Evidence map›Paper›PMID 29343520›Full record

ReviewCancer research2018

Evidence for the ISG15-Specific Deubiquitinase USP18 as an Antineoplastic Target.

Lisa Maria Mustachio, Yun Lu, Masanori Kawakami, Jason Roszik, Sarah J Freemantle, Xi Liu, Ethan Dmitrovsky

Abstract readReview
In one paragraph

Review in Cancer research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

33 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. ISGylation: is our genome yearning for such a modification?Acta biochimica et biophysica Sinica · 2025
    Review
  10. Article
  11. [Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2024
    Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. The Functional Roles of ISG15/ISGylation in Cancer.Molecules (Basel, Switzerland) · 2023
    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

7 authors at 3 institutions in 1 country.

Lisa Maria MustachioDepartment of Thoracic/Head and Neck Medical Oncology, The University of Texas MD Anderson Cancer Center, Houston, Texas.
Yun LuDepartment of Pharmacology and Toxicology, Geisel School of Medicine at Dartmouth, Hanover, New Hampshire.
Masanori KawakamiDepartment of Thoracic/Head and Neck Medical Oncology, The University of Texas MD Anderson Cancer Center, Houston, Texas.
Jason RoszikDepartment of Melanoma Medical Oncology, The University of Texas MD Anderson Cancer Center, Houston, Texas.
Sarah J FreemantleDepartment of Comparative Biosciences, College of Veterinary Medicine, University of Illinois, Illinois.
Xi LiuDepartment of Thoracic/Head and Neck Medical Oncology, The University of Texas MD Anderson Cancer Center, Houston, Texas.
Ethan DmitrovskyDepartment of Thoracic/Head and Neck Medical Oncology, The University of Texas MD Anderson Cancer Center, Houston, Texas. edmitrovsky@mdanderson.org.
The University of Texas MD Anderson Cancer Center · USDartmouth College · USIllinois College · US

Funding

RETINOID CANCER PREVENTION MECHANISMSR01CA087546 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI DMITROVSKY, ETHAN · 2000 to 2015
$4.1M
Targeting Anaphase Catastrophe to Combat Lung CancerR01CA190722 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI KURIE, JONATHAN M · 2015 to 2019
$1.8M
NCI NIH HHS R01 CA087546NCI NIH HHS R01 CA190722
6 · The paper itself

Abstract

Ubiquitination and ubiquitin-like posttranslational modifications (PTM) regulate activity and stability of oncoproteins and tumor suppressors. This implicates PTMs as antineoplastic targets. One way to alter PTMs is to inhibit activity of deubiquitinases (DUB) that remove ubiquitin or ubiquitin-like proteins from substrate proteins. Roles of DUBs in carcinogenesis have been intensively studied, yet few inhibitors exist. Prior work provides a basis for the ubiquitin-specific protease 18 (USP18) as an antineoplastic target. USP18 is the major DUB that removes IFN-stimulated gene 15 (ISG15) from conjugated proteins. Prior work discovered that engineered loss of USP18 increases ISGylation and in contrast to its gain decreases cancer growth by destabilizing growth-regulatory proteins. Loss of USP18 reduced cancer cell growth by triggering apoptosis. Genetic loss of USP18 repressed cancer formation in engineered murine lung cancer models. The translational relevance of USP18 was confirmed by finding its expression was deregulated in malignant versus normal tissues. Notably, the recent elucidation of the USP18 crystal structure offers a framework for developing an inhibitor to this DUB. This review summarizes strong evidence for USP18 as a previously unrecognized pharmacologic target in oncology.

Indexed as

Molecular Targeted TherapyAntineoplastic AgentsCytokinesEndopeptidasesHumansNeoplasmsUbiquitinsUbiquitin ThiolesteraseAntineoplastic AgentsCytokinesEndopeptidasesISG15 protein, humanUbiquitinsUbiquitin ThiolesteraseUSP18 protein, human

Identifiers

PMID29343520
PMCPMC6080720
OpenAlexW2793872780

What OpenQuestion holds

Textmetadata
LicenceTDM
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.