Evidence map›Paper›PMID 41366248›Full record

ArticleNature communications2025

Implementing N-terminomics and machine learning to probe Nt-arginylation.

Shinyeong Ju, Laxman Nawale, Seonjeong Lee, Jung Gi Kim, Hankyul Lee, Narae Park, Dong Hyun Kim, Hyunjoo Cha-Molstad, Cheolju Lee

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 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

9 authors.

Shinyeong Ju *Chemical and Biological Integrative Research Center, Korea Institute of Science and Technology, Seoul, Republic of Korea.ORCID http://orcid.org/0000-0001-5483-4690
Laxman Nawale *Nucleic Acid Therapeutics Research Center, Korea Research Institute of Bioscience and Biotechnology, Ochang, Republic of Korea.
Seonjeong Lee *Chemical and Biological Integrative Research Center, Korea Institute of Science and Technology, Seoul, Republic of Korea.
Jung Gi KimNucleic Acid Therapeutics Research Center, Korea Research Institute of Bioscience and Biotechnology, Ochang, Republic of Korea.
Hankyul LeeChemical and Biological Integrative Research Center, Korea Institute of Science and Technology, Seoul, Republic of Korea.ORCID http://orcid.org/0009-0002-5371-0447
Narae ParkChemical and Biological Integrative Research Center, Korea Institute of Science and Technology, Seoul, Republic of Korea.ORCID http://orcid.org/0009-0005-5513-2566
Dong Hyun KimCancer Metastasis Branch, Division of Cancer Biology, National Cancer Center, Goyang, Republic of Korea.ORCID http://orcid.org/0000-0002-7463-209X
Hyunjoo Cha-MolstadNucleic Acid Therapeutics Research Center, Korea Research Institute of Bioscience and Biotechnology, Ochang, Republic of Korea. hcha@kribb.ac.kr.ORCID http://orcid.org/0000-0003-3676-7150
Cheolju LeeChemical and Biological Integrative Research Center, Korea Institute of Science and Technology, Seoul, Republic of Korea. clee270@kist.re.kr.ORCID http://orcid.org/0000-0001-8482-4696

Funding

Korea Institute of Science and Technology (KIST) Grand ChallengeNational Research Foundation of Korea (NRF) RS-2022-NR068428National Research Foundation of Korea (NRF) RS-2023-00279134National Research Foundation of Korea (NRF) RS-2024-00444177
6 · The paper itself

Abstract

N-terminal arginylation (Nt-arginylation) is a multifunctional post-translational modification (PTM) with roles in protein quality control, organelle homeostasis and stress signaling, but its study has been limited by technical challenges. Here, we develop an integrated approach combining N-terminomics with machine learning-based filtering to identify in cellulo Nt-arginylation. Using Arg-starting missed cleavage peptides as proxies for ATE1-mediated arginylation, we train a transfer learning model to predict mass spectra and retention times. By applying the prediction models with an additional statistical filter, we identify 134 Nt-arginylation sites in thapsigargin-treated HeLa cells. Arginylation is enriched in proteins from various organelles, especially at caspase cleavage and signal peptide processing sites. Eight of twelve tested proteins are further validated for their interaction with p62 ZZ domain. Temporal profiling reveals that ATF4 increases early post-stress, followed by arginylation at caspase-3 substrates and ER signal-cleaved proteins. Our approach enables sensitive detection of rare N-terminal modifications, offering potential for biomarker and drug target discovery.

Indexed as

ArginineMachine LearningProtein Processing, Post-TranslationalProteomicsActivating Transcription Factor 4Caspase 3HeLa CellsHumansThapsigarginActivating Transcription Factor 4ArginineATF4 protein, humanCaspase 3Thapsigargin

Identifiers

PMID41366248
PMCPMC12780112

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LicenceCC BY-NC-ND
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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.