Results 11 to 20 of about 28,928 (224)
Bat eyes have ultraviolet-sensitive cone photoreceptors. [PDF]
PLoS ONE, 2009 Mammalian retinae have rod photoreceptors for night vision and cone photoreceptors for daylight and colour vision. For colour discrimination, most mammals possess two cone populations with two visual pigments (opsins) that have absorption maxima at short
Brigitte Müller +5 more
doaj +3 more sources
Broad-Band Activatable White-Opsin. [PDF]
PLoS ONE, 2015 Currently, the use of optogenetic sensitization of retinal cells combined with activation/inhibition has the potential to be an alternative to retinal implants that would require electrodes inside every single neuron for high visual resolution.
Subrata Batabyal +4 more
doaj +2 more sources
Science Signaling, 2011 The G protein–coupled receptor opsin acts as a phospholipid flippase.
Elizabeth M. Adler
openaire +2 more sources
Molecular Biology and Evolution, 2022 Abstract Opsins, the protein moieties of animal visual photo-pigments, have emerged as moonlighting proteins with diverse, light-dependent and -independent physiological functions. This raises the need to revise some basic assumptions concerning opsin expression, structure, classification, and evolution.
Roberto Feuda +2 more
openaire +4 more sources
A Müller Glia-Retinal Pigment Epithelium Apical Network Surrounding Cone Outer Segments in Fish and Mouse. [PDF]
GliaMüller glia and the retinal pigment epithelium interact around cone outer segment in the subretinal space of both zebrafish and mouse. The contacts are established early during development but subsequent to outer segment emergence. ABSTRACT Homeostasis of the vertebrate retina critically depends on two non‐neuronal cell populations, Müller glia and the
Sharkova M +6 more
europepmc +2 more sources
Current Biology, 2002 What are opsins? Opsins are generally considered members of the superfamily of G-protein coupled receptors. But not all opsins activate a G-protein. Their distinguishing features are a 7 transmembrane α-helical structure, and an ability to bind a vitamin A chromophore, retinaldehyde, using a lysine in the 7th α-helix.
Foster, Russell, Bellingham, James
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Opsin Is a Phospholipid Flippase [PDF]
Current Biology, 2011 Polar lipids must flip-flop rapidly across biological membranes to sustain cellular life [1, 2], but flipping is energetically costly [3] and its intrinsic rate is low. To overcome this problem, cells have membrane proteins that function as lipid transporters (flippases) to accelerate flipping to a physiologically relevant rate.
Sakmar, TP +9 more
openaire +4 more sources
Opsins: Evolution in Waiting [PDF]
Current Biology, 2005 Complete vertebrate genome sequencing has revealed a remarkable stability and uniformity in the protein-coding gene set, which at first glance might suggest that gene duplication events are relatively rare. This may be a red herring, or at least a red cichlid, as the Lake Malawi cichlid fishes show rapid and extensive duplication and diversification of
Trezise, A. E. O., Collin, S. P.
openaire +5 more sources
Opsin vs opsin: New materials for biotechnological applications [PDF]
Journal of Applied Physics, 2014 The need of new diagnostic methods satisfying, as an early detection, a low invasive procedure and a cost-efficient value, is orienting the technological research toward the use of bio-integrated devices, in particular, bio-sensors. The set of know-why necessary to achieve this goal is wide, from biochemistry to electronics and is summarized in an ...
ALFINITO, ELEONORA, REGGIANI, Lino
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Unconventional Roles of Opsins [PDF]
Annual Review of Cell and Developmental Biology, 2017 Rhodopsin is the classical light sensor. Although rhodopsin has long been known to be important for image formation in the eye, the requirements for opsins in non–image formation and in extraocular light sensation were revealed much later. Most recent is the demonstration that an opsin in the fruit fly, Drosophila melanogaster, is expressed in ...
Leung, Nicole Y, Montell, Craig
openaire +5 more sources