Evidence map›Paper›PMID 32583064›Full record

ReviewProtein & cell2021

Role of glycosylation in TGF-β signaling and epithelial-to-mesenchymal transition in cancer.

Jing Zhang, Peter Ten Dijke, Manfred Wuhrer, Tao Zhang

Open access · diamondAbstract readReview
In one paragraph

Review in Protein & cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed, 1 pooled it
4.8field-weighted citation impact, top 4% 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

59 citing papers in PubMed, 1 synthesis or guideline pooled it, 105 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
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  12. GALNT1 emerges as a potential therapeutic target in breast cancer.Journal of cancer research and clinical oncology · 2026
    Article
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  15. Article
  16. GalNAc-Transferases in Cancer.Biomedicines · 2025
    Review
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  19. Article
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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

4 authors at 1 institution in 1 country.

Jing ZhangOncode Institute and Cell Chemical Biology, Leiden University Medical Center, 2300 RC, Leiden, The Netherlands.ORCID 0000-0002-0137-6902
Peter Ten DijkeOncode Institute and Cell Chemical Biology, Leiden University Medical Center, 2300 RC, Leiden, The Netherlands. P.ten_Dijke@lumc.nl.ORCID 0000-0002-7234-342X
Manfred WuhrerCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands.ORCID 0000-0002-0814-4995
Tao ZhangCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands.ORCID 0000-0003-0427-9953
Leiden University Medical Center · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation is a common posttranslational modification on membrane-associated and secreted proteins that is of pivotal importance for regulating cell functions. Aberrant glycosylation can lead to uncontrolled cell proliferation, cell-matrix interactions, migration and differentiation, and has been shown to be involved in cancer and other diseases. The epithelial-to-mesenchymal transition is a key step in the metastatic process by which cancer cells gain the ability to invade tissues and extravasate into the bloodstream. This cellular transformation process, which is associated by morphological change, loss of epithelial traits and gain of mesenchymal markers, is triggered by the secreted cytokine transforming growth factor-β (TGF-β). TGF-β bioactivity is carefully regulated, and its effects on cells are mediated by its receptors on the cell surface. In this review, we first provide a brief overview of major types of glycans, namely, N-glycans, O-glycans, glycosphingolipids and glycosaminoglycans that are involved in cancer progression. Thereafter, we summarize studies on how the glycosylation of TGF-β signaling components regulates TGF-β secretion, bioavailability and TGF-β receptor function. Then, we review glycosylation changes associated with TGF-β-induced epithelial-to-mesenchymal transition in cancer. Identifying and understanding the mechanisms by which glycosylation affects TGF-β signaling and downstream biological responses will facilitate the identification of glycans as biomarkers and enable novel therapeutic approaches.

Indexed as

Epithelial-Mesenchymal TransitionSignal TransductionHumansNeoplasm ProteinsNeoplasmsNeoplasm Proteinscancerepithelial-to-mesenchymal transitionglycosphingolipidsN-glycosylationO-glycosylationtransforming growth factor-β

Identifiers

PMID32583064
PMCPMC7862465
OpenAlexW3037783644

What OpenQuestion holds

Textmetadata
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.