Evidence map›Paper›PMID 33951246›Full record

ArticleAngewandte Chemie (International ed. in English)2021

Comprehensive Analysis of Binding Sites in Tubulin.

Tobias Mühlethaler, Dario Gioia, Andrea E Prota, May E Sharpe, Andrea Cavalli, Michel O Steinmetz

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

40 citing papers in PubMed, 82 citations in OpenAlex.

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  13. Identification of a ligand-binding site on tubulin mediating the tubulin-RB3 interaction.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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 3 institutions in 2 countries.

Tobias MühlethalerLaboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institut, 5232, Villigen PSI, Switzerland.ORCID 0000-0001-8437-6619
Dario GioiaComputational & Chemical Biology, Istituto Italiano di Tecnologia, via Morego, 30, 16163, Genova, Italy.ORCID 0000-0003-0560-1799
Andrea E ProtaLaboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institut, 5232, Villigen PSI, Switzerland.ORCID 0000-0003-0875-5339
May E SharpeSwiss Light Source, Paul Scherrer Institut, 5232, Villigen PSI, Switzerland.ORCID 0000-0002-3880-7438
Andrea CavalliComputational & Chemical Biology, Istituto Italiano di Tecnologia, via Morego, 30, 16163, Genova, Italy.ORCID 0000-0002-6370-1176
Michel O SteinmetzLaboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institut, 5232, Villigen PSI, Switzerland.ORCID 0000-0001-6157-3687
Paul Scherrer Institute · CHItalian Institute of Technology · ITUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tubulin plays essential roles in vital cellular activities and is the target of a wide range of proteins and ligands. Here, using a combined computational and crystallographic fragment screening approach, we addressed the question of how many binding sites exist in tubulin. We identified 27 distinct sites, of which 11 have not been described previously, and analyzed their relationship to known tubulin-protein and tubulin-ligand interactions. We further observed an intricate pocket communication network and identified 56 chemically diverse fragments that bound to 10 distinct tubulin sites. Our results offer a unique structural basis for the development of novel small molecules for use as tubulin modulators in basic research applications or as drugs. Furthermore, our method lays down a framework that may help to discover new pockets in other pharmaceutically important targets and characterize them in terms of chemical tractability and allosteric modulation.

Indexed as

LigandsAllosteric RegulationBinding SitesCrystallography, X-RayMolecular Dynamics SimulationProtein BindingTubulinTubulin ModulatorsLigandsTubulinTubulin Modulatorscrystallographic fragment screeningmicrotubulesmolecular dynamics simulationprotein-ligand interactionstubulin

Identifiers

PMID33951246
PMCPMC8251789
OpenAlexW3158446307

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.