M
M. Carter Cornwall
Researcher at Boston University
Publications - 34
Citations - 1860
M. Carter Cornwall is an academic researcher from Boston University. The author has contributed to research in topics: Visual phototransduction & Retinal. The author has an hindex of 20, co-authored 33 publications receiving 1778 citations. Previous affiliations of M. Carter Cornwall include Medical University of South Carolina.
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Journal ArticleDOI
Adaptation in Vertebrate Photoreceptors
TL;DR: There is increasing evidence that the second messenger responsible for the modulation of the transduction cascade during background adaptation is primarily, if not exclusively, Ca(2+), whose intracellular free concentration is decreased by illumination.
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Intra-retinal visual cycle required for rapid and complete cone dark adaptation.
TL;DR: It is found that the Müller cells in the salamander neural retina promote cone-specific pigment regeneration and dark adaptation that are independent of the pigment epithelium.
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A Visual Pigment Expressed in Both Rod and Cone Photoreceptors
Jian Xing Ma,Sergey L. Znoiko,Kashelle L. Othersen,James C. Ryan,Joydip Das,Tomoki Isayama,Masahiro Kono,Daniel D. Oprian,D. Wesley Corson,M. Carter Cornwall,David A. Cameron,Ferenc I. Hárosi,Clint L. Makino,Rosalie K. Crouch +13 more
TL;DR: Results from immunohistochemistry, spectrophotometry, and single-cell RT-PCR demonstrate that, in the tiger salamander, the green rods and blue-sensitive cones contain the same opsin, suggesting that neither the cell topology or the transducin is sufficient to differentiate the rod and the cone response.
Journal ArticleDOI
Noncovalent occupancy of the retinal-binding pocket of opsin diminishes bleaching adaptation of retinal cones
Jing Jin,Rosalie K. Crouch,D. Wesley Corson,Bernice M. Katz,E F MacNichol,M. Carter Cornwall +5 more
TL;DR: Evidence is presented that in solitary cone photoreceptors isolated from the salamander retina, the latter effect is due to the presence of free opsin in the outer segment and this "opsin adaptation" can be reversed by treating the cells with synthetic retinoids similar to 11-cis retinal but having polyene chains too short to form protonated Schiff base attachments to opsin.
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Breaking the covalent bond--a pigment property that contributes to desensitization in cones
Vladimir J. Kefalov,Maureen E. Estevez,Massahiro Kono,Patrice W. Goletz,Rosalie K. Crouch,M. Carter Cornwall,King Wai Yau +6 more
TL;DR: It is demonstrated that the formation of the covalent bond between opsin and 11-cis retinal is reversible in darkness in amphibian red cones, but essentially irreversible in red rods, contributing to the sensitivity difference between rods and cones.