『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
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登録内容 (EID=139275)

EID=139275EID:139275, Map:0, LastModified:2012年10月12日(金) 17:04:02, Operator:[三木 ちひろ], Avail:TRUE, Censor:0, Owner:[[学科長]/[徳島大学.薬学部.薬学科]], Read:継承, Write:継承, Delete:継承.
種別 (必須): 学術論文 (審査論文) [継承]
言語 (必須): 英語 [継承]
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審査 (推奨):
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組織 (推奨):
著者 (必須): 1.吉村 好之
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2. (英) Ichinose Tatsuya (日) (読)
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3.山内 卓
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題名 (必須): (英) Phosphorylation of tau protein to sites found in Alzheimer's disease brain is catalyzed by Ca2+/calmodulin-dependent protein kinase II as demonstrated tandem mass spectrometry  (日)    [継承]
副題 (任意):
要約 (任意): (英) Neuronal Ca2+/calmodulin-dependent protein kinase II (CaMKII) is one of the most abundant protein kinases in the brain, and phosphorylates a broad range of substrate proteins. The phosphorylation of microtubule tau by CaMKII was investigated using tandem mass spectrometry (MS/MS). Recombinant human tau was phosphorylated at Thr212, Ser214, Ser262, and Ser356 by CaMKII. The phosphorylation of these sites is found in paired helical filament (PHF)-tau. In addition to these sites, Ser131 and Thr135 were phosphorylated by CaMKII. Phosphorylation at Ser131, Thr135, Thr212 and Ser214 by CaMKII has not been reported previously. Thr212 and Ser214 are in the consensus phosphorylation sequence of CaMKII (RXXS/T), and non-fetal-type phosphorylation sites of tau. Non-fetal-type phosphorylation may produce PHF-tau. These results suggested that CaMKII is involved in the phosphorylation of tau in Alzheimer's disease brain.  (日)    [継承]
キーワード (推奨): 1. (英) Ca2+/calmodulin-dependent protein kinase II (CaMKII) (日) (読) [継承]
2. (英) Tau (日) (読) [継承]
3.リン酸化 (phosphorylation) [継承]
4. (英) Alzheimers disease (日) (読) [継承]
5. (英) Paired helical filaments (日) (読) [継承]
発行所 (推奨): Elsevier Science [継承]
誌名 (必須): Neuroscience Letters ([Elsevier Science])
(pISSN: 0304-3940, eISSN: 1872-7972)

ISSN (任意): 0304-3940
ISSN: 0304-3940 (pISSN: 0304-3940, eISSN: 1872-7972)
Title: Neuroscience letters
Title(ISO): Neurosci Lett
Publisher: Elsevier Ireland Ltd
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
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(必須): 353 [継承]
(必須): 3 [継承]
(必須): 185 188 [継承]
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年月日 (必須): 西暦 2003年 12月 26日 (平成 15年 12月 26日) [継承]
URL (任意):
DOI (任意): 10.1016/j.neulet.2003.09.037    (→Scopusで検索) [継承]
PMID (任意): 14665412    (→Scopusで検索) [継承]
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備考 (任意): 1.(英) Article.Affiliation: Department of Biochemistry, Faculty of Pharmaceutical Sciences, The University of Tokushima, Shomachi 1, Tokushima 770-8505, Japan.  (日)    [継承]
2.(英) Article.PublicationTypeList.PublicationType: Comparative Study  (日)    [継承]
3.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
4.(英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't  (日)    [継承]

標準的な表示

和文冊子 ● Yoshiyuki Yoshimura, Tatsuya Ichinose and Takashi Yamauchi : Phosphorylation of tau protein to sites found in Alzheimer's disease brain is catalyzed by Ca2+/calmodulin-dependent protein kinase II as demonstrated tandem mass spectrometry, Neuroscience Letters, Vol.353, No.3, 185-188, 2003.
欧文冊子 ● Yoshiyuki Yoshimura, Tatsuya Ichinose and Takashi Yamauchi : Phosphorylation of tau protein to sites found in Alzheimer's disease brain is catalyzed by Ca2+/calmodulin-dependent protein kinase II as demonstrated tandem mass spectrometry, Neuroscience Letters, Vol.353, No.3, 185-188, 2003.

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