M
Masahiro Hosaka
Researcher at Akita Prefectural University
Publications - 71
Citations - 5033
Masahiro Hosaka is an academic researcher from Akita Prefectural University. The author has contributed to research in topics: Secretogranin III & Chromogranin A. The author has an hindex of 30, co-authored 70 publications receiving 4726 citations. Previous affiliations of Masahiro Hosaka include Niigata University & University of Tsukuba.
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Journal ArticleDOI
A conformational switch in syntaxin during exocytosis: role of munc18
Irina Dulubova,Shuzo Sugita,Sandra Hill,Masahiro Hosaka,Imma Fernandez,Thomas C. Südhof,Josep Rizo +6 more
TL;DR: The results indicate that syntaxin binds to munc18‐1 in a closed conformation and suggest that this conformation represents an essential intermediate in exocytosis, and suggest a model whereby syntaxin undergoes a large conformational switch that mediates the transition between the syntaxin–munc 18‐1 complex and the core complex.
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Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway.
Masahiro Hosaka,Masami Nagahama,Won-Sin Kim,Toshio Watanabe,Kiyotaka Hatsuzawa,J Ikemizu,Kazuo Murakami,Kazuhisa Nakayama +7 more
TL;DR: Results indicate that the basic pair and the RXK/RR sequence are the signals for precursor cleavages catalyzed by PC3 within the regulated secretory pathway and by furin within the constitutive pathway, respectively.
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Phosphorescent Light-Emitting Iridium Complexes Serve as a Hypoxia-Sensing Probe for Tumor Imaging in Living Animals
Shaojuan Zhang,Masahiro Hosaka,Toshitada Yoshihara,Kazuya Negishi,Yasuhiko Iida,Seiji Tobita,Toshiyuki Takeuchi +6 more
TL;DR: Red light-emitting Ir(btp)(2)(acac) (BTP) presented hypoxia-dependent light emission in culture cell lines, whose intensity was in parallel with hypoxIA-inducible factor-1alpha images, and iridium complex materials have a vast potential for imaging hypoxic lesions such as tumor tissues.
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A phospho-switch controls the dynamic association of synapsins with synaptic vesicles.
TL;DR: It is demonstrated that synapsin phosphorylation in the A domain, at the onlyosphorylation site shared by all synapsins, dissociatessynapsins from synaptic vesicles and suggests a novel mechanism by which proteins reversibly bind to membranes using a phosphorylated-dependent phospholipid-binding domain.
Journal ArticleDOI
Identification of the fourth member of the mammalian endoprotease family homologous to the yeast Kex2 protease. Its testis-specific expression.
Kazuhisa Nakayama,Won-Sin Kim,Seiji Torii,Masahiro Hosaka,Tsutomu Nakagawa,J Ikemizu,Tadashi Baba,Kazuo Murakami +7 more
TL;DR: A mouse testis cDNA encoded a 655-residue protein, designated PC4, containing a bacterial subtilisin-like catalytic domain closely related to those of the recently characterized precursor-processing endoproteases, furin, PC1/PC3, PC2, and Kex2.