Evidence map›Paper›PMID 30699938›Full record

ReviewCells2019

Targeting Hedgehog Signalling through the Ubiquitylation Process: The Multiple Roles of the HECT-E3 Ligase Itch.

Paola Infante, Ludovica Lospinoso Severini, Flavia Bernardi, Francesca Bufalieri, Lucia Di Marcotullio

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

15 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Ubiquitin E3 Ligases and p53 in Doxorubicin-Induced Cardiotoxicity.International journal of molecular sciences · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. The Role of HECT-Type E3 Ligase in the Development of Cardiac Disease.International journal of molecular sciences · 2021
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
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 3 institutions in 1 country.

Paola InfanteCenter for Life NanoScience@Sapienza, Istituto Italiano di Tecnologia, 00161 Rome, Italy. paola.infante@iit.it.
Ludovica Lospinoso SeveriniDepartment of Molecular Medicine, University of Rome La Sapienza, 00161 Rome, Italy. ludovica.lospinososeverini@uniroma1.it.ORCID 0000-0002-1032-5496
Flavia BernardiDepartment of Molecular Medicine, University of Rome La Sapienza, 00161 Rome, Italy. flavia.bernardi@uniroma1.it.
Francesca BufalieriDepartment of Molecular Medicine, University of Rome La Sapienza, 00161 Rome, Italy. francesca.bufalieri@uniroma1.it.ORCID 0000-0002-9571-318X
Lucia Di MarcotullioDepartment of Molecular Medicine, University of Rome La Sapienza, 00161 Rome, Italy. lucia.dimarcotullio@uniroma1.it.
Sapienza University of Rome · ITIstituto Pasteur · ITItalian Institute of Technology · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hedgehog signalling (Hh) is a developmental conserved pathway strongly involved in cancers when deregulated. This important pathway is orchestrated by numerous regulators, transduces through distinct routes and is finely tuned at multiple levels. In this regard, ubiquitylation processes stand as essential for controlling Hh pathway output. Although this post-translational modification governs proteins turnover, it is also implicated in non-proteolytic events, thereby regulating the most important cellular functions. The HECT E3 ligase Itch, well known to control immune response, is emerging to have a pivotal role in tumorigenesis. By illustrating Itch specificities on Hh signalling key components, here we review the role of this HECT E3 ubiquitin ligase in suppressing Hh-dependent tumours and explore its potential as promising target for innovative therapeutic approaches.

Indexed as

Signal TransductionUbiquitinationAnimalsHedgehog ProteinsHumansModels, BiologicalUbiquitin-Protein LigasesHedgehog ProteinsUbiquitin-Protein LigasescancerGLI1HedgehogItchNumbPatched1SuFuubiquitylationβ-arrestin2

Identifiers

PMID30699938
PMCPMC6407099
OpenAlexW2913266125

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.