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The Amyloid Precursor Protein Has a Flexible Transmembrane Domain and Binds Cholesterol

Insights into AmyloidogenesisThe amyloid- beta (A beta ) peptides associated with Alzheimer's disease are generated by cleavage of the transmembrane C-terminal domain (C99) of the amyloid precursor protein by the enzyme gamma -secretase. Barrett et al. (p. 1168) used nuclear magnetic resonance (NMR)... Full description

Journal Title: Science June 1, 2012, Vol.336(6085), pp.1168-1171
Main Author: Barrett, Paul
Other Authors: Song, Yuanli , Van Horn, Wade , Hustedt, Eric , Schafer, Johanna , Hadziselimovic, Arina , Beel, Andrew , Sanders, Charles
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0036-8075 ; DOI: 10.1126/science.1219988
Link: http://search.proquest.com/docview/1808087681/
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recordid: proquest1808087681
title: The Amyloid Precursor Protein Has a Flexible Transmembrane Domain and Binds Cholesterol
format: Article
creator:
  • Barrett, Paul
  • Song, Yuanli
  • Van Horn, Wade
  • Hustedt, Eric
  • Schafer, Johanna
  • Hadziselimovic, Arina
  • Beel, Andrew
  • Sanders, Charles
subjects:
  • Precursors
  • Titration
  • Alzheimer'S Disease
  • Proteins
  • Electron Paramagnetic Resonance
  • Cholesterol
  • Nuclear Magnetic Resonance
  • Cleavage
  • Miscellaneous Sciences (So)
ispartof: Science, June 1, 2012, Vol.336(6085), pp.1168-1171
description: Insights into AmyloidogenesisThe amyloid- beta (A beta ) peptides associated with Alzheimer's disease are generated by cleavage of the transmembrane C-terminal domain (C99) of the amyloid precursor protein by the enzyme gamma -secretase. Barrett et al. (p. 1168) used nuclear magnetic resonance (NMR) and electron paramagnetic resonance spectroscopy to show that C99 contains surface-associated N- and C-terminal helices and a flexibly curved transmembrane helix that is well suited to processive cleavage by gamma -secretase. Elevated cholesterol levels have been found to increase A beta generation. NMR titration together with mutagenesis revealed a binding site for cholesterol within C99 that included a motif previously implicated in protein oligomerization.
language: eng
source:
identifier: ISSN: 0036-8075 ; DOI: 10.1126/science.1219988
fulltext: no_fulltext
issn:
  • 00368075
  • 0036-8075
url: Link


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titleThe Amyloid Precursor Protein Has a Flexible Transmembrane Domain and Binds Cholesterol
creatorBarrett, Paul ; Song, Yuanli ; Van Horn, Wade ; Hustedt, Eric ; Schafer, Johanna ; Hadziselimovic, Arina ; Beel, Andrew ; Sanders, Charles
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ispartofScience, June 1, 2012, Vol.336(6085), pp.1168-1171
identifierISSN: 0036-8075 ; DOI: 10.1126/science.1219988
subjectPrecursors ; Titration ; Alzheimer'S Disease ; Proteins ; Electron Paramagnetic Resonance ; Cholesterol ; Nuclear Magnetic Resonance ; Cleavage ; Miscellaneous Sciences (So)
descriptionInsights into AmyloidogenesisThe amyloid- beta (A beta ) peptides associated with Alzheimer's disease are generated by cleavage of the transmembrane C-terminal domain (C99) of the amyloid precursor protein by the enzyme gamma -secretase. Barrett et al. (p. 1168) used nuclear magnetic resonance (NMR) and electron paramagnetic resonance spectroscopy to show that C99 contains surface-associated N- and C-terminal helices and a flexibly curved transmembrane helix that is well suited to processive cleavage by gamma -secretase. Elevated cholesterol levels have been found to increase A beta generation. NMR titration together with mutagenesis revealed a binding site for cholesterol within C99 that included a motif previously implicated in protein oligomerization.
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titleThe Amyloid Precursor Protein Has a Flexible Transmembrane Domain and Binds Cholesterol
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abstractInsights into AmyloidogenesisThe amyloid- beta (A beta ) peptides associated with Alzheimer's disease are generated by cleavage of the transmembrane C-terminal domain (C99) of the amyloid precursor protein by the enzyme gamma -secretase. Barrett et al. (p. 1168) used nuclear magnetic resonance (NMR) and electron paramagnetic resonance spectroscopy to show that C99 contains surface-associated N- and C-terminal helices and a flexibly curved transmembrane helix that is well suited to processive cleavage by gamma -secretase. Elevated cholesterol levels have been found to increase A beta generation. NMR titration together with mutagenesis revealed a binding site for cholesterol within C99 that included a motif previously implicated in protein oligomerization.
doi10.1126/science.1219988
urlhttp://search.proquest.com/docview/1808087681/
eissn10959203
date2012-06-01