Evidence map›Paper›PMID 26861501›Full record

ArticleScientific reports2016

Absence of N-terminal acetyltransferase diversification during evolution of eukaryotic organisms.

Om Singh Rathore, Alexandra Faustino, Pedro Prudêncio, Petra Van Damme, Cymon J Cox, Rui Gonçalo Martinho

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

27 citing papers in PubMed, 47 citations in OpenAlex.

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  17. NAA50 Is an Enzymatically ActivePlant physiology · 2020
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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.

Om Singh RathoreDepartment of Biomedical Sciences and Medicine, Faro, Portugal.
Alexandra FaustinoDepartment of Biomedical Sciences and Medicine, Faro, Portugal.
Pedro PrudêncioDepartment of Biomedical Sciences and Medicine, Faro, Portugal.
Petra Van DammeDepartment of Medical Protein Research, VIB, B-9000 Ghent, Belgium.
Cymon J CoxCenter of Marine Sciences, University of Algarve, Faro, Portugal.
Rui Gonçalo MartinhoDepartment of Biomedical Sciences and Medicine, Faro, Portugal.
Hospital de Faro EPE · PTUniversity of Algarve · PTVIB-UGent Center for Medical Biotechnology · BE

Funding

Worldwide Cancer Research 10-0553
6 · The paper itself

Abstract

Protein N-terminal acetylation is an ancient and ubiquitous co-translational modification catalyzed by a highly conserved family of N-terminal acetyltransferases (NATs). Prokaryotes have at least 3 NATs, whereas humans have six distinct but highly conserved NATs, suggesting an increase in regulatory complexity of this modification during eukaryotic evolution. Despite this, and against our initial expectations, we determined that NAT diversification did not occur in the eukaryotes, as all six major human NATs were most likely present in the Last Eukaryotic Common Ancestor (LECA). Furthermore, we also observed that some NATs were actually secondarily lost during evolution of major eukaryotic lineages; therefore, the increased complexity of the higher eukaryotic proteome occurred without a concomitant diversification of NAT complexes.

Indexed as

Biological EvolutionAcetylationAmino Acid SequenceAnimalsArabidopsisDrosophila melanogasterEukaryotic CellsGenetic VariationHumansN-Terminal AcetyltransferasesProteomeSaccharomyces cerevisiaeSequence AlignmentN-Terminal AcetyltransferasesProteome

Identifiers

PMID26861501
PMCPMC4748286
OpenAlexW2394990151

What OpenQuestion holds

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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.