C
Clint L. Makino
Researcher at Boston University
Publications - 69
Citations - 3726
Clint L. Makino is an academic researcher from Boston University. The author has contributed to research in topics: Visual phototransduction & Rhodopsin. The author has an hindex of 30, co-authored 65 publications receiving 3521 citations. Previous affiliations of Clint L. Makino include Florida State University & California Institute of Technology.
Papers
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Journal ArticleDOI
Morphological, physiological, and biochemical changes in rhodopsin knockout mice
Janis Lem,Nataliia V. Krasnoperova,Peter D. Calvert,Bela Kosaras,David A. Cameron,Massimo Nicolò,Clint L. Makino,Richard L. Sidman +7 more
TL;DR: Physiological and biochemical experiments showed that rods from mice with a single opsin gene were approximately50% less sensitive to light, had accelerated flash-response kinetics, and contained approximately 50% more phosducin than wild-type controls.
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A rhodopsin gene mutation responsible for autosomal dominant retinitis pigmentosa results in a protein that is defective in localization to the photoreceptor outer segment
TL;DR: Data indicate that rhodopsin's carboxy-terminus is required for efficient transportation to or retention in the outer segment of the photoreceptor cell body.
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Phototransduction in transgenic mice after targeted deletion of the rod transducin α-subunit
Peter D. Calvert,N. V. Krasnoperova,Arkady Lyubarsky,Arkady Lyubarsky,T. Isayama,Massimo Nicolò,Bela Kosaras,G. Wong,K. S. Gannon,Robert F. Margolskee,Richard L. Sidman,Edward N. Pugh,Clint L. Makino,Janis Lem +13 more
TL;DR: Most if not all rods use a single transducin type in phototransduction, as expected for a cone, but had a rod-like spectral sensitivity and flash response kinetics that were slow, even for rods.
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Prolonged photoresponses in transgenic mouse rods lacking arrestin
Jun Xu,Robert L. Dodd,Clint L. Makino,Clint L. Makino,Melvin I. Simon,Denis A. Baylor,Jeannie Chen,Jeannie Chen +7 more
TL;DR: The intensity dependence of the photoresponse in rods lacking arrestin further suggests that, although arrestin is required for normal signal termination, it does not participate directly in light adaptation.
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Mechanisms of rhodopsin inactivation in vivo as revealed by a COOH-terminal truncation mutant
TL;DR: Comparison of normal and prolonged single photon responses indicated that rhodopsin begins to be quenched before the peak of the electrical response and that quenching limits the response amplitude.