Evidence map›Paper›PMID 42681021›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Methods to Study Arginylation of Tubulin.

Brittany MacTaggart, Anna Kashina

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Brittany MacTaggartDepartment of Biomedical Sciences, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Anna KashinaDepartment of Biomedical Sciences, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA. akashina@upenn.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arginylation is a posttranslational modification in which arginine is transferred from a tRNA molecule onto a protein by arginyltransferase 1 (ATE1). Previous studies have found that Ate1 knockout causes cytoskeletal defects at both the cellular and organismal levels, but the protein targets of arginylation that mediate these effects remain poorly defined. Some of the Ate1 knockout phenotypes have been linked to β-actin arginylation, but more recently, the role of tubulin arginylation has become an active area of study. Here, we describe methods for studying the arginylation of tubulin both in vitro and from cell/tissue extracts.

Indexed as

AminoacyltransferasesArginineProtein Processing, Post-TranslationalTubulinAnimalsHumansMiceProteomicsAminoacyltransferasesArgininearginyltransferaseTubulinArginylationArginyltransferasePosttranslational modificationProteomicsTubulin

Identifiers

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Registered trials

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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.