Evidence map›Paper›PMID 27284046›Full record

ReviewBiochemical Society transactions2016

Purification of bacterial membrane sensor kinases and biophysical methods for determination of their ligand and inhibitor interactions.

Rohanah Hussain, Stephen E Harding, Charlotte S Hughes, Pikyee Ma, Simon G Patching, Shalini Edara, Giuliano Siligardi, Peter J F Henderson, Mary K Phillips-Jones

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Molecular mechanisms of vancomycin resistance.Protein science : a publication of the Protein Society · 2020
    Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. 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

9 authors at 4 institutions in 1 country.

Rohanah HussainDiamond Light Source Ltd., Diamond House, Harwell Science and Innovation Campus, Didcot, Oxfordshire, OX11 0DE, U.K. MPhillips-Jones@uclan.ac.uk rohanah.hussain@diamond.ac.uk.
Stephen E HardingNational Centre for Macromolecular Hydrodynamics, University of Nottingham, Sutton Bonington, Leicestershire, LE12 5RD, U.K.
Charlotte S HughesDiamond Light Source Ltd., Diamond House, Harwell Science and Innovation Campus, Didcot, Oxfordshire, OX11 0DE, U.K. Membranes, Membrane Proteins & Peptides Research Group, School of Pharmacy & Biomedical Sciences, University of Central Lancashire, Preston, Lancashire, PR1 2HE, U.K.
Pikyee MaFaculty of Biological Sciences, University of Leeds, Leeds, West Yorkshire, LS2 9JT, U.K.
Simon G PatchingFaculty of Biological Sciences, University of Leeds, Leeds, West Yorkshire, LS2 9JT, U.K.
Shalini EdaraFaculty of Biological Sciences, University of Leeds, Leeds, West Yorkshire, LS2 9JT, U.K.
Giuliano SiligardiDiamond Light Source Ltd., Diamond House, Harwell Science and Innovation Campus, Didcot, Oxfordshire, OX11 0DE, U.K.
Peter J F HendersonFaculty of Biological Sciences, University of Leeds, Leeds, West Yorkshire, LS2 9JT, U.K.
Mary K Phillips-JonesMembranes, Membrane Proteins & Peptides Research Group, School of Pharmacy & Biomedical Sciences, University of Central Lancashire, Preston, Lancashire, PR1 2HE, U.K. MPhillips-Jones@uclan.ac.uk rohanah.hussain@diamond.ac.uk.
University of Leeds · GBDiamond Light Source · GBUniversity of Lancashire · GBUniversity of Nottingham · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D001641/1
6 · The paper itself

Abstract

This article reviews current methods for the reliable heterologous overexpression in Escherichia coli and purification of milligram quantities of bacterial membrane sensor kinase (MSK) proteins belonging to the two-component signal transduction family of integral membrane proteins. Many of these methods were developed at Leeds alongside Professor Steve Baldwin to whom this review is dedicated. It also reviews two biophysical methods that we have adapted successfully for studies of purified MSKs and other membrane proteins-synchrotron radiation circular dichroism (SRCD) spectroscopy and analytical ultracentrifugation (AUC), both of which are non-immobilization and matrix-free methods that require no labelling strategies. Other techniques such as isothermal titration calorimetry (ITC) also share these features but generally require high concentrations of material. In common with many other biophysical techniques, both of these biophysical methods provide information regarding membrane protein conformation, oligomerization state and ligand binding, but they possess the additional advantage of providing direct assessments of whether ligand binding interactions are accompanied by conformational changes. Therefore, both methods provide a powerful means by which to identify and characterize inhibitor binding and any associated protein conformational changes, thereby contributing valuable information for future drug intervention strategies directed towards bacterial MSKs.

Indexed as

Protein Kinase InhibitorsBacteriaBacterial ProteinsHistidine KinaseLigandsMembrane ProteinsTransgenesBacterial ProteinsHistidine KinaseLigandsMembrane ProteinsProtein Kinase Inhibitorsanalytical ultracentrifugationcircular dichroismhistidine kinasemembrane sensor kinasetwo-component system

Identifiers

PMID27284046
PMCPMC4900758
OpenAlexW2416702071

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.