Evidence map›Paper›PMID 30126853›Full record

ReviewBioscience reports2018

USP18 - a multifunctional component in the interferon response.

Anja Basters, Klaus-Peter Knobeloch, Günter Fritz

Abstract readReview
In one paragraph

Review in Bioscience reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
–field-weighted citation impact
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

65 citing papers in PubMed.

  1. Trial
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. RTP4 Suppresses Colorectal Cancer Progression via MHC-I-Mediated CD8Journal of cellular and molecular medicine · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

5 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.

Anja BastersFriedrich Miescher Institute for Biomedical Research, Quantitative Biology, Basel, Switzerland anja.basters@fmi.ch.
Klaus-Peter KnobelochFaculty of Medicine, Institute of Neuropathology, University of Freiburg, Freiburg, Germany.
Günter FritzFaculty of Medicine, Institute of Neuropathology, University of Freiburg, Freiburg, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin-specific proteases (USPs) represent the largest family of deubiquitinating enzymes (DUB). These proteases cleave the isopeptide bond between ubiquitin and a lysine residue of a ubiquitin-modified protein. USP18 is a special member of the USP family as it only deconjugates the ubiquitin-like protein ISG15 (interferon-stimulated gene (ISG) 15) from target proteins but is not active towards ubiquitin. Independent of its protease activity, USP18 functions as a major negative regulator of the type I interferon response showing that USP18 is - at least - a bifunctional protein. In this review, we summarise our current knowledge of protease-dependent and -independent functions of USP18 and discuss the structural basis of its dual activity.

Indexed as

CytokinesEndopeptidasesHumansInterferon Type IPeptide HydrolasesProtein ConformationProteolysisSignal TransductionUbiquitinUbiquitinsUbiquitin ThiolesteraseCytokinesEndopeptidasesInterferon Type IISG15 protein, humanPeptide HydrolasesUbiquitinUbiquitinsUbiquitin ThiolesteraseUSP18 protein, humaninterferonsISG15proteaseubiquitin like modifier proteinsUSP18

Identifiers

PMID30126853
PMCPMC6240716

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.