Evidence map›Paper›PMID 39322788›Full record

ArticleNature chemical biology2025

Direct mapping of tyrosine sulfation states in native peptides by nanopore.

Hongyan Niu, Meng-Yin Li, Yan Gao, Jun-Ge Li, Jie Jiang, Yi-Lun Ying, Yi-Tao Long

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

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  11. Nanopore-Based Detection of Protein Posttranslational Modifications.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  12. Article
  13. Article
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  15. Article
  16. Regulation of Protein Transport in Functionalized PET Nanopores.The journal of physical chemistry. B · 2025
    Article
  17. 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

7 authors.

Hongyan Niu *Molecular Sensing and Imaging Center, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, China.ORCID http://orcid.org/0009-0005-0860-3687
Meng-Yin Li *Molecular Sensing and Imaging Center, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, China. mengyinli@nju.edu.cn.ORCID http://orcid.org/0000-0002-0347-4194
Yan GaoMolecular Sensing and Imaging Center, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, China.
Jun-Ge LiMolecular Sensing and Imaging Center, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, China.
Jie JiangMolecular Sensing and Imaging Center, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, China.
Yi-Lun YingMolecular Sensing and Imaging Center, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, China.ORCID http://orcid.org/0000-0001-6217-256X
Yi-Tao LongMolecular Sensing and Imaging Center, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, China. yitaolong@nju.edu.cn.ORCID http://orcid.org/0000-0003-2571-7457

Funding

National Natural Science Foundation of China (National Science Foundation of China) 22027806National Natural Science Foundation of China (National Science Foundation of China) 22207054National Natural Science Foundation of China (National Science Foundation of China) 22334006
6 · The paper itself

Abstract

Sulfation is considered the most prevalent post-translational modification (PTM) on tyrosine; however, its importance is frequently undervalued due to difficulties in direct and unambiguous determination from phosphorylation. Here we present a sequence-independent strategy to directly map and quantify the tyrosine sulfation states in universal native peptides using an engineered protein nanopore. Molecular dynamics simulations and nanopore mutations reveal specific interactions between tyrosine sulfation and the engineered nanopore, dominating identification across diverse peptide sequences. We show a nanopore framework to discover tyrosine sulfation in unknown peptide fragments digested from a native protein and determine the sequence of the sulfated fragment based on current blockade enhancement induced by sulfation. Moreover, our method allows direct observation of peptide sulfation in ultra-low abundance, down to 1%, and distinguishes it from isobaric phosphorylation. This sequence-independent strategy suggests the potential of nanopore to explore specific PTMs in real-life samples and at the omics level.

Indexed as

NanoporesPeptidesSulfatesTyrosineAmino Acid SequenceMolecular Dynamics SimulationPhosphorylationProtein Processing, Post-TranslationalPeptidesSulfatesTyrosine

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.