Evidence map›Paper›PMID 30890028›Full record

ReviewOpen biology2019

The molecular, cellular and pathophysiological roles of iRhom pseudoproteases.

Iqbal Dulloo, Sonia Muliyil, Matthew Freeman

Open access · goldAbstract readReview
In one paragraph

Review in Open biology, 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
4.8field-weighted citation impact, top 4% 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, 74 citations in OpenAlex.

  1. Trial
  2. Article
  3. Exploring the repertoire of rhomboid proteases inFrontiers in cellular and infection microbiology · 2026
    Article
  4. Review
  5. Structural insights into the activation and inhibition of the ADAM17-iRhom2 complex.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Iqbal DullooDunn School of Pathology, University of Oxford , South Parks Road, Oxford OX1 3RE , UK.
Sonia MuliyilDunn School of Pathology, University of Oxford , South Parks Road, Oxford OX1 3RE , UK.
Matthew FreemanDunn School of Pathology, University of Oxford , South Parks Road, Oxford OX1 3RE , UK.
University of Oxford · GB

Funding

Wellcome TrustWellcome Trust 101035/Z/13/Z
6 · The paper itself

Abstract

iRhom proteins are catalytically inactive relatives of rhomboid intramembrane proteases. There is a rapidly growing body of evidence that these pseudoenzymes have a central function in regulating inflammatory and growth factor signalling and consequent roles in many diseases. iRhom pseudoproteases have evolved new domains from their proteolytic ancestors, which are integral to their modular regulation and functions. Although we cannot yet conclude the full extent of their molecular and cellular mechanisms, there is a clearly emerging theme that they regulate the stability and trafficking of other membrane proteins. In the best understood case, iRhoms act as regulatory cofactors of the ADAM17 protease, controlling its function of shedding cytokines and growth factors. It seems likely that as the involvement of iRhoms in human diseases is increasingly recognized, they will become the focus of pharmaceutical interest, and here we discuss what is known about their molecular mechanisms and relevance in known pathologies.

Indexed as

Gene Expression RegulationMutationADAM17 ProteinAnimalsGenetic Predisposition to DiseaseHumansIntracellular Signaling Peptides and ProteinsKidney DiseasesPhylogenyProtein TransportStomach NeoplasmsADAM17 ProteinIntracellular Signaling Peptides and ProteinsRHBDF2 protein, humanADAM17inflammationmembrane proteinpseudoenzymerhomboidtrafficking

Identifiers

PMID30890028
PMCPMC6451368
OpenAlexW2924146786

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.