Edaravone inhibits the conformational transition of amyloid-β42: insights from molecular dynamics simulations-Reference-Cited by-同舟云学术

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Edaravone inhibits the conformational transition of amyloid-β42: insights from molecular dynamics simulations

Published:2019-06-25 Issue:8 Volume:38 Page:2377-2388
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Liu Fufeng¹²³,Ma Zheng³,Sang Jingcheng³,Lu Fuping¹²³

Affiliation:

1. Key Laboratory of Industrial Fermentation Microbiology, Tianjin University of Science & Technology, Ministry of Education, Tianjin, PR China;

2. Tianjin Key Laboratory of Industrial Microbiology, Tianjin University of Science & Technology, Tianjin, PR China;

3. College of Biotechnology, Tianjin University of Science & Technology, Tianjin, PR China

Funder

National Natural Science Foundation of China

Natural Science Foundation of Tianjin from the Tianjin Municipal Science and Technology Commission

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2019.1632225

Reference79 articles.

1. Protein aggregation: From background to inhibition strategies

2. Vitamin B12 offers neuronal cell protection by inhibiting Aβ-42 amyloid fibrillation

3. Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease

4. Effect of graphene oxide on the conformational transitions of amyloid beta peptide: A molecular dynamics simulation study

5. Revisiting the earliest signatures of amyloidogenesis: Roadmaps emerging from computational modeling and experiment

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