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Gamma-secretase activating protein is a therapeutic target for Alzheimer's diseaseThe α-helical content of the transmembrane domain of the British dementia protein-2 (Bri2) determines its processing by signal peptide peptidase-like 2b (SPPL2b)The novel membrane protein TMEM59 modulates complex glycosylation, cell surface expression, and secretion of the amyloid precursor proteinSubstrate requirements for SPPL2b-dependent regulated intramembrane proteolysisGeneration of amyloid-β is reduced by the interaction of calreticulin with amyloid precursor protein, presenilin and nicastrinThe dynamic role of beta-catenin in synaptic plasticityGenetic of Alzheimer's Disease: A Narrative Review ArticleMitochondrial dysfunction: different routes to Alzheimer's disease therapyStructural biology of presenilin 1 complexesStructural and dynamic study of the transmembrane domain of the amyloid precursor proteinAbeta, oxidative stress in Alzheimer disease: evidence based on proteomics studiesTrafficking and proteolytic processing of APPDifferential Inhibition of Signal Peptide Peptidase Family Members by Established γ-Secretase InhibitorsDictyostelium possesses highly diverged presenilin/gamma-secretase that regulates growth and cell-fate specification and can accurately process human APP: a system for functional studies of the presenilin/gamma-secretase complex.Cross-talk of membrane lipids and Alzheimer-related proteins.The C-terminal threonine of Aβ43 nucleates toxic aggregation via structural and dynamical changes in monomers and protofibrils.Beta-amyloid precursor protein mutants respond to gamma-secretase modulatorsRegulated intramembrane proteolysis of the frontotemporal lobar degeneration risk factor, TMEM106B, by signal peptide peptidase-like 2a (SPPL2a).A presenilin-1 mutation identified in familial Alzheimer disease with cotton wool plaques causes a nearly complete loss of gamma-secretase activityAcute gamma-secretase inhibition of nonhuman primate CNS shifts amyloid precursor protein (APP) metabolism from amyloid-beta production to alternative APP fragments without amyloid-beta reboundAltered levels and distribution of amyloid precursor protein and its processing enzymes in Niemann-Pick type C1-deficient mouse brainsγ-secretase-dependent cleavage initiates notch signaling from the plasma membraneAmyloid precursor protein (APP) mediated regulation of ganglioside homeostasis linking Alzheimer's disease pathology with ganglioside metabolism.Phosphorylation of nicastrin by SGK1 leads to its degradation through lysosomal and proteasomal pathways.Foamy virus envelope protein is a substrate for signal peptide peptidase-like 3 (SPPL3).Secretome analysis identifies novel signal Peptide peptidase-like 3 (Sppl3) substrates and reveals a role of Sppl3 in multiple Golgi glycosylation pathways.Shedding of glycan-modifying enzymes by signal peptide peptidase-like 3 (SPPL3) regulates cellular N-glycosylationHeteromers of amyloid precursor protein in cerebrospinal fluid.Expansion of type II CAAX proteases reveals evolutionary origin of γ-secretase subunit APH-1Coordinated increase of γ-secretase reaction products in the plasma of some female Japanese sporadic Alzheimer's disease patients: quantitative analysis of p3-Alcα with a new ELISA system.CoREST acts as a positive regulator of Notch signaling in the follicle cells of Drosophila melanogasterAn NSAID-like compound, FT-9, preferentially inhibits gamma-secretase cleavage of the amyloid precursor protein compared to its effect on amyloid precursor-like protein 1.Membrane-microdomain localization of amyloid β-precursor protein (APP) C-terminal fragments is regulated by phosphorylation of the cytoplasmic Thr668 residue.Substrate recruitment of γ-secretase and mechanism of clinical presenilin mutations revealed by photoaffinity mapping.Chemical Biology, Molecular Mechanism and Clinical Perspective of γ-Secretase Modulators in Alzheimer's DiseaseProteolytic Processing of Neuregulin 1 Type III by Three Intramembrane-cleaving ProteasesPresenilin transgenic mice as models of Alzheimer's disease.Palmitoylation of amyloid precursor protein regulates amyloidogenic processing in lipid raftsA role for WNT/β-catenin signaling in the neural mechanisms of behavior.Paradoxical condensation of copper with elevated beta-amyloid in lipid rafts under cellular copper deficiency conditions: implications for Alzheimer disease
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P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 23 July 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Intramembrane proteolysis by gamma-secretase.
@en
Intramembrane proteolysis by gamma-secretase.
@nl
type
label
Intramembrane proteolysis by gamma-secretase.
@en
Intramembrane proteolysis by gamma-secretase.
@nl
prefLabel
Intramembrane proteolysis by gamma-secretase.
@en
Intramembrane proteolysis by gamma-secretase.
@nl
P2860
P356
P1476
Intramembrane proteolysis by gamma-secretase.
@en
P2093
Harald Steiner
P2860
P304
29627-29631
P356
10.1074/JBC.R800010200
P407
P577
2008-07-23T00:00:00Z