Evidence map›Paper›PMID 39079947›Full record

ArticleNature chemistry2024

Single-electron transfer between sulfonium and tryptophan enables site-selective photo crosslinking of methyllysine reader proteins.

Feng Feng, Yingxiao Gao, Qun Zhao, Ting Luo, Qingyun Yang, Nan Zhao, Yihang Xiao, Yusong Han, Jinheng Pan, Shan Feng and 2 more

Abstract read
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In one paragraph

Article in Nature chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Review
  2. Review
  3. Development of Dimethylsulfonium Probes for Broad Profiling of Methyllysine Reader Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Review
  5. Review
  6. Article
  7. 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.

Feng Feng *Department of Chemistry, Zhejiang University, Hangzhou, China.
Yingxiao Gao *Department of Chemistry, Fudan University, Shanghai, China.ORCID 0009-0009-6002-8519
Qun Zhao *State Key Laboratory of Medical Proteomics, National Chromatographic R. & A. Center, CAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, China.
Ting LuoDepartment of Chemistry, School of Science, Westlake University, Hangzhou, China.
Qingyun YangDepartment of Chemistry, School of Science, Westlake University, Hangzhou, China.
Nan ZhaoState Key Laboratory of Medical Proteomics, National Chromatographic R. & A. Center, CAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, China.
Yihang XiaoDepartment of Chemistry, School of Science, Westlake University, Hangzhou, China.
Yusong HanDepartment of Chemistry, School of Science, Westlake University, Hangzhou, China.
Jinheng PanKey Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, China.
Shan FengKey Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, China.
Lihua ZhangState Key Laboratory of Medical Proteomics, National Chromatographic R. & A. Center, CAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, China.ORCID 0000-0003-3798-2047
Mingxuan WuDepartment of Chemistry, School of Science, Westlake University, Hangzhou, China. wumingxuan@westlake.edu.cn.ORCID 0000-0003-4721-0825

Funding

National Natural Science Foundation of China (National Science Foundation of China) 22161132006National Natural Science Foundation of China (National Science Foundation of China) 22322411
6 · The paper itself

Abstract

The identification of readers, an important class of proteins that recognize modified residues at specific sites, is essential to uncover the biological roles of post-translational modifications. Photoreactive crosslinkers are powerful tools for investigating readers. However, existing methods usually employ synthetically challenging photoreactive warheads, and their high-energy intermediates generated upon irradiation, such as nitrene and carbene, may cause substantial non-specific crosslinking. Here we report dimethylsulfonium as a methyllysine mimic that binds to specific readers and subsequently crosslinks to a conserved tryptophan inside the binding pocket through single-electron transfer under ultraviolet irradiation. The crosslinking relies on a protein-templated σ-π electron donor-acceptor interaction between sulfonium and indole, ensuring excellent site selectivity for tryptophan in the active site and orthogonality to other methyllysine readers. This method could escalate the discovery of methyllysine readers from complex cell samples. Furthermore, this photo crosslinking strategy could be extended to develop other types of microenvironment-dependent conjugations to site-specific tryptophan.

Indexed as

LysineSulfonium CompoundsTryptophanCross-Linking ReagentsElectron TransportHumansPhotochemical ProcessesProteinsUltraviolet RaysCross-Linking ReagentsLysineProteinsSulfonium CompoundsTryptophan

Identifiers

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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.