scholarly journals Evaluation of Cu(i) binding to the E2 domain of the amyloid precursor protein – a lesson in quantification of metal binding to proteinsvialigand competition

Metallomics ◽  
2018 ◽  
Vol 10 (1) ◽  
pp. 108-119 ◽  
Author(s):  
Tessa R. Young ◽  
Anthony G. Wedd ◽  
Zhiguang Xiao
Keyword(s):  
Systematic Review ◽  
Amyloid Precursor Protein ◽  
Metal Binding ◽  
Protein A ◽  
Ternary Complexes ◽  
Precursor Protein ◽  
Physiological Functions ◽  
Protein Affinity ◽  
General Conditions

APP E2 forms stable Cu(i)-mediated ternary complexes with several competing ligands, but not upon addition of heparin. This allows a systematic review of general conditions for quantification of metal–protein affinity and new insights into the physiological functions of APP.

scholarly journals The physiological functions of the β-amyloid precursor protein APP

2012 ◽  
Vol 217 (3-4) ◽  
pp. 325-329 ◽  
Author(s):  
Ulrike C. Müller ◽  
Claus U. Pietrzik ◽  
Thomas Deller
Keyword(s):  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Physiological Functions ◽  
Β Amyloid

scholarly journals LDL receptor-related protein, a multifunctional ApoE receptor, binds secreted β-amyloid precursor protein and mediates its degradation

Cell ◽  
1995 ◽  
Vol 82 (2) ◽  
pp. 331-340 ◽  
Author(s):  
Maria Z Kounnas ◽  
Robert D Moir ◽  
G.William Rebeck ◽  
Ashley I Bush ◽  
W.Scott Argraves ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Protein A ◽  
Ldl Receptor ◽  
Precursor Protein ◽  
Related Protein ◽  
Apoe Receptor ◽  
Β Amyloid

scholarly journals Impacts of Membrane Biophysics in Alzheimer's Disease: From Amyloid Precursor Protein Processing to AβPeptide-Induced Membrane Changes

2011 ◽  
Vol 2011 ◽  
pp. 1-12 ◽  
Author(s):  
Sholpan Askarova ◽  
Xiaoguang Yang ◽  
James C.-M. Lee
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Precursor Protein ◽  
Conformational Changes ◽  
Senile Plaques ◽  
Critical Role ◽  
Protein A ◽  
Precursor Protein ◽  
Amyloid Precursor Protein Processing ◽  
Membrane Composition

An increasing amount of evidence supports the notion that cytotoxic effects of amyloid-βpeptide (Aβ), the main constituent of senile plaques in Alzheimer's disease (AD), are strongly associated with its ability to interact with membranes of neurons and other cerebral cells. Aβis derived from amyloidogenic cleavage of amyloid precursor protein (AβPP) byβ- andγ-secretase. In the nonamyloidogenic pathway, AβPP is cleaved byα-secretases. These two pathways compete with each other, and enhancing the non-amyloidogenic pathway has been suggested as a potential pharmacological approach for the treatment of AD. Since AβPP,α-,β-, andγ-secretases are membrane-associated proteins, AβPP processing and Aβproduction can be affected by the membrane composition and properties. There is evidence that membrane composition and properties, in turn, play a critical role in Aβcytotoxicity associated with its conformational changes and aggregation into oligomers and fibrils. Understanding the mechanisms leading to changes in a membrane's biophysical properties and how they affect AβPP processing and Aβtoxicity should prove to provide new therapeutic strategies for prevention and treatment of AD.

Bacterial and cell-free production of APP671-726 containing amyloid precursor protein transmembrane and metal-binding domains

2013 ◽  
Vol 78 (11) ◽  
pp. 1263-1271 ◽  
Author(s):  
O. V. Bocharova ◽  
A. S. Urban ◽  
K. D. Nadezhdin ◽  
E. V. Bocharov ◽  
A. S. Arseniev
Keyword(s):  
Amyloid Precursor Protein ◽  
Metal Binding ◽  
Precursor Protein ◽  
Binding Domains
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