ArticleBiochemistry2010
Conservation of molecular interactions stabilizing bovine and mouse rhodopsin.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 28 citations in OpenAlex.
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Single Molecule Force Spectroscopy to Probe Intermediates and Energetics of Membrane Protein Folding.Chemical reviews · 2026Review
- Aggregation of the Constitutively Active K296E Rhodopsin Mutant Contributes to Retinal Degeneration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Understanding the Rhodopsin Worldview Through Atomic Force Microscopy (AFM): Structure, Stability, and Activity Studies.Chemical record (New York, N.Y.) · 2023Review
- Retinal degeneration in mice expressing the constitutively active G90D rhodopsin mutant.Human molecular genetics · 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
- New views on phototransduction from atomic force microscopy and single molecule force spectroscopy on native rods.Scientific reports · 2017Article
- Forced Unfolding Mechanism of Bacteriorhodopsin as Revealed by Coarse-Grained Molecular Dynamics.Biophysical journal · 2016Article
- Misfolded opsin mutants display elevated β-sheet structure.FEBS letters · 2015Article
- Rhodopsin Forms Nanodomains in Rod Outer Segment Disc Membranes of the Cold-Blooded Xenopus laevis.PloS one · 2015Article
- Nanodomain organization of rhodopsin in native human and murine rod outer segment disc membranes.Biochimica et biophysica acta · 2015Article
- Dynamic single-molecule force spectroscopy of rhodopsin in native membranes.Methods in molecular biology (Clifton, N.J.) · 2015Article
- Structural approaches to understanding retinal proteins needed for vision.Current opinion in cell biology · 2014Review
- Atomic force microscopy: a multifaceted tool to study membrane proteins and their interactions with ligands.Biochimica et biophysica acta · 2014Review
- Kinetic, energetic, and mechanical differences between dark-state rhodopsin and opsin.Structure (London, England : 1993) · 2013Article
- Cholesterol increases kinetic, energetic, and mechanical stability of the human β2-adrenergic receptor.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Ligand-specific interactions modulate kinetic, energetic, and mechanical properties of the human β2 adrenergic receptor.Structure (London, England : 1993) · 2012Article
- Structural, energetic, and mechanical perturbations in rhodopsin mutant that causes congenital stationary night blindness.The Journal of biological chemistry · 2012Article
- Action of molecular switches in GPCRs--theoretical and experimental studies.Current medicinal chemistry · 2012Review
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 2 countries.
Funding
Abstract
Rhodopsin is the light receptor that initiates phototransduction in rod photoreceptor cells. The structure and function of rhodopsin are tightly linked to molecular interactions that stabilize and determine the receptor's functional state. Single-molecule force spectroscopy (SMFS) was used to localize and quantify molecular interactions that structurally stabilize bovine and mouse rhodopsin from native disk membranes of rod photoreceptor cells. The mechanical unfolding of bovine and mouse rhodopsin revealed nine major unfolding intermediates, each intermediate defining a structurally stable segment in the receptor. These stable structural segments had similar localization and occurrence in both bovine and mouse samples. For each structural segment, parameters describing their unfolding energy barrier were determined by dynamic SMFS. No major differences were observed between bovine and mouse rhodopsin, thereby implying that the structures of both rhodopsins are largely stabilized by similar molecular interactions.
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What OpenQuestion holds
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.