Impact of Bilayer Lipid Composition on the Structure and Topology of the Transmembrane Amyloid Precursor C99 Protein-Reference-Cited by-同舟云学术

Impact of Bilayer Lipid Composition on the Structure and Topology of the Transmembrane Amyloid Precursor C99 Protein

Published:2014-03-11 Issue:11 Volume:136 Page:4093-4096
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Song Yuanli¹,Mittendorf Kathleen F.¹,Lu Zhenwei¹,Sanders Charles R.¹

Affiliation:

1. Department of Biochemistry and Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-8725, United States

Funder

National Institutes of Health

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja4114374

Reference31 articles.

1. The Amyloid Precursor Protein Has a Flexible Transmembrane Domain and Binds Cholesterol

2. Perturbations of the Straight Transmembrane α-Helical Structure of the Amyloid Precursor Protein Affect Its Processing by γ-Secretase

3. Transmembrane Fragment Structures of Amyloid Precursor Protein Depend on Membrane Surface Curvature

4. The Backbone Dynamics of the Amyloid Precursor Protein Transmembrane Helix Provides a Rationale for the Sequential Cleavage Mechanism of γ-Secretase

5. Dynamics and Cleavability at the α-Cleavage Site of APP(684-726) in Different Lipid Environments

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