<strong>The <em>trans</em> isomer of Tau peptide is prone to aggregate, and WW domain of Pin1 drastically decreases its aggregation</strong>

Teikichi Ikura; Naoya Tochio; Ryosuke Kawasaki; Mizuki Matsuzaki; Akihiro Narita; Mahito Kikumoto; Naoko Utsunomiya Tate; Shin-ichi Tate; Nobutoshi Ito

[1LBA-112] **The trans isomer of Tau peptide is prone to aggregate, and WW domain of Pin1 drastically decreases its aggregation**

〇Teikichi Ikura¹, Naoya Tochio^2,3, Ryosuke Kawasaki⁴, Mizuki Matsuzaki⁵, Akihiro Narita⁵, Mahito Kikumoto⁵, Naoko Utsunomiya Tate³, Shin-ichi Tate^2,4, Nobutoshi Ito¹ (1.Med Res Inst, Tokyo Med & Dent Univ, 2.RcMcD, Hiroshima Univ, 3.Fac of Pharm-Sci, Teikyo Univ, 4.Dept of Math & Life Sci, Grad Sch of Sci, Hiroshima Univ, 5.Struct Biol Res Center, Grad Sch of Sci, Nagoya Univ)

Pin1, WW domain, Tau protein, neurofibrillary tangles, Alzheimer's disease

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The 41st Annual Meeting of the Molecular Biology Society of Japan

[1LBA-112] **The trans isomer of Tau peptide is prone to aggregate, and WW domain of Pin1 drastically decreases its aggregation**

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The 41st Annual Meeting of the Molecular Biology Society of Japan

[1LBA-112] The trans isomer of Tau peptide is prone to aggregate, and WW domain of Pin1 drastically decreases its aggregation

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[1LBA-112] **The trans isomer of Tau peptide is prone to aggregate, and WW domain of Pin1 drastically decreases its aggregation**