The biological and pathological function of the presenilin-1 Deltaexon 9 mutation is independent of its defect to undergo proteolytic processing.
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Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulationSyntaxin 5 interacts with presenilin holoproteins, but not with their N- or C-terminal fragments, and affects beta-amyloid peptide productionPresenilin and nicastrin regulate each other and determine amyloid beta-peptide production via complex formationLoss-of-function presenilin mutations in Alzheimer disease. Talking Point on the role of presenilin mutations in Alzheimer diseaseAssembly, trafficking and function of gamma-secretaseTailoring of membrane proteins by alternative splicing of pre-mRNA.Alzheimer's disease-linked mutations in presenilin-1 result in a drastic loss of activity in purified γ-secretase complexes.Presenilin/γ-secretase regulates neurexin processing at synapsesGenetics and biology of Alzheimer's disease and frontotemporal lobar degenerationA presenilin-1 mutation identified in familial Alzheimer disease with cotton wool plaques causes a nearly complete loss of gamma-secretase activityPresenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Abeta 42 productionThe Role of presenilins in gamma-secretase activity.Presenilin and gamma-secretase: structure meets function.Activation and intrinsic gamma-secretase activity of presenilin 1.Structure of gamma-secretase and its trimeric pre-activation intermediate by single-particle electron microscopy.The presenilin hypothesis of Alzheimer's disease: evidence for a loss-of-function pathogenic mechanism.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.Separation of presenilin function in amyloid beta-peptide generation and endoproteolysis of Notch.Presenilin function and gamma-secretase activity.Murine Aβ over-production produces diffuse and compact Alzheimer-type amyloid deposits.A presenilin dimer at the core of the gamma-secretase enzyme: insights from parallel analysis of Notch 1 and APP proteolysisDeducing the transmembrane domain organization of presenilin-1 in gamma-secretase by cysteine disulfide cross-linking.Molecular genetics of Alzheimer's disease: an update.Biological function of Presenilin and its role in AD pathogenesisEvidence For and Against a Pathogenic Role of Reduced γ-Secretase Activity in Familial Alzheimer's Disease.Caspase cleaved presenilin-1 is part of active gamma-secretase complexes.Secretion of the Notch-1 Abeta-like peptide during Notch signaling.Presenilin-1 D257A and D385A mutants fail to cleave Notch in their endoproteolyzed forms, but only presenilin-1 D385A mutant can restore its gamma-secretase activity with the compensatory overexpression of normal C-terminal fragment.Baculoviruses expressing the human familial Alzheimer's disease presenilin 1 mutation lacking exon 9 increase levels of an amyloid beta-like protein in Sf9 cells.Identification of a beta-secretase activity, which truncates amyloid beta-peptide after its presenilin-dependent generation.PEN-2 is an integral component of the gamma-secretase complex required for coordinated expression of presenilin and nicastrin.A pathogenic presenilin-1 deletion causes abberrant Abeta 42 production in the absence of congophilic amyloid plaques.A loss of function mutant of the presenilin homologue SEL-12 undergoes aberrant endoproteolysis in Caenorhabditis elegans and increases abeta 42 generation in human cells.Generation and deposition of Aβ43 by the virtually inactive presenilin-1 L435F mutant contradicts the presenilin loss-of-function hypothesis of Alzheimer's disease.Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane.Selecting cells with different Alzheimer's disease gamma-secretase activity using FACS. Differential effect on presenilin exon 9 gamma- and epsilon-cleavage.Functional domains in presenilin 1: the Tyr-288 residue controls gamma-secretase activity and endoproteolysis.Insensitivity to Abeta42-lowering nonsteroidal anti-inflammatory drugs and gamma-secretase inhibitors is common among aggressive presenilin-1 mutations.Mapping the Binding Site of BMS-708163 on γ-Secretase with Cleavable Photoprobes.De novo deleterious genetic variations target a biological network centered on Aβ peptide in early-onset Alzheimer disease.
P2860
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P2860
The biological and pathological function of the presenilin-1 Deltaexon 9 mutation is independent of its defect to undergo proteolytic processing.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
The biological and pathologica ...... ndergo proteolytic processing.
@en
type
label
The biological and pathologica ...... ndergo proteolytic processing.
@en
prefLabel
The biological and pathologica ...... ndergo proteolytic processing.
@en
P2093
P2860
P356
P1476
The biological and pathologica ...... ndergo proteolytic processing.
@en
P2093
Baumeister R
P2860
P304
P356
10.1074/JBC.274.12.7615
P407
P577
1999-03-01T00:00:00Z