Evidence map›Paper›PMID 36439127›Full record

ArticleFrontiers in immunology2022

Impact of ATP-citrate lyase catalytic activity and serine 455 phosphorylation on histone acetylation and inflammatory responses in human monocytic THP-1 cells.

Monica Dominguez, Verena Truemper, Ana Carolina Mota, Bernhard Brüne, Dmitry Namgaladze

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. New insights into the ACLY-mediated metabolic and epigenetic interplay in macrophages.Journal of enzyme inhibition and medicinal chemistry · 2026
    Review
  3. Article
  4. Article
  5. iScience · 2026
    Article
  6. Article
  7. Article
  8. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Monica DominguezInstitute of Biochemistry I, Faculty of Medicine, Goethe-University Frankfurt, Frankfurt, Germany.
Verena TruemperInstitute of Biochemistry I, Faculty of Medicine, Goethe-University Frankfurt, Frankfurt, Germany.
Ana Carolina MotaInstitute of Biochemistry I, Faculty of Medicine, Goethe-University Frankfurt, Frankfurt, Germany.
Bernhard BrüneInstitute of Biochemistry I, Faculty of Medicine, Goethe-University Frankfurt, Frankfurt, Germany.
Dmitry NamgaladzeInstitute of Biochemistry I, Faculty of Medicine, Goethe-University Frankfurt, Frankfurt, Germany.
Goethe University Frankfurt · DEDeutschen Konsortium für Translationale Krebsforschung · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATP-citrate lyase (ACLY) is a key enzyme provoking metabolic and epigenetic gene regulation. Molecularly, these functions are exerted by the provision of acetyl-coenzyme A, which is then used as a substrate for

Indexed as

HistonesSerineAcetylationAdenosine TriphosphateATP Citrate (pro-S)-LyaseHumansLipopolysaccharidesMultienzyme ComplexesOxo-Acid-LyasesPhosphorylationProto-Oncogene Proteins c-aktTHP-1 CellsAdenosine TriphosphateATP Citrate (pro-S)-Lyasecitrate (pro-3S)-lyaseHistonesLipopolysaccharidesMultienzyme ComplexesOxo-Acid-LyasesProto-Oncogene Proteins c-aktSerineATP-citrate lyasehistone acetylationinflammationmacrophagesmetabolism

Identifiers

PMID36439127
PMCPMC9686385
OpenAlexW4308868781

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.