Evidence map›Paper›PMID 30934872›Full record

ReviewCancers2019

Importance of TRAIL Molecular Anatomy in Receptor Oligomerization and Signaling. Implications for Cancer Therapy.

Javier Naval, Diego de Miguel, Ana Gallego-Lleyda, Alberto Anel, Luis Martinez-Lostao

Open access · goldAbstract readReview
In one paragraph

Review in Cancers, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

44 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Clustering of Membrane Receptors: Insights from DNA Origami-Based Approaches.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Review
  8. Article
  9. Review
  10. Review
  11. Targeting the MAtrix REgulating MOtif abolishes several hallmarks of cancer, triggering antitumor immunity.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Review
  13. Targeting apoptotic pathways for cancer therapy.The Journal of clinical investigation · 2024
    Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Therapeutic targeting of TRAIL death receptors.Biochemical Society transactions · 2023
    Review
  20. 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

5 authors at 1 institution in 2 countries.

Javier NavalDepartamento de Bioquímica, Biología Moleculary Celular, Universidad de Zaragoza, 50009 Zaragoza, Spain. jnaval@unizar.es.ORCID 0000-0003-2156-8378
Diego de MiguelDepartamento de Bioquímica, Biología Moleculary Celular, Universidad de Zaragoza, 50009 Zaragoza, Spain. diego_demiguel@hotmail.com.
Ana Gallego-LleydaDepartamento de Bioquímica, Biología Moleculary Celular, Universidad de Zaragoza, 50009 Zaragoza, Spain. 577565@unizar.es.
Alberto AnelDepartamento de Bioquímica, Biología Moleculary Celular, Universidad de Zaragoza, 50009 Zaragoza, Spain. anel@unizar.es.ORCID 0000-0002-5175-8394
Luis Martinez-LostaoInstituto de Investigación Sanitaria de Aragón (ISS), 50009 Zaragoza, Spain. lumartin@unizar.es.
Universidad de Zaragoza · ES

Funding

Instituto de Salud Carlos III PI16/00526Ministerio de Economía, Industria y Competitividad, Gobierno de España SAF2016-76338-R
6 · The paper itself

Abstract

(TNF)-related apoptosis-inducing ligand (TRAIL) is able to activate the extrinsic apoptotic pathway upon binding to DR4/TRAIL-R1 and/or DR5/TRAIL-R2 receptors. Structural data indicate that TRAIL functions as a trimer that can engage three receptor molecules simultaneously, resulting in receptor trimerization and leading to conformational changes in TRAIL receptors. However, receptor conformational changes induced by the binding of TRAIL depend on the molecular form of this death ligand, and not always properly trigger the apoptotic cascade. In fact, TRAIL exhibits a much stronger pro-apoptotic activity when is found as a transmembrane protein than when it occurs as a soluble form and this enhanced biological activity is directly linked to its ability to cluster TRAIL receptors in supra-molecular structures. In this regard, cells involved in tumor immunosurveillance, such as activated human T cells, secrete endogenous TRAIL as a transmembrane protein associated with lipid microvesicles called exosomes upon T-cell reactivation. Consequently, it seems clear that a proper oligomerization of TRAIL receptors, which leads to a strong apoptotic signaling, is crucial for inducing apoptosis in cancer cells upon TRAIL treatment. In this review, the current knowledge of oligomerization status of TRAIL receptors is discussed as well as the implications for cancer treatment when using TRAIL-based therapies.

Indexed as

apoptosiscancerclusterizationimmunotherapyoligomerizationTRAIL

Identifiers

PMID30934872
PMCPMC6521207
OpenAlexW2922684595

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.