Evidence map›Paper›PMID 38335294›Full record

ArticleScience advances2024

The protein carboxymethyltransferase-dependent aspartate salvage pathway plays a crucial role in the intricate metabolic network of

Maureen Micaletto, Sebastien Fleurier, Sara Dion, Erick Denamur, Ivan Matic

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 42% 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

5 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. 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

5 authors at 2 institutions in 1 country.

Maureen MicalettoInstitut Cochin, Université Paris Cité, INSERM U1016, CNRS UMR 8104, 75014 Paris, France.ORCID 0009-0003-6822-2582
Sebastien FleurierInstitut Cochin, Université Paris Cité, INSERM U1016, CNRS UMR 8104, 75014 Paris, France.
Sara DionIAME, Université de Paris, INSERM U1137, Université Sorbonne Paris Nord, 75018 Paris, France.
Erick DenamurIAME, Université de Paris, INSERM U1137, Université Sorbonne Paris Nord, 75018 Paris, France.ORCID 0000-0002-7860-1717
Ivan MaticInstitut Cochin, Université Paris Cité, INSERM U1016, CNRS UMR 8104, 75014 Paris, France.ORCID 0000-0003-0393-1241
Centre National de la Recherche Scientifique · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein carboxymethyltransferase (Pcm) is a highly evolutionarily conserved enzyme that initiates the conversion of abnormal isoaspartate to aspartate residues. While it is commonly believed that Pcm facilitates the repair of damaged proteins, a number of observations suggest that it may have another role in cell functioning. We investigated whether Pcm provides a means for

Indexed as

Aspartic AcidEscherichia coliAnimalsAnti-Bacterial AgentsMammalsMetabolic Networks and PathwaysProtein D-Aspartate-L-Isoaspartate MethyltransferaseAnti-Bacterial AgentsAspartic AcidProtein D-Aspartate-L-Isoaspartate Methyltransferase

Identifiers

PMID38335294
PMCPMC10857468
OpenAlexW4391677800

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.