Evidence map›Paper›PMID 33432111›Full record

ReviewCell death and differentiation2021

The role of E3 ubiquitin ligases in the development and progression of glioblastoma.

Luke M Humphreys, Paul Smith, Zhuoyao Chen, Shahd Fouad, Vincenzo D'Angiolella

Open access · hybridAbstract readReview
In one paragraph

Review in Cell death and differentiation, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

47 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Beyond the membrane: rethinking EGFR signaling in physiology and cancer.Cellular and molecular life sciences : CMLS · 2026
    Review
  6. Computational Pipelines for Protein Ubiquitylation Analysis and Prediction.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. ApoE Inhibits the Progression of Glioma by Activating Immune Function.Journal of cellular and molecular medicine · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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

5 authors at 1 institution in 1 country.

Luke M HumphreysDepartment of Oncology, Medical Research Council Institute for Radiation Oncology, University of Oxford, Oxford, UK. luke.humphreys@oncology.ox.ac.uk.ORCID http://orcid.org/0000-0003-0804-6620
Paul SmithDepartment of Oncology, Medical Research Council Institute for Radiation Oncology, University of Oxford, Oxford, UK.
Zhuoyao ChenDepartment of Oncology, Medical Research Council Institute for Radiation Oncology, University of Oxford, Oxford, UK.
Shahd FouadDepartment of Oncology, Medical Research Council Institute for Radiation Oncology, University of Oxford, Oxford, UK.
Vincenzo D'AngiolellaDepartment of Oncology, Medical Research Council Institute for Radiation Oncology, University of Oxford, Oxford, UK. vincenzo.dangiolella@oncology.ox.ac.uk.
University of Oxford · GB

Funding

Medical Research Council MC_UU_00001/7
6 · The paper itself

Abstract

Despite recent advances in our understanding of the disease, glioblastoma (GB) continues to have limited treatment options and carries a dismal prognosis for patients. Efforts to stratify this heterogeneous malignancy using molecular classifiers identified frequent alterations in targetable proteins belonging to several pathways including the receptor tyrosine kinase (RTK) and mitogen-activated protein kinase (MAPK) signalling pathways. However, these findings have failed to improve clinical outcomes for patients. In almost all cases, GB becomes refractory to standard-of-care therapy, and recent evidence suggests that disease recurrence may be associated with a subpopulation of cells known as glioma stem cells (GSCs). Therefore, there remains a significant unmet need for novel therapeutic strategies. E3 ubiquitin ligases are a family of >700 proteins that conjugate ubiquitin to target proteins, resulting in an array of cellular responses, including DNA repair, pro-survival signalling and protein degradation. Ubiquitin modifications on target proteins are diverse, ranging from mono-ubiquitination through to the formation of polyubiquitin chains and mixed chains. The specificity in substrate tagging and chain elongation is dictated by E3 ubiquitin ligases, which have essential regulatory roles in multiple aspects of brain cancer pathogenesis. In this review, we begin by briefly summarising the histological and molecular classification of GB. We comprehensively describe the roles of E3 ubiquitin ligases in RTK and MAPK, as well as other, commonly altered, oncogenic and tumour suppressive signalling pathways in GB. We also describe the role of E3 ligases in maintaining glioma stem cell populations and their function in promoting resistance to ionizing radiation (IR) and chemotherapy. Finally, we consider how our knowledge of E3 ligase biology may be used for future therapeutic interventions in GB, including the use of blood-brain barrier permeable proteolysis targeting chimeras (PROTACs).

Indexed as

Signal TransductionAnimalsAntineoplastic AgentsBrain NeoplasmsGlioblastomaHumansPolyubiquitinProtein BindingProteolysisUbiquitinationUbiquitin-Protein LigasesAntineoplastic AgentsPolyubiquitinUbiquitin-Protein Ligases

Identifiers

PMID33432111
PMCPMC7862665
OpenAlexW3119273654

What Socratic 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 Socratic graph.