Relevant bibliographies by topics / Channelrhodopsin

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Channelrhodopsin'

Author: Grafiati
Published: 4 June 2021
Last updated: 11 March 2023

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Journal articles on the topic "Channelrhodopsin"

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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 (November 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 advantage of PsChR2 compared to classical channelrhodopsin CrChR2 is the blue shift of its excitation spectrum, which opens the possibility for its application in all-optical electrophysiology experiments that require the separation of the maxima of the spectra of channelrhodopsins used for the stimulation of neurons and the maxima of the excitation spectra of various red fluorescent probes. We compared the response (generation of action potentials) of neurons expressing CrChR2 and PsChR2 to light stimuli at 530 and 550 nm commonly used for the excitation of red fluorescent probes. The 530-nm light was significantly (3.7 times) less efficient in the activation of neurons expressing PsChR2 vs. CrChR2-expressing neurons. The light at 550 nm, even at the maximal used intensity, failed to stimulate neurons expressing either of the studied opsins. This indicates that the PsChR2 channelrhodopsin from the alga P. subcordiformis is a promising optogenetic tool, both in terms of its frequency characteristics and possibility of its application for neuronal stimulation with a short-wavelength (blue, 470 nm) light accompanied by simultaneous recording of various physiological processes using fluorescent probes.
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Sineshchekov, Oleg A., Hai Li, Elena G. Govorunova, and John L. Spudich. "Photochemical reaction cycle transitions during anion channelrhodopsin gating." Proceedings of the National Academy of Sciences 113, no. 14 (March 21, 2016): E1993—E2000. http://dx.doi.org/10.1073/pnas.1525269113.

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A recently discovered family of natural anion channelrhodopsins (ACRs) have the highest conductance among channelrhodopsins and exhibit exclusive anion selectivity, which make them efficient inhibitory tools for optogenetics. We report analysis of flash-induced absorption changes in purified wild-type and mutant ACRs, and of photocurrents they generate in HEK293 cells. Contrary to cation channelrhodopsins (CCRs), the ion conducting state of ACRs develops in an L-like intermediate that precedes the deprotonation of the retinylidene Schiff base (i.e., formation of an M intermediate). Channel closing involves two mechanisms leading to depletion of the conducting L-like state: (i) Fast closing is caused by a reversible L⇔M conversion. Glu-68 in Guillardia theta ACR1 plays an important role in this transition, likely serving as a counterion and proton acceptor at least at high and neutral pH. Incomplete suppression of M formation in the GtACR1_E68Q mutant indicates the existence of an alternative proton acceptor. (ii) Slow closing of the channel parallels irreversible depletion of the M-like and, hence, L-like state. Mutation of Cys-102 that strongly affected slow channel closing slowed the photocycle to the same extent. The L and M intermediates were in equilibrium in C102A as in the WT. In the position of Glu-123 in channelrhodopsin-2, ACRs contain a noncarboxylate residue, the mutation of which to Glu produced early Schiff base proton transfer and strongly inhibited channel activity. The data reveal fundamental differences between natural ACR and CCR conductance mechanisms and their underlying photochemistry, further confirming that these proteins form distinct families of rhodopsin channels.
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Schneider, Franziska, Christiane Grimm, and Peter Hegemann. "Biophysics of Channelrhodopsin." Annual Review of Biophysics 44, no. 1 (June 22, 2015): 167–86. http://dx.doi.org/10.1146/annurev-biophys-060414-034014.

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Ernst, Oliver P., Pedro A. Sánchez Murcia, Peter Daldrop, Satoshi P. Tsunoda, Suneel Kateriya, and Peter Hegemann. "Photoactivation of Channelrhodopsin." Journal of Biological Chemistry 283, no. 3 (November 9, 2007): 1637–43. http://dx.doi.org/10.1074/jbc.m708039200.

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Channelrhodopsins (ChRs) are light-gated ion channels that control photomovement of microalgae. In optogenetics, ChRs are widely applied for light-triggering action potentials in cells, tissues, and living animals, yet the spectral properties and photocycle of ChR remain obscure. In this study, we cloned a ChR from the colonial alga Volvox carteri, VChR. After electrophysiological characterization in Xenopus oocytes, VChR was expressed in COS-1 cells and purified. Time-resolved UV-visible spectroscopy revealed a pH-dependent equilibrium of two dark species, D470/D480. Laser flashes converted both with τ ≈ 200 μs into major photointermediates P510/P530, which reverted back to the dark states with τ ≈ 15-100 ms. Both intermediates were assigned to conducting states. Three early intermediates P500/P515 and P390 were detected on a ns to μs time scale. The spectroscopic and electrical data were unified in a photocycle model. The functional expression of VChR we report here paves the way toward a broader structure/function analysis of the recently identified class of light-gated ion channels.
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Lórenz-Fonfría, Víctor A., Tom Resler, Nils Krause, Christopher Engelhard, Robert Bittl, Mirka Neumann-Verhoefen, Josef Wachtveitl, et al. "Gating in channelrhodopsin." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1837 (July 2014): e105. http://dx.doi.org/10.1016/j.bbabio.2014.05.251.

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Erofeev, Alexander, Evgenii Gerasimov, Anastasia Lavrova, Anastasia Bolshakova, Eugene Postnikov, Ilya Bezprozvanny, and Olga L. Vlasova. "Light Stimulation Parameters Determine Neuron Dynamic Characteristics." Applied Sciences 9, no. 18 (September 5, 2019): 3673. http://dx.doi.org/10.3390/app9183673.

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Optogenetics is a recently developed technique that is widely used to study neuronal function. In optogenetic experiments, neurons encode opsins (channelrhodopsins, halorhodopsins or their derivatives) by means of viruses, plasmids or genetic modification (transgenic lines). Channelrhodopsin are light activated ion channels. Their expression in neurons allows light-dependent control of neuronal activity. The duration and frequency of light stimulation in optogenetic experiments is critical for stable, robust and reproducible experiments. In this study, we performed systematic analyses of these parameters using primary cultures of hippocampal neurons transfected with channelrhodopsin-2 (ChR2). The main goal of this work was to identify the optimal parameters of light stimulation that would result in stable neuronal activity during a repeated light pulse train. We demonstrated that the dependency of the photocurrent on the light pulse duration is described by a right-skewed bell-shaped curve, while the dependence on the stimulus intensity is close to linear. We established that a duration between 10–30 ms of stimulation was the minimal time necessary to achieve a full response. Obtained results will be useful in planning and interpretation of optogenetic experiments.
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Berndt, Andre, Soo Yeun Lee, Jonas Wietek, Charu Ramakrishnan, Elizabeth E. Steinberg, Asim J. Rashid, Hoseok Kim, et al. "Structural foundations of optogenetics: Determinants of channelrhodopsin ion selectivity." Proceedings of the National Academy of Sciences 113, no. 4 (December 22, 2015): 822–29. http://dx.doi.org/10.1073/pnas.1523341113.

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The structure-guided design of chloride-conducting channelrhodopsins has illuminated mechanisms underlying ion selectivity of this remarkable family of light-activated ion channels. The first generation of chloride-conducting channelrhodopsins, guided in part by development of a structure-informed electrostatic model for pore selectivity, included both the introduction of amino acids with positively charged side chains into the ion conduction pathway and the removal of residues hypothesized to support negatively charged binding sites for cations. Engineered channels indeed became chloride selective, reversing near −65 mV and enabling a new kind of optogenetic inhibition; however, these first-generation chloride-conducting channels displayed small photocurrents and were not tested for optogenetic inhibition of behavior. Here we report the validation and further development of the channelrhodopsin pore model via crystal structure-guided engineering of next-generation light-activated chloride channels (iC++) and a bistable variant (SwiChR++) with net photocurrents increased more than 15-fold under physiological conditions, reversal potential further decreased by another ∼15 mV, inhibition of spiking faithfully tracking chloride gradients and intrinsic cell properties, strong expression in vivo, and the initial microbial opsin channel-inhibitor–based control of freely moving behavior. We further show that inhibition by light-gated chloride channels is mediated mainly by shunting effects, which exert optogenetic control much more efficiently than the hyperpolarization induced by light-activated chloride pumps. The design and functional features of these next-generation chloride-conducting channelrhodopsins provide both chronic and acute timescale tools for reversible optogenetic inhibition, confirm fundamental predictions of the ion selectivity model, and further elucidate electrostatic and steric structure–function relationships of the light-gated pore.
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Hegemann, Peter, Sabine Ehlenbeck, and Dietrich Gradmann. "Multiple Photocycles of Channelrhodopsin." Biophysical Journal 89, no. 6 (December 2005): 3911–18. http://dx.doi.org/10.1529/biophysj.105.069716.

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Watanabe, Hiroshi C., Kai Welke, Franziska Schneider, Satoshi Tsunoda, Feng Zhang, Karl Deisseroth, Peter Hegemann, and Marcus Elstner. "Structural Model of Channelrhodopsin." Journal of Biological Chemistry 287, no. 10 (January 11, 2012): 7456–66. http://dx.doi.org/10.1074/jbc.m111.320309.

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Nikolic, Konstantin, Nir Grossman, Matthew S. Grubb, Juan Burrone, Chris Toumazou, and Patrick Degenaar. "Photocycles of Channelrhodopsin-2." Photochemistry and Photobiology 85, no. 1 (January 2009): 400–411. http://dx.doi.org/10.1111/j.1751-1097.2008.00460.x.

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Dissertations / Theses on the topic "Channelrhodopsin"

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Berndt, André. "Mechanismus und anwendungsbezogene Optimierung von Channelrhodopsin-2." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2011. http://dx.doi.org/10.18452/16350.

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Channelrhodopsin-2 ist ein lichtaktivierter Kationenkanal, der zur nichtinvasiven Steuerung neuronaler Aktivität verwendet wird. Einige grundlegende Eigenschaften dieses Proteins sind bereits bekannt, aber die molekularen Mechanismen des Ionentransports und der Aktivierung liegen noch weitgehend im Dunkeln. Ziel dieser Studie war es, anhand von Mutationsstudien die Funktion einzelner Aminosäuren zu bestimmen. Dazu habe ich gezielt potentiell wichtige Reste substituiert und die Channelrhodopsin-2-Varianten elektrophysiologisch untersucht. Um die aufgetretenen Änderungen beim Ionentransport und den Kanalkinetiken zu erklären, habe ich verschiedene mathematische Modelle an die experimentellen Daten angepasst. Dabei stellte sich heraus, dass die Reste H134 und E90 Schlüsselpositionen für den Protonentransport sind. Außerdem haben auch die Reste E235 und D253 einen großen Einfluss auf den Ladungstransport. Dagegen wird die Kanalöffnung von C128 und D156 kontrolliert. Des Weiteren kontrolliert E123 die Übergänge zwischen leitenden und nichtleitenden Zuständen von Channelrhodopsin-2. Aus der zielgerichteten Mutation von Aminosäuren resultierten Varianten, die langsamere oder schnellere Kinetiken hatten oder eine bessere Expression zeigten als der Wildtyp. Das Anwendungspotential der modifizierten Kanäle wurde in Kooperationen mit neurophysiologischen Arbeitsgruppen untersucht. Dadurch konnten drei neue Typen von Channelrhodopsinen in die Neurophysiologie eingeführt werden. Die step-functions opsins führen zu einer anhaltenden Membrandepolarisation, die die Erregbarkeit von Neuronen gegenüber synaptischen Inputs erhöht. ChETA erlaubt das zeitlich präzise Auslösen von Aktionspotentialen auch bei sehr hohen Anregungsfrequenzen. T159C und E123T/T159C ermöglichen durch ihre großen Photoströme und optimierten Kinetiken eine hohe Zuverlässigkeit bei der optischen Steuerung neuronaler Aktivität. Dadurch wird das Anwendungsspektrum von Channelrhodopsin-2 erheblich erweitert.
Channelrhodopsin-2 is a light-activated cation channel which has become a very useful tool in neurophysiology, since it allows the noninvasive control of neural activity. Some of the basic features of this channel are known from previous studies, but the molecular mechanisms of ion translocation and activation are largely unknown. The aim of my thesis is to elucidate the function of single amino acids by mutational studies. I replaced potentially important residues and probed the constructs by electrophysiological measurements under various conditions. Additionally, I fitted the experimental data to several mathematical models in order to explain changes in ion permeabilities and channel kinetics and I assigned particular functions to the mutated residues. Apparently, H134 and E90 are key positions for the proton transportation. Mutations at E235 and D253 also strongly influence ion translocation, whereas C128 and D156 obviously control the channel opening. Moreover, I found that E123 is a key element for the channel activation which controls the transitions between conducting and non-conducting states of Channelrhodopsin-2. The genetically modified Channelrhodopsin-2-variants provide several favorable features, such as, a slower or faster channel opening and closing or an optimized expression. Therefore, we tested the potential of promising constructs for applications in collaboration with neurophysiology laboratories. Finally, we introduced three new tools. First, step-function opsins induce a sustained membrane depolarization which sensitizes neurons to native synaptic inputs. Second, the ChETA variant allows the temporally precise generation of action potentials even at high stimulation frequencies. Third, T159C and E123T/T159C provide large photocurrents and optimized kinetics resulting in an improved performance in the noninvasive control of neural activity. In summary, this significantly broadens the range of application for channelrhodopsin-2.
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Krause, Nils [Verfasser]. "Structural rearrangements upon opening of Channelrhodopsin-2 / Nils Krause." Berlin : Freie Universität Berlin, 2016. http://d-nb.info/1106250842/34.

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Scott, Nadia Aleyna. "Optical probing of hemodynamic responses in vivo with channelrhodopsin-2." Thesis, University of British Columbia, 2011. http://hdl.handle.net/2429/36449.

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Maintenance of neuronal function depends on the timely delivery of oxygen and glucose through changes in blood flow that are linked to the level of ongoing neuronal and glial activity, yet the mechanisms underlying this stimulus-dependent control of blood flow remain unclear. Here, using transgenic mice expressing channelrhodopsin-2 in a subset of layer 5b pyramidal neurons, we report that changes in intrinsic optical signals and blood flow can be evoked by activation of channelrhodopsin-2 neurons without direct involvement of other cell types. We have used a combination of imaging and pharmacology to examine the importance of glutamatergic synaptic signaling in neurovascular coupling. In contrast to sensory-evoked responses, we observed that glutamate-dependent neuronal signalling is not essential for the production of channelrhodopsin-evoked hemodynamic responses. Our results rather suggest that ChR2-activated neurons are coupled to the surrounding vasculature through a glutamate-dependent astrocytic pathway mediated by the Group I metabotropic glutamate receptor mGluR5.
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Resler, Tom [Verfasser]. "Time-Resolved Analysis of Protonation Dynamics in Channelrhodopsin-2 / Tom Resler." Berlin : Freie Universität Berlin, 2017. http://d-nb.info/1135969256/34.

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Shen, Yi-Chung. "Development of Red-Shifted Channelrhodopsin Variants Having Chemically Modified Retinylidene Chromophore." Kyoto University, 2019. http://hdl.handle.net/2433/242648.

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Gökce, Onur. "Channelrhodopsin assisted synapse identity mapping reveals clustering of layer 5 intralaminar inputs." Diss., Ludwig-Maximilians-Universität München, 2014. http://nbn-resolving.de/urn:nbn:de:bvb:19-179689.

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Whitaker, Jessica Rae. "LIGHT-ACTIVATION OF CHANNELRHODOPSIN-2 EXPRESSED IN HINDLIMB MUSCLE OF LIVING CHICK EMBRYOS." OpenSIUC, 2016. https://opensiuc.lib.siu.edu/theses/1997.

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The importance of activity during the development of central components of the nervous system such as the visual system has long been recognized (Wiesel & Hubel 1963) and it is beginning to be understood that sensory experience and motor behavior are equally important for neuromuscular development (Brumley et al. 2015; Sharp & Bekoff 2015). The chick embryo model has proven to be especially useful in studying the relationships among motor behavior, sensory experience, and neuromuscular development (Oppenheim et al. 1978; Sharp & Bekoff 2001) due to its accessibility and early onset of movement behavior. Traditionally, neuromuscular blockers have been used to broadly study the role of neural activity and muscle activity during development (Oppenheim et al. 1978; Ding et al. 1983). In order to noninvasively alter neural activity in specific populations of cells, the Sharp lab has developed an optogenetic approach that allows the expression of ChIEF, a variant of channelrhodopsin-2, in the spinal cord of living chick embryos (Sharp & Fromherz 2011). In order to better understand the unique role that muscle activity plays in neuromuscular development, it would be advantageous to directly and noninvasively control muscle activity through light-activation of ChIEF expressed in muscle fibers. Therefore, the primary objective of this thesis research was to achieve ChIEF expression in the plasma membrane of myotubes in living chick embryos. Initial attempts to express ChIEF in chick muscle resulted in low success rates. The CAG promoter in pPB-ChIEF-Tom, the plasmid vector that encodes ChIEF, was likely hindering expression of ChIEF in muscle tissue. Therefore, standard molecular cloning techniques were used to replace the CAG promoter with the myosin light chain promoter which was known to drive transgene expression in chick muscle (Wang et al. 2011). The new DNA construct that resulted from modifying pPB-ChIEF-Tom was identified as pPB-MLC-ChIEF-Tom (mChIEF). ChIEF was successfully expressed in hindlimb muscles of chick embryos via somite electroporation of mChIEF and observed between E7 and E18. Expression patterns corresponded with the current understanding of muscle progenitor contributions of somites to hindlimb muscles (Rees et al. 2003). ChIEF was located in the outer membrane of muscle fibers on E9, E14, and E18 when tissue was histologically examined in conjunction with myosin heavy chain immunofluorescence. Importantly, light-activation of ChIEF in the hindlimb muscle of living chick embryos resulted in muscle contraction and light-evoked hindlimb movements. In addition to demonstrating the functionality of ChIEF expression, an effort was made to characterize the effects of altered parameters of light stimuli on light-evoked movement and determine whether light-evoked muscle contraction could be used to imitate normal, neuronal muscle control. Light intensity was directly related to amplitude and rate of light-evoked movement. Light duration was directly related to amplitude and latency of peak movement. Unfused and fused tetanus were observed when bursts of short duration light pulses with varying interpulse intervals were used to activate ChIEF. This thesis research strongly suggests that light-activation of ChIEF expressed in living, chick embryo hindlimb muscle results in muscle contractions in manner similar to normal, neurally-driven muscle contraction.
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Richards, Ryan. "Molecular and structural determinants that contribute to channel function and gating in channelrhodopsin-2." Digital WPI, 2016. https://digitalcommons.wpi.edu/etd-dissertations/481.

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The green algae Chlamydomonas reinhardtii senses light through two photosensory proteins, channelrhodopsin-1 (ChR1) and channelrhodopsin-2 (ChR2). The initial discovery of these two photoreceptors introduced a new class of light-gated ion channels. ChR2 is an inwardly-rectified ion channel that is selective for cations of multiple valencies. Similar to microbial-rhodopsin ion pumps, ChR2 has a seven transmembrane domain motif that binds the chromophore all-trans retinal through a protonated Schiff base linkage. Physiologically, ChR2 functions to depolarize the membrane which initiates a signaling cascade triggering phototactic response. This fundamental property has been pivotal in pioneering the field of optogenetics, where excitable cells can be manipulated by light. ChR2 reliably causes neuronal spiking with high spatial and temporal control. Moreover, the recent discovery of new chloride-conducting channelrhodopsins (ChloCs) has further expanded the optogenetic toolbox. Although structurally similar to microbial-rhodopsin ion pumps, ChR2 undergoes more complex conformational rearrangements that lead to ion conductance. Currently, the molecular basis for ChR2 gating remains unresolved. Revealing the specific structural interactions that modulate ChR2 function have important implications in understanding the intricacies of ion transport and molecular differences between ion pumps, channels, and transporters. Here we describe a combined computational and experimental approach to elucidate the mechanism of ion conductance, channel gating, and structure-function relationship of ChR2. Our results have contributed to expanding our understanding of the fundamental properties of ion channels.
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Thompson, Mark David, and Mark David Thompson. "Channelrhodopsin-1: Cellular Localization and Role in Eyespot Assembly and Placement in Chlamydomonas reinhardtii." Diss., The University of Arizona, 2016. http://hdl.handle.net/10150/620817.

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The eyespot of the single-celled alga Chlamydomonas aids the cell in detecting the direction of light in the environment. The complex assembly and asymmetric placement of the eyespot provides a model to ask questions about assembly and asymmetric placement of organelles. Understanding the mechanisms that underlie assembly and asymmetric placement of the eyespot can be applied more broadly to their functions in other eukaryotic organisms. This study sought to understand the role of a key protein in those processes, Channelrhodopsin-1 (ChR1). ChR1 was found to localize along the entire length of the D4 rootlet from the region around the daughter basal body to the eyespot. ChR1 was found to primarily localize to the plasma membrane side of the D4, suggesting that ChR1 was being pulled through the plasma membrane from the region around the basal bodies to the eyespot. Further, ChR1 was found to be able to localize to the eyespot even with the truncation of the large cytoplasmic C-terminal domain, suggesting that ChR1 is able to complex with another protein that is being trafficked to the eyespot. One such protein was thought to be ChR2, the other light-activated ion channel localized to the eyespot. Efforts to isolate a mutation in ChR2 were unsuccessful. Initial efforts were made in this dissertation to perform proteomic studies of ChR1 and identify its interacting partners. ChR1 is not the master regulator of either placement or assembly of the eyespot, but work in this study lays the groundwork to further investigate transport of ChR1 and interacting proteins to the eyespot and their role in assembly of the eyespot.
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Engelhard, Christopher [Verfasser]. "Correlating Structure and Function: An EPR Study on Cryptochromes, LOV Proteins and Channelrhodopsin / Christopher Engelhard." Berlin : Freie Universität Berlin, 2016. http://d-nb.info/1100388524/34.

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Books on the topic "Channelrhodopsin"

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Dempski, Robert E., ed. Channelrhodopsin. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-0830-2.

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Dempski, Robert E. Channelrhodopsin: Methods and Protocols. Springer, 2020.

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Dempski, Robert E. Channelrhodopsin: Methods and Protocols. Springer, 2021.

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Book chapters on the topic "Channelrhodopsin"

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Hegemann, Peter. "Channelrhodopsin." In Encyclopedia of Biophysics, 265–68. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_801.

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VanGordon, Monika R. "Molecular Dynamics Simulations of Channelrhodopsin Chimera, C1C2." In Methods in Molecular Biology, 3–15. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0830-2_1.

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Knes, Anna S., Charlotte M. Freeland, and Mike J. F. Robinson. "Optogenetic Stimulation of the Central Amygdala Using Channelrhodopsin." In Methods in Molecular Biology, 351–76. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0830-2_20.

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Sineshchekov, Oleg A., Elena G. Govorunova, and John L. Spudich. "Probing Channelrhodopsin Electrical Activity in Algal Cell Populations." In Methods in Molecular Biology, 85–96. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0830-2_6.

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Sugano, Eriko, and Hiroshi Tomita. "Establishment of Gene Therapy Using Channelrhodopsin-2 to Treat Blindness." In Optogenetics, 341–52. Tokyo: Springer Japan, 2015. http://dx.doi.org/10.1007/978-4-431-55516-2_24.

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Ganjawala, Tushar H., and Zhuo-Hua Pan. "Selecting Channelrhodopsin Constructs for Optimal Visual Restoration in Differing Light Conditions." In Methods in Molecular Biology, 189–99. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0830-2_12.

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Ozdemir, Yagmur Idil, Christina A. Hansen, Mohamed A. Ramy, Eileen L. Troconis, Lauren D. McNeil, and Josef G. Trapani. "Recording Channelrhodopsin-Evoked Field Potentials and Startle Responses from Larval Zebrafish." In Methods in Molecular Biology, 201–20. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0830-2_13.

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Smith, Kelly M., and Brett A. Graham. "Channelrhodopsin-2 Assisted Circuit Mapping in the Spinal Cord Dorsal Horn." In Neuromethods, 347–73. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2039-7_18.

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Wang, Xi, and Yue Cheng. "Optical Manipulation of Perfused Mouse Heart Expressing Channelrhodopsin-2 in Rhythm Control." In Methods in Molecular Biology, 377–90. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0830-2_21.

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Prignano, Lindsey, Lauren Herchenroder, and Robert E. Dempski. "Characterizing Channelrhodopsin Channel Properties Via Two-Electrode Voltage Clamp and Kinetic Modeling." In Methods in Molecular Biology, 49–63. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0830-2_4.

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Conference papers on the topic "Channelrhodopsin"

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Reutsky, Inna, David Ben-Shimol, Nairouz Farah, Shulamit Levenberg, and Shy Shoham. "Patterned optical activation of Channelrhodopsin II expressing retinal ganglion cells." In 2007 3rd International IEEE/EMBS Conference on Neural Engineering. IEEE, 2007. http://dx.doi.org/10.1109/cne.2007.369609.

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Chen, Fangyi, Tao Wu, Teresa Wilson, Hrebesh Subhash, Irina Omelchenko, Michael Bateschell, Lingyan Wang, John Brigande, Zhi-Gen Jiang, and Alfred Nuttall. "Expression and function of channelrhodopsin 2 in mouse outer hair cells." In SPIE BiOS, edited by Samarendra K. Mohanty and Nitish V. Thakor. SPIE, 2013. http://dx.doi.org/10.1117/12.2003114.

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Guk Bae Kim, J. R. Cho, Hee-Sup Shin, and Jee Hyun Choi. "Cortical mapping of the optically evoked responses in channelrhodopsin-2 mouse model." In 2011 33rd Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2011. http://dx.doi.org/10.1109/iembs.2011.6091669.

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Wong, Jonathan, Oscar Abilez, and Ellen Kuhl. "Computational Modelling of Optogenetics in Cardiac Cells." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80810.

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Channelrhodopsin-2 (ChR2) is a light-activated ion channel that can allow scientists to electrically activate cells via optical stimulation. Using a combination of existing computational electrophysiological and mechanical cardiac cell models with a novel ChR2 ion channel model, we created a model for ChR2-transduced cardiac myocytes. We implemented this model into a commonly available finite element platform and simulated both the single cell and the tissue electromechanical response. Our simulations show that it is possible to stimulate cardiac tissue optically with ChR2-transduced cells.
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Hirooka, Masaya, Sze Ping Beh, Toshifumi Asano, Yoshitake Akiyama, Takayuki Hoshino, Keita Hoshino, Hidenobu Tsujimura, Kikuo Iwabuchi, and Keisuke Morishima. "Evaluation and optical control of somatic muscle micro bioactuator of channelrhodopsin transgenic Drosophila melanogaster." In 2014 IEEE 27th International Conference on Micro Electro Mechanical Systems (MEMS). IEEE, 2014. http://dx.doi.org/10.1109/memsys.2014.6765608.

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Polito, Raffaella, Valeria Giliberti, Maria Eleonora Temperini, Eglof Ritter, Matthias Broser, Peter Hegemann, Ljiljana Puskar, Ulrich Schade, Leonetta Baldassarre, and Michele Ortolani. "Light-induced conformational changes of two different Channelrhodopsin mutants probed by difference mid-Infrared microspectroscopy with Synchrotron radiation." In 2020 45th International Conference on Infrared, Millimeter and Terahertz Waves (IRMMW-THz). IEEE, 2020. http://dx.doi.org/10.1109/irmmw-thz46771.2020.9370989.

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Kim, Hyeonyu, Devin Neal, and H. Harry Asada. "Towards the Development of Optogenetically-Controlled Skeletal Muscle Actuators." In ASME 2013 Dynamic Systems and Control Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/dscc2013-4062.

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Engineered skeletal muscle tissue has the potential to be used as dual use actuator and stress-bearing material providing numerous degrees of freedom and with significant active stress generation. To exploit the potential features, however, technologies must be established to generate mature muscle strips that can be controlled with high fidelity. Here, we present a method for creating mature 3-D skeletal muscle tissues that contract in response to optical activation stimuli. The muscle strips are fascicle-like, consisting of several mm-long multi-nucleate muscle cells bundled together. We have found that applying a tension to the fascicle-like muscle tissue promotes maturation of the muscle. The fascicle-like muscle tissue is controlled with high spatiotemporal resolution based on optogenetic coding. The mouse myoblasts C2C12 were transfected with Channelrhodopsin-2 to enable light (∼470 nm) to control muscle contraction. The 3D muscle tissue not only twitches in response to an impulse light beam, but also exhibits a type of tetanus, a prolonged contraction of continuous stimuli, for the first time. In the following, the materials and culturing method used for 3D muscle generation is presented, followed by experimental results of muscle constructs and optogenetic control of the 3D muscle tissue.
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Nikolic, Konstantin, Patrick Degenaar, and Chris Toumazou. "Modeling and Engineering aspects of ChannelRhodopsin2 System for Neural Photostimulation." In Conference Proceedings. Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2006. http://dx.doi.org/10.1109/iembs.2006.260766.

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Nikolic, Konstantin, Patrick Degenaar, and Chris Toumazou. "Modeling and Engineering aspects of ChannelRhodopsin2 System for Neural Photostimulation." In Conference Proceedings. Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2006. http://dx.doi.org/10.1109/iembs.2006.4397730.

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Asim, Muhammad Nabeel, Muhammad Ali Ibrahim, Muhammad Imran Malik, Andreas Dengel, and Sheraz Ahmed. "ChrSLoc-Net: Machine Learning-Based Prediction of Channelrhodopsins Proteins within Plasma Membrane." In 2021 IEEE EMBS International Conference on Biomedical and Health Informatics (BHI). IEEE, 2021. http://dx.doi.org/10.1109/bhi50953.2021.9508615.

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