Evidence map›Paper›PMID 25229188›Full record

ArticleToxins2014

Biochemical characterization of the SPATE members EspPα and EspI.

André Weiss, David Kortemeier, Jens Brockmeyer

Open access · goldAbstract read
In one paragraph

Article in Toxins, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

3 authors.

André WeissInstitute of Food Chemistry, Corrensstraße 45, 48149 Münster, Germany.
David KortemeierInstitute of Food Chemistry, Corrensstraße 45, 48149 Münster, Germany.
Jens BrockmeyerInstitute of Food Chemistry, Corrensstraße 45, 48149 Münster, Germany. jbrockm@uni-muenster.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The activity of serine proteases is influenced by their substrate specificity as well as by the physicochemical conditions. Here, we present the characterization of key biochemical features of the two SPATE members EspPα and EspI from Shiga-toxin producing Escherichia coli (STEC) and enterohemorrhagic E. coli (EHEC). Both proteases show high activity at conditions mimicking the human blood stream. Optimal activities were observed at slightly alkaline pH and low millimolar concentrations of the divalent cations Ca2+ and Mg2+ at physiological temperatures indicating a function in the human host. Furthermore, we provide the first cleavage profile for EspI demonstrating pronounced specificity of this protease.

Indexed as

CalciumChromogenic CompoundsEscherichia coli ProteinsHydrogen-Ion ConcentrationMagnesiumOligopeptidesProteolysisSerine EndopeptidasesSubstrate SpecificityTemperatureVirulence FactorsCalciumChromogenic CompoundsEscherichia coli ProteinsEspI protein, E coliEspP protein, E coliMagnesiumOligopeptidesSerine EndopeptidasesVirulence Factors

Identifiers

PMID25229188
PMCPMC4179157
OpenAlexW2062016579

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.