PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1.
about
Ferritin light chain interacts with PEN-2 and affects γ-secretase activitySyntaxin 5 interacts with presenilin holoproteins, but not with their N- or C-terminal fragments, and affects beta-amyloid 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.Ubiquilin regulates presenilin endoproteolysis and modulates gamma-secretase components, Pen-2 and nicastrinTrafficking regulation of proteins in Alzheimer's diseaseToward the structure of presenilin/γ-secretase and presenilin homologsAPP processing in Alzheimer's diseaseA conserved GXXXG motif in APH-1 is critical for assembly and activity of the gamma-secretase complexProteolytic processing of Alzheimer's β-amyloid precursor proteinAssembly, trafficking and function of gamma-secretasePen-2 is incorporated into the gamma-secretase complex through binding to transmembrane domain 4 of presenilin 1Evidence that assembly of an active gamma-secretase complex occurs in the early compartments of the secretory pathwayGamma-secretase complex assembly within the early secretory pathwayAph-1 associates directly with full-length and C-terminal fragments of gamma-secretase substratesAn E3 ubiquitin ligase, Synoviolin, is involved in the degradation of immature nicastrin, and regulates the production of amyloid beta-proteinTake five--BACE and the gamma-secretase quartet conduct Alzheimer's amyloid beta-peptide generation.PGC-1α overexpression exacerbates β-amyloid and tau deposition in a transgenic mouse model of Alzheimer's disease.Altered neuronal gene expression in brain regions differentially affected by Alzheimer's disease: a reference data set.Both the sequence and length of the C terminus of PEN-2 are critical for intermolecular interactions and function of presenilin complexes.Assembly, maturation, and trafficking of the gamma-secretase complex in Alzheimer's disease.Specific domains in anterior pharynx-defective 1 determine its intramembrane interactions with nicastrin and presenilin.Increased expression of PS1 is sufficient to elevate the level and activity of γ-secretase in vivo.Phosphorylation of nicastrin by SGK1 leads to its degradation through lysosomal and proteasomal pathways.Evidence that the COOH terminus of human presenilin 1 is located in extracytoplasmic space.Transcriptional regulation of PEN-2, a key component of the gamma-secretase complex, by CREBReduced Alzheimer's disease ß-amyloid deposition in transgenic mice expressing S-palmitoylation-deficient APH1aL and nicastrin.Activation and intrinsic gamma-secretase activity of presenilin 1.And four equals one: presenilin takes the gamma-secretase role by itself.5-lipoxygenase as an endogenous modulator of amyloid β formation in vivo.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.The γ-secretase complex: from structure to function.Transcriptional Regulation of TMP21 by NFAT.Functional and topological analysis of Pen-2, the fourth subunit of the gamma-secretase complex.Pathological and physiological functions of presenilins.Pharmacologic blockade of 5-lipoxygenase improves the amyloidotic phenotype of an Alzheimer's disease transgenic mouse model involvement of γ-secretaseStructure of gamma-secretase and its trimeric pre-activation intermediate by single-particle electron microscopy.Adeno-associated virus-mediated brain delivery of 5-lipoxygenase modulates the AD-like phenotype of APP mice.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.
P2860
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P2860
PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1.
@ast
PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1.
@en
PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1.
@nl
type
label
PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1.
@ast
PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1.
@en
PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1.
@nl
prefLabel
PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1.
@ast
PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1.
@en
PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1.
@nl
P2093
P356
P1476
PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1.
@en
P2093
Benny S Kim
Gopal Thinakaran
Hahn-Jun Lee
Hongqiao Li
Sanjiv Shah
Tae-Wan Kim
Wen-jie Luo
P304
P356
10.1074/JBC.C200648200
P407
P577
2003-01-08T00:00:00Z