Structural Optimization and Biological Evaluation of Substituted Bisphenol A Derivatives as β-Amyloid Peptide Aggregation Inhibitors-Reference-Cited by-同舟云学术

Structural Optimization and Biological Evaluation of Substituted Bisphenol A Derivatives as β-Amyloid Peptide Aggregation Inhibitors

Published:2010-07-21 Issue:15 Volume:53 Page:5449-5466
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Zhou Yu¹,Jiang Chunyi¹,Zhang Yaping²,Liang Zhongjie¹,Liu Wenfeng¹³,Wang Liefeng⁴,Luo Cheng¹,Zhong Tingting²,Sun Yi²,Zhao Linxiang³,Xie Xin¹,Jiang Hualiang¹,Zhou Naiming²,Liu Dongxiang¹,Liu Hong¹

Affiliation:

1. State Key Laboratory of Drug Research

2. Institute of Biochemistry, College of Life Sciences, Zijingang Campus, Zhejiang University, Hangzhou, Zhejiang, 310058, China

3. School of Pharmaceutical Engineering, Shenyang Pharmaceutical University, Shenyang, Liaoning 110016, China

4. Laboratory of Receptor-Based Bio-Medicine, School of Life Sciences and Technology, Tongji University, Shanghai 200092, China

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm1000584

Reference36 articles.

1. The Presenilins in Alzheimer's Disease--Proteolysis Holds the Key

2. Aging renders the brain vulnerable to amyloid β-protein neurotoxicity

3. Designing Peptide Inhibitors for Oligomerization and Toxicity of Alzheimer's β-Amyloid Peptide

4. Inhibitor Discovery Targeting the Intermediate Structure of β-Amyloid Peptide on the Conformational Transition Pathway: Implications in the Aggregation Mechanism of β-Amyloid Peptide

5. Homocysteic acid induces intraneuronal accumulation of neurotoxic Aβ42: Implications for the pathogenesis of Alzheimer's disease

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