Evidence map›Paper›PMID 37345829›Full record

ArticleeLife2023

Differential modification of the C-terminal tails of different α-tubulins and their importance for microtubule function in vivo.

Mengjing Bao, Ruth E Dörig, Paula Maria Vazquez-Pianzola, Dirk Beuchle, Beat Suter

Open access · goldAbstract read
In one paragraph

Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

6 citing papers in PubMed, 7 citations in OpenAlex.

  1. Regulatory landscape of widespread stop codon readthrough inbioRxiv : the preprint server for biology · 2026
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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

5 authors at 1 institution in 2 countries.

Mengjing BaoInstitute of Cell Biology, University of Bern, Bern, Switzerland.
Ruth E DörigInstitute of Cell Biology, University of Bern, Bern, Switzerland.
Paula Maria Vazquez-PianzolaInstitute of Cell Biology, University of Bern, Bern, Switzerland.
Dirk BeuchleInstitute of Cell Biology, University of Bern, Bern, Switzerland.
Beat SuterInstitute of Cell Biology, University of Bern, Bern, Switzerland.ORCID 0000-0002-0510-746X
University of Bern · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubules (MTs) are built from α-/β-tubulin dimers and used as tracks by kinesin and dynein motors to transport a variety of cargos, such as mRNAs, proteins, and organelles, within the cell. Tubulins are subjected to several post-translational modifications (PTMs). Glutamylation is one of them, and it is responsible for adding one or more glutamic acid residues as branched peptide chains to the C-terminal tails of both α- and β-tubulin. However, very little is known about the specific modifications found on the different tubulin isotypes in vivo and the role of these PTMs in MT transport and other cellular processes in vivo. In this study, we found that in

Indexed as

KinesinsTubulinAnimalsDrosophilaGlutamic AcidMicrotubulesProtein Processing, Post-TranslationalGlutamic AcidKinesinsTubulinaxonal transportcell biologydevelopmental biologyD. melanogastermicrotubule transportoogenesisTttamylation

Identifiers

PMID37345829
PMCPMC10335831
OpenAlexW4381597356

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.