Evidence map›Paper›PMID 31637018›Full record

ArticleSignal transduction and targeted therapy

Global profiling of O-GlcNAcylated and/or phosphorylated proteins in hepatoblastoma.

Hang Song, Ji Ma, Zhixuan Bian, Shuhua Chen, Jiabei Zhu, Jing Wang, Nan Huang, Minzhi Yin, Fenyong Sun, Min Xu and 1 more

Open access · goldAbstract read
In one paragraph

Article in Signal transduction and targeted therapy. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

21 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Frontiers in immunology · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. TargetingFrontiers in oncology · 2022
    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

11 authors at 3 institutions in 1 country.

Hang Song *1Department of Laboratory Medicine, Shanghai Children's Medical Center, School of Medicine, Shanghai Jiaotong University, 200127 Shanghai, China.
Ji Ma *1Department of Laboratory Medicine, Shanghai Children's Medical Center, School of Medicine, Shanghai Jiaotong University, 200127 Shanghai, China.
Zhixuan Bian *1Department of Laboratory Medicine, Shanghai Children's Medical Center, School of Medicine, Shanghai Jiaotong University, 200127 Shanghai, China.
Shuhua ChenDepartment of Laboratory Medicine, Yunfu People's Hospital, 527300 Guangdong, China.
Jiabei Zhu1Department of Laboratory Medicine, Shanghai Children's Medical Center, School of Medicine, Shanghai Jiaotong University, 200127 Shanghai, China.
Jing Wang3Department of Surgery, Shanghai Children's Medical Center, School of Medicine, Shanghai Jiaotong University, 200127 Shanghai, China.
Nan Huang4Department of Laboratory Medicine, Shanghai Tenth People's Hospital of Tongji University, 200072 Shanghai, China.
Minzhi Yin5Department of Pathology, Shanghai Children's Medical Center, School of Medicine, Shanghai Jiaotong University, 200127 Shanghai, China.
Fenyong Sun4Department of Laboratory Medicine, Shanghai Tenth People's Hospital of Tongji University, 200072 Shanghai, China.
Min Xu3Department of Surgery, Shanghai Children's Medical Center, School of Medicine, Shanghai Jiaotong University, 200127 Shanghai, China.
Qiuhui Pan1Department of Laboratory Medicine, Shanghai Children's Medical Center, School of Medicine, Shanghai Jiaotong University, 200127 Shanghai, China.
Shanghai Children's Medical Center · CNShanghai Tenth People's Hospital · CNTongji University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

O-linked-β-N-acetylglucosamine (O-GlcNAc) glycosylation (O-GlcNAcylation) and phosphorylation are critical posttranslational modifications that are involved in regulating the functions of proteins involved in tumorigenesis and the development of various solid tumors. However, a detailed characterization of the patterns of these modifications at the peptide or protein level in hepatoblastoma (HB), a highly malignant primary hepatic tumor with an extremely low incidence in children, has not been performed. Here, we examined O-GlcNAc-modified or phospho-modified peptides and proteins in HB through quantitative proteomic analysis of HB tissues and paired normal liver tissues. Our results identified 114 O-GlcNAcylated peptides belonging to 78 proteins and 3494 phosphorylated peptides in 2088 proteins. Interestingly, 41 proteins were modified by both O-GlcNAcylation and phosphorylation. These proteins are involved in multiple molecular and cellular processes, including chromatin remodeling, transcription, translation, transportation, and organelle organization. In addition, we verified the accuracy of the proteomics results and found a competitive inhibitory effect between O-GlcNAcylation and phosphorylation of HSPB1. Further, O-GlcNAcylation modification of HSPB1 promoted proliferation and enhanced the chemotherapeutic resistance of HB cell lines in vitro. Collectively, our research suggests that O-GlcNAc-modified and/or phospho-modified proteins may play a crucial role in the pathogenesis of HB.

Indexed as

EpigeneticsMolecular medicine

Identifiers

PMID31637018
PMCPMC6799812
OpenAlexW2980216853

What OpenQuestion holds

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LicenceCC BY
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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.