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Shunsuke Kobayashi
Researcher at Nihon University
Publications - 44
Citations - 1422
Shunsuke Kobayashi is an academic researcher from Nihon University. The author has contributed to research in topics: RNA & Transcription (biology). The author has an hindex of 15, co-authored 43 publications receiving 1324 citations. Previous affiliations of Shunsuke Kobayashi include Toho University.
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Journal ArticleDOI
Glycogen synthase kinase 3β is identical to tau protein kinase I generating several epitopes of paired helical filaments
Koichi Ishiguro,Akiko Shiratsuchi,Showbu Sato,Akira Omori,Manabu Arioka,Shunsuke Kobayashi,Tsuneko Uchida,Kazutomo Imahori +7 more
TL;DR: The amino acid sequence of TPKI is presented, which is identical to glycogen synthase kinase 3β (GSK3β), and it is found that TPKI activity was inseparable from GSK3 activity throughout the purification procedure.
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Identification of mRNA/Protein (mRNP) Complexes Containing Purα, mStaufen, Fragile X Protein, and Myosin Va and their Association with Rough Endoplasmic Reticulum Equipped with a Kinesin Motor
Sachiyo Ohashi,Katsuya Koike,Akira Omori,Sachiyo Ichinose,Susumu Ohara,Shunsuke Kobayashi,Taka-Aki Sato,Kaijiro Anzai +7 more
TL;DR: It is proposed that this rough endoplasmic reticulum structure may form the molecular machinery that mediates and regulates multistep transport of polyribosomes along microtubules and actin filaments, as well as localized translation in the somatodendritic compartment.
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Identification of the 23 kDa subunit of tau protein kinase II as a putative activator of cdk5 in bovine brain
Koichi Ishiguro,Shunsuke Kobayashi,Akira Onion,Masako Takamatsu,Sayuri Yonekura,Kaijiro Anzai,Kazutomo Imahori,Tsuneko Uchida +7 more
TL;DR: It is suggested that the 23 kDa subunit, but not cyclin, activates cdk5 in neuronal cells, which no longer exhibit cell cycling but are terminally differentiated cells.
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Brain-specific small RNA transcript of the identifier sequences is present as a 10 S ribonucleoprotein particle.
TL;DR: It is demonstrated that BC-1 RNA is not free but complexed with proteins to form a 10 S RNP in the cytoplasm, which is not associated with cy toplasmic structures such as polysomes/ribosomes or microsomes.
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Local Somatodendritic Translation and Hyperphosphorylation of Tau Protein Triggered by AMPA and NMDA Receptor Stimulation
TL;DR: It is demonstrated that alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) and N- methyl-d-aspartate (NMDA) stimulation redistributes tau to the somato-dendritic region of neurons where it may trigger neurodegeneration.