Evidence map›Paper›PMID 39203397›Full record

ArticleMicroorganisms2024

Lysine Phoshoglycerylation Is Widespread in Bacteria and Overlaps with Acylation.

Stefan Mikkat, Michael Kreutzer, Nadja Patenge

Abstract read
In one paragraph

Article in Microorganisms, 2024. 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
–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

1 citing paper in PubMed.

  1. Review
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

3 authors.

Stefan MikkatCore Facility Proteome Analysis, Rostock University Medical Center, 18057 Rostock, Germany.ORCID 0000-0002-8109-8235
Michael KreutzerMedical Research Center, Rostock University Medical Center, 18057 Rostock, Germany.ORCID 0000-0003-3331-7584
Nadja PatengeInstitute of Medical Microbiology, Virology and Hygiene, Rostock University Medical Center, 18057 Rostock, Germany.ORCID 0000-0002-6716-1592

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphoglycerylation is a non-enzymatic protein modification in which a phosphoglyceryl moiety is covalently bound to the ε-amino group of lysine. It is enriched in glycolytic enzymes from humans and mice and is thought to provide a feedback mechanism for regulating glycolytic flux. We report the first proteomic analysis of this post-translational modification in bacteria by profiling phosphoglyceryl-lysine during the growth of

Indexed as

acetylationimmonium and diagnostic ionsphosphoglycerylationphosphoglyceryl-lysinepost-translational modificationproteomicsStreptococcus pyogenes

Identifiers

PMID39203397
PMCPMC11356508

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.