Evidence map›Paper›PMID 42446724›Full record

ArticleMedicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents2026

Site-Specific incorporation of lysine acetyl-methylation into proteins.

Jingxiang Zhao, Xinlong Guo, Xuelian Ren, Jiyang Yu, Xiaohan Song, He Huang

Abstract read
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Article in Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

6 authors.

Jingxiang ZhaoSchool of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.
Xinlong GuoState Key Laboratory of Chemical Biology, Shanghai Institute of Materia Medica, Shanghai, 201203, China.
Xuelian RenState Key Laboratory of Chemical Biology, Shanghai Institute of Materia Medica, Shanghai, 201203, China.
Jiyang YuKey Laboratory of Glyco-drug Research of Zhejiang Province, School of Pharmaceutical Science and Technology, Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences, Hangzhou, 310024, China.
Xiaohan SongKey Laboratory of Glyco-drug Research of Zhejiang Province, School of Pharmaceutical Science and Technology, Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences, Hangzhou, 310024, China.
He HuangSchool of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China. hhuang@simm.ac.cn.

Funding

National Natural Science Foundation of China 22277125Natural Science Foundation of Shanghai 23ZR1474600Noncommunicable Chronic Diseases-National Science and Technology Major Project 2023ZD0507800Shandong Laboratory Program SYS202205Shandong Provincial Natural Science Foundation ZR2024MB112Strategic Priority Research Program of the Chinese Academy of Sciences XDB1060000Taishan Scholars Program tstp20240845
6 · The paper itself

Abstract

Lysine acetyl-methylation (Kam) is a novel protein post-translational modification (PTM) recently identified on histone H4, yet its biological functions on non-histone proteins remain largely unexplored. Here, we engineered an orthogonal Methanosarcina barkeri pyrrolysyl-tRNA synthetase (MbPylRS) variant and tRNA

Indexed as

LysineProteinsAmino Acyl-tRNA SynthetasesHumansMethanosarcina barkeriMethylationProtein Processing, Post-TranslationalAmino Acyl-tRNA SynthetasesLysineProteinsFunctional characterizationGenetic Code ExpansionLysine acetyl-methylationPost-translational modificationSite-specific incorporation

Identifiers

PMID42446724

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.