[NMR paper] Expression, purification and micelle reconstruction of the transmembrane domain of the human amyloid precursor protein for NMR studies
Expression, purification and micelle reconstruction of the transmembrane domain of the human amyloid precursor protein for NMR studies
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...
[ASAP] Substrate Determinants for Unwinding Activity of the DExH/D-Box Protein RNA Helicase A
Substrate Determinants for Unwinding Activity of the DExH/D-Box Protein RNA Helicase A
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b01025/20181115/images/medium/bi-2018-01025w_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b01025
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http://feeds.feedburner.com/~r/acs/bichaw/~4/FPCroLUgV7c
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11-25-2018 06:02 AM
Proton-Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin
Proton-Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin
Meaghan E. Ward, Lichi Shi, Evelyn Lake, Sridevi Krishnamurthy, Howard Hutchins, Leonid S. Brown and Vladimir Ladizhansky
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja207137h/aop/images/medium/ja-2011-07137h_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja207137h
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10-09-2011 06:15 AM
Proton Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin.
Proton Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin.
Proton Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin.
J Am Chem Soc. 2011 Sep 16;
Authors: Ward ME, Shi L, Lake EM, Krishnamurthy S, Hutchins H, Brown LS, Ladizhansky V
Abstract
We used high-resolution proton-detected multidimensional NMR to study the solvent-exposed parts of an integral seven-helical membrane proton pump proteorhodopsin...
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09-17-2011 08:21 PM
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
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...
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02-02-2011 12:40 PM
[NMR paper] Redesign of a four-helix bundle protein by phage display coupled with proteolysis and
Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography.
Related Articles Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography.
J Mol Biol. 2002 Oct 18;323(2):253-62
Authors: Chu R, Takei J, Knowlton JR, Andrykovitch M, Pei W, Kajava AV, Steinbach PJ, Ji X, Bai Y
To test whether it is practical to use phage display coupled with proteolysis for protein design, we...