a single site; however, this binding is complex with an overall K(d) of 46 microM, but also showing a real or apparent very high affinity (K(d) = 0.4 microM) for a subset of 25% of the tubulin. Eribulin also binds microtubules with a maximum stoichiometry of 14.7 +/- 1.3 molecules per microtubule (K(d) = 3.5 microM), strongly suggesting the presence of a relatively high-affinity binding site at microtubule ends. At 100 nM, the concentration that inhibits microtubule plus end growth by 50%, we found that one molecule of eribulin is bound per two microtubules, indicating that the binding of a single eribulin molecule at a microtubule end can potently inhibit its growth. Eribulin does not suppress dynamic instability at microtubule minus ends. Preincubation of microtubules with 2 or 4 microM vinblastine induced additional lower-affinity eribulin binding sites, most likely at splayed microtubule ends. Overall, our results indicate that eribulin binds with high affinity to microtubule plus ends and thereby suppresses dynamic instability.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1021/bi901810u

Cites

28 of 28 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 28 references

Cited by

See all 330

Metadata

Authors
Smith, J. A., Wilson, L., Azarenko, O., Zhu, X., Lewis, B. M., Littlefield, B. A., & Jordan, M. A.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2010-01-20
Volume
49
Issue
6
Pages
1331-1337
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi901810u
OpenAlex
W2018563247
Cited by
330
References
28
FWCI
6.49
Type
journal article
Language
en
Open access
green

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Eribulin Binds at Microtubule Ends to a Single Site on Tubulin To Suppress Dynamic Instability. https://app.cochat.ai/papers/10.1021/bi901810u
The paper
Smith, J. A., Wilson, L., Azarenko, O., Zhu, X., Lewis, B. M., Littlefield, B. A., & Jordan, M. A. (2010). Eribulin Binds at Microtubule Ends to a Single Site on Tubulin To Suppress Dynamic Instability. Biochemistry. https://doi.org/10.1021/bi901810u

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.