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Yoshikazu Imanishi
Researcher at Case Western Reserve University
Publications - 62
Citations - 4009
Yoshikazu Imanishi is an academic researcher from Case Western Reserve University. The author has contributed to research in topics: Rhodopsin & Visual phototransduction. The author has an hindex of 33, co-authored 60 publications receiving 3715 citations. Previous affiliations of Yoshikazu Imanishi include University of Washington & Wright State University.
Papers
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Journal ArticleDOI
Lecithin-retinol Acyltransferase Is Essential for Accumulation of All-trans-Retinyl Esters in the Eye and in the Liver
Matthew Batten,Yoshikazu Imanishi,Tadao Maeda,Daniel C. Tu,Alexander R. Moise,Darin Bronson,Daniel E. Possin,Russell N. Van Gelder,Wolfgang Baehr,Krzysztof Palczewski +9 more
TL;DR: The histological analysis and electron microscopy of the retina for 6–8-week-old Lrat-/- mice revealed that the rod outer segments are ∼35% shorter than those of Lrat+/+ mice, whereas other neuronal layers appear normal andScotopic and photopic electroretinograms as well as pupillary constriction analyses revealed that rod and cone visual functions are severely attenuated at an early age.
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Essential role of Ca2+-binding protein 4, a Cav1.4 channel regulator, in photoreceptor synaptic function.
Françoise Haeseleer,Yoshikazu Imanishi,Tadao Maeda,Daniel E. Possin,Akiko Maeda,Amy S. Lee,Fred Rieke,Krzysztof Palczewski +7 more
TL;DR: Observations indicate that CaBP4 is important for normal synaptic function, probably through regulation of Ca2+ influx and neurotransmitter release in photoreceptor synaptic terminals.
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Pharmacological Chaperone-mediated in Vivo Folding and Stabilization of the P23H-opsin Mutant Associated with Autosomal Dominant Retinitis Pigmentosa
Syed Mohammed Noorwez,Vladimir A. Kuksa,Yoshikazu Imanishi,Li Zhu,Slawomir Filipek,Krzysztof Palczewski,Shalesh Kaushal +6 more
TL;DR: In this paper, a pharmacological chaperone, 11-cis-7-ring retinal, was used to induce the in vivo folding of P23H-opsin and the rescued protein formed pigment, acquired mature glycosylation, and was transported to the cell surface.
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Dual-substrate Specificity Short Chain Retinol Dehydrogenases from the Vertebrate Retina
Françoise Haeseleer,Geeng Fu Jang,Yoshikazu Imanishi,C.A.G.G. Driessen,Masazumi Matsumura,Peter S. Nelson,Krzysztof Palczewski +6 more
TL;DR: Three enzymes from a novel subfamily of four retinol dehydrogenases (RDH11–14) that display dual-substrate specificity are described, uniquely metabolizing all-trans- andcis-retinols with C15 pro-Rspecificity.
Journal ArticleDOI
Noninvasive two-photon imaging reveals retinyl ester storage structures in the eye.
TL;DR: Results indicate that RESTs located close to the RPE plasma membrane are essential components in 11-cis-retinal production, and are absent in the eyes of Lrat −/− mice deficient in retinyl ester synthesis.