Evidence map›Paper›PMID 35085786›Full record

ArticleMolecular & cellular proteomics : MCP2022

Simple But Efficacious Enrichment of Integral Membrane Proteins and Their Interactions for In-Depth Membrane Proteomics.

Pornparn Kongpracha, Pattama Wiriyasermkul, Noriyoshi Isozumi, Satomi Moriyama, Yoshikatsu Kanai, Shushi Nagamori

Open access · goldAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 41 citations in OpenAlex.

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  17. Stress resilience-enhancing drugs preserve tissue structure and function in degenerating retina via phosphodiesterase inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

6 authors at 3 institutions in 1 country.

Pornparn KongprachaDepartment of Laboratory Medicine, The Jikei University School of Medicine, Tokyo, Japan; Department of Collaborative Research for Biomolecular Dynamics, Nara Medical University, Nara, Japan.
Pattama WiriyasermkulDepartment of Laboratory Medicine, The Jikei University School of Medicine, Tokyo, Japan; Department of Collaborative Research for Biomolecular Dynamics, Nara Medical University, Nara, Japan.
Noriyoshi IsozumiDepartment of Bio-system Pharmacology, Graduate School of Medicine, Osaka University, Osaka, Japan.
Satomi MoriyamaDepartment of Collaborative Research for Biomolecular Dynamics, Nara Medical University, Nara, Japan.
Yoshikatsu KanaiDepartment of Bio-system Pharmacology, Graduate School of Medicine, Osaka University, Osaka, Japan.
Shushi NagamoriDepartment of Laboratory Medicine, The Jikei University School of Medicine, Tokyo, Japan; Department of Collaborative Research for Biomolecular Dynamics, Nara Medical University, Nara, Japan. Electronic address: snagamori@nagamori-lab.jp.
Jikei University School of Medicine · JPThe University of Osaka · JPNara Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane proteins play essential roles in various cellular processes, such as nutrient transport, bioenergetic processes, cell adhesion, and signal transduction. Proteomics is one of the key approaches to exploring membrane proteins comprehensively. Bottom-up proteomics using LC-MS/MS has been widely used in membrane proteomics. However, the low abundance and hydrophobic features of membrane proteins, especially integral membrane proteins, make it difficult to handle the proteins and are the bottleneck for identification by LC-MS/MS. Herein, to improve the identification and quantification of membrane proteins, we have stepwisely evaluated methods of membrane enrichment for the sample preparation. The enrichment methods of membranes consisted of precipitation by ultracentrifugation and treatment by urea or alkaline solutions. The best enrichment method in the study, washing with urea after isolation of the membranes, resulted in the identification of almost twice as many membrane proteins compared with samples without the enrichment. Notably, the method significantly enhances the identified numbers of multispanning transmembrane proteins, such as solute carrier transporters, ABC transporters, and G-protein-coupled receptors, by almost sixfold. Using this method, we revealed the profiles of amino acid transport systems with the validation by functional assays and found more protein-protein interactions, including membrane protein complexes and clusters. Our protocol uses standard procedures in biochemistry, but the method was efficient for the in-depth analysis of membrane proteome in a wide range of samples.

Indexed as

Membrane ProteinsProteomicsChromatography, LiquidProteomeTandem Mass SpectrometryUreaMembrane ProteinsProteomeUreaalkalineprotein complexprotein–protein interactiontransmembrane domaintransporterurea

Identifiers

PMID35085786
PMCPMC9062332
OpenAlexW4207026380

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.