Inhibiting Aggregation of β-Amyloid by Folded and Unfolded Forms of Fimbrial Protein of Gram-Negative Bacteria-Reference-Cited by-同舟云学术

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Inhibiting Aggregation of β-Amyloid by Folded and Unfolded Forms of Fimbrial Protein of Gram-Negative Bacteria

Published:2017-09-29 Issue:28 Volume:2 Page:9058-9062
ISSN:2365-6549
Container-title:ChemistrySelect
language:en
Short-container-title:ChemistrySelect

Author:

Yamamoto Keisuke¹,Oyaizu Misa¹,Takahashi Tsuyoshi²,Watanabe Yoshihito¹,Shoji Osami¹³

Affiliation:

1. Department of Chemistry, Graduate School of Science; Research Center for Materials Science; Nagoya University, Furo-cho, Chikusa; Nagoya 464-8602 Japan

2. Department of Chemistry and Chemical Biology; School of Science and Technology; Gunma University; 1-5-1, Tenjin-cho, Kiryu Gunma 376-8515 Japan

3. Core Research for Evolutional Science and Technology; Japan Science and Technology Agency; 5 Sanbancho, Chiyoda-ku Tokyo 102-0075 Japan

Funder

Nanotechnology Plataform Program (Molecule and Material Synthesis) of the Minstry of Education, Cultre, Sports, Sciece and Technology (MEXT), Japan

MEXT/JSPS KAKENHI

Grant-in-Aid for Exploratory Research and JSPS KAKENHI

Publisher

Wiley

Subject

General Chemistry

Reference30 articles.

1. Current advances in the treatment of Alzheimer's disease: focused on considerations targeting Aβ and tau

2. The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics

3. Targeting the β secretase BACE1 for Alzheimer's disease therapy

4. γ-Secretase inhibitors and modulators

5. New protein kinase C activator regulates amyloid precursor protein processing in vitro by increasing α-secretase activity

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