Evidence map›Paper›PMID 28842471›Full record

ReviewJournal of cell science2017

ISGylation - a key to lock the cell gates for preventing the spread of threats.

Carolina Villarroya-Beltri, Susana Guerra, Francisco Sánchez-Madrid

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in Journal of cell science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
8.5field-weighted citation impact, top 2% 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

101 citing papers in PubMed, 173 citations in OpenAlex.

  1. Article
  2. BAG2 Condensates Couple Proteostasis to CD8bioRxiv : the preprint server for biology · 2026
    Article
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  6. Article
  7. Article
  8. Review
  9. Ubiquitination in cancer: mechanisms and therapeutic opportunities.Cancer communications (London, England) · 2025
    Review
  10. Review
  11. Exosome: an overview on enhanced biogenesis by small molecules.Naunyn-Schmiedeberg's archives of pharmacology · 2025
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

41 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

Carolina Villarroya-BeltriVascular Pathophysiology Area, Centro Nacional de Investigaciones Cardiovasculares (CNIC), 28029 Madrid, Spain.ORCID http://orcid.org/0000-0001-5303-0762
Susana GuerraPreventive Medicine Department, Facultad de Medicina, Universidad Autónoma de Madrid, 28029 Madrid, Spain.
Francisco Sánchez-MadridVascular Pathophysiology Area, Centro Nacional de Investigaciones Cardiovasculares (CNIC), 28029 Madrid, Spain fsmadrid@salud.madrid.org.
Instituto de Salud Carlos III · ESUniversidad Autónoma de Madrid · ES

Funding

European Research Council 294340
6 · The paper itself

Abstract

Interferon stimulated gene 15 (ISG15) is an ubiquitin-like protein whose expression and conjugation to targets (ISGylation) is induced by infection, interferon (IFN)-α and -β, ischemia, DNA damage and aging. Attention has historically focused on the antiviral effects of ISGylation, which blocks the entry, replication or release of different intracellular pathogens. However, recently, new functions of ISGylation have emerged that implicate it in multiple cellular processes, such as DNA repair, autophagy, protein translation and exosome secretion. In this Review, we discuss the induction and conjugation of ISG15, as well as the functions of ISGylation in the prevention of infections and in cancer progression. We also offer a novel perspective with regard to the latest findings on this pathway, with special attention to the role of ISGylation in the inhibition of exosome secretion, which is mediated by fusion of multivesicular bodies with lysosomes. Finally, we propose that under conditions of stress or infection, ISGylation acts as a defense mechanism to inhibit normal protein translation by modifying protein kinase R (PKR, also known as EIF2AK2), while any newly synthesized proteins are being tagged and thus marked as potentially dangerous. Then, the endosomal system is re-directed towards protein degradation at the lysosome, to effectively 'lock' the cell gates and thus prevent the spread of pathogens, prions and deleterious aggregates through exosomes.

Indexed as

AnimalsBacterial InfectionsCellsHumansInterferonsModels, BiologicalNeoplasmsVirus DiseasesInterferonsExosomesISG15PathogenPost-translational modificationUbiquitin-like

Identifiers

PMID28842471
OpenAlexW2745948512

What OpenQuestion holds

Textmetadata
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.