Aph-1 contributes to the stabilization and trafficking of the gamma-secretase complex through mechanisms involving intermolecular and intramolecular interactions.
about
Ubiquilin regulates presenilin endoproteolysis and modulates gamma-secretase components, Pen-2 and nicastrinThe role of APP and BACE1 trafficking in APP processing and amyloid-β generationProteolytic processing of Alzheimer's β-amyloid precursor proteinPen-2 is incorporated into the gamma-secretase complex through binding to transmembrane domain 4 of presenilin 1SRG3 interacts directly with the major components of the SWI/SNF chromatin remodeling complex and protects them from proteasomal degradationAssembly, maturation, and trafficking of the gamma-secretase complex in Alzheimer's disease.Gamma-secretase subunits associate in intracellular membrane compartments in Arabidopsis thaliana.Drosophila models of neurodegenerative diseaseAn alternative interpretation of the amyloid Abeta hypothesis with regard to the pathogenesis of Alzheimer's diseaseCharacterization of an atypical gamma-secretase complex from hematopoietic originFunctional analysis of the transmembrane domains of presenilin 1: participation of transmembrane domains 2 and 6 in the formation of initial substrate-binding site of gamma-secretase.Phosphorylation of nicastrin by SGK1 leads to its degradation through lysosomal and proteasomal pathways.Reduced Alzheimer's disease ß-amyloid deposition in transgenic mice expressing S-palmitoylation-deficient APH1aL and nicastrin.A synthetic antibody fragment targeting nicastrin affects assembly and trafficking of γ-secretase.Structure of gamma-secretase and its trimeric pre-activation intermediate by single-particle electron microscopy.Presenilin transmembrane domain 8 conserved AXXXAXXXG motifs are required for the activity of the γ-secretase complexChemical 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.The role of presenilin and its interacting proteins in the biogenesis of Alzheimer's beta amyloidSorting through the cell biology of Alzheimer's disease: intracellular pathways to pathogenesis.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.Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease.Toward structural elucidation of the gamma-secretase complex.Single chain variable fragment against nicastrin inhibits the gamma-secretase activity.The structure and function of Alzheimer's gamma secretase enzyme complex.Therapeutic intervention for Alzheimer's disease with γ-secretase inhibitors: still a viable option?Membrane trafficking pathways in Alzheimer's disease.Advances in the identification of γ-secretase inhibitors for the treatment of Alzheimer's disease.Structural biology of presenilins and signal peptide peptidases.Development and mechanism of γ-secretase modulators for Alzheimer's disease.Physiological and pathological roles of the γ-secretase complex.Rer1p competes with APH-1 for binding to nicastrin and regulates gamma-secretase complex assembly in the early secretory pathway.Comparison of presenilin 1 and presenilin 2 γ-secretase activities using a yeast reconstitution system.Abeta42 overproduction associated with structural changes in the catalytic pore of gamma-secretase: common effects of Pen-2 N-terminal elongation and fenofibrate.Ubiquitin-proteasome pathway mediates degradation of APH-1.Amyloidogenic processing but not amyloid precursor protein (APP) intracellular C-terminal domain production requires a precisely oriented APP dimer assembled by transmembrane GXXXG motifs.Nicastrin is dispensable for gamma-secretase protease activity in the presence of specific presenilin mutations.Transmembrane domain 9 of presenilin determines the dynamic conformation of the catalytic site of gamma-secretase.Hydrogen Sulfide Selectively Inhibits γ-Secretase Activity and Decreases Mitochondrial Aβ Production in Neurons from APP/PS1 Transgenic Mice.Effects and Mechanism of Huannao Yicong Decoction Extract on the Ethology of Transgenic APP/PS1 Mice.
P2860
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P2860
Aph-1 contributes to the stabilization and trafficking of the gamma-secretase complex through mechanisms involving intermolecular and intramolecular interactions.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
Aph-1 contributes to the stabi ...... d intramolecular interactions.
@en
type
label
Aph-1 contributes to the stabi ...... d intramolecular interactions.
@en
prefLabel
Aph-1 contributes to the stabi ...... d intramolecular interactions.
@en
P2093
P2860
P356
P1476
Aph-1 contributes to the stabi ...... d intramolecular interactions.
@en
P2093
Kaoru Saigo
Kumiko Ui-Tei
Makiko Tsuruoka
Manabu Niimura
Nobumasa Takasugi
Noriko Isoo
Takeshi Iwatsubo
Yuichi Morohashi
P2860
P304
12967-12975
P356
10.1074/JBC.M409829200
P407
P577
2005-01-11T00:00:00Z