Evidence map›Paper›PMID 20070259›Full record

ReviewThe Biochemical journal2010

Taking the plunge: integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysis.

Sinisa Urban

Open access · greenAbstract readReview
In one paragraph

Review in The Biochemical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

30 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. How does the exosite of rhomboid protease affect substrate processing and inhibition?Protein science : a publication of the Protein Society · 2017
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Novel tripod amphiphiles for membrane protein analysis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2013
    Article
  9. Article
  10. Article
  11. The mammalian endoplasmic reticulum-associated degradation system.Cold Spring Harbor perspectives in biology · 2013
    Review
  12. Article
  13. Article
  14. Glucose-neopentyl glycol (GNG) amphiphiles for membrane protein study.Chemical communications (Cambridge, England) · 2013
    Article
  15. Activity-based probes for rhomboid proteases discovered in a mass spectrometry-based assay.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. Article
  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

1 author at 1 institution 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
Howard Hughes Medical Institute · US

Funding

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

Abstract

Rhomboid proteases are a fascinating class of enzymes that combine a serine protease active site within the core of an integral membrane protein. Despite having key roles in animal cell signalling and microbial pathogenesis, the membrane-immersed nature of these enzymes had long imposed obstacles to elucidating their biochemical mechanisms. But recent multidisciplinary approaches, including eight crystal structures, four computer simulations and nearly 100 engineered mutants interrogated in vivo and in vitro, are coalescing into an integrated model for one rhomboid orthologue in particular, bacterial GlpG. The protein creates a central hydrated microenvironment immersed below the membrane surface to support hydrolysis by its serine protease-like catalytic apparatus. Four conserved architectural elements in particular act as 'keystones' to stabilize this structure, and the lateral membrane-embedded L1 loop functions as a 'flotation device' to position the protease tilted in the membrane. Complex interplay between lateral substrate gating by rhomboid, substrate unwinding and local membrane thinning leads to intramembrane proteolysis of selected target proteins. Although far from complete, studies with GlpG currently offer the best prospect for achieving a thorough and sophisticated understanding of a simplified intramembrane protease.

Indexed as

Gene Expression Regulation, BacterialAnimalsAspartic Acid EndopeptidasesCatalysisCatalytic DomainCell MembraneComputer SimulationDNA-Binding ProteinsEndopeptidasesEscherichia coli ProteinsHumansMembrane ProteinsModels, BiologicalPeptide HydrolasesPresenilinsProtein ConformationAspartic Acid EndopeptidasesDNA-Binding ProteinsEndopeptidasesEscherichia coli ProteinsGlpG protein, E coliMembrane ProteinsPeptide HydrolasesPresenilinssignal peptide peptidase

Identifiers

PMID20070259
PMCPMC3131108
OpenAlexW2009308107

What OpenQuestion holds

Textmetadata
LicenceTDM
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.