Evidence map›Paper›PMID 41782991›Full record

ArticleMaterials today. Bio2026

Application of a novel myristoylproteomics approach identifies GLIPR2 as a key pro-ferroptotic substrate in non-small cell lung cancer.

Yikun Wang, Susu Guo, Wanxin Guo, Xiaoting Tian, Yayou Miao, Shiyu Qiu, Xiangfei Xue, Yongjie Wang, Jiangtao Cui, Xin Xu and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Materials today. Bio, 2026. 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

12 authors.

Yikun WangDepartment of Clinical Laboratory Medicine, Shanghai Chest Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200030, China.
Susu GuoDepartment of Clinical Laboratory Medicine, Shanghai Chest Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200030, China.
Wanxin GuoShanghai Institute of Thoracic Oncology, Shanghai Chest Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200030, China.
Xiaoting TianShanghai Institute of Thoracic Oncology, Shanghai Chest Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200030, China.
Yayou MiaoShanghai Institute of Thoracic Oncology, Shanghai Chest Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200030, China.
Shiyu QiuDepartment of Clinical Laboratory Medicine, Shanghai Chest Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200030, China.
Xiangfei XueDepartment of Clinical Laboratory Medicine, Shanghai Chest Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200030, China.
Yongjie WangDepartment of Radiation Oncology, Shanghai Chest Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200030, China.
Jiangtao CuiShanghai Institute of Thoracic Oncology, Shanghai Chest Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200030, China.
Xin XuShanghai Institute of Thoracic Oncology, Shanghai Chest Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200030, China.
Jiayi WangDepartment of Clinical Laboratory Medicine, Shanghai Chest Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200030, China.
Xiao ZhangShanghai Institute of Thoracic Oncology, Shanghai Chest Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200030, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein myristoylation, catalyzed by N-myristoyltransferases (NMT1 and NMT2), is a key co- and post-translational modification involved in cellular signaling, yet its role in ferroptosis remains poorly defined. Here, we developed a novel myristoylproteomics workflow leveraging click chemistry to comprehensively profile N-myristoylated proteins within NSCLC cells. We found that NMT1 and NMT2 expression positively correlates with ferroptosis sensitivity. Genetic or pharmacological inhibition of NMT attenuated ferroptosis, whereas their overexpression enhanced it. Using our optimized quantitative myristoylproteomics platform, we identified GLIPR2 as a novel myristoylated protein with elevated modification levels in ferroptosis-sensitive cells. Functional studies confirmed that GLIPR2 promotes ferroptosis, and this pro-ferroptotic activity of GLIPR2 requires its N-myristoylation, as a myristoylation-deficient mutant (G2A) failed to restore ferroptosis sensitivity. Our work establishes a robust proteomic methodology for mapping protein myristoylation and uncovers the NMT1/NMT2-GLIPR2 axis as a pivotal regulator of ferroptosis. These findings propose new therapeutic strategies for NSCLC.

Indexed as

Cell deathChemical proteomicsClick chemistryNMT substratesTargeted therapy

Identifiers

PMID41782991
PMCPMC12955691

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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.