Polymorphic Associations and Structures of the Cross-Seeding of Aβ1–42 and hIAPP1–37 Polypeptides-Reference-Cited by-同舟云学术

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Polymorphic Associations and Structures of the Cross-Seeding of Aβ1–42 and hIAPP1–37 Polypeptides

Published:2015-07-24 Issue:8 Volume:55 Page:1628-1639
ISSN:1549-9596
Container-title:Journal of Chemical Information and Modeling
language:en
Short-container-title:J. Chem. Inf. Model.

Author:

Zhang Mingzhen,Hu Rundong,Chen Hong,Gong Xiong,Zhou Feimeng¹,Zhang Li²,Zheng Jie

Affiliation:

1. Department of Chemistry and Biochemistry, California State University, Los Angeles, Los Angeles, California 90032, United States

2. Department of Geriatric Neurology, Nanjing Brain Hospital Affiliated to Nanjing Medical University, Nanjing, Jiangsu 210029, China

Funder

Division of Chemical, Bioengineering, Environmental, and Transport Systems

Alzheimer's Association

Publisher

American Chemical Society (ACS)

Subject

Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jcim.5b00166

Reference87 articles.

1. Natural oligomers of the amyloid-β protein specifically disrupt cognitive function

2. Protein Aggregation in the Brain: The Molecular Basis for Alzheimer’s and Parkinson’s Diseases

3. Islet Amyloid in Type 2 Diabetes, and the Toxic Oligomer Hypothesis

4. Islet Amyloid and Type 2 Diabetes Mellitus

5. Membrane Disruption and Early Events in the Aggregation of the Diabetes Related Peptide IAPP from a Molecular Perspective

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1. Proteomic evidence for amyloidogenic cross-seeding in fibrinaloid microclots;2024-07-17

2. Heterotypic Seeding Generates Mixed Amyloid Polymorphs;Small Science;2024-06-22

3. Identification of hybrid amyloid strains assembled from amyloid-β and human islet amyloid polypeptide;Nanotechnology;2023-09-28

4. Amyloid Protein Cross-Seeding Provides a New Perspective on Multiple Diseases In Vivo;Biomacromolecules;2022-12-12

5. Electric Field Effect on Inhibiting the Co-fibrillation of Amyloid Peptides by Modulating the Aggregation Pathway;Langmuir;2022-09-29

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