Results 11 to 20 of about 17,118 (247)

Channelrhodopsins: From Phototaxis to Optogenetics [PDF]

open access: hybridBiochemistry (Moscow), 2023
Abstract Channelrhodopsins stand out among other retinal proteins because of their capacity to generate passive ionic currents following photoactivation. Owing to that, channelrhodopsins are widely used in neuroscience and cardiology as instruments for optogenetic manipulation of the activity of excitable cells ...
Elena G. Govorunova   +1 more
openalex   +3 more sources

Dual-color optical activation and suppression of neurons with high temporal precision [PDF]

open access: yeseLife
A well-known phenomenon in the optogenetic toolbox is that all light-gated ion channels, including red-shifted channelrhodopsins (ChRs), are activated by blue light, whereas blue-shifted ChRs are minimally responsive to longer wavelengths.
Noëmie Mermet-Joret   +11 more
doaj   +2 more sources

Biophysics of Channelrhodopsin [PDF]

open access: bronzeAnnual Review of Biophysics, 2015
Channelrhodopsins (ChRs) are directly light-gated ion channels that function as sensory photoreceptors in flagellated green algae, allowing these algae to identify optimal light conditions for growth. In neuroscience, ChRs constitute the most versatile tools for the light-induced activation of selected cells or cell types with unprecedented precision ...
Franziska Schneider   +2 more
openalex   +3 more sources

Ion Selectivity and Competition in Channelrhodopsins [PDF]

open access: bronzeBiophysical Journal, 2013
Channelrhodopsins are light-gated ion channels of green algae. They are widely used for the analysis of neuronal networks using light in the emerging field of optogenetics. Under steady-state light conditions, the two open states, O1 and O2, mediate the photocurrents with different ion conductance and selectivity.
Franziska Schneider   +2 more
openalex   +4 more sources

Potassium-selective channelrhodopsins

open access: yesBiophysics and Physicobiology, 2023
Since their discovery 21 years ago, channelrhodopsins have come of age and have become indispensable tools for optogenetic control of excitable cells such as neurons and myocytes. Potential therapeutic utility of channelrhodopsins has been proven by partial vision restoration in a human patient.
Elena G. Govorunova   +2 more
openaire   +4 more sources

Photoactivation of Channelrhodopsin [PDF]

open access: yesJournal of Biological Chemistry, 2008
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.
Oliver P, Ernst   +5 more
openaire   +2 more sources

Multiple Photocycles of Channelrhodopsin [PDF]

open access: yesBiophysical Journal, 2005
Two rhodopsins with intrinsic ion conductance have been identified recently in Chlamydomonas reinhardtii. They were named "channelrhodopsins" ChR1 and ChR2. Both were expressed in Xenopus laevis oocytes, and their properties were studied qualitatively by two electrode voltage clamp techniques. ChR1 is specific for H+, whereas ChR2 conducts Na+, K+, Ca2+
Hegemann, Peter   +2 more
openaire   +3 more sources

Photocycles of Channelrhodopsin‐2 [PDF]

open access: yesPhotochemistry and Photobiology, 2009
AbstractRecent developments have used light‐activated channels or transporters to modulate neuronal activity. One such genetically‐encoded modulator of activity, channelrhodopsin‐2 (ChR2), depolarizes neurons in response to blue light. In this work, we first conducted electrophysiological studies of the photokinetics of hippocampal cells expressing ...
Nikolic, Konstantin   +5 more
openaire   +3 more sources

Intramolecular Proton Transfer in Channelrhodopsins [PDF]

open access: bronzeBiophysical Journal, 2013
Channelrhodopsins serve as photoreceptors that control the motility behavior of green flagellate algae and act as light-gated ion channels when heterologously expressed in animal cells. Here, we report direct measurements of proton transfer from the retinylidene Schiff base in several channelrhodopsin variants expressed in HEK293 cells.
Oleg A. Sineshchekov   +4 more
openalex   +3 more sources

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