ArticleMethods in molecular biology (Clifton, N.J.)2015
Dynamic single-molecule force spectroscopy of rhodopsin in native membranes.
Article in Methods in molecular biology (Clifton, N.J.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
The trial behind it
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
10 citing papers in PubMed.
- Atomic force microscopy-single-molecule force spectroscopy unveils GPCR cell surface architecture.Communications biology · 2022Article
- Single-cell fluidic force microscopy reveals stress-dependent molecular interactions in yeast mating.Communications biology · 2021Article
- Force-clamp spectroscopy identifies a catch bond mechanism in a Gram-positive pathogen.Nature communications · 2020Article
- Differentiating between Inactive and Active States of Rhodopsin by Atomic Force Microscopy in Native Membranes.Analytical chemistry · 2019Article
- 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
- New views on phototransduction from atomic force microscopy and single molecule force spectroscopy on native rods.Scientific reports · 2017Article
- Structural Heterogeneity of CNGA1 Channels Revealed by Electrophysiology and Single-Molecule Force Spectroscopy.ACS omega · 2016Article
- Impact of reduced rhodopsin expression on the structure of rod outer segment disc membranes.Biochemistry · 2015Article
- Rhodopsin Forms Nanodomains in Rod Outer Segment Disc Membranes of the Cold-Blooded Xenopus laevis.PloS one · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Membrane proteins are an important class of proteins in biology and therapeutics. Understanding the dynamic nature of the molecular interactions that stabilize membrane protein structure is critical to dissect the mechanism of action and dysfunction of these proteins. Single-molecule force spectroscopy (SMFS) and dynamic SMFS (DFS) are emerging nanotechniques that allow the study of membrane proteins under the physiologically relevant conditions of a lipid bilayer and buffer conditions. These techniques directly probe the molecular interactions underlying protein structure and reveal unique insights about their properties. Outlined in this report will be procedures on how to conduct SMFS and DFS on rhodopsin in native retinal membranes. Rhodopsin is a membrane protein belonging to the G protein-coupled receptor family of proteins, one of the largest families of proteins in nature.
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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.