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Akikazu Fujita
Researcher at Kagoshima University
Publications - 97
Citations - 5058
Akikazu Fujita is an academic researcher from Kagoshima University. The author has contributed to research in topics: Sulfonylurea receptor & Contraction (grammar). The author has an hindex of 37, co-authored 95 publications receiving 4741 citations. Previous affiliations of Akikazu Fujita include University of Queensland & Nagoya University.
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Immunogold evidence suggests that coupling of K+ siphoning and water transport in rat retinal Müller cells is mediated by a coenrichment of Kir4.1 and AQP4 in specific membrane domains
Erlend A. Nagelhus,Yoshiyuki Horio,Atsushi Inanobe,Akikazu Fujita,Finn‐m. Haug,Søren Nielsen,Yoshihisa Kurachi,Ole Petter Ottersen +7 more
TL;DR: By its highly differentiated distribution of AQP4, the Müller cell may be able to direct the water flux to select extracellular compartments while protecting others (the subretinal space) from inappropriate volume changes.
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Ultrastructural identification of uncoated caveolin-independent early endocytic vehicles
Matthew Kirkham,Akikazu Fujita,Rahul Chadda,Susan J. Nixon,Teymuras V. Kurzchalia,Deepak Sharma,Richard E. Pagano,John F. Hancock,Satyajit Mayor,Robert G. Parton +9 more
TL;DR: Using quantitative light microscopy and a modified immunoelectron microscopic technique, the entry pathway of the cholera toxin binding subunit (CTB) in primary embryonic fibroblasts is characterized and the major carriers involved in initial entry of CTB were identified as uncoated tubular or ring-shaped structures.
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An inwardly rectifying K(+) channel, Kir4.1, expressed in astrocytes surrounds synapses and blood vessels in brain.
Kayoko Higashi,Akikazu Fujita,Atsushi Inanobe,Masayuki Tanemoto,Katsumi Doi,Takeshi Kubo,Yoshihisa Kurachi +6 more
TL;DR: Data suggest that Kir4.1 is expressed in a limited population of brain astrocytes and may play a specific role in the glial K(+)-buffering action.
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Cytoplasmic Lipid Droplets Are Sites of Convergence of Proteasomal and Autophagic Degradation of Apolipoprotein B
TL;DR: Observations indicate that both proteasomal and autophagy/lysosomal degradation of ApoB occur around CLDs and that the CLD surface functions as a unique platform for convergence of the two pathways.
Journal ArticleDOI
Gangliosides GM1 and GM3 in the Living Cell Membrane Form Clusters Susceptible to Cholesterol Depletion and Chilling
Akikazu Fujita,Jinglei Cheng,Minako Hirakawa,Koichi Furukawa,Susumu Kusunoki,Toyoshi Fujimoto +5 more
TL;DR: The present method enabled to capture the molecular distribution of lipids in the cell membrane, and demonstrated that GM1 and GM3 form clusters that are susceptible to cholesterol depletion and chilling.