Evidence map›Paper›PMID 24900887›Full record

ArticleACS medicinal chemistry letters2014

High content screening of diverse compound libraries identifies potent modulators of tubulin dynamics.

Luca Laraia, Jamie Stokes, Amy Emery, Grahame J McKenzie, Ashok R Venkitaraman, David R Spring

Open access · greenAbstract read
In one paragraph

Article in ACS medicinal chemistry letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.0field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Structures of potent anticancer compounds bound to tubulin.Protein science : a publication of the Protein Society · 2015
    Article
  5. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Luca LaraiaDepartment of Chemistry, University of Cambridge , Cambridge CB2 1EW, U.K. ; MRC Cancer Unit, University of Cambridge , Hutchison/MRC Research Centre, Biomedical Campus, Cambridge CB2 0XZ, U.K.
Jamie StokesDepartment of Chemistry, University of Cambridge , Cambridge CB2 1EW, U.K. ; MRC Cancer Unit, University of Cambridge , Hutchison/MRC Research Centre, Biomedical Campus, Cambridge CB2 0XZ, U.K.
Amy EmeryMRC Cancer Unit, University of Cambridge , Hutchison/MRC Research Centre, Biomedical Campus, Cambridge CB2 0XZ, U.K.
Grahame J McKenzieMRC Cancer Unit, University of Cambridge , Hutchison/MRC Research Centre, Biomedical Campus, Cambridge CB2 0XZ, U.K.
Ashok R VenkitaramanMRC Cancer Unit, University of Cambridge , Hutchison/MRC Research Centre, Biomedical Campus, Cambridge CB2 0XZ, U.K.
David R SpringDepartment of Chemistry, University of Cambridge , Cambridge CB2 1EW, U.K.
Hutchison/MRC Research Centre · GBUniversity of Cambridge · GB

Funding

Cancer Research UK 6934Medical Research Council G1001521Medical Research Council G1001522Medical Research Council MC_U105359877Medical Research Council MC_UU_12022/1Medical Research Council MC_UU_12022/8
6 · The paper itself

Abstract

Tubulin modulating agents such as the taxanes are among the most effective antimitotic cancer drugs, although resistance and toxicity present significant problems in their clinical use. However, most tubulin modulators are derived from complex natural products, which can make modification of their structure to address these problems difficult. Here, we report the discovery of new antimitotic compounds with simple structures that can be rapidly synthesized, through the phenotypic screening of a diverse compound library for the induction of mitotic arrest. We first identified a compound, which induced mitotic arrest in human cells at submicromolar concentrations. Its simple structure enabled rapid exploration of activity, defining a biphenylacetamide moiety required for activity, A family of analogues was synthesized, yielding optimized compounds that caused mitotic arrest and cell death in the low nanomolar range, comparable to clinically used antimitotic agents. These compounds can be synthesized in 1-3 steps and good yields. We show that one such compound targets tubulin, partially inhibiting colchicine but not vinblastine binding, suggesting that it acts allosterically to the known colchicine-binding site. Thus, our results exemplify the use of phenotypic screening to identify novel antimitotic compounds from diverse chemical libraries and characterize a family of biphenylacetamides (biphenabulins) that show promise for further development.

Indexed as

allostericantimitoticscolchicinePhenotypic screeningtubulin

Identifiers

PMID24900887
PMCPMC4027768
OpenAlexW2078177462

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.