『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
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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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カテゴリ (推奨):
共著種別 (推奨):
学究種別 (推奨):
組織 (推奨): 1.大阪大学 [継承]
著者 (必須): 1.郷田 秀一郎 ([長崎大学])
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学籍番号 (推奨):
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2. (英) Takano Kazufumi (日) 高野 和文 (読) たかの かずふみ
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3. (英) Yamagata Yuriko (日) 山縣 (読) やまがた ゆりこ
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4. (英) Maki Saori (日) 眞木 さおり (読) まき さおり
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5. (英) Namba Keiichi (日) 難波 啓一 (読) なんば けいいち
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6. (英) Yutani Katsuhide (日) 油谷 克英 (読) ゆたに かつひで
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題名 (必須): (英) Elongation in a beta-Structure Promotes Amyloid-Like Fibril Formation of Human Lysozyme.  (日)    [継承]
副題 (任意):
要約 (任意): (英) To understand the mechanism of amyloid fibril formation of a protein, we examined wild-type and three mutant human lysozymes containing both amyloidogenic and non-amyloidogenic proteins: I56T (amyloidogenic); EAEA, which has four additional residues (Glu-Ala-Glu-Ala-) at the N-terminus located on a beta-structure; and EAEA-I56T, which is an I56T mutant of EAEA. All formed amyloid-like fibrils through an in the increase contents of alpha-helix with increasing concentration of ethanol. The order of propensity for amyloid-like fibril formation in highly concentrated ethanol solution is EAEA-I56T > EAEA > I56T > wild-type. This order is almost the reverse of the order of conformational stability of these proteins, wild-type > EAEA > I56T > EAEA-I56T. The important views in this work are as follows. (i) Artificially modified proteins formed amyloid fibrils in vitro. This means that amyloid formation is a generic property of polypeptide chains. (ii) The amyloidogenic mutation Ile56 to Thr caused the destabilization and promoted fibril formation in the wild-type and EAEA human lysozymes, indicating that instability facilitates amyloid formation. (iii) The mutant protein EAEA human lysozyme had higher propensity for fibril formation than the amyloidogenic mutant protein, indicating that amyloid formation is controlled not only by stability but also by other factors. In this case, appending polypeptide chains to a beta-structure accelerated amyloid formation.  (日)    [継承]
キーワード (推奨): 1. (英) Amino Acid Substitution (日) (読) [継承]
2. (英) Amyloid (日) (読) [継承]
3. (英) Enzyme Stability (日) (読) [継承]
4. (英) Ethanol (日) (読) [継承]
5. (英) Humans (日) (読) [継承]
6. (英) Kinetics (日) (読) [継承]
7. (英) Microscopy, Electron (日) (読) [継承]
8. (英) Models, Molecular (日) (読) [継承]
9. (英) Muramidase (日) (読) [継承]
10. (英) Protein Denaturation (日) (読) [継承]
11. (英) Protein Folding (日) (読) [継承]
12. (英) Protein Structure, Secondary (日) (読) [継承]
13. (英) Thermodynamics (日) (読) [継承]
14. (英) X-Ray Diffraction (日) (読) [継承]
発行所 (推奨):
誌名 (必須): The Journal of Biochemistry ([日本生化学会])
(pISSN: 0021-924X, eISSN: 1756-2651)

ISSN (任意): 0021-924X
ISSN: 0021-924X (pISSN: 0021-924X, eISSN: 1756-2651)
Title: Journal of biochemistry
Title(ISO): J Biochem
Supplier: Oxford University Press
Publisher: Oxford University Press
 (NLM Catalog  (医中誌Web  (J-STAGE  (Scopus  (CrossRef (Scopus information is found. [need login])
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(必須): 132 [継承]
(必須): 4 [継承]
(必須): 655 661 [継承]
都市 (任意): 東京 (Tokyo/[日本国]) [継承]
年月日 (必須): 西暦 2002年 10月 初日 (平成 14年 10月 初日) [継承]
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DOI (任意):
PMID (任意): 12359083    (→Scopusで検索) [継承]
NAID (任意):
WOS (任意): 000178387800022 [継承]
Scopus (任意): 2-s2.0-0036775896 [継承]
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備考 (任意): 1.(英) Article.DataBankList.DataBank.DataBankName: PDB  (日)    [継承]
2.(英) Article.DataBankList.DataBank.AccessionNumberList.AccessionNumber: 1IOC  (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 ● Shuichiro Goda, Kazufumi Takano, Yuriko Yamagata, Saori Maki, Keiichi Namba and Katsuhide Yutani : Elongation in a beta-Structure Promotes Amyloid-Like Fibril Formation of Human Lysozyme., The Journal of Biochemistry, Vol.132, No.4, 655-661, 2002.
欧文冊子 ● Shuichiro Goda, Kazufumi Takano, Yuriko Yamagata, Saori Maki, Keiichi Namba and Katsuhide Yutani : Elongation in a beta-Structure Promotes Amyloid-Like Fibril Formation of Human Lysozyme., The Journal of Biochemistry, Vol.132, No.4, 655-661, 2002.

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