Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-beta precursor protein and Notch
about
Human CRB2 inhibits gamma-secretase cleavage of amyloid precursor protein by binding to the presenilin complexTransmembrane protein 147 (TMEM147) is a novel component of the Nicalin-NOMO protein complexCD147 is a regulatory subunit of the gamma-secretase complex in Alzheimer's disease amyloid beta-peptide productionAssociation of gamma-secretase with lipid rafts in post-Golgi and endosome membranes.Nicastrin is critical for stability and trafficking but not association of other presenilin/gamma-secretase components.Conditional forebrain inactivation of nicastrin causes progressive memory impairment and age-related neurodegenerationStructural biology of presenilin 1 complexesA conserved GXXXG motif in APH-1 is critical for assembly and activity of the gamma-secretase complexProteolytic processing of Alzheimer's β-amyloid precursor proteinA nine-transmembrane domain topology for presenilin 1Assembly, trafficking and function of gamma-secretaseEvidence that assembly of an active gamma-secretase complex occurs in the early compartments of the secretory pathwayBACE1 inhibition induces a specific cerebrospinal fluid β-amyloid pattern that identifies drug effects in the central nervous systemΓ-secretase components as predictors of breast cancer outcomePresenilin-1, nicastrin, amyloid precursor protein, and gamma-secretase activity are co-localized in the lysosomal membraneAph-1 associates directly with full-length and C-terminal fragments of gamma-secretase substratesTailoring of membrane proteins by alternative splicing of pre-mRNA.Altered neuronal gene expression in brain regions differentially affected by Alzheimer's disease: a reference data set.Presenilin-1 C410Y Alzheimer disease plaques contain synaptic proteins.Assembly, maturation, and trafficking of the gamma-secretase complex in Alzheimer's disease.Allosteric modulation of PS1/gamma-secretase conformation correlates with amyloid beta(42/40) ratio.Pyroglutamate-amyloid-β and glutaminyl cyclase are colocalized with amyloid-β in secretory vesicles and undergo activity-dependent, regulated secretion.Gamma-secretase-regulated proteolysis of the Notch receptor by mitochondrial intermediate peptidasePhosphorylation of nicastrin by SGK1 leads to its degradation through lysosomal and proteasomal pathways.Recent advances in the understanding of the role of the endocannabinoid system in liver diseases.Characterization of presenilin complexes from mouse and human brain using Blue Native gel electrophoresis reveals high expression in embryonic brain and minimal change in complex mobility with pathogenic presenilin mutations.A synthetic antibody fragment targeting nicastrin affects assembly and trafficking of γ-secretase.Physiologic and pathologic events mediated by intramembranous and juxtamembranous proteolysis.p53-dependent control of transactivation of the Pen2 promoter by presenilinsPresenilin function and gamma-secretase activity.The endocannabinoid, anandamide, augments Notch-1 signaling in cultured cortical neurons exposed to amyloid-β and in the cortex of aged ratsWnt5a controls Notch1 signaling through CaMKII-mediated degradation of the SMRT corepressor proteinDifferent cofactor activities in gamma-secretase assembly: evidence for a nicastrin-Aph-1 subcomplex.Pen-2 is dispensable for endoproteolysis of presenilin 1, and nicastrin-Aph subcomplex is important for both γ-secretase assembly and substrate recruitmentThe role of presenilin and its interacting proteins in the biogenesis of Alzheimer's beta amyloidNotch1 modulates oxidative stress induced cell death through suppression of apoptosis signal-regulating kinase 1.Alzheimer's disease: the lipid connection.Nicastrin is required for APP but not Notch processing, while Aph-1 is dispensable for processing of both APP and Notch.Substrate specificity of gamma-secretase and other intramembrane proteases.Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease.
P2860
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P248
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P2860
Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-beta precursor protein and Notch
description
2002 nî lūn-bûn
@nan
2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Mammalian APH-1 interacts with ...... ta precursor protein and Notch
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Mammalian APH-1 interacts with ...... ta precursor protein and Notch
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Mammalian APH-1 interacts with ...... ta precursor protein and Notch
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Mammalian APH-1 interacts with ...... ta precursor protein and Notch
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Mammalian APH-1 interacts with ...... ta precursor protein and Notch
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Mammalian APH-1 interacts with ...... ta precursor protein and Notch
@en
Mammalian APH-1 interacts with ...... ta precursor protein and Notch
@en-gb
Mammalian APH-1 interacts with ...... ta precursor protein and Notch
@nl
prefLabel
Mammalian APH-1 interacts with ...... ta precursor protein and Notch
@ast
Mammalian APH-1 interacts with ...... ta precursor protein and Notch
@en
Mammalian APH-1 interacts with ...... ta precursor protein and Notch
@en-gb
Mammalian APH-1 interacts with ...... ta precursor protein and Notch
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P2093
P2860
P921
P3181
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Mammalian APH-1 interacts with ...... ta precursor protein and Notch
@en
P2093
Hongqiao Li
Sanjiv Shah
Sheu-Fen Lee
Weiping Han
P2860
P304
P3181
P356
10.1074/JBC.M208164200
P407
P577
2002-11-22T00:00:00Z