Comprehensive analysis of the molecular docking of small molecule inhibitors to the Aβ1–40peptide and its Osaka-mutant: insights into the molecular mechanisms of Aβ-peptide inhibition-Reference-Cited by-同舟云学术

Comprehensive analysis of the molecular docking of small molecule inhibitors to the Aβ1–40peptide and its Osaka-mutant: insights into the molecular mechanisms of Aβ-peptide inhibition

Published:2019-12-09 Issue:15 Volume:38 Page:4536-4566
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Salahuddin Parveen¹,Khan Rizwan Hasan²^ORCID,Uversky Vladimir N.³⁴⁵^ORCID

Affiliation:

1. DISC, Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India;

2. Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India;

3. Protein Research Group, Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, Russia;

4. Department of Biological Sciences, Faculty of Sciences, King Abdulaziz University, Jeddah, Saudi Arabia;

5. Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, USA

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2019.1697367

Reference99 articles.

1. Tetracycline prevents Aβ oligomer toxicity through an atypical supramolecular interaction

2. Structural requirements for the flavonoid fisetin in inhibiting fibril formation of amyloid β protein

3. Ascorbic acid inhibits human insulin aggregation and protects against amyloid induced cytotoxicity

4. Vitamin k3 inhibits protein aggregation: Implication in the treatment of amyloid diseases

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