Evidence map›Paper›PMID 41759738›Full record

ArticleThe Journal of biological chemistry2026

Optimization of protein UFMylation modification method and its application in substrate identification in human cells.

Yaoyao Fang, Xue Wang, Juexi Dong, Xingling Yi, Zhaopeng Lv, Chen Bu, Xianliang Ma, Yu-Sheng Cong, Qian Liang

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. UFMylation of Pyruvate Dehydrogenase Regulates Mitochondrial Metabolism.bioRxiv : the preprint server for biology · 2026
    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

9 authors.

Yaoyao FangZhejiang Key Laboratory of Medical Epigenetics, School of Basic Medical Sciences, Hangzhou Normal University, Hangzhou, China.
Xue WangZhejiang Key Laboratory of Medical Epigenetics, School of Basic Medical Sciences, Hangzhou Normal University, Hangzhou, China.
Juexi DongZhejiang Key Laboratory of Medical Epigenetics, School of Basic Medical Sciences, Hangzhou Normal University, Hangzhou, China.
Xingling YiMicrometer Biotechnology Co., Ltd, Hangzhou, China.
Zhaopeng LvMicrometer Biotechnology Co., Ltd, Hangzhou, China.
Chen BuMicrometer Biotechnology Co., Ltd, Hangzhou, China.
Xianliang MaMicrometer Biotechnology Co., Ltd, Hangzhou, China.
Yu-Sheng CongZhejiang Key Laboratory of Medical Epigenetics, School of Basic Medical Sciences, Hangzhou Normal University, Hangzhou, China. Electronic address: yscong@hznu.edu.cn.
Qian LiangZhejiang Key Laboratory of Medical Epigenetics, School of Basic Medical Sciences, Hangzhou Normal University, Hangzhou, China. Electronic address: lq@hznu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

UFMylation plays an essential role in regulating intracellular physiological and pathological processes. Accumulating evidence has demonstrated that dysregulation of UFMylation is closely associated with the progression of various diseases, including cancers and developmental disorders. However, efficient and specific methods for detecting UFMylated substrate proteins remain challenging. In this study, we generated the UFM1-specific protease 1/2 knockout (UFSP1

Indexed as

ProteinsHEK293 CellsHumansProtein Processing, Post-TranslationalSubstrate SpecificityUbiquitin-Protein LigasesProteinsUbiquitin-Protein LigasesUFM1 protein, humanDDRGK1substrateUFL1UFMylationUFSP

Identifiers

PMID41759738
PMCPMC13018929

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.