ArticleThe Journal of biological chemistry2012
Structural, energetic, and mechanical perturbations in rhodopsin mutant that causes congenital stationary night blindness.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 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
- Dark continuous noise from mutant G90D-rhodopsin predominantly underlies congenital stationary night blindness.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Understanding the Rhodopsin Worldview Through Atomic Force Microscopy (AFM): Structure, Stability, and Activity Studies.Chemical record (New York, N.Y.) · 2023Review
- Correlation between the Serum Concentration of Vitamin A and Disease Severity in Patients Carrying p.G90D inInternational journal of molecular sciences · 2023Article
- Stationary and Progressive Phenotypes Caused by the p.G90D Mutation in Rhodopsin Gene.International journal of molecular sciences · 2021Article
- Light Dynamics of the Retinal-Disease-Relevant G90D Bovine Rhodopsin Mutant.Angewandte Chemie (International ed. in English) · 2020Article
- 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
- Seeing and sensing single G protein-coupled receptors by atomic force microscopy.Current opinion in cell biology · 2019Review
- Effect of dietary docosahexaenoic acid on rhodopsin content and packing in photoreceptor cell membranes.Biochimica et biophysica acta. Biomembranes · 2018Article
- Structural role of the T94I rhodopsin mutation in congenital stationary night blindness.EMBO reports · 2016Article
- Priorities and trends in the study of proteins in eye research, 1924-2014.Proteomics. Clinical applications · 2015Article
- Dynamic single-molecule force spectroscopy of rhodopsin in native membranes.Methods in molecular biology (Clifton, N.J.) · 2015Article
- Mechanical stability of bivalent transition metal complexes analyzed by single-molecule force spectroscopy.Beilstein journal of organic chemistry · 2015Article
- Atomic force microscopy: a multifaceted tool to study membrane proteins and their interactions with ligands.Biochimica et biophysica acta · 2014Review
- Constitutively active rhodopsin and retinal disease.Advances in pharmacology (San Diego, Calif.) · 2014Review
- Peptide transporter DtpA has two alternate conformations, one of which is promoted by inhibitor binding.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Kinetic, energetic, and mechanical differences between dark-state rhodopsin and opsin.Structure (London, England : 1993) · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Several point mutations in rhodopsin cause retinal diseases including congenital stationary night blindness and retinitis pigmentosa. The mechanism by which a single amino acid residue substitution leads to dysfunction is poorly understood at the molecular level. A G90D point mutation in rhodopsin causes constitutive activity and leads to congenital stationary night blindness. It is unclear which perturbations the mutation introduces and how they can cause the receptor to be constitutively active. To reveal insight into these mechanisms, we characterized the perturbations introduced into dark state G90D rhodopsin from a transgenic mouse model expressing exclusively the mutant rhodopsin in rod photoreceptor cells. UV-visible absorbance spectroscopy revealed hydroxylamine accessibility to the chromophore-binding pocket of dark state G90D rhodopsin, which is not detected in dark state wild-type rhodopsin but is detected in light-activated wild-type rhodopsin. Single-molecule force spectroscopy suggested that the structural changes introduced by the mutation are small. Dynamic single-molecule force spectroscopy revealed that, compared with dark state wild-type rhodopsin, the G90D mutation decreased energetic stability and increased mechanical rigidity of most structural regions in the dark state mutant receptor. The observed structural, energetic, and mechanical changes in dark state G90D rhodopsin provide insights into the nature of perturbations caused by a pathological point mutation. Moreover, these changed properties observed for dark state G90D rhodopsin are consistent with properties expected for an active state.
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