The multiple-step cleavage of amyloid precursor protein (APP) generates amyloid-? peptides (A?), highly toxic molecules causing Alzheimer's disease (AD). The nonspecific cleavage between the transmembrane region of APP (APPTM) and ?-secretase is the key step of A? generation. Reconstituting APPTM under physiologically-relevant conditions is crucial to investigate how it interacts with ?-secretase and for future AD drug discovery. Although producing recombinant APPTM was reported before, the...
[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
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/0YhCYVxyXp8
More...
nmrlearner
Journal club
0
06-27-2018 01:51 AM
[NMR paper] Cloning, Expression, Isotope Labeling, and Purification of Transmembrane Protein MerF from Mercury Resistant Enterobacter sp. AZ-15 for NMR Studies.
Cloning, Expression, Isotope Labeling, and Purification of Transmembrane Protein MerF from Mercury Resistant Enterobacter sp. AZ-15 for NMR Studies.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.frontiersin.org-alerts-logo-logo_LinkOut.jpg Related Articles Cloning, Expression, Isotope Labeling, and Purification of Transmembrane Protein MerF from Mercury Resistant Enterobacter sp. AZ-15 for NMR Studies.
Front Microbiol. 2017;8:1250
Authors: Amin A, Latif Z
Abstract
Mercury resistant (Hg(R))...
nmrlearner
Journal club
0
07-25-2017 07:46 PM
[NMR paper] Expression, purification and reconstitution of the C-terminal transmembrane domain of scavenger receptor BI into detergent micelles for NMR analysis.
Expression, purification and reconstitution of the C-terminal transmembrane domain of scavenger receptor BI into detergent micelles for NMR analysis.
Expression, purification and reconstitution of the C-terminal transmembrane domain of scavenger receptor BI into detergent micelles for NMR analysis.
Protein Expr Purif. 2014 Nov 12;
Authors: Chadwick AC, Jensen DR, Peterson FC, Volkman BF, Sahoo D
Abstract
Scavenger receptor class B type I (SR-BI), the high density lipoprotein (HDL) receptor, is important for the delivery of...
nmrlearner
Journal club
0
12-03-2014 04:05 PM
[NMR paper] Expression, purification, and micelle reconstitution of antimicrobial Piscidin 1 and Piscidin 3 for NMR studies.
Expression, purification, and micelle reconstitution of antimicrobial Piscidin 1 and Piscidin 3 for NMR studies.
Expression, purification, and micelle reconstitution of antimicrobial Piscidin 1 and Piscidin 3 for NMR studies.
Protein Expr Purif. 2014 Aug 12;
Authors: Chen W, Cotten ML
Abstract
Piscidin 1 and piscidin 3, which were discovered in the mast cells of hybrid striped sea bass, are homologous antimicrobial peptides that are active against drug-resistant bacteria. Piscidin 1, the more antimicrobial and hemolytic...
nmrlearner
Journal club
0
08-19-2014 11:21 AM
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...
nmrlearner
Journal club
0
09-13-2011 08:27 PM
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Protein Expr Purif. 2011 Feb 11;
Authors: Wang X, Gill Jr RL, Zhu Q, Tian F
LR11 (SorLA) is a recently identified neuronal protein that interacts with amyloid precursor protein (APP), a central player...
nmrlearner
Journal club
0
02-16-2011 07:40 PM
Evidence from solid-state NMR for nonhelical conformations in the transmembrane domain of the amyloid precursor protein.
Evidence from solid-state NMR for nonhelical conformations in the transmembrane domain of the amyloid precursor protein.
Evidence from solid-state NMR for nonhelical conformations in the transmembrane domain of the amyloid precursor protein.
Biophys J. 2011 Feb 2;100(3):711-9
Authors: Lu JX, Yau WM, Tycko R
The amyloid precursor protein (APP) is subject to proteolytic processing by ?-secretase within neuronal membranes, leading to Alzheimer's disease-associated ?-amyloid peptide production by cleavage near the midpoint of the*single...
Expression, purification and micelle reconstruction of the transmembrane domain of the human amyloid precursor protein for NMR studies
Linear Mode
