Perturbations of the straight transmembrane α-helical structure of the amyloid precursor protein affect its processing by γ-secretase.
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Rotameric preferences of a protein spin label at edge-strand β-sheet sites.Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulationsLost region in amyloid precursor protein (APP) through TALEN-mediated genome editing alters mitochondrial morphology.Impact of membrane lipid composition on the structure and stability of the transmembrane domain of amyloid precursor protein.Molecular mechanism of the intramembrane cleavage of the β-carboxyl terminal fragment of amyloid precursor protein by γ-secretase.Impact of bilayer lipid composition on the structure and topology of the transmembrane amyloid precursor C99 proteinStructural and biochemical differences between the Notch and the amyloid precursor protein transmembrane domains.Backbone Hydrogen Bond Strengths Can Vary Widely in Transmembrane Helices.
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Perturbations of the straight transmembrane α-helical structure of the amyloid precursor protein affect its processing by γ-secretase.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 27 January 2014
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Perturbations of the straight ...... its processing by γ-secretase.
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Perturbations of the straight ...... its processing by γ-secretase.
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type
label
Perturbations of the straight ...... its processing by γ-secretase.
@en
Perturbations of the straight ...... its processing by γ-secretase.
@nl
prefLabel
Perturbations of the straight ...... its processing by γ-secretase.
@en
Perturbations of the straight ...... its processing by γ-secretase.
@nl
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Perturbations of the straight ...... its processing by γ-secretase
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Matteo Dal Peraro
Mitko Dimitrov
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P304
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10.1074/JBC.M113.470781
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P577
2014-01-27T00:00:00Z