The Amyloid Precursor Protein C-Terminal Fragment C100 Occurs in Monomeric and Dimeric Stable Conformations and Binds γ-Secretase Modulators-Reference-Cited by-同舟云学术

The Amyloid Precursor Protein C-Terminal Fragment C100 Occurs in Monomeric and Dimeric Stable Conformations and Binds γ-Secretase Modulators

Published:2011-01-11 Issue:5 Volume:50 Page:828-835
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Botev Anne¹,Munter Lisa-Marie¹,Wenzel Ringo²,Richter Luise¹,Althoff Veit¹,Ismer Jochen³,Gerling Ulla¹,Weise Christoph¹,Koksch Beate¹,Hildebrand Peter W.³,Bittl Robert²,Multhaup Gerd¹

Affiliation:

1. Institut für Chemie und Biochemie, Freie Universität Berlin, Thielallee 63, 14195 Berlin, Germany

2. Institut für Experimentalphysik, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany

3. Institut für Medizinische Physik und Biophysik, Charité Berlin, Ziegelstrasse 5-9, 10117 Berlin, Germany

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi1014002

Reference19 articles.

1. Homophilic Interactions of the Amyloid Precursor Protein (APP) Ectodomain Are Regulated by the Loop Region and Affect β-Secretase Cleavage of APP

2. The X-Ray Structure of an Antiparallel Dimer of the Human Amyloid Precursor Protein E2 Domain

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

4. Role of Amyloid- Glycine 33 in Oligomerization, Toxicity, and Neuronal Plasticity

5. No alterations of hippocampal neuronal number and synaptic bouton number in a transgenic mouse model expressing the β-cleaved C-terminal APP fragment

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