Familial Alzheimer’s mutations within APPTM increase Aβ42 production by enhancing accessibility of ε-cleavage site

Familial Alzheimer’s mutations within APPTM increase Aβ42 production by enhancing accessibility of ε-cleavage site

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http://www.wikidata.org/entity/Q27681185
Alzheimer's disease--a panorama glimpseStructural Mechanism of the Interaction of Alzheimer Disease Aβ Fibrils with the Non-steroidal Anti-inflammatory Drug (NSAID) Sulindac SulfideStructural heterogeneity in transmembrane amyloid precursor protein homodimer is a consequence of environmental selection.Extension of a protein docking algorithm to membranes and applications to amyloid precursor protein dimerization.Deposition of C-terminally truncated Aβ species Aβ37 and Aβ39 in Alzheimer's disease and transgenic mouse models.Evolutionary-guided de novo structure prediction of self-associated transmembrane helical proteins with near-atomic accuracy.Interplay of endoplasmic reticulum stress and autophagy in neurodegenerative disorders.Alzheimer's disease-associated mutations increase amyloid precursor protein resistance to γ-secretase cleavage and the Aβ42/Aβ40 ratioImpact of membrane lipid composition on the structure and stability of the transmembrane domain of amyloid precursor protein.How amyloid precursor protein protects itself from cleavage.The amyloid-beta forming tripeptide cleavage mechanism of γ-secretase.Backbone Hydrogen Bond Strengths Can Vary Widely in Transmembrane Helices.Dominant negative effect of the loss-of-function γ-secretase mutants on the wild-type enzyme through heterooligomerization.The Role of microRNAs in Alzheimer's Disease and Their Therapeutic Potentials.Binding of Bexarotene to the Amyloid Precursor Protein Transmembrane Domain in Liposomes Alters its α-Helical Conformation but Inhibits γ-Secretase Non-Selectively.Mechanism of Allosteric Coupling into and through the Plasma Membrane by EGFR.Coupled Transmembrane Substrate Docking and Helical Unwinding in Intramembrane Proteolysis of Amyloid Precursor Protein
P2860

Familial Alzheimer’s mutations within APPTM increase Aβ42 production by enhancing accessibility of ε-cleavage site

Item
http://www.wikidata.org/entity/Q27681185
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2014 nî lūn-bûn
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2014 թուականին հրատարակուած գիտական յօդուած
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2014 թվականին հրատարակված գիտական հոդված
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2014年の論文
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2014年論文
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2014年論文
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2014年論文
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name
Familial Alzheimer’s mutations ...... cessibility of ε-cleavage site
@ast
Familial Alzheimer’s mutations ...... cessibility of ε-cleavage site
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Familial Alzheimer’s mutations ...... cessibility of ε-cleavage site
@nl
type
label
Familial Alzheimer’s mutations ...... cessibility of ε-cleavage site
@ast
Familial Alzheimer’s mutations ...... cessibility of ε-cleavage site
@en
Familial Alzheimer’s mutations ...... cessibility of ε-cleavage site
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prefLabel
Familial Alzheimer’s mutations ...... cessibility of ε-cleavage site
@ast
Familial Alzheimer’s mutations ...... cessibility of ε-cleavage site
@en
Familial Alzheimer’s mutations ...... cessibility of ε-cleavage site
@nl
P1433
P1476
P2093
P2860
P2888
P304
P31
P3181
P356
P407
P478
P577
P6179
P698
P921
P932
P3181
P356
P1433
P1476
Familial Alzheimer’s mutations ...... cessibility of ε-cleavage site
@en
P2093
P2860
P2888
P304
P31
P3181
P356
P407
P478
P577
P6179
P698
P921
P932