Functional analysis of the transmembrane domains of presenilin 1: participation of transmembrane domains 2 and 6 in the formation of initial substrate-binding site of gamma-secretase.
about
Structural biology of presenilin 1 complexesTargeting the γ-/β-secretase interaction reduces β-amyloid generation and ameliorates Alzheimer's disease-related pathogenesisAllosteric regulation of γ-secretase activity by a phenylimidazole-type γ-secretase modulator.The FAM3 superfamily member ILEI ameliorates Alzheimer's disease-like pathology by destabilizing the penultimate amyloid-β precursor.Structural interactions between inhibitor and substrate docking sites give insight into mechanisms of human PS1 complexes.Presenilin transmembrane domain 8 conserved AXXXAXXXG motifs are required for the activity of the γ-secretase complexPhenylpiperidine-type γ-secretase modulators target the transmembrane domain 1 of presenilin 1Cutting in on a secretase pas de deuxThe matricellular protein thrombospondin-1 globally regulates cardiovascular function and responses to stress via CD47.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.Roles of the membrane-reentrant β-hairpin-like loop of RseP protease in selective substrate cleavageSampling the conformational space of the catalytic subunit of human γ-secretaseSubstrate ectodomain is critical for substrate preference and inhibition of γ-secretase.Binding of longer Aβ to transmembrane domain 1 of presenilin 1 impacts on Aβ42 generationStructural biology of presenilins and signal peptide peptidases.Biological function of Presenilin and its role in AD pathogenesisMolecular mechanism of intramembrane proteolysis by γ-secretase.Polar transmembrane-based amino acids in presenilin 1 are involved in endoplasmic reticulum localization, Pen2 protein binding, and γ-secretase complex stabilizationDynamic Nature of presenilin1/γ-Secretase: Implication for Alzheimer's Disease Pathogenesis.Contribution of the γ-secretase subunits to the formation of catalytic pore of presenilin 1 protein.Characterizing the structural ensemble of γ-secretase using a multiscale molecular dynamics approachCompetition between homodimerization and cholesterol binding to the C99 domain of the amyloid precursor protein.Allosteric Modulation of Intact γ-Secretase Structural Dynamics.Structural and Chemical Biology of Presenilin Complexes.Important functional role of residue x of the presenilin GxGD protease active site motif for APP substrate cleavage specificity and substrate selectivity of γ-secretase.
P2860
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P2860
Functional analysis of the transmembrane domains of presenilin 1: participation of transmembrane domains 2 and 6 in the formation of initial substrate-binding site of gamma-secretase.
description
2010 nî lūn-bûn
@nan
2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Functional analysis of the tra ...... nding site of gamma-secretase.
@ast
Functional analysis of the tra ...... nding site of gamma-secretase.
@en
type
label
Functional analysis of the tra ...... nding site of gamma-secretase.
@ast
Functional analysis of the tra ...... nding site of gamma-secretase.
@en
prefLabel
Functional analysis of the tra ...... nding site of gamma-secretase.
@ast
Functional analysis of the tra ...... nding site of gamma-secretase.
@en
P2093
P2860
P356
P1476
Functional analysis of the tra ...... inding site of gamma-secretase
@en
P2093
Aya Tominaga
Image Image Image Image
Image Image Image
Naoto Watanabe
Shizuka Takagi
Takeshi Iwatsubo
P2860
P304
19738-19746
P356
10.1074/JBC.M110.101287
P407
P577
2010-04-23T00:00:00Z