Evidence map›Paper›PMID 26435887›Full record

ArticleWorm

New links between protein N-terminal acetylation, dauer diapause, and the insulin/IGF-1 signaling pathway in Caenorhabditis elegans.

Kurt Warnhoff, Kerry Kornfeld

Open access · bronzeAbstract read
In one paragraph

Article in Worm. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. G3 (Bethesda, Md.) · 2017
    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.

Kurt WarnhoffDepartment of Developmental Biology; Washington University School of Medicine ; St. Louis, MO USA.
Kerry KornfeldDepartment of Developmental Biology; Washington University School of Medicine ; St. Louis, MO USA.
University of Missouri–St. Louis · US

Funding

TRANSCRIPTIONAL REGULATION OF ZINC HOMEOSTASISR01GM068598 · NIGMS · WASHINGTON UNIVERSITY · PI KORNFELD, KERRY · 2003 to 2025
$5.3M
IDENTIFICATION OF DRUGS THAT DELAY AGINGR01AG026561 · NIA · WASHINGTON UNIVERSITY · PI KORNFELD, KERRY · 2006 to 2017
$3.3M
NIA NIH HHS R01 AG026561NIGMS NIH HHS R01 GM068598
6 · The paper itself

Abstract

Protein N-terminal acetylation is a widespread posttranslational modification in eukaryotes that is catalyzed by N-terminal acetyltransferases (NATs). The biochemical activity of NATs has been characterized extensively, whereas the biological function of NATs is only beginning to be defined. Here we comment on recent progress in understanding the function of NAT activity in C. elegans based on the characterization of natc-1 by Warnhoff et al. (2014) and daf-31 by Chen et al. (2014).(1,2) natc-1 encodes an auxiliary subunit of the NatC complex and modulates stress tolerance, dauer entry, and adult lifespan. daf-31 encodes the catalytic subunit of the NatA complex and affects dauer entry, dauer formation, and adult lifespan. The analysis of these genes and genetic studies of NATs in other organisms suggests protein N-terminal acetylation plays an evolutionarily conserved role in promoting growth and development and inhibiting stress resistance. Furthermore, we propose that NATs may regulate growth and development in response to external cues such as nutrient deprivation and other physiologic stresses.

Indexed as

C. elegansdaf-31dauerinsulin/IGF-1 pathwaynatc-1N-terminal acetylationstress tolerance

Identifiers

PMID26435887
PMCPMC4589988
OpenAlexW594316733

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.