Evidence map›Paper›PMID 19458713›Full record

ReviewNature2009

How intramembrane proteases bury hydrolytic reactions in the membrane.

Elinor Erez, Deborah Fass, Eitan Bibi

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Review
  2. Review
  3. Structural insights into human signal peptide peptidase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Monomer Choice InfluencesBiomacromolecules · 2023
    Article
  8. Article
  9. Review
  10. The Nuclear Translocation of Heme Oxygenase-1 in Human Diseases.Frontiers in cell and developmental biology · 2022
    Review
  11. Article
  12. Article
  13. Both positional and chemical variables controlThe Journal of biological chemistry · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Structural Symmetry in Membrane Proteins.Annual review of biophysics · 2015
    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

3 authors.

Elinor ErezDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
Deborah Fass
Eitan Bibi

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intramembrane proteolysis is increasingly seen as a regulatory step in a range of diverse processes, including development, organelle shaping, metabolism, pathogenicity and degenerative disease. Initial scepticism over the existence of intramembrane proteases was soon replaced by intense exploration of their catalytic mechanisms, substrate specificities, regulation and structures. Crystal structures of metal-dependent and serine intramembrane proteases have revealed active sites embedded in the plane of the membrane but accessible by water, a requirement for hydrolytic reactions. Efforts to understand how these membrane-bound proteases carry out their reactions have started to yield results.

Indexed as

AnimalsAspartic Acid EndopeptidasesCell MembraneHumansHydrolysisMembrane ProteinsMetalloproteasesPeptide HydrolasesSerine EndopeptidasesSubstrate SpecificityAspartic Acid EndopeptidasesMembrane ProteinsMetalloproteasesPeptide HydrolasesSerine Endopeptidases

Identifiers

PMID19458713

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.