Evidence map›Paper›PMID 35773581›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Purification of Membrane Proteins Overexpressed in Saccharomyces cerevisiae.

Landon Haslem, Marina Brown, Xin A Zhang, Jennifer M Hays, Franklin A Hays

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

Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 83% 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

1 citing paper in PubMed, 0 citations in OpenAlex.

  1. Other Techniques.Advances in biochemical engineering/biotechnology · 2026
    Review
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 1 institution in 1 country.

Landon HaslemDepartment of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
Marina BrownDepartment of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
Xin A ZhangStephenson Cancer Center, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
Jennifer M HaysDepartment of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
Franklin A HaysDepartment of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA. Franklin-Hays@ouhsc.edu.
University of Oklahoma Health Sciences Center · US

Funding

Virtual Reality and Augmented Reality CoreP20GM103650 · NIGMS · UNIVERSITY OF NEVADA RENO · PI WEBSTER, MICHAEL A · 2012 to 2022
$20.9M
Tetraspanin-enriched microdomains and endothelial barrier functionR01HL132553 · NHLBI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI ZHANG, XIN A · 2017 to 2020
$1.5M
How Tetraspanins Regulate SepsisR01GM135547 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI ZHANG, XIN A · 2020 to 2023
$1.4M
Deciphering ShcA-mediated ROS Production as a Novel Intervention Strategy in Diabetes TherapyR01GM118599 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI HAYS, FRANKLIN ALAN · 2016 to 2019
$1.1M
Molecular and in vivo Determinants of p66Shc-Mediated ROS Function in Cardiovascular HealthF30HL149279 · NHLBI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI HASLEM, LANDON H. · 2019 to 2022
$184k
NHLBI NIH HHS F30 HL149279NHLBI NIH HHS R01 HL132553NIGMS NIH HHS P20 GM103650NIGMS NIH HHS R01 GM118599NIGMS NIH HHS R01 GM135547
6 · The paper itself

Abstract

Membrane protein (MP) functional and structural characterization requires large quantities of high-purity protein for downstream studies. Barriers to MP characterization include ample overexpression, solubilization, and purification of target proteins while maintaining native activity and structure. These barriers can be overcome by utilizing an efficient purification protocol in a high-yield eukaryotic expression system such as Saccharomyces cerevisiae. S. cerevisiae offers improved protein folding and posttranslational modifications compared to prokaryotic expression systems. This chapter contains practices used to overcome barriers of solubilization and purification using S. cerevisiae that are broadly applicable to diverse membrane associated, and membrane integrated, protein targets.

Indexed as

Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMembrane ProteinsProtein FoldingProtein Processing, Post-TranslationalProtein TransportRecombinant ProteinsMembrane ProteinsRecombinant ProteinsSaccharomyces cerevisiae ProteinsChromatographyMembrane proteinProtein productionPurificationSaccharomyces cerevisiae

Identifiers

PMID35773581
PMCPMC9400948
OpenAlexW4285201298

What OpenQuestion holds

Textmetadata
LicenceTDM
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.