Evidence map›Paper›PMID 42603217›Full record

ReviewCancer metastasis reviews2026

N-Acetyltransferase 10 (NAT10) at the crossroads of metabolism, immunology, and cancer biology.

Peng Xu, Qin Yan

Abstract readReview
PubMed Publisher
In one paragraph

Review in Cancer metastasis reviews, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Peng XuDepartment of Pathology, Yale School of Medicine, New Haven, CT, 06520, USA.
Qin YanDepartment of Pathology, Yale School of Medicine, New Haven, CT, 06520, USA. qin.yan@yale.edu.ORCID https://orcid.org/0000-0003-4077-453X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The multi-functional protein N-acetyltransferase 10 (NAT10), highly conserved from bacteria to human, is a versatile enzyme with an N-acetyltransferase domain, an RNA helicase domain, and a tRNA-binding domain, known for its ability to acetylate proteins and multiple RNA species. Specifically, NAT10 was reported to catalyze the N4-acetylcytidine (ac4C) modification on tRNA, rRNA, mRNA, and even viral RNA and to regulate translation efficiency, RNA stability, and eventually gene expression. NAT10 draws increasing attention for its emerging roles in rewiring metabolism, including amino acid, lipid, and glucose metabolism, and modulating immune responses to drive cancer progression, metastasis, and therapeutic resistance. In this review, we provide a conceptual framework of how the dysfunction of the highly conserved NAT10 leads to tumorigenesis, metastasis, and therapeutic resistance. We also summarize the major findings that reveal how NAT10 regulates cancer metabolism and immune responses. Lastly, we review the opportunities and challenges of targeting NAT10 to treat cancer and overcome drug resistance.

Indexed as

NeoplasmsN-Terminal Acetyltransferase EAnimalsHumansN-Terminal AcetyltransferasesNAT10 protein, humanN-Terminal Acetyltransferase EN-Terminal AcetyltransferasesDrug resistanceImmunologyMetabolismMetastasisN4-acetylcytidine (ac4C)NAT10

Identifiers

What OpenQuestion holds

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Registered trials

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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.