[ASAP] The Human Amyloid Precursor Protein Binds Copper Ions Dominated by a Picomolar-Affinity Site in the Helix-Rich E2 Domain
The Human Amyloid Precursor Protein Binds Copper Ions Dominated by a Picomolar-Affinity Site in the Helix-Rich E2 Domain
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00572/20180626/images/medium/bi-2018-00572h_0012.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00572
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Expression, purification, and reconstitution of the transmembrane domain of the human amyloid precursor protein for NMR studies.
Expression, purification, and reconstitution of the transmembrane domain of the human amyloid precursor protein for NMR studies.
Expression, purification, and reconstitution of the transmembrane domain of the human amyloid precursor protein for NMR studies.
Protein Expr Purif. 2011 Aug 31;
Authors: Chen W, Gamache E, Richardson D, Du Z, Wang C
Abstract
Alzheimer's disease (AD) is the most common type of dementia in elderly people. Senile plaques, a pathologic hallmark of AD, are composed of amyloid ? peptide (A?). A? aggregation produces...
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09-13-2011 08:27 PM
[NMR paper] Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasm
Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR.
Related Articles Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR.
J Mol Biol. 2001 Mar 30;307(3):871-84
Authors: Ramelot TA, Nicholson LK
The cytoplasmic tail of the amyloid precursor protein (APPc) interacts with several cellular factors implicated in intracellular signaling or proteolytic production of amyloid beta peptide found in senile plaques of Alzheimer's disease...
A thermodynamic investigation of amyloid precursor protein processing by human ?-secretase | Communications Biology - Nature.com
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