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Dynamics of oligomer and amyloid fibril formation by yeast prion Sup35 observed by high-speed atomic force microscopy.
Konno, Hiroki; Watanabe-Nakayama, Takahiro; Uchihashi, Takayuki; Okuda, Momoko; Zhu, Liwen; Kodera, Noriyuki; Kikuchi, Yousuke; Ando, Toshio; Taguchi, Hideki.
Afiliação
  • Konno H; World Premier International Research Center Initiative Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa-shi, 920-1192 Ishikawa, Japan.
  • Watanabe-Nakayama T; World Premier International Research Center Initiative Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa-shi, 920-1192 Ishikawa, Japan.
  • Uchihashi T; Department of Physics, Nagoya University, 464-8602 Nagoya, Japan.
  • Okuda M; Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, 444-8787 Aichi, Japan.
  • Zhu L; School of Life Science and Technology, Tokyo Institute of Technology, Midori-ku, 226-8503 Yokohama, Japan.
  • Kodera N; Imaging Research Division, Bio-Atomic Force Microscopy Frontier Research Center, College of Science and Engineering, Kanazawa University, Kakuma-machi, Kanazawa-shi, 920-1192 Ishikawa, Japan.
  • Kikuchi Y; World Premier International Research Center Initiative Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa-shi, 920-1192 Ishikawa, Japan.
  • Ando T; School of Natural System, College of Science and Engineering, Kanazawa University, Kakuma-machi, Kanazawa, 920-1192 Ishikawa, Japan.
  • Taguchi H; World Premier International Research Center Initiative Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa-shi, 920-1192 Ishikawa, Japan; tando@staff.kanazawa-u.ac.jp taguchi@bio.titech.ac.jp.
Proc Natl Acad Sci U S A ; 117(14): 7831-7836, 2020 04 07.
Article em En | MEDLINE | ID: mdl-32213585
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Fatores de Terminação de Peptídeos / Microscopia de Força Atômica / Proteínas de Saccharomyces cerevisiae / Proteínas Priônicas / Amiloide Idioma: En Ano de publicação: 2020 Tipo de documento: Article
Texto completo
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XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Fatores de Terminação de Peptídeos / Microscopia de Força Atômica / Proteínas de Saccharomyces cerevisiae / Proteínas Priônicas / Amiloide Idioma: En Ano de publicação: 2020 Tipo de documento: Article