Evidence map›Paper›PMID 32057756›Full record

ArticleBiochimica et biophysica acta. Biomembranes2020

Application of fluorescence correlation spectroscopy to study substrate binding in styrene maleic acid lipid copolymer encapsulated ABCG2.

Aaron J Horsey, Deborah A Briggs, Nicholas D Holliday, Stephen J Briddon, Ian D Kerr

Open access · hybridAbstract read
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.8field-weighted citation impact, top 13% 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

9 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Detergent-Free Membrane Protein Purification Using SMA Polymer.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  6. Article
  7. Biological insights from SMA-extracted proteins.Biochemical Society transactions · 2021
    Review
  8. Article
  9. Structure and function of proteins in membranes and nanodiscs.Biochimica et biophysica acta. Biomembranes · 2021
    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

5 authors at 3 institutions in 1 country.

Aaron J HorseySchool of Life Sciences, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH, UK.
Deborah A BriggsSchool of Life Sciences, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH, UK.
Nicholas D HollidaySchool of Life Sciences, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH, UK.
Stephen J BriddonSchool of Life Sciences, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH, UK; Centre of Membrane Proteins and Receptors, University of Birmingham and University of Nottingham, The Midlands, UK. Electronic address: Stephen.briddon@nottingham.ac.uk.
Ian D KerrSchool of Life Sciences, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH, UK. Electronic address: ian.kerr@nottingham.ac.uk.
University of Nottingham · GBQueen's Medical Centre · GBUniversity of Birmingham · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J014508/1
6 · The paper itself

Abstract

ABCG2 is one of a trio of human ATP binding cassette transporters that have the ability to bind and transport a diverse array of chemical substrates out of cells. This so-called "multidrug" transport has numerous physiological consequences including effects on how drugs are absorbed into and eliminated from the body. Understanding how ABCG2 is able to interact with multiple drug substrates remains an important goal in transporter biology. Most drugs are believed to interact with ABCG2 through the hydrophobic lipid bilayer and experimental systems for ABCG2 study need to incorporate this. We have exploited styrene maleic acid to solubilise ABCG2 from HEK293T cells overexpressing the transporter, and confirmed by dynamic light scattering and fluorescence correlation spectroscopy (FCS) that this results in the extraction of SMA lipid copolymer (SMALP) particles that are uniform in size and contain a dimer of ABCG2, which is the predominant physiological state. FCS was further employed to measure the diffusion of a fluorescent ABCG2 substrate (BODIPY-prazosin) in the presence and absence of SMALP particles of purified ABCG2. Autocorrelation analysis of FCS traces enabled the mathematical separation of free BODIPY-prazosin from drug bound to ABCG2 and allowed us to show that combining SMALP extraction with FCS can be used to study specific drug: transporter interactions.

Indexed as

ATP Binding Cassette Transporter, Subfamily G, Member 2DiffusionHEK293 CellsHumansLipidsMaleatesPolystyrenesPrazosinProtein BindingSpectrometry, FluorescenceSubstrate SpecificityATP Binding Cassette Transporter, Subfamily G, Member 2LipidsMaleatesmaleic acidPolystyrenesPrazosinstyrofoamABC transporterFluorescenceFluorescence correlation spectroscopyMembrane proteinMultidrug resistancePharmacologyPhoton counting histogramSMALP

Identifiers

PMID32057756
PMCPMC7156912
OpenAlexW3005545693

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.