Evidence map›Paper›PMID 37010771›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Development of New Tools for the Studies of Protein Arginylation.

Anna S Kashina

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. 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

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

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

1 author.

Anna S KashinaDepartment of Animal Biology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA, USA. akashina@upenn.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Studies of posttranslational modifications present many unique challenges, stemming from their role as the major drivers of biological complexity. Perhaps the most immediate challenge to researchers working on virtually any posttranslational modification is the shortage of reliable easy-to-use tools that can enable massive identification and characterization of posttranslationally modified proteins, as well as their functional modulation in vitro and in vivo. In the case of protein arginylation, which utilizes charged Arg-tRNA that is also used by the ribosomes, detection and labeling of arginylated proteins is especially difficult, because of the necessity of distinguishing these proteins from the products of conventional translation. As of now, this difficulty remains the major obstacle to new researchers entering the field. This chapter discusses some of the strategies for developing antibodies for arginylation detection, as well as some general considerations for development of other tools for studies of arginylation.

Indexed as

AminoacyltransferasesArginineProtein Processing, Post-TranslationalProteinsProteolysisAminoacyltransferasesArginineProteinsArginylation antibodiesArginylation detectionTools for the studies of posttranslational modifications

Identifiers

PMID37010771

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.