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Gamma-secretase complex assembly within the early secretory pathway

Gamma-secretase complex assembly within the early secretory pathway

http://www.wikidata.org/entity/Q28297818

about

Transmembrane protein 147 (TMEM147) is a novel component of the Nicalin-NOMO protein complex Decreased CALM expression reduces Aβ42 to total Aβ ratio through clathrin-mediated endocytosis of γ-secretase The role of APP and BACE1 trafficking in APP processing and amyloid-β generation Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway Assembly, trafficking and function of gamma-secretase Pen-2 is incorporated into the gamma-secretase complex through binding to transmembrane domain 4 of presenilin 1 Phenylbutyric acid rescues endoplasmic reticulum stress-induced suppression of APP proteolysis and prevents apoptosis in neuronal cells Aph-1 associates directly with full-length and C-terminal fragments of gamma-secretase substrates Presenilin 1 and Presenilin 2 Target γ-Secretase Complexes to Distinct Cellular Compartments.Assembly, maturation, and trafficking of the gamma-secretase complex in Alzheimer's disease.Synaptic and endosomal localization of active gamma-secretase in rat brain.Mutation analysis of the presenilin 1 N-terminal domain reveals a broad spectrum of gamma-secretase activity toward amyloid precursor protein and other substrates.Reduced Alzheimer's disease ß-amyloid deposition in transgenic mice expressing S-palmitoylation-deficient APH1aL and nicastrin.Alzheimer's disease beta-amyloid peptides are released in association with exosomes.The γ-secretase complex: from structure to function.Chemical cross-linking provides a model of the gamma-secretase complex subunit architecture and evidence for close proximity of the C-terminal fragment of presenilin with APH-1.β-arrestin1 regulates γ-secretase complex assembly and modulates amyloid-β pathology.Substrate specificity of gamma-secretase and other intramembrane proteases.Pen2 and presenilin-1 modulate the dynamic equilibrium of presenilin-1 and presenilin-2 gamma-secretase complexes.Glu-333 of nicastrin directly participates in gamma-secretase activity.Single chain variable fragment against nicastrin inhibits the gamma-secretase activity.The structure and function of Alzheimer's gamma secretase enzyme complex.Assembly of the presenilin γ-/ε-secretase complex.Development and mechanism of γ-secretase modulators for Alzheimer's disease.Rer1p competes with APH-1 for binding to nicastrin and regulates gamma-secretase complex assembly in the early secretory pathway.Glu(332) in the Nicastrin ectodomain is essential for gamma-secretase complex maturation but not for its activity.Biogenesis of gamma-secretase early in the secretory pathway.Endoplasmic reticulum retention of the gamma-secretase complex component Pen2 by Rer1.Aph-1 contributes to the stabilization and trafficking of the gamma-secretase complex through mechanisms involving intermolecular and intramolecular interactions.Modifications and Trafficking of APP in the Pathogenesis of Alzheimer's Disease.Alphabeta hinders nuclear targeting of AICD and Fe65 in primary neuronal cultures.Intramembrane proteolysis of β-amyloid precursor protein by γ-secretase is an unusually slow process.Tyrosine 687 phosphorylated Alzheimer's amyloid precursor protein is retained intracellularly and exhibits a decreased turnover rate.Conserved residues in juxtamembrane region of the extracellular domain of nicastrin are essential for gamma-secretase complex formation

P2860

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P2860

Gamma-secretase complex assembly within the early secretory pathway

http://www.wikidata.org/entity/Q28297818

description

2005 nî lūn-bûn

@nan

2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի փետրվարին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

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name

Gamma-secretase complex assembly within the early secretory pathway

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Gamma-secretase complex assembly within the early secretory pathway

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Gamma-secretase complex assembly within the early secretory pathway

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type

label

Gamma-secretase complex assembly within the early secretory pathway

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Gamma-secretase complex assembly within the early secretory pathway

@en

Gamma-secretase complex assembly within the early secretory pathway

@nl

prefLabel

Gamma-secretase complex assembly within the early secretory pathway

@ast

Gamma-secretase complex assembly within the early secretory pathway

@en

Gamma-secretase complex assembly within the early secretory pathway

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P1433

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P1433

Journal of Biological Chemistry

P1476

Gamma-secretase complex assembly within the early secretory pathway

@en

P2093

Christoph Kaether

http://www.w3.org/2001/XMLSchema#string

Harald Steiner

http://www.w3.org/2001/XMLSchema#string

Mark S Shearman

http://www.w3.org/2001/XMLSchema#string

P2860

Presenilin and nicastrin regulate each other and determine amyloid beta-peptide production via complex formation

The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics

A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targeting and endocytosis of CD3 chains

Photoactivated gamma-secretase inhibitors directed to the active site covalently label presenilin 1

The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases

Identification of signal peptide peptidase, a presenilin-type aspartic protease

Functional gamma-secretase complex assembly in Golgi/trans-Golgi network: interactions among presenilin, nicastrin, Aph1, Pen-2, and gamma-secretase substrates

APH-1 interacts with mature and immature forms of presenilins and nicastrin and may play a role in maturation of presenilin.nicastrin complexes

Signal peptide peptidase forms a homodimer that is labeled by an active site-directed gamma-secretase inhibitor

Endoproteolytic processing and stabilization of wild-type and mutant presenilin

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6471-8

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scholarly article

P356

10.1074/JBC.M409106200

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P433

8

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P478

280

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P50

Christian Haass

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2005-02-25T00:00:00Z

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P698

15591316

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