ArticleBiophysical journal2004
Membrane model for the G-protein-coupled receptor rhodopsin: hydrophobic interface and dynamical structure.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 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
59 citing papers in PubMed, 142 citations in OpenAlex.
- Unraveling allosteric signaling of G protein-coupled receptors (GPCRs) by single-molecule fluorescence.Biophysical reviews · 2026Review
- Hidden water's influence on rhodopsin activation.Biophysical journal · 2024Review
- Exploring GPCR conformational dynamics using single-molecule fluorescence.Methods (San Diego, Calif.) · 2024Review
- Article
- Interdisciplinary biophysical studies of membrane proteins bacteriorhodopsin and rhodopsin.Biophysical reviews · 2023Review
- Regulation of membrane protein structure and function by their lipid nano-environment.Nature reviews. Molecular cell biology · 2023Review
- Phospholipid headgroups govern area per lipid and emergent elastic properties of bilayers.Biophysical journal · 2022Article
- Insights into Membrane Curvature Sensing and Membrane Remodeling by Intrinsically Disordered Proteins and Protein Regions.The Journal of membrane biology · 2022Review
- Hydration-mediated G-protein-coupled receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Exploration of the dynamic interplay between lipids and membrane proteins by hydrostatic pressure.Nature communications · 2022Article
- Activation of G-protein-coupled receptors is thermodynamically linked to lipid solvation.Biophysical journal · 2021Article
- Structure, dynamics and lipid interactions of serotonin receptors: excitements and challenges.Biophysical reviews · 2020Review
- Quantum Mechanical and Molecular Mechanics Modeling of Membrane-Embedded Rhodopsins.The Journal of membrane biology · 2019Review
- Membrane curvature regulates ligand-specific membrane sorting of GPCRs in living cells.Nature chemical biology · 2017Article
- Cholesterol-induced suppression of membrane elastic fluctuations at the atomistic level.Chemistry and physics of lipids · 2016Review
- Micelle-Enhanced Bioorthogonal Labeling of Genetically Encoded Azido Groups on the Lipid-Embedded Surface of a GPCR.Chembiochem : a European journal of chemical biology · 2015Article
- Retinal ligand mobility explains internal hydration and reconciles active rhodopsin structures.Biochemistry · 2014Article
- Coarse-grained molecular dynamics provides insight into the interactions of lipids and cholesterol with rhodopsin.Advances in experimental medicine and biology · 2014Article
- Genetically-encoded molecular probes to study G protein-coupled receptors.Journal of visualized experiments : JoVE · 2013Article
- Surface plasmon resonance applied to G protein-coupled receptors.Biomedical spectroscopy and imaging · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Rhodopsin is the only member of the pharmacologically important superfamily of G-protein-coupled receptors with a known structure at atomic resolution. A molecular dynamics model of rhodopsin in a POPC phospholipid bilayer was simulated for 15 ns, revealing a conformation significantly different from the recent crystal structures. The structure of the bilayer compared with a protein-free POPC control indicated hydrophobic matching with the nonpolar interface of the receptor, in agreement with deuterium NMR experiments. A new generalized molecular surface method, based on a three-dimensional Voronoi cell construction for atoms with different radii, was developed to quantify cross-sectional area profiles for the protein, lipid acyl chains and headgroups, and water. Thus, it was possible to investigate the bilayer deformation due to curvature of the individual lipid monolayers. Moreover, the generalized molecular surface derived hydrophobic interface allowed benchmarking of the hydropathy sequence analysis, an important structural genomics tool. Five water molecules diffused into internal hydration sites during the simulation, yielding a total of 12 internal waters. The cytoplasmic loops and the C-terminal tail, containing the G-protein recognition and protein sorting sequences, exhibited a high mobility, in marked contrast to the extracellular and transmembrane domains. The proposed functional coupling of the highly conserved ERY motif to the lipid-water interface via the cytoplasmic loops provides insight into lipid effects on G-protein-coupled receptor activation in terms of a flexible surface model, involving the spontaneous monolayer curvature.
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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.