ArticleeLife2016
Pre-transition effects mediate forces of assembly between transmembrane proteins.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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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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.
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Who cites it
28 citing papers in PubMed, 68 citations in OpenAlex.
- PROTEIN-PROTEIN INTERACTION NETWORKS CAN BE HIGHLY SENSITIVE TO THE MEMBRANE PHASE TRANSITION.bioRxiv : the preprint server for biology · 2025Article
- Protein-protein interaction networks can be highly sensitive to the membrane phase transition.ArXiv · 2025Article
- Markov models and long-term memory in ion channels: A contradiction in terms?Biophysical journal · 2025Article
- Hydrophobic mismatch drives self-organization of designer proteins into synthetic membranes.Nature communications · 2024Article
- Role of the membrane anchor in the regulation of Lck activity.The Journal of biological chemistry · 2022Article
- Amphiphilic Membrane Environments Regulate Enzymatic Behaviors ofACS bio & med chem Au · 2022Article
- Folding and misfolding of potassium channel monomers during assembly and tetramerization.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A rapid and highly sensitive biomarker detection platform based on a temperature-responsive liposome-linked immunosorbent assay.Scientific reports · 2020Article
- Exploring polar headgroup interactions between sphingomyelin and ceramide with infrared spectroscopy.Scientific reports · 2020Article
- Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria.The Journal of biological chemistry · 2020Review
- Exploring the impact of proteins on the line tension of a phase-separating ternary lipid mixture.The Journal of chemical physics · 2019Article
- Computational Modeling of Realistic Cell Membranes.Chemical reviews · 2019Review
- Understanding Membrane Domain-Partitioning Thermodynamics of Transmembrane Domains with Potential of Mean Force Calculations.The journal of physical chemistry. B · 2019Article
- Regimes of Complex Lipid Bilayer Phases Induced by Cholesterol Concentration in MD Simulation.Biophysical journal · 2018Article
- Ion channels can be allosterically regulated by membrane domains near a de-mixing critical point.The Journal of general physiology · 2018Article
- Understanding Conformational Dynamics of Complex Lipid Mixtures Relevant to Biology.The Journal of membrane biology · 2018Review
- A Rationale for Mesoscopic Domain Formation in Biomembranes.Biomolecules · 2018Article
- Clustering and separation of hydrophobic nanoparticles in lipid bilayer explained by membrane mechanics.Scientific reports · 2018Article
- Lipid-Protein Interactions Are Unique Fingerprints for Membrane Proteins.ACS central science · 2018Article
- Membrane-mediated interaction drives mitochondrial ATPase assembly and cristae formation.The Journal of general physiology · 2018Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We present a mechanism for a generic, powerful force of assembly and mobility for transmembrane proteins in lipid bilayers. This force is a pre-transition (or pre-melting) effect for the first-order transition between ordered and disordered phases in the membrane. Using large-scale molecular simulation, we show that a protein with hydrophobic thickness equal to that of the disordered phase embedded in an ordered bilayer stabilizes a microscopic order-disorder interface. The stiffness of that interface is finite. When two such proteins approach each other, they assemble because assembly reduces the net interfacial energy. Analogous to the hydrophobic effect, we refer to this phenomenon as the 'orderphobic effect'. The effect is mediated by proximity to the order-disorder phase transition and the size and hydrophobic mismatch of the protein. The strength and range of forces arising from this effect are significantly larger than those that could arise from membrane elasticity for the membranes considered.
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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.