Gamma-secretase catalyzes sequential cleavages of the AbetaPP transmembrane domain.
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Intracellular Calcium Dysregulation: Implications for Alzheimer's DiseaseRole of the Retromer Complex in Neurodegenerative DiseasesAlzheimer's disease-linked mutations in presenilin-1 result in a drastic loss of activity in purified γ-secretase complexes.Presenilins and the gamma-secretase: still a complex problem.Combined treatment with a BACE inhibitor and anti-Aβ antibody gantenerumab enhances amyloid reduction in APPLondon mice.Targets for AD treatment: conflicting messages from γ-secretase inhibitorsEvidence of a novel mechanism for partial γ-secretase inhibition induced paradoxical increase in secreted amyloid β proteinLysine 624 of the amyloid precursor protein (APP) is a critical determinant of amyloid β peptide length: support for a sequential model of γ-secretase intramembrane proteolysis and regulation by the amyloid β precursor protein (APP) juxtamembrane reCellular FLICE-like Inhibitory Protein (c-FLIP) and PS1-associated Protein (PSAP) Mediate Presenilin 1-induced γ-Secretase-dependent and -independent Apoptosis, Respectively.Isoflurane anesthesia promotes cognitive impairment by inducing expression of β-amyloid protein-related factors in the hippocampus of aged rats.Pen-2 is dispensable for endoproteolysis of presenilin 1, and nicastrin-Aph subcomplex is important for both γ-secretase assembly and substrate recruitmentLysophosphatidic acid induces increased BACE1 expression and Aβ formation.The role of γ-secretase activating protein (GSAP) and imatinib in the regulation of γ-secretase activity and amyloid-β generation.Nicastrin is required for APP but not Notch processing, while Aph-1 is dispensable for processing of both APP and Notch.Alzheimer's disease-associated mutations increase amyloid precursor protein resistance to γ-secretase cleavage and the Aβ42/Aβ40 ratioTreatment strategies targeting amyloid β-protein.Turnover of C99 is controlled by a crosstalk between ERAD and ubiquitin-independent lysosomal degradation in human neuroglioma cells.Evidence that enzyme processivity mediates differential Aβ production by PS1 and PS2Major carboxyl terminal fragments generated by γ-secretase processing of the Alzheimer amyloid precursor are 50 and 51 amino acids long.Aging and neurogenesis, a lesion from Alzheimer's disease.Distribution and expression of Pen-2 in the central nervous system of APP/PS1 double transgenic mice.The dynamics of Aβ distribution after γ-secretase inhibitor treatment, as determined by experimental and modelling approaches in a wild type rat.APP/Aβ structural diversity and Alzheimer's disease pathogenesis.
P2860
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P2860
Gamma-secretase catalyzes sequential cleavages of the AbetaPP transmembrane domain.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Gamma-secretase catalyzes sequential cleavages of the AbetaPP transmembrane domain.
@en
Gamma-secretase catalyzes sequential cleavages of the AbetaPP transmembrane domain.
@nl
type
label
Gamma-secretase catalyzes sequential cleavages of the AbetaPP transmembrane domain.
@en
Gamma-secretase catalyzes sequential cleavages of the AbetaPP transmembrane domain.
@nl
prefLabel
Gamma-secretase catalyzes sequential cleavages of the AbetaPP transmembrane domain.
@en
Gamma-secretase catalyzes sequential cleavages of the AbetaPP transmembrane domain.
@nl
P2860
P356
P1476
Gamma-secretase catalyzes sequential cleavages of the AbetaPP transmembrane domain
@en
P2093
P2860
P304
P356
10.3233/JAD-2009-0957
P50
P577
2009-01-01T00:00:00Z