APH1 polar transmembrane residues regulate the assembly and activity of presenilin complexes - Wikidata - awgldk - TriplyDB

APH1 polar transmembrane residues regulate the assembly and activity of presenilin complexes

APH1 polar transmembrane residues regulate the assembly and activity of presenilin complexes

http://www.wikidata.org/entity/Q37269196

about

Cellular mechanisms of γ-secretase substrate selection, processing and toxicity Structural biology of presenilin 1 complexes An atomic structure of human γ-secretase Aph-1 associates directly with full-length and C-terminal fragments of gamma-secretase substrates Proliferation, differentiation and amyloid-β production in neural progenitor cells isolated from TgCRND8 mice.Specific domains in anterior pharynx-defective 1 determine its intramembrane interactions with nicastrin and presenilin.Phosphorylation of nicastrin by SGK1 leads to its degradation through lysosomal and proteasomal pathways.The γ-secretase complex: from structure to function.Presenilins and γ-secretase: structure, function, and role in Alzheimer Disease.Assembly of the presenilin γ-/ε-secretase complex.Membrane trafficking pathways in Alzheimer's disease.The very many faces of presenilins and the γ-secretase complex.Polar transmembrane-based amino acids in presenilin 1 are involved in endoplasmic reticulum localization, Pen2 protein binding, and γ-secretase complex stabilization Pen-2 is essential for γ-secretase complex stability and trafficking but partially dispensable for endoproteolysis.Modification of γ-secretase by nitrosative stress links neuronal ageing to sporadic Alzheimer's disease.Alterations in phosphatidylethanolamine levels affect the generation of Aβ.Structural and Chemical Biology of Presenilin Complexes.Presenilins as Drug Targets for Alzheimer's Disease-Recent Insights from Cell Biology and Electrophysiology as Novel Opportunities in Drug Development.

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P2860

APH1 polar transmembrane residues regulate the assembly and activity of presenilin complexes

http://www.wikidata.org/entity/Q37269196

description

article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

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scientific article published on 15 April 2009

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

APH1 polar transmembrane resid ...... tivity of presenilin complexes

@en

APH1 polar transmembrane resid ...... ivity of presenilin complexes.

@nl

type

label

APH1 polar transmembrane resid ...... tivity of presenilin complexes

@en

APH1 polar transmembrane resid ...... ivity of presenilin complexes.

@nl

prefLabel

APH1 polar transmembrane resid ...... tivity of presenilin complexes

@en

APH1 polar transmembrane resid ...... ivity of presenilin complexes.

@nl

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P356

JBC.M109.000067

P1433

Journal of Biological Chemistry

P1476

APH1 polar transmembrane resid ...... tivity of presenilin complexes

@en

P2093

Christopher Böhm

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

Fusheng Chen

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

Gerold Schmitt-Ulms

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

Jean Sevalle

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

Paul E Fraser

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Philip C Wong

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

Raphaëlle Pardossi-Piquard

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Seung-Pil Yang

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

Soshi Kanemoto

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

Tong Li

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

P2860

Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing

Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-beta precursor protein and Notch

The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains beta-catenin

Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo

Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease

TMP21 is a presenilin complex component that modulates gamma-secretase but not epsilon-secretase activity

Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment

Crystal structure of rhodopsin: A G protein-coupled receptor

Structural basis for intramembrane proteolysis by rhomboid serine proteases

Open-cap conformation of intramembrane protease GlpG

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16298-16307

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scholarly article

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10.1074/JBC.M109.000067

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24

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284

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Frédéric Checler

Peter Henry St George-Hyslop

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2009-04-15T00:00:00Z

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19369254

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transmembrane protein

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