ArticlePloS one2019
Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM).
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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Who cites it
7 citing papers in PubMed.
- Exploring the Diversity and Function of the SPFH-Domain Containing Proteins in Pseudomonas aeruginosa.Environmental microbiology reports · 2026Article
- Escherichia coli SPFH Membrane Microdomain Proteins HflKC Contribute to Aminoglycoside and Oxidative Stress Tolerance.Microbiology spectrum · 2023Article
- Plasma Membrane-Cell Wall Feedback in Bacteria.Journal of bacteriology · 2023Review
- Article
- New Antimicrobial Peptide with Two CRAC Motifs: Activity againstMicroorganisms · 2022Article
- Introduction and adaptation of an emerging pathogen to olive trees in Italy.Microbial genomics · 2021Article
- Regulation of the First Committed Step in Lipopolysaccharide Biosynthesis Catalyzed by LpxC Requires the Essential Protein LapC (YejM) and HslVU Protease.International journal of molecular sciences · 2020Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane microdomains or lipid rafts compartmentalize cellular processes by laterally organizing membrane components. Such sub-membrane structures were mainly described in eukaryotic cells, but, recently, also in bacteria. Here, the protein content of lipid rafts in Escherichia coli was explored by mass spectrometry analyses of Detergent Resistant Membranes (DRM). We report that at least three of the four E. coli flotillin homologous proteins were found to reside in DRM, along with 77 more proteins. Moreover, the proteomic data were validated by subcellular localization, using immunoblot assays and fluorescence microscopy of selected proteins. Our results confirm the existence of lipid raft-like microdomains in the inner membrane of E. coli and represent the first comprehensive profiling of proteins in these bacterial membrane platforms.
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