Relevant bibliographies by topics / Fluorescent opsins

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Fluorescent opsins'

Author: Grafiati
Published: 14 March 2023
Last updated: 31 July 2025

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Journal articles on the topic "Fluorescent opsins"

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Mackin, Robert D., Ruth A. Frey, Carmina Gutierrez, et al. "Endocrine regulation of multichromatic color vision." Proceedings of the National Academy of Sciences 116, no. 34 (2019): 16882–91. http://dx.doi.org/10.1073/pnas.1904783116.

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Vertebrate color vision requires spectrally selective opsin-based pigments, expressed in distinct cone photoreceptor populations. In primates and in fish, spectrally divergent opsin genes may reside in head-to-tail tandem arrays. Mechanisms underlying differential expression from such arrays have not been fully elucidated. Regulation of human red (LWS) vs. green (MWS) opsins is considered a stochastic event, whereby upstream enhancers associate randomly with promoters of the proximal or distal gene, and one of these associations becomes permanent. We demonstrate that, distinct from this stocha
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Cocurullo, Maria, Periklis Paganos, Rossella Annunziata, Danila Voronov, and Maria Ina Arnone. "Single-Cell Transcriptomic Analysis Reveals the Molecular Profile of Go-Opsin Photoreceptor Cells in Sea Urchin Larvae." Cells 12, no. 17 (2023): 2134. http://dx.doi.org/10.3390/cells12172134.

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The ability to perceive and respond to light stimuli is fundamental not only for spatial vision but also to many other light-mediated interactions with the environment. In animals, light perception is performed by specific cells known as photoreceptors and, at molecular level, by a group of GPCRs known as opsins. Sea urchin larvae possess a group of photoreceptor cells (PRCs) deploying a Go-Opsin (Opsin3.2) which have been shown to share transcription factors and morphology with PRCs of the ciliary type, raising new questions related to how this sea urchin larva PRC is specified and whether it
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FEI, YIJIAN, and THOMAS E. HUGHES. "Transgenic expression of the jellyfish green fluorescent protein in the cone photoreceptors of the mouse." Visual Neuroscience 18, no. 4 (2001): 615–23. http://dx.doi.org/10.1017/s0952523801184117.

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The goal of this study was to determine whether the jellyfish green fluorescent protein (GFP) could be used in transgenic mice to label and purify cone photoreceptors from the living retina. We created a transgene containing the 5′ regulatory sequence of the human red pigment gene (pR6.5 lacZ clone; kindly provided by J. Nathans & Y. Wang), fused to the GFP coding sequence. This transgene was used to generate seven lines of PCR-positive founders. Three of the lines had bright green fluorescent cone photoreceptors. The GFP fills the entire cell. Two mouse lines had only a few (∼10–100) fluo
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Idzhilova, Olga S., Gulnur R. Smirnova, Lada E. Petrovskaya, Darya A. Kolotova, Mikhail A. Ostrovsky, and Alexey Y. Malyshev. "Cationic Channelrhodopsin from the Alga Platymonas subcordiformis as a Promising Optogenetic Tool." Biochemistry (Moscow) 87, no. 11 (2022): 1327–34. http://dx.doi.org/10.1134/s0006297922110116.

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Abstract The progress in optogenetics largely depends on the development of light-activated proteins as new molecular tools. Using cultured hippocampal neurons, we compared the properties of two light-activated cation channels – classical channelrhodopsin-2 from Chlamydomonas reinhardtii (CrChR2) and recently described channelrhodopsin isolated from the alga Platymonas subcordiformis (PsChR2). PsChR2 ensured generation of action potentials by neurons when activated by the pulsed light stimulation with the frequencies up to 40-50 Hz, while the upper limit for CrChR2 was 20-30 Hz. An important a
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Nikolaev, Dmitrii M., Andrey A. Shtyrov, Sergey Yu Vyazmin, Andrey V. Vasin, Maxim S. Panov, and Mikhail N. Ryazantsev. "Fluorescence of the Retinal Chromophore in Microbial and Animal Rhodopsins." International Journal of Molecular Sciences 24, no. 24 (2023): 17269. http://dx.doi.org/10.3390/ijms242417269.

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Fluorescence of the vast majority of natural opsin-based photoactive proteins is extremely low, in accordance with their functions that depend on efficient transduction of absorbed light energy. However, several recently proposed classes of engineered rhodopsins with enhanced fluorescence, along with the discovery of a new natural highly fluorescent rhodopsin, NeoR, opened a way to exploit these transmembrane proteins as fluorescent sensors and draw more attention to studies on this untypical rhodopsin property. Here, we review the available data on the fluorescence of the retinal chromophore
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Athanasiou, Dimitra, Maria Kosmaoglou, Naheed Kanuga, et al. "BiP prevents rod opsin aggregation." Molecular Biology of the Cell 23, no. 18 (2012): 3522–31. http://dx.doi.org/10.1091/mbc.e12-02-0168.

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Mutations in rod opsin—the light-sensitive protein of rod cells—cause retinitis pigmentosa. Many rod opsin mutations lead to protein misfolding, and therefore it is important to understand the role of molecular chaperones in rod opsin biogenesis. We show that BiP (HSPA5) prevents the aggregation of rod opsin. Cleavage of BiP with the subtilase cytotoxin SubAB results in endoplasmic reticulum (ER) retention and ubiquitylation of wild-type (WT) rod opsin (WT–green fluorescent protein [GFP]) at the ER. Fluorescence recovery after photobleaching reveals that WT-GFP is usually mobile in the ER. By
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Idzhilova, O. S., D. E. Kolotova, G. R. Smirnova, et al. "NON-SELECTIVE EXPRESSION OF SHORT-WAVELENGTH CONE OPSIN IMPROVES LEARNING IN MICE WITH RETINAL DEGENERATION IN A VISUALLY GUIDED TASK." Доклады Российской академии наук. Науки о жизни 510, no. 1 (2023): 297–302. http://dx.doi.org/10.31857/s268673892360005x.

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Here, we explore the potential of an animal opsin non-selectively expressed in various neuronal elements of the degenerative retina to restore impaired visual function. In this study, a knockout murine model of inherited retinal distrophy was used. Animals were injected intravitreally with either a virus carrying gene of the short-wavelength cone opsin associated with a reporter fluorescent protein, or a control virus carrying the sequence of a modified fluorescent protein that had an enhanced membrane tropism. The viral transduction induced pronounced opsin expression in ganglion, bipolar, an
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MAUCK, MATTHEW C., KATHERINE MANCUSO, JAMES A. KUCHENBECKER, et al. "Longitudinal evaluation of expression of virally delivered transgenes in gerbil cone photoreceptors." Visual Neuroscience 25, no. 3 (2008): 273–82. http://dx.doi.org/10.1017/s0952523808080577.

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Delivery of foreign opsin genes to cone photoreceptors using recombinant adeno-associated virus (rAAV) is a potential tool for studying the basic mechanisms underlying cone based vision and for treating vision disorders. We used an in vivo retinal imaging system to monitor, over time, expression of virally-delivered genes targeted to cone photoreceptors in the Mongolian gerbil (Meriones unguiculatus). Gerbils have a well-developed photopic visual system, with 11–14% of their photoreceptors being cones. We used replication deficient serotype 5 rAAV to deliver a gene for green fluorescent protei
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Polans, A. S., L. G. Altman, and D. S. Papermaster. "Immunocytochemical binding of anti-opsin N-terminal-specific antibodies to the extracellular surface of rod outer segment plasma membranes. Fixation induces antibody binding." Journal of Histochemistry & Cytochemistry 34, no. 5 (1986): 659–64. http://dx.doi.org/10.1177/34.5.2939131.

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We have examined the binding of anti-opsin antibodies to the plasma membrane of frog retinal rod outer segments (ROS) by fluorescence light microscopy and electron microscopy. Polyclonal and monoclonal antibodies specific for the N-terminal domain of opsin were observed to bind to the extracellular surface of ROS plasma membrane of aldehyde-fixed but not of unfixed retinas. This reaction was found regardless of whether purified ROS, rhodopsin, opsin, or an N-terminal peptide of opsin was used as the immunogen. The fixation-induced binding of these antibodies contrasts with the more frequently
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Ullrich, Sybille, Ronnie Gueta, and Georg Nagel. "Degradation of channelopsin-2 in the absence of retinal and degradation resistance in certain mutants." Biological Chemistry 394, no. 2 (2013): 271–80. http://dx.doi.org/10.1515/hsz-2012-0256.

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Abstract Channelrhodopsin-2 is a light-gated cation channel from the green alga Chlamydomonas reinhardtii. It is functional in animal cells and therefore widely used for light-activated depolarization, especially in neurons. To achieve a fully functional protein, the chromophore all-trans-retinal is needed. It has not been investigated whether or not the apoprotein is stable without its cofactor until now. Here we show that channelopsin-2 (Chop2, protein without bound retinal) is much more prone to degradation than channelrhodopsin-2 (protein with retinal). Constructs of Chop2 fused to yellow
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Dissertations / Theses on the topic "Fluorescent opsins"

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Pérez, María del Carmen Marín. "Benchmarking and applications of a computational photobiology tool for design of novel and highly fluorescent rhodopsin proteins." Doctoral thesis, Università di Siena, 2019. http://hdl.handle.net/11365/1070289.

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In recent years, world economy and technological advancement have been transformed by Genomics, which allows us to study, design and build biologically relevant molecules. Genomics is already deeply embedded in industries as diverse as pharmaceutical, food and agricultural, environmental and bio-tech in general. Fast and cheap tools for gene sequencing, protein expression and analysis are commonly used for high-throughput genomic-related studies. However, due to experimental difficulties and long time scales (e.g., protein crystallization), protein structure determination, and thus the fundam
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Comar, William D. Ph D. "ESTABLISHING AND MANIPULATING THE DIMERIC INTERFACE OF VISUAL/NON-VISUAL OPSINS." University of Akron / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=akron152882487417841.

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Book chapters on the topic "Fluorescent opsins"

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Backhaus, Hendrik, Nicolas Ruffini, Anna Wierczeiko, and Albrecht Stroh. "An All-Optical Physiology Pipeline Toward Highly Specific and Artifact-Free Circuit Mapping." In Neuromethods. Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-2764-8_5.

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AbstractAll-optical physiology of neuronal microcircuits requires the integration of optogenetic perturbation and optical imaging, efficient opsin and indicator co-expression, and tailored illumination schemes. It furthermore demands concepts for system integration and a dedicated analysis pipeline for calcium transients in an event-related manner. Here, firstly, we put forward a framework for the specific requirements for technical system integration particularly focusing on temporal precision. Secondly, we devise a step-by-step guide for the image analysis in the context of an all-optical ph
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