Evidence map›Paper›PMID 32999380›Full record

ArticleScientific reports2020

The rapid "teabag" method for high-end purification of membrane proteins.

Jenny Hering, Julie Winkel Missel, Liying Zhang, Anders Gunnarsson, Marie Castaldo, Per Amstrup Pedersen, Margareta Ek, Pontus Gourdon, Harm Jan Snijder

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Over-Production of the Human SLC7A10 inInternational journal of molecular sciences · 2023
    Article
  2. Review
  3. Article
  4. The high-throughput production of membrane proteins.Emerging topics in life sciences · 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

9 authors at 3 institutions in 2 countries.

Jenny Hering *Structure, Biophysics and FBLG, Discovery Sciences, R&D, AstraZeneca, Gothenburg, Sweden.
Julie Winkel Missel *Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark.
Liying ZhangDepartment of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark.
Anders GunnarssonStructure, Biophysics and FBLG, Discovery Sciences, R&D, AstraZeneca, Gothenburg, Sweden.
Marie CastaldoDiscovery Biology, Discovery Sciences, R&D, AstraZeneca, Gothenburg, Sweden.
Per Amstrup PedersenDepartment of Biology, University of Copenhagen, Copenhagen, Denmark.
Margareta EkStructure, Biophysics and FBLG, Discovery Sciences, R&D, AstraZeneca, Gothenburg, Sweden.
Pontus GourdonDepartment of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark.
Harm Jan SnijderDiscovery Biology, Discovery Sciences, R&D, AstraZeneca, Gothenburg, Sweden. arjan.snijder@astrazeneca.com.
AstraZeneca (Sweden) · SEUniversity of Copenhagen · DKUniversity of Gothenburg · SE

Funding

Marie Curie 637295
6 · The paper itself

Abstract

Overproduction and purification of membrane proteins are generally challenging and time-consuming procedures due to low expression levels, misfolding, and low stability once extracted from the membrane. Reducing processing steps and shortening the timespan for purification represent attractive approaches to overcome some of these challenges. We have therefore compared a fast "teabag" purification method with conventional purification for five different membrane proteins (MraY, AQP10, ClC-1, PAR2 and KCC2). Notably, this new approach reduces the purification time significantly, and the quality of the purified membrane proteins is equal to or exceeds conventional methods as assessed by size exclusion chromatography, SDS-PAGE and downstream applications such as ITC, crystallization and cryo-EM. Furthermore, the method is scalable, applicable to a range of affinity resins and allows for parallelization. Consequently, the technique has the potential to substantially simplify purification efforts of membrane proteins in basic and applied sciences.

Indexed as

Electrophoresis, Polyacrylamide GelMembrane ProteinsMembrane Proteins

Identifiers

PMID32999380
PMCPMC7528119
OpenAlexW3091380737

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.