Evidence map›Paper›PMID 41130980›Full record

ArticleNature communications2025

Engineering unnatural cells with a 21st amino acid as a living epigenetic sensor.

Yu Hu, Yixian Wang, Linqi Cheng, Chenhang Wang, Yijie Liu, Yufei Wang, Yuda Chen, Shudan Yang, Yiming Guo, Shiyu Jiang and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. 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

12 authors.

Yu HuDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, USA.ORCID http://orcid.org/0009-0007-2217-1459
Yixian WangDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, USA.
Linqi ChengDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, USA.ORCID http://orcid.org/0000-0001-6520-1856
Chenhang WangDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, USA.
Yijie LiuDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, USA.ORCID http://orcid.org/0009-0002-3792-4947
Yufei WangDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, USA.
Yuda ChenDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, USA.
Shudan YangDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, USA.
Yiming GuoDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, USA.
Shiyu JiangDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, USA.ORCID http://orcid.org/0000-0001-9450-7379
Kaiqiang YangDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, USA.
Han XiaoDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, USA. han.xiao@rice.edu.ORCID http://orcid.org/0000-0002-4311-971X

Funding

Engineering Proteins with Noncanonical Amino AcidsR35GM133706 · NIGMS · RICE UNIVERSITY · PI Han Xiao · 2019 to 2026
$2.9M
Division of Intramural Research, National Institute of Allergy and Infectious Diseases (Division of Intramural Research of the NIAID) R01-AI165079NIGMS NIH HHS R35 GM133706United States Department of Defense | United States Army | Army Medical Command | Congressionally Directed Medical Research Programs (CDMRP) HT9425-23-1-0494United States Department of Defense | United States Army | Army Medical Command | Congressionally Directed Medical Research Programs (CDMRP) T9425-23-1-0494United States Department of Defense | United States Army | Army Medical Command | Congressionally Directed Medical Research Programs (CDMRP) W81XWH-21-1-0789U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R35-GM133706Welch Foundation C-1970
6 · The paper itself

Abstract

Living animals rely extensively on post-translational modifications (PTMs) to regulate protein activity, stability, subcellular localization, and protein-protein interactions. These modifications are tightly controlled by the balance of "writer" and "eraser" enzymes, which add or remove PTMs on proteins. Current strategies to measure writer and eraser activities in living animals largely depend on invasive methods, such as single-cell sequencing, quantitative mass spectrometry, or activity-based probes, which often lack cell or tissue specificity. In this study, we report the development of autonomous cells-both prokaryotic and eukaryotic-with the ability to biosynthesize and genetically encode acetyllysine using the genetic code expansion technology. These engineered living sensors with a site-specific acetyllysine modification can be transplanted into living animals, enabling real-time monitoring of PTM dynamics in living cells and animals. We further demonstrate the utility of these cells in tracking deacetylase activity and assessing the effects of deacetylase inhibitors on PTM dynamics in living animals in real time.

Indexed as

Amino AcidsCell EngineeringEpigenesis, GeneticLysineAnimalsBiosensing TechniquesGenetic CodeHEK293 CellsHumansMiceProtein Processing, Post-TranslationalAmino AcidsLysine

Identifiers

PMID41130980
PMCPMC12549914

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.