Detergent-dependent dissociation of active gamma-secretase reveals an interaction between Pen-2 and PS1-NTF and offers a model for subunit organization within the complex.
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Nicastrin is critical for stability and trafficking but not association of other presenilin/gamma-secretase components.Ubiquilin regulates presenilin endoproteolysis and modulates gamma-secretase components, Pen-2 and nicastrinElectron microscopic structure of purified, active gamma-secretase reveals an aqueous intramembrane chamber and two pores.The role of APP and BACE1 trafficking in APP processing and amyloid-β generationToward the structure of presenilin/γ-secretase and presenilin homologsStructural biology of presenilin 1 complexesIdentification of the novel activity-driven interaction between synaptotagmin 1 and presenilin 1 links calcium, synapse, and amyloid betaA nine-transmembrane domain topology for presenilin 1Pen-2 is incorporated into the gamma-secretase complex through binding to transmembrane domain 4 of presenilin 1A C-terminal region of signal peptide peptidase defines a functional domain for intramembrane aspartic protease catalysisAph-1 associates directly with full-length and C-terminal fragments of gamma-secretase substratesTailoring of membrane proteins by alternative splicing of pre-mRNA.Structural basis of human γ-secretase assembly.Alzheimer's disease-linked mutations in presenilin-1 result in a drastic loss of activity in purified γ-secretase complexes.Assembly, maturation, and trafficking of the gamma-secretase complex in Alzheimer's disease.Gene expression profiling in cells with enhanced gamma-secretase activity.Phenotypic analysis of images of zebrafish treated with Alzheimer's gamma-secretase inhibitors.Modulation of gamma-secretase reduces beta-amyloid deposition in a transgenic mouse model of Alzheimer's disease.Cryoelectron microscopy structure of purified gamma-secretase at 12 A resolution.Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity.Specific domains in anterior pharynx-defective 1 determine its intramembrane interactions with nicastrin and presenilin.Crystal structure of the γ-secretase component nicastrin.Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases.Amyloid precursor protein selective gamma-secretase inhibitors for treatment of Alzheimer's disease.Functional and topological analysis of Pen-2, the fourth subunit of the gamma-secretase complex.Experimental detection of proteolytic activity in a signal peptide peptidase of Arabidopsis thaliana.gamma-Secretase substrate selectivity can be modulated directly via interaction with a nucleotide-binding site.Structural interactions between inhibitor and substrate docking sites give insight into mechanisms of human PS1 complexes.γ-Secretase processing and effects of γ-secretase inhibitors and modulators on long Aβ peptides in cells.Presenilins and γ-secretase: structure, function, and role in Alzheimer Disease.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.The topology of pen-2, a γ-secretase subunit, revisited: evidence for a reentrant loop and a single pass transmembrane domain.Presenilin function and gamma-secretase activity.Pen-2 is dispensable for endoproteolysis of presenilin 1, and nicastrin-Aph subcomplex is important for both γ-secretase assembly and substrate recruitmentβ-arrestin1 regulates γ-secretase complex assembly and modulates amyloid-β pathology.A faster migrating variant masquerades as NICD when performing in vitro gamma-secretase assays with bacterially expressed Notch substratesStructural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease.Gamma-secretase inhibition and modulation for Alzheimer's disease.Toward structural elucidation of the gamma-secretase complex.Inhibition and modulation of gamma-secretase for Alzheimer's disease
P2860
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P2860
Detergent-dependent dissociation of active gamma-secretase reveals an interaction between Pen-2 and PS1-NTF and offers a model for subunit organization within the complex.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Detergent-dependent dissociati ...... ganization within the complex.
@en
type
label
Detergent-dependent dissociati ...... ganization within the complex.
@en
prefLabel
Detergent-dependent dissociati ...... ganization within the complex.
@en
P2093
P356
P1433
P1476
Detergent-dependent dissociati ...... ganization within the complex.
@en
P2093
Beth L Ostaszewski
Dennis J Selkoe
Matthew J LaVoie
Michael S Wolfe
W Taylor Kimberly
Wenjuan Ye
P304
P356
10.1021/BI035748J
P407
P577
2004-01-01T00:00:00Z