A loss of function mutation of presenilin-2 interferes with amyloid beta-peptide production and notch signaling.
about
Presenilin 2 interacts with sorcin, a modulator of the ryanodine receptorAutosomal recessive hypercholesterolemia protein interacts with and regulates the cell surface level of Alzheimer's amyloid beta precursor proteinPresenilin and nicastrin regulate each other and determine amyloid beta-peptide production via complex formationPresenilins are essential for regulating neurotransmitter releaseAmyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid raftsCellular mechanisms of γ-secretase substrate selection, processing and toxicityToward the structure of presenilin/γ-secretase and presenilin homologsLysosome and calcium dysregulation in Alzheimer's disease: partners in crimeComplex regulation of γ-secretase: from obligatory to modulatory subunitsRegulation of transcription of the human presenilin-1 gene by ets transcription factors and the p53 protooncogeneAssembly, trafficking and function of gamma-secretasePresenilin-1, nicastrin, amyloid precursor protein, and gamma-secretase activity are co-localized in the lysosomal membranePartial loss of presenilin impairs age-dependent neuronal survival in the cerebral cortexPresenilin 1 and presenilin 2 have differential effects on the stability and maturation of nicastrin in Mammalian brainProteolysis of chimeric beta-amyloid precursor proteins containing the Notch transmembrane domain yields amyloid beta-like peptides.An in vivo assay for the identification of target proteases which cleave membrane-associated substrates.Direct visualization of the gamma secretase-generated carboxyl-terminal domain of the amyloid precursor protein: association with Fe65 and translocation to the nucleus.Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein (APP).A gamma-secretase inhibitor blocks Notch signaling in vivo and causes a severe neurogenic phenotype in zebrafishPresenilins regulate synaptic plasticity and mitochondrial calcium homeostasis in the hippocampal mossy fiber pathwayDifferential contribution of the three Aph1 genes to gamma-secretase activity in vivoNotch signaling is required for the formation of mesangial cells from a stromal mesenchyme precursor during kidney development.Dissociated phenotypes in presenilin transgenic mice define functionally distinct gamma-secretases.Cell surface presenilin-1 participates in the gamma-secretase-like proteolysis of Notch.Presenilin conditional double knockout mice exhibit decreases in drebrin a at hippocampal CA1 synapsesPresenilin-dependent gamma-secretase activity modulates thymocyte development.Activity-dependent isolation of the presenilin- gamma -secretase complex reveals nicastrin and a gamma substrate.Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Abeta 42 productionRegulation of APP cleavage by alpha-, beta- and gamma-secretases.Modeling presenilin-dependent familial Alzheimer's disease: emphasis on presenilin substrate-mediated signaling and synaptic function.The Role of presenilins in gamma-secretase activity.Presenilin and gamma-secretase: structure meets function.Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated protein-1 proteins bind to AbetaPP and modulate its processing in an isoform-specific manner.Structure, mechanism and inhibition of gamma-secretase and presenilin-like proteasesSecretases as targets for drug design in Alzheimer's disease.Rapamycin promotes beta-amyloid production via ADAM-10 inhibition.Physiologic and pathologic events mediated by intramembranous and juxtamembranous proteolysis.Presenilin-1 knockin mice reveal loss-of-function mechanism for familial Alzheimer's disease.Presenilin complexes with the C-terminal fragments of amyloid precursor protein at the sites of amyloid beta-protein generation.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.
P2860
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P2860
A loss of function mutation of presenilin-2 interferes with amyloid beta-peptide production and notch signaling.
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
A loss of function mutation of ...... roduction and notch signaling.
@en
type
label
A loss of function mutation of ...... roduction and notch signaling.
@en
prefLabel
A loss of function mutation of ...... roduction and notch signaling.
@en
P2093
P356
P1476
A loss of function mutation of ...... roduction and notch signaling.
@en
P2093
Baumeister R
Fechteler K
Iwatsubo T
P304
28669-28673
P356
10.1074/JBC.274.40.28669
P407
P577
1999-10-01T00:00:00Z