Evidence map›Paper›PMID 34309396›Full record

ArticleJournal of bacteriology2021

Sirtuin-Dependent Reversible Lysine Acetylation Controls the Activity of Acetyl Coenzyme A Synthetase in Campylobacter jejuni.

Victoria L Jeter, Jorge C Escalante-Semerena

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of bacteriology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 51% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
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 at 1 institution in 1 country.

Victoria L JeterDepartment of Microbiology, University of Georgia, Athens, Georgia, USA.ORCID 0000-0001-7267-466X
Jorge C Escalante-SemerenaDepartment of Microbiology, University of Georgia, Athens, Georgia, USA.ORCID 0000-0001-7428-2811
University of Georgia · US

Funding

Analysis of the Metabolic Capabilities of Prokaryotic CellsR35GM130399 · NIGMS · UNIVERSITY OF GEORGIA · PI JORGE C ESCALANTE · 2019 to 2026
$5.5M
NIGMS NIH HHS R35 GM130399
6 · The paper itself

Abstract

Posttranslational modifications are mechanisms for rapid control of protein function used by cells from all domains of life. Acetylation of the epsilon amino group (

Indexed as

AcetylationAmino Acid SequenceCampylobacter jejuniCoenzyme A LigasesGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicLysineSirtuinsCoenzyme A LigasesLysineSirtuinsacetyl-CoA synthetaseCampylobacter jejuniCobB sirtuin deacylaseGCN5-related acetyltransferasesGNATsposttranslational modificationsprotein acetylationreversible lysine acetylation

Identifiers

PMID34309396
PMCPMC8459764
OpenAlexW3185823781

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.