Evidence map›Paper›PMID 18787557›Full record

ArticleEMBO reports2008

Structural insight into the inhibition of tubulin by vinca domain peptide ligands.

Anthony Cormier, Matthieu Marchand, Raimond B G Ravelli, Marcel Knossow, Benoît Gigant

Open access · greenAbstract read
In one paragraph

Article in EMBO reports, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

46 citing papers in PubMed, 164 citations in OpenAlex.

  1. Review
  2. Impact of C-Terminal AmideMolecules (Basel, Switzerland) · 2026
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  7. Design, synthesis, and bioevaluation of 1Journal of enzyme inhibition and medicinal chemistry · 2024
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  9. More than just an eagle killer: The freshwater cyanobacteriumProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Review
  11. Review
  12. The interaction of spongistatin 1 with tubulin.Archives of biochemistry and biophysics · 2022
    Article
  13. Structural convergence for tubulin binding of CPAP and vinca domain microtubule inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Interaction of diazonamide A with tubulin.Archives of biochemistry and biophysics · 2020
    Article
  18. Article
  19. Article
  20. Review
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

5 authors at 3 institutions in 2 countries.

Anthony CormierLaboratoire d'Enzymologie et Biochimie Structurales, CNRS, Bat. 34, 1 avenue de la Terrasse, 91198 Gif-sur-Yvette, France.
Matthieu Marchand
Raimond B G Ravelli
Marcel Knossow
Benoît Gigant
Laboratoire d'Enzymologie et Biochimie Structurales · FRCentre National de la Recherche Scientifique · FREuropean Molecular Biology Laboratory · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tubulin vinca domain is the target of widely different microtubule inhibitors that interfere with the binding of vinblastine. Although all these ligands inhibit the hydrolysis of GTP, they affect nucleotide exchange to variable extents. The structures of two vinca domain antimitotic peptides--phomopsin A and soblidotin (a dolastatin 10 analogue)--bound to tubulin in a complex with a stathmin-like domain show that their sites partly overlap with that of vinblastine and extend the definition of the vinca domain. The structural data, together with the biochemical results from the ligands we studied, highlight two main contributors in nucleotide exchange: the flexibility of the tubulin subunits' arrangement at their interfaces and the residues in the carboxy-terminal part of the beta-tubulin H6-H7 loop. The structures also highlight common features of the mechanisms by which vinca domain ligands favour curved tubulin assemblies and destabilize microtubules.

Indexed as

LigandsMicrotubulesModels, MolecularMycotoxinsOligopeptidesProtein Structure, TertiaryTubulinVinblastineLigandsMycotoxinsOligopeptidesphomopsinsoblidotinTubulinVinblastine

Identifiers

PMID18787557
PMCPMC2581847
OpenAlexW2008447052

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.