Equimolar production of amyloid beta-protein and amyloid precursor protein intracellular domain from beta-carboxyl-terminal fragment by gamma-secretase.
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Neurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratioDecreased CALM expression reduces Aβ42 to total Aβ ratio through clathrin-mediated endocytosis of γ-secretaseWhen loss is gain: reduced presenilin proteolytic function leads to increased Abeta42/Abeta40. Talking Point on the role of presenilin mutations in Alzheimer diseaseLoss-of-function presenilin mutations in Alzheimer disease. Talking Point on the role of presenilin mutations in Alzheimer diseaseThe amyloid precursor protein: beyond amyloidModulators of γ-secretase activity can facilitate the toxic side-effects and pathogenesis of Alzheimer's diseaseAllosteric regulation of rhomboid intramembrane proteolysisChanged membrane integration and catalytic site conformation are two mechanisms behind the increased Aβ42/Aβ40 ratio by presenilin 1 familial Alzheimer-linked mutations.Aberrant amyloid precursor protein (APP) processing in hereditary forms of Alzheimer disease caused by APP familial Alzheimer disease mutations can be rescued by mutations in the APP GxxxG motif.The 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.The secretases: enzymes with therapeutic potential in Alzheimer disease.Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process.Modulation of γ-secretase activity by multiple enzyme-substrate interactions: implications in pathogenesis of Alzheimer's diseaseMutation analysis of the presenilin 1 N-terminal domain reveals a broad spectrum of gamma-secretase activity toward amyloid precursor protein and other substrates.Alzheimer presenilin-1 mutations dramatically reduce trimming of long amyloid β-peptides (Aβ) by γ-secretase to increase 42-to-40-residue Aβ.The pathogenic aβ43 is enriched in familial and sporadic Alzheimer diseaseA synthetic antibody fragment targeting nicastrin affects assembly and trafficking of γ-secretase.Functional and topological analysis of Pen-2, the fourth subunit of the gamma-secretase complex.Dissociation between the processivity and total activity of γ-secretase: implications for the mechanism of Alzheimer's disease-causing presenilin mutations.Lysine 624 of the amyloid precursor protein (APP) is a critical determinant of amyloid β peptide length: support for a sequential model of γ-secretase intramembrane proteolysis and regulation by the amyloid β precursor protein (APP) juxtamembrane rePhenylpiperidine-type γ-secretase modulators target the transmembrane domain 1 of presenilin 1An NSAID-like compound, FT-9, preferentially inhibits gamma-secretase cleavage of the amyloid precursor protein compared to its effect on amyloid precursor-like protein 1.γ-Secretase Modulators and APH1 Isoforms Modulate γ-Secretase Cleavage but Not Position of ε-Cleavage of the Amyloid Precursor Protein (APP).The mechanism of γ-Secretase dysfunction in familial Alzheimer disease.Substrate recruitment of γ-secretase and mechanism of clinical presenilin mutations revealed by photoaffinity mapping.Altered γ-secretase activity in mild cognitive impairment and Alzheimer's disease.Chemical Biology, Molecular Mechanism and Clinical Perspective of γ-Secretase Modulators in Alzheimer's DiseaseAmyloid Precursor Protein (APP) Metabolites APP Intracellular Fragment (AICD), Aβ42, and Tau in Nuclear Roles.The A673T mutation in the amyloid precursor protein reduces the production of β-amyloid protein from its β-carboxyl terminal fragment in cellsSecond generation γ-secretase modulators exhibit different modulation of Notch β and Aβ production.β-arrestin1 regulates γ-secretase complex assembly and modulates amyloid-β pathology.Effect of Presenilin Mutations on APP Cleavage; Insights into the Pathogenesis of FADEfficacy of SPI-1865, a novel gamma-secretase modulator, in multiple rodent models.A TAG on to the neurogenic functions of APPA helix-to-coil transition at the epsilon-cut site in the transmembrane dimer of the amyloid precursor protein is required for proteolysis.Mutant presenilin 1 increases the expression and activity of BACE1Molecular genetics of Alzheimer's disease: an update.Substrate ectodomain is critical for substrate preference and inhibition of γ-secretase.Structure and mechanism of intramembrane protease.Gamma-secretase catalyzes sequential cleavages of the AbetaPP transmembrane domain.
P2860
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P2860
Equimolar production of amyloid beta-protein and amyloid precursor protein intracellular domain from beta-carboxyl-terminal fragment by gamma-secretase.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh-hant
name
Equimolar production of amyloi ...... l fragment by gamma-secretase.
@en
Equimolar production of amyloi ...... l fragment by gamma-secretase.
@nl
type
label
Equimolar production of amyloi ...... l fragment by gamma-secretase.
@en
Equimolar production of amyloi ...... l fragment by gamma-secretase.
@nl
prefLabel
Equimolar production of amyloi ...... l fragment by gamma-secretase.
@en
Equimolar production of amyloi ...... l fragment by gamma-secretase.
@nl
P2093
P2860
P356
P1476
Equimolar production of amyloi ...... l fragment by gamma-secretase.
@en
P2093
Mako Takami
Naoshi Dohmae
Nobuto Kakuda
Satoko Osawa
Satoru Funamoto
Sousuke Yagishita
Yasuo Ihara
P2860
P304
14776-14786
P356
10.1074/JBC.M513453200
P407
P577
2006-04-04T00:00:00Z