Evidence map›Paper›PMID 40631560›Full record

ReviewBiochemical Society transactions2025

The rise of AMPylation: from bacterial beginnings to modern implications in health and disease.

Meghomukta Mukherjee, Anju Sreelatha

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. AMPylation: key roles in biological regulation across prokaryotes and eukaryotes.Frontiers in cellular and infection microbiology · 2026
    Review
  2. Ribonuclease RNase Z is an evolutionarily conserved deAMPylase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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.

Meghomukta MukherjeeDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas TX 75390, U.S.A.
Anju SreelathaDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas TX 75390, U.S.A.ORCID 0000-0001-9485-0214

Funding

UT Southwestern NORCP30DK127984 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI JAY D. HORTON · 2022 to 2026
$7.4M
NIDDK NIH HHS P30 DK127984
6 · The paper itself

Abstract

Protein AMPylation is a post-translational modification in which adenosine monophosphate (AMP) from ATP is covalently attached to a target protein via a phosphodiester bond. This reaction is catalyzed by AMPylases, a diverse group of enzymes containing adenylyltransferase, filamentation induced by cyclic AMP (FIC), or kinase domains. As a reversible modification, AMPylation is dynamically regulated by both writer enzymes (AMPylases) and eraser enzymes (deAMPylases). Since its initial discovery in bacterial nitrogen metabolism in 1967, AMPylation has been recognized as a critical regulatory mechanism in both prokaryotic and eukaryotic systems. Recent studies link AMPylation to neurological disorders, diabetes, and cancer metastasis, underscoring its physiological and pathological significance. In this review, we present an overview of the discovery of AMPylases and deAMPylases, highlighting their role in cellular signaling, stress response, and host-pathogen interactions.

Indexed as

Adenosine MonophosphateBacteriaProtein Processing, Post-TranslationalAnimalsHost-Pathogen InteractionsHumansNeoplasmsNucleotidyltransferasesSignal TransductionAdenosine MonophosphateNucleotidyltransferasesadenylylationAMP transferaseFIC domainpost-translational modificationunfolded protein response

Identifiers

PMID40631560
PMCPMC12409994

What OpenQuestion holds

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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.