Evidence map›Paper›PMID 24099002›Full record

ReviewBiochimica et biophysica acta2013

Function of site-2 proteases in bacteria and bacterial pathogens.

Jessica S Schneider, Michael S Glickman

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

29 citing papers in PubMed, 51 citations in OpenAlex.

  1. Inhibitory proteins ofJournal of bacteriology · 2025
    Article
  2. The Involvement of thePlants (Basel, Switzerland) · 2025
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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 1 institution in 1 country.

Jessica S SchneiderImmunology Program, Memorial Sloan Kettering Cancer Center, 1275 York Ave., New York, NY 10065, USA; Program in Immunology and Microbial Pathogenesis, Weill Cornell Graduate School of Biomedical Sciences, USA.
Michael S Glickman
Memorial Sloan Kettering Cancer Center · US

Funding

IMMUNOLOGY RESEARCH TRAINING PROGRAMT32AI007621 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI CESARMAN, ETHEL · 1999 to 2014
$3.4M
Molecular Analysis of the Rip1 Virulence Pathway of M. tuberculosisR01AI080628 · NIAID · SLOAN-KETTERING INST CAN RESEARCH · PI GLICKMAN, MICHAEL S · 2009 to 2010
$942k
NIAID NIH HHS R01 AI080628NIAID NIH HHS T32 AI007621
6 · The paper itself

Abstract

Site-2 proteases (S2Ps) are a class of intramembrane metalloproteases named after the founding member of this protein family, human S2P, which control cholesterol and fatty acid biosynthesis by cleaving Sterol Regulatory Element Binding Proteins which control cholesterol and fatty acid biosynthesis. S2Ps are widely distributed in bacteria and participate in diverse pathways that control such diverse functions as membrane integrity, sporulation, lipid biosynthesis, pheromone production, virulence, and others. The most common signaling mechanism mediated by S2Ps is the coupled degradation of transmembrane anti-Sigma factors to activate ECF Sigma factor regulons. However, additional signaling mechanisms continue to emerge as more prokaryotic S2Ps are characterized, including direct proteolysis of membrane embedded transcription factors and proteolysis of non-transcriptional membrane proteins or membrane protein remnants. In this review we seek to comprehensively review the functions of S2Ps in bacteria and bacterial pathogens and attempt to organize these proteases into conceptual groups that will spur further study. This article is part of a Special Issue entitled: Intramembrane Proteases.

Indexed as

Gene Expression Regulation, BacterialBacterial ProteinsGram-Negative BacteriaGram-Positive BacteriaLipid MetabolismMembrane ProteinsMetalloendopeptidasesMutationPheromonesProteolysisSignal TransductionSubstrate SpecificityTranscription FactorsVirulence FactorsBacterial ProteinsMembrane ProteinsMetalloendopeptidasesPheromonesTranscription FactorsVirulence FactorsBacterial signal transductionSite two protease

Identifiers

PMID24099002
PMCPMC4097180
OpenAlexW2109550988

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.