Evidence map›Paper›PMID 18440799›Full record

ReviewCurrent opinion in structural biology2008

Core principles of intramembrane proteolysis: comparison of rhomboid and site-2 family proteases.

Sinisa Urban, Yigong Shi

Abstract readComparative StudyReview
In one paragraph

Review in Current opinion in structural biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Three-dimensional structure of the signal peptide peptidase.The Journal of biological chemistry · 2011
    Article
  9. Article
  10. Article
  11. Article
  12. Participation of transmembrane domain 1 of presenilin 1 in the catalytic pore structure of the γ-secretase.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010
    Article
  13. New insights into S2P signaling cascades: regulation, variation, and conservation.Protein science : a publication of the Protein Society · 2010
    Review
  14. The PARL family of mitochondrial rhomboid proteases.Seminars in cell & developmental biology · 2010
    Review
  15. Review
  16. Intramembrane proteolytic cleavage of a membrane-tethered transcription factor by a metalloprotease depends on ATP.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  17. Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  18. Review
  19. Structure and mechanism of intramembrane protease.Seminars in cell & developmental biology · 2009
    Review
  20. Toward structural elucidation of the gamma-secretase complex.Structure (London, England : 1993) · 2009
    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

2 authors.

Sinisa UrbanDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. surban@jhmi.edu
Yigong Shi

Funding

Biochemistry of Intramembrane Proteases From PathogensR01AI066025 · NIAID · JOHNS HOPKINS UNIVERSITY · PI NATHANS, JEREMY · 2005 to 2019
$4.9M
NIAID NIH HHS R01 AI066025NIAID NIH HHS R01AI066025Wellcome Trust
6 · The paper itself

Abstract

Cleavage of proteins within their membrane-spanning segments is an ancient regulatory mechanism that has evolved to control a myriad of cellular processes in all forms of life. Although three mechanistic families of enzymes have been discovered that catalyze hydrolysis within the water-excluding environment of the membrane, how they achieve this improbable reaction has been both a point of controversy and skepticism. The crystal structures of rhomboid and site-2 protease, two different classes of intramembrane proteases, have been solved recently. Combined with current biochemical analyses, this advance provides an unprecedented view of how nature has solved the problem of facilitating hydrolysis within membranes in two independent instances. We focus on detailing the similarities between these unrelated enzymes to define core biochemical principles that govern this conserved regulatory mechanism.

Indexed as

HydrolysisMembrane ProteinsModels, MolecularPeptide HydrolasesSubstrate SpecificityMembrane ProteinsPeptide Hydrolases

Identifiers

PMID18440799
PMCPMC2572676

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.