ArticleBiophysical journal2016
Dynamics and Interactions of OmpF and LPS: Influence on Pore Accessibility and Ion Permeability.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed, 74 citations in OpenAlex.
- Lipopolysaccharide insertion and vesicle mediated turnover drive growth independent outer membrane adaptation in Escherichia coli.Nature communications · 2026Article
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- Selection of porin and LPS mutants during infection by phage T4 facilitates the emergence of β-lactam resistance in Escherichia coli.npj antimicrobials and resistance · 2026Article
- The structure of the bacterial outer membrane transporter FusA enabled by addition of the native lipid lipopolysaccharide.Journal of structural biology: X · 2025Article
- Dynamics and Interactions of OmpF Porin in an Asymmetric Bacterial Outer Membrane including LPS, ECA, and CPS.Biomacromolecules · 2025Article
- Improved Free-Energy Estimates for the Permeation of Bulky Antibiotic Molecules through Porin Channels Using Temperature-Accelerated Sliced Sampling.Journal of chemical theory and computation · 2025Article
- Recent Advances in Modeling Membrane β-Barrel Proteins Using Molecular Dynamics Simulations: From Their Lipid Environments to Their Assemblies.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Physical properties of the bacterial outer membrane.Nature reviews. Microbiology · 2022Review
- Model architectures for bacterial membranes.Biophysical reviews · 2022Review
- Review
- Challenges for the development of a universal vaccine against leptospirosis revealed by the evaluation of 22 vaccine candidates.Frontiers in cellular and infection microbiology · 2022Article
- Engineering the Outer Membrane Could Facilitate Better Bacterial Performance and Effectively Enhance Poly-3-Hydroxybutyrate Accumulation.Applied and environmental microbiology · 2021Article
- Outer membrane permeability: Antimicrobials and diverse nutrients bypass porins inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Whole Is Bigger than the Sum of Its Parts: Drug Transport in the Context of Two Membranes with Active Efflux.Chemical reviews · 2021Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Insights into the structure of Escherichia coli outer membrane as the target for engineering microbial cell factories.Microbial cell factories · 2021Review
- Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria.The Journal of biological chemistry · 2020Review
- Broadening Activity of Polymyxin by Quaternary Ammonium Grafting.ACS infectious diseases · 2020Article
- Article
- Computational Modeling of Realistic Cell Membranes.Chemical reviews · 2019Review
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 4 countries.
Funding
Abstract
The asymmetric outer membrane of Gram-negative bacteria is formed of the inner leaflet with phospholipids and the outer leaflet with lipopolysaccharides (LPS). Outer membrane protein F (OmpF) is a trimeric porin responsible for the passive transport of small molecules across the outer membrane of Escherichia coli. Here, we report the impact of different levels of heterogeneity in LPS environments on the structure and dynamics of OmpF using all-atom molecular dynamics simulations. The simulations provide insight into the flexibility and dynamics of LPS components that are highly dependent on local environments, with lipid A being the most rigid and O-antigen being the most flexible. Increased flexibility of O-antigen polysaccharides is observed in heterogeneous LPS systems, where the adjacent O-antigen repeating units are weakly interacting and thus more dynamic, compared to homogeneous LPS systems in which LPS interacts strongly with each other with limited overall flexibility due to dense packing. The model systems were validated by comparing molecular-level details of interactions between OmpF surface residues and LPS core sugars with experimental data, establishing the importance of LPS core oligosaccharides in shielding OmpF surface epitopes recognized by monoclonal antibodies. There are LPS environmental influences on the movement of bulk ions (K(+) and Cl(-)), but the ion selectivity of OmpF is mainly affected by bulk ion concentration.
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Registered trials
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.