GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Aβ42-Reference-Cited by-同舟云学术

GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Aβ42

Published:2007-03-01 Issue:6 Volume:26 Page:1702-1712
ISSN:0261-4189
Container-title:The EMBO Journal
language:
Short-container-title:EMBO J

Author:

Munter Lisa-Marie,Voigt Philipp,Harmeier Anja,Kaden Daniela,Gottschalk Kay E,Weise Christoph,Pipkorn Rüdiger,Schaefer Michael,Langosch Dieter,Multhaup Gerd

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Reference63 articles.

1. Eukaryotic CTR Copper Uptake Transporters Require Two Faces of the Third Transmembrane Domain for Helix Packing, Oligomerization, and Function

2. A Cell Biological Perspective on Alzheimer's Disease

3. The GxxxG motif of the transmembrane domain of subunit e is involved in the dimerization/oligomerization of the yeast ATP synthase complex in the mitochondrial membrane

4. Regulation of Amyloid Protein Precursor (APP) Binding to Collagen and Mapping of the Binding Sites on APP and Collagen Type I

5. Amyloid -protein (A ) assembly: A 40 and A 42 oligomerize through distinct pathways

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