Evidence map›Paper›PMID 38577373›Full record

ArticleChemical science2024

A pyridinium-based strategy for lysine-selective protein modification and chemoproteomic profiling in live cells.

Chuan Wan, Dongyan Yang, Chunli Song, Mingchan Liang, Yuhao An, Chenshan Lian, Chuan Dai, Yuxin Ye, Feng Yin, Rui Wang and 1 more

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2024. 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
5.2field-weighted citation impact, top 4% of its field
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, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. One-Step Maleimide-Based Dual Functionalization of Protein N-Termini.Angewandte Chemie (International ed. in English) · 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

11 authors at 4 institutions in 1 country.

Chuan WanCollege of Health Science and Environmental Engineering, Shenzhen Technology University Shenzhen 518118 P. R. China.
Dongyan YangCollege of Chemistry and Chemical Engineering, Zhongkai University of Agriculture and Engineering Guangzhou 510225 P. R. China.
Chunli SongPingshan Translational Medicine Center, Shenzhen Bay Laboratory Shenzhen 518118 P. R. China yinfeng@szbl.ac.cn wangrui@szbl.ac.cn lizg@szbl.ac.cn.
Mingchan LiangPingshan Translational Medicine Center, Shenzhen Bay Laboratory Shenzhen 518118 P. R. China yinfeng@szbl.ac.cn wangrui@szbl.ac.cn lizg@szbl.ac.cn.
Yuhao AnPingshan Translational Medicine Center, Shenzhen Bay Laboratory Shenzhen 518118 P. R. China yinfeng@szbl.ac.cn wangrui@szbl.ac.cn lizg@szbl.ac.cn.ORCID https://orcid.org/0009-0006-0224-9709
Chenshan LianPingshan Translational Medicine Center, Shenzhen Bay Laboratory Shenzhen 518118 P. R. China yinfeng@szbl.ac.cn wangrui@szbl.ac.cn lizg@szbl.ac.cn.
Chuan DaiPingshan Translational Medicine Center, Shenzhen Bay Laboratory Shenzhen 518118 P. R. China yinfeng@szbl.ac.cn wangrui@szbl.ac.cn lizg@szbl.ac.cn.
Yuxin YePingshan Translational Medicine Center, Shenzhen Bay Laboratory Shenzhen 518118 P. R. China yinfeng@szbl.ac.cn wangrui@szbl.ac.cn lizg@szbl.ac.cn.
Feng YinPingshan Translational Medicine Center, Shenzhen Bay Laboratory Shenzhen 518118 P. R. China yinfeng@szbl.ac.cn wangrui@szbl.ac.cn lizg@szbl.ac.cn.
Rui WangPingshan Translational Medicine Center, Shenzhen Bay Laboratory Shenzhen 518118 P. R. China yinfeng@szbl.ac.cn wangrui@szbl.ac.cn lizg@szbl.ac.cn.ORCID https://orcid.org/0000-0003-3830-4133
Zigang LiState Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School Shenzhen 518055 P. R. China lizg.sz@pku.edu.cn.ORCID https://orcid.org/0000-0002-4649-1592
Shenzhen Bay Laboratory · CNPeking University · CNShenzhen Technology University · CNZhongkai University of Agriculture and Engineering · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein active states are dynamically regulated by various modifications; thus, endogenous protein modification is an important tool for understanding protein functions and networks in complicated biological systems. Here we developed a new pyridinium-based approach to label lysine residues under physiological conditions that is low-toxicity, efficient, and lysine-selective. Furthermore, we performed a large-scale analysis of the ∼70% lysine-selective proteome in MCF-7 cells using activity-based protein profiling (ABPP). We quantifically assessed 1216 lysine-labeled peptides in cell lysates and identified 386 modified lysine sites including 43 mitochondrial-localized proteins in live MCF-7 cells. Labeled proteins significantly preferred the mitochondria. This pyridinium-based methodology demonstrates the importance of analyzing endogenous proteins under native conditions and provides a robust chemical strategy utilizing either lysine-selective protein labeling or spatiotemporal profiling in a living system.

Identifiers

PMID38577373
PMCPMC10988577
OpenAlexW4392751532

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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.