Results 31 to 40 of about 18,496 (258)

Morphological Plasticity of the Retina of Viperidae Snakes Is Associated With Ontogenetic Changes in Ecology and Behavior

Frontiers in Neuroanatomy, 2022
Snakes of the Viperidae family have retinas adapted to low light conditions, with high packaging of rod-photoreceptors containing the rhodopsin photopigment (RH1), and three types of cone-photoreceptors, large single and double cones with long-wavelength
Juliana H. Tashiro, Dora F. Ventura, Einat Hauzman   +2 more
doaj   +1 more source

Blue light regenerates functional visual pigments in mammals through a retinyl-phospholipid intermediate. [PDF]

, 2017
The light absorbing chromophore in opsin visual pigments is the protonated Schiff base of 11-cis-retinaldehyde (11cRAL). Absorption of a photon isomerizes 11cRAL to all-trans-retinaldehyde (atRAL), briefly activating the pigment before it dissociates ...
Fain, Gordon L, Hakobyan, Hayk, Ingram, Norianne T, Kaylor, Joanna J, Travis, Gabriel H, Tsan, Avian, Xu, Tongzhou   +6 more
core   +1 more source

Mechanisms of Opsin Activation [PDF]

Journal of Biological Chemistry, 1996
Rhodopsin is constrained in an inactive conformation by interactions with 11-cis-retinal including formation of a protonated Schiff base with Lys296. Upon photoisomerization, major structural rearrangements that involve protonation of the active site Glu113 and cytoplasmic acidic residues, including Glu134, lead to the formation of the active form of ...
J, Buczyłko, J C, Saari, R K, Crouch, K, Palczewski   +3 more
openaire   +2 more sources

Opsin expression predicts male nuptial color in threespine stickleback. [PDF]

, 2018
Theoretical models of sexual selection suggest that male courtship signals can evolve through the build-up of genetic correlations between the male signal and female preference.
Bolnick, Daniel I, Brock, Chad D, Rennison, Diana, Veen, Thor   +3 more
core   +2 more sources

Immunolocalization of arthropsin in the onychophoran Euperipatoides rowelli (Peripatopsidae)

Frontiers in Neuroanatomy, 2016
Opsins are light-sensitive proteins that play a key role in animal vision and are related to the ancient photoreceptive molecule rhodopsin found in unicellular organisms. In general, opsins involved in vision comprise two major groups: the rhabdomeric (r-
Isabell Schumann, Isabell Schumann, Lars Hering, Georg Mayer   +3 more
doaj   +1 more source

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   +3 more sources

S-opsin knockout mice with the endogenous M-opsin gene replaced by an L-opsin variant [PDF]

Visual Neuroscience, 2013
AbstractSpecific variants of human long-wavelength (L) and middle-wavelength (M) cone opsin genes have recently been associated with a variety of vision disorders caused by cone malfunction, including red-green color vision deficiency, blue cone monochromacy, myopia, and cone dystrophy. Strikingly, unlike disease-causing mutations in rhodopsin, most of
Scott H, Greenwald, James A, Kuchenbecker, Daniel K, Roberson, Maureen, Neitz, Jay, Neitz   +4 more
openaire   +2 more sources

Rpgrip1 is required for rod outer segment development and ciliary protein trafficking in zebrafish [PDF]

, 2017
The authors would like to thank the Royal Society of London, the National Eye Research Centre, the Visual Research Trust, Fight for Sight, the W.H. Ross Foundation, the Rosetrees Trust, and the Glasgow Children’s Hospital Charity for supporting this work.
A Eblimit, A Hameed, AF Wright, AI Hollander den, B Kennedy, BW Draper, C Insinna, C Turney, CA Murga-Zamalloa, CM Louie, CS Mellersh, D Deretic, D Mustafi, DH Hong, EM Morrow, F Liu, G Stearns, G Ying, H Patil, H Wang, HH Arts, J Kim, J Wang, J Won, JC Booij, JE Westfall, JM Corless, JP Boylan, KL Cerveny, KL Coene, L Sang, MM Humphries, MV Nachury, O Rinner, OL Moritz, P Castagnet, PD Alfinito, PH Balm, R Bachmann-Gagescu, R Roepman, R Roepman, S Gerber, SC Neuhauss, SE Brockerhoff, SR Patnaik, TA Mavlyutov, TP Dryja, V Traverso, VS Lopes, X Shu, X Shu, X Shu., Y Wada., Y Zhao, YV Makhankov   +54 more
core   +4 more sources

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, Menon, I, Huber, T, Sanyal, S, Banerjee, S, Barré, P, Canis, S, Warren, JD, Hwa, J, Menon, AK   +9 more
openaire   +4 more sources

Ciliary Transport of Opsin [PDF]

, 2009
As part of the renewal of photoreceptor outer segment disk membranes, membrane proteins are transported along the region of the cilium, connecting the inner and outer segments. Genetics studies have indicated the role of motor proteins in this transport.
Deepti, Trivedi, David S, Williams
openaire   +2 more sources