Evidence map›Paper›PMID 30066130›Full record

ArticleEuropean biophysics journal : EBJ2018

Production of membrane proteins for characterisation of their pheromone-sensing and antimicrobial resistance functions.

Aalishaa A Azam, Jean M Kinder, G Nasir Khan, Ade Alase, Pikyee Ma, Yang Liu, James R Ault, Peter J F Henderson, Babur Z Chowdhry, Bruce D Alexander and 2 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in European biophysics journal : EBJ, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.7field-weighted citation impact, top 24% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Review
  3. Molecular mechanisms of vancomycin resistance.Protein science : a publication of the Protein Society · 2020
    Review
  4. Article
  5. 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

12 authors at 4 institutions in 1 country.

Aalishaa A AzamAMR Biophysics Group, School of Pharmacy and Biomedical Sciences, University of Central Lancashire, Preston, Lancashire, PR1 2HE, UK.
Jean M KinderAMR Biophysics Group, School of Pharmacy and Biomedical Sciences, University of Central Lancashire, Preston, Lancashire, PR1 2HE, UK.
G Nasir KhanAstbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Ade AlaseAstbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Pikyee MaAstbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Yang LiuAstbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
James R AultAstbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Peter J F HendersonAstbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Babur Z ChowdhryDepartment of Pharmaceutical, Chemical and Environmental Sciences, University of Greenwich, Central Avenue, Chatham, Kent, ME4 4TB, UK.
Bruce D AlexanderDepartment of Pharmaceutical, Chemical and Environmental Sciences, University of Greenwich, Central Avenue, Chatham, Kent, ME4 4TB, UK.
Stephen E HardingNational Centre for Macromolecular Hydrodynamics, School of Biosciences, University of Nottingham, Sutton Bonington, Loughborough, Leicestershire, LE12 5RD, UK.
Mary K Phillips-JonesAMR Biophysics Group, School of Pharmacy and Biomedical Sciences, University of Central Lancashire, Preston, Lancashire, PR1 2HE, UK. sbamp5@exmail.nottingham.ac.uk.ORCID http://orcid.org/0000-0002-0362-4690
University of Leeds · GBUniversity of Greenwich · GBUniversity of Lancashire · GBUniversity of Nottingham · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D001641/1Biotechnology and Biological Sciences Research Council BB/M013081/1University of Central Lancashire Innovation FundWellcome TrustWellcome Trust 094232
6 · The paper itself

Abstract

Despite the importance of membrane proteins in cellular processes, studies of these hydrophobic proteins present major technical challenges, including expression and purification for structural and biophysical studies. A modified strategy of that proposed previously by Saidijam et al. (2005) and others, for the routine expression of bacterial membrane proteins involved in environmental sensing and antimicrobial resistance (AMR), is proposed which results in purification of sufficient proteins for biophysical experiments. We report expression successes amongst a collection of enterococcal vancomycin resistance membrane proteins: VanT

Indexed as

Drug Resistance, BacterialAmino Acid SequenceAnti-Bacterial AgentsMembrane ProteinsPheromonesProtein DenaturationSolubilityTemperatureAnti-Bacterial AgentsMembrane ProteinsPheromonesAnalytical ultracentrifugationCircular dichroism spectroscopyEnterococciHistidine kinaseMembrane proteinsPheromone sensorsStreptococcus pneumoniaeVancomycin resistance

Identifiers

PMID30066130
PMCPMC6182600
OpenAlexW2885197148

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.