Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis.
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Ubiquilin regulates presenilin endoproteolysis and modulates gamma-secretase components, Pen-2 and nicastrinPen-2 is incorporated into the gamma-secretase complex through binding to transmembrane domain 4 of presenilin 1Presenilin-dependent gamma-secretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of NotchThe large hydrophilic loop of presenilin 1 is important for regulating gamma-secretase complex assembly and dictating the amyloid beta peptide (Abeta) Profile without affecting Notch processing.Presenilin/γ-secretase regulates neurexin processing at synapsesPresenilin-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.The multiple paradoxes of presenilins.Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases.Activation and intrinsic gamma-secretase activity of presenilin 1.Pathological and physiological functions of presenilins.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.Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease.Intramembrane proteolysis by gamma-secretase.Involvement of presenilin holoprotein upregulation in calcium dyshomeostasis of Alzheimer's disease.Contribution of the γ-secretase subunits to the formation of catalytic pore of presenilin 1 protein.Presenilins mediate a dual intramembranous gamma-secretase cleavage of Notch-1.Random mutagenesis of presenilin-1 identifies novel mutants exclusively generating long amyloid beta-peptides.Functional implications of the presenilin dimerization: reconstitution of gamma-secretase activity by assembly of a catalytic site at the dimer interface of two catalytically inactive presenilins.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.Complex N-linked glycosylated nicastrin associates with active gamma-secretase and undergoes tight cellular regulation.The first proline of PALP motif at the C terminus of presenilins is obligatory for stabilization, complex formation, and gamma-secretase activities of presenilins.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.Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane.Functional domains in presenilin 1: the Tyr-288 residue controls gamma-secretase activity and endoproteolysis.Identification of gamma-secretase inhibitor potency determinants on presenilin.SorLA signaling by regulated intramembrane proteolysis.Influence of solubilization and AD-mutations on stability and structure of human presenilins.Insensitivity to Abeta42-lowering nonsteroidal anti-inflammatory drugs and gamma-secretase inhibitors is common among aggressive presenilin-1 mutations.The nonconserved hydrophilic loop domain of presenilin (PS) is not required for PS endoproteolysis or enhanced abeta 42 production mediated by familial early onset Alzheimer's disease-linked PS variants.
P2860
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P2860
Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Amyloidogenic function of the ...... he absence of endoproteolysis.
@en
type
label
Amyloidogenic function of the ...... he absence of endoproteolysis.
@en
prefLabel
Amyloidogenic function of the ...... he absence of endoproteolysis.
@en
P2093
P356
P1433
P1476
Amyloidogenic function of the ...... he absence of endoproteolysis.
@en
P2093
Jacobsen H
Loetscher H
P304
14600-14605
P356
10.1021/BI9914210
P407
P577
1999-11-01T00:00:00Z