Evidence map›Paper›PMID 22035660›Full record

ReviewGenome biology2011

The rhomboid protease family: a decade of progress on function and mechanism.

Sinisa Urban, Seth W Dickey

Open access · bronzeAbstract readReview
In one paragraph

Review in Genome biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
5.2field-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

47 citing papers in PubMed, 86 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Exploring the repertoire of rhomboid proteases inFrontiers in cellular and infection microbiology · 2026
    Article
  6. Article
  7. Article
  8. Metal cofactor stabilization by a partner protein is a widespread strategy employed for amidase activation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Article
  11. Inactive rhomboid proteins RHBDF1 and RHBDF2 (iRhoms): a decade of research in murine models.Mammalian genome : official journal of the International Mammalian Genome Society · 2021
    Review
  12. Article
  13. Review
  14. Discovery of New Microneme Proteins inFrontiers in veterinary science · 2021
    Article
  15. Transcriptome of theInternational journal of molecular sciences · 2020
    Article
  16. Article
  17. Membrane protein takes the brakes off.Science (New York, N.Y.) · 2019
    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

2 authors at 2 institutions in 1 country.

Sinisa UrbanHoward Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. surban@jhmi.edu
Seth W Dickey
Howard Hughes Medical Institute · USJohns Hopkins University · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Rhomboid proteases are the largest family of enzymes that hydrolyze peptide bonds within the cell membrane. Although discovered to be serine proteases only a decade ago, rhomboid proteases are already considered to be the best understood intramembrane proteases. The presence of rhomboid proteins in all domains of life emphasizes their importance but makes their evolutionary history difficult to chart with confidence. Phylogenetics nevertheless offers three guiding principles for interpreting rhomboid function. The near ubiquity of rhomboid proteases across evolution suggests broad, organizational roles that are not directly essential for cell survival. Functions have been deciphered in only about a dozen organisms and fall into four general categories: initiating cell signaling in animals, facilitating bacterial quorum sensing, regulating mitochondrial homeostasis, and dismantling adhesion complexes of parasitic protozoa. Although in no organism has the full complement of rhomboid function yet been elucidated, links to devastating human disease are emerging rapidly, including to Parkinson's disease, type II diabetes, cancer, and bacterial and malaria infection. Rhomboid proteases are unlike most proteolytic enzymes, because they are membrane-immersed; understanding how the membrane immersion affects their function remains a key challenge.

Indexed as

AnimalsCell MembraneDNA-Binding ProteinsDrosophilaDrosophila ProteinsEndopeptidasesEnzyme ActivationEpidermal Growth FactorEscherichia coliEscherichia coli ProteinsHomeostasisHumansMembrane ProteinsMitochondriaPhylogenyProteolysisDNA-Binding ProteinsDrosophila ProteinsEndopeptidasesEpidermal Growth FactorEscherichia coli ProteinsGlpG protein, E coliMembrane Proteinsspi protein, Drosophila

Identifiers

PMID22035660
PMCPMC3333768
OpenAlexW2109961287

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.