Effects of Point Substitutions on the Structure of Toxic Alzheimer’s β-Amyloid Channels: Atomic Force Microscopy and Molecular Dynamics Simulations-Reference-Cited by-同舟云学术

Effects of Point Substitutions on the Structure of Toxic Alzheimer’s β-Amyloid Channels: Atomic Force Microscopy and Molecular Dynamics Simulations

Published:2012-03-28 Issue:14 Volume:51 Page:3031-3038
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Connelly Laura¹,Jang Hyunbum²,Teran Arce Fernando¹,Ramachandran Srinivasan¹,Kagan Bruce L.³,Nussinov Ruth²⁴,Lal Ratnesh¹

Affiliation:

1. Departments of Bioengineering and Mechanical and Aerospace Engineering and Material Science Program, University of California, San Diego, La Jolla, California 92093, United States

2. Basic Science Program, SAIC-Frederick, Inc., Center for Cancer Research Nanobiology Program, Frederick National Laboratory for Cancer Research, Frederick, Maryland 21702, United States

3. Department of Psychiatry, David Geffen School of Medicine, Semel Institute for Neuroscience and Human Behavior, University of California, Los Angeles, California 90024, United States

4. Department of Human Molecular Genetics and Biochemistry, Sackler School of Medicine, Tel Aviv University, Tel Aviv 69978, Israel

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi300257e

Reference43 articles.

1. Alzheimer's disease

2. Protein Misfolding, Functional Amyloid, and Human Disease

3. Polymorphism of amyloid β peptide in different environments: implications for membrane insertion and pore formation

4. Amyloidogenic Protein-Membrane Interactions: Mechanistic Insight from Model Systems

5. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein

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