ArticleBiochimica et biophysica acta2015
Nanodomain organization of rhodopsin in native human and murine rod outer segment disc membranes.
Article in Biochimica et biophysica acta, 2015. 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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Who cites it
28 citing papers in PubMed, 38 citations in OpenAlex.
- Understanding the Rhodopsin Worldview Through Atomic Force Microscopy (AFM): Structure, Stability, and Activity Studies.Chemical record (New York, N.Y.) · 2023Review
- Kinetics of cone specific G-protein signaling in avian photoreceptor cells.Frontiers in molecular neuroscience · 2023Article
- Supramolecular organization of rhodopsin in rod photoreceptor cell membranes.Pflugers Archiv : European journal of physiology · 2021Review
- Differential Aggregation Properties of Mutant Human and Bovine Rhodopsin.Biochemistry · 2021Article
- A hybrid stochastic/deterministic model of single photon response and light adaptation in mouse rods.Computational and structural biotechnology journal · 2021Article
- Loss of PRCD alters number and packaging density of rhodopsin in rod photoreceptor disc membranes.Scientific reports · 2020Article
- Differential adaptations in rod outer segment disc membranes in different models of congenital stationary night blindness.Biochimica et biophysica acta. Biomembranes · 2020Article
- Article
- Rhodopsin Oligomerization and Aggregation.The Journal of membrane biology · 2019Review
- Differentiating between Inactive and Active States of Rhodopsin by Atomic Force Microscopy in Native Membranes.Analytical chemistry · 2019Article
- Seeing and sensing single G protein-coupled receptors by atomic force microscopy.Current opinion in cell biology · 2019Review
- Investigating the Nanodomain Organization of Rhodopsin in Native Membranes by Atomic Force Microscopy.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Detection of misfolded rhodopsin aggregates in cells by Förster resonance energy transfer.Methods in cell biology · 2019Article
- Raftophilic rhodopsin-clusters offer stochastic platforms for G protein signalling in retinal discs.Communications biology · 2019Article
- A Rationale for Mesoscopic Domain Formation in Biomembranes.Biomolecules · 2018Article
- The Retinitis Pigmentosa-Linked Mutations in Transmembrane Helix 5 of Rhodopsin Disrupt Cellular Trafficking Regardless of Oligomerization State.Biochemistry · 2018Article
- Misfolded rhodopsin mutants display variable aggregation properties.Biochimica et biophysica acta. Molecular basis of disease · 2018Article
- Effect of dietary docosahexaenoic acid on rhodopsin content and packing in photoreceptor cell membranes.Biochimica et biophysica acta. Biomembranes · 2018Article
- Adaptations in rod outer segment disc membranes in response to environmental lighting conditions.Biochimica et biophysica acta. Molecular cell research · 2017Article
- Molecular basis for photoreceptor outer segment architecture.Progress in retinal and eye research · 2016Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Biological membranes display distinct domains that organize membrane proteins and signaling molecules to facilitate efficient and reliable signaling. The organization of rhodopsin, a G protein-coupled receptor, in native rod outer segment disc membranes was investigated by atomic force microscopy. Atomic force microscopy revealed that rhodopsin is arranged into domains of variable size, which we refer to herein as nanodomains, in native membranes. Quantitative analysis of 150 disc membranes revealed that the physical properties of nanodomains are conserved in humans and mice and that the properties of individual disc membranes can be variable. Examining the variable properties of disc membranes revealed some of the factors contributing to the size of rod outer segment discs and the formation of nanodomains in the membrane. The diameter of rod outer segment discs was dependent on the number of rhodopsin molecules incorporated into the membrane but independent of the spatial density of rhodopsin. The number of nanodomains present in a single disc was also dependent on the number of rhodopsin molecules incorporated into the membrane. The size of the nanodomains was largely independent of the number or spatial density of rhodopsin in the membrane.
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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.