Evidence map›Paper›PMID 28212757›Full record

ArticleCell chemical biology2017

A Prob(e)able Route to Lysine Acylation.

Gregory R Wagner, Matthew D Hirschey

Open access · bronzeAbstract readComment
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 47% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Emerging Roles for SIRT5 in Metabolism and Cancer.Antioxidants & redox signaling · 2018
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Gregory R WagnerDuke Molecular Physiology Institute and the Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham, NC 27701, USA; Department of Medicine, Division of Endocrinology, Metabolism, and Nutrition, Durham, NC 27710, USA.
Matthew D HirscheyDuke Molecular Physiology Institute and the Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham, NC 27701, USA; Department of Medicine, Division of Endocrinology, Metabolism, and Nutrition, Durham, NC 27710, USA; Department of Pharmacology & Cancer Biology and Duke University Medical Center, Durham, NC 27710, USA. Electronic address: matthew.hirschey@duke.edu.
Duke Medical Center · USDuke University Hospital · US

Funding

Endocrinology and Metabolism Training ProgramT32DK007012 · NIDDK · DUKE UNIVERSITY · PI DAVID A. D'ALESSIO · 1986 to 2026
$6.8M
Studies on the Mechanisms by which SIRT5 Regulates Aging and DiseaseR01AG045351 · NIA · DUKE UNIVERSITY · PI HIRSCHEY, MATTHEW D · 2014 to 2023
$4.4M
NIA NIH HHS R01 AG045351NIDDK NIH HHS T32 DK007012
6 · The paper itself

Abstract

Non-enzymatic modification of proteins by acyl-CoA species involved in intermediary metabolism is a possible explanation for widespread protein acylation. In this issue, Kulkarni et al. (2017) develop a set of chemoproteomic probes to interrogate the role of malonyl-CoA in mediating protein malonylation and find malonylation influences glycolysis in cancer cells.

Indexed as

LysineProteinsAcylationAcyl Coenzyme AMalonyl Coenzyme AAcyl Coenzyme ALysineMalonyl Coenzyme AProteins

Identifiers

PMID28212757
PMCPMC5503691
OpenAlexW2587947359

What OpenQuestion holds

Textmetadata
LicenceTDM
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.