Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein.
about
Substrate requirements for SPPL2b-dependent regulated intramembrane proteolysisViral infection and human disease--insights from minimotifsSynthetic Peptides as Protein Mimicsγ-Secretase inhibitors and modulators.Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domainFamilial Alzheimer’s mutations within APPTM increase Aβ42 production by enhancing accessibility of ε-cleavage siteThe same gamma-secretase accounts for the multiple intramembrane cleavages of APPCharacterization of a presenilin-mediated amyloid precursor protein carboxyl-terminal fragment gamma. Evidence for distinct mechanisms involved in gamma -secretase processing of the APP and Notch1 transmembrane domains.Proteolysis of chimeric beta-amyloid precursor proteins containing the Notch transmembrane domain yields amyloid beta-like peptides.Familial Alzheimer disease-linked presenilin 1 variants enhance production of both Abeta 1-40 and Abeta 1-42 peptides that are only partially sensitive to a potent aspartyl protease transition state inhibitor of "gamma-secretase".Generation of C-terminally truncated amyloid-beta peptides is dependent on gamma-secretase activity.The amyloid-beta (Abeta) peptide pattern in cerebrospinal fluid in Alzheimer's disease: evidence of a novel carboxyterminally elongated Abeta peptide.New Alzheimer amyloid beta responsive genes identified in human neuroblastoma cells by hierarchical clustering.The familial Alzheimer's disease APPV717I mutation alters APP processing and Tau expression in iPSC-derived neurons.Cellular mechanisms of beta-amyloid production and secretionCentral angiotensin II stimulation promotes β amyloid production in Sprague Dawley rats.Beta-amyloid precursor protein mutants respond to gamma-secretase modulatorsThe initial substrate-binding site of gamma-secretase is located on presenilin near the active siteThe intramembrane cleavage site of the amyloid precursor protein depends on the length of its transmembrane domain.Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process.The Role of presenilins in gamma-secretase activity.Secretases as therapeutic targets for the treatment of Alzheimer's disease.Activation and intrinsic gamma-secretase activity of presenilin 1.Differential regulation of amyloid precursor protein/presenilin 1 interaction during Aβ40/42 [corrected] production detected using fusion constructs.Secretases as targets for drug design in Alzheimer's disease.Phorbol 12-myristate 13-acetate-induced release of the colony-stimulating factor 1 receptor cytoplasmic domain into the cytosol involves two separate cleavage eventsEnzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate.{gamma}-Secretase Substrate Concentration Modulates the Abeta42/Abeta40 Ratio: IMPLICATIONS FOR ALZHEIMER DISEASE.Implications of amyloid precursor protein and subsequent beta-amyloid production to the pharmacotherapy of Alzheimer's disease.Aspartic proteases involved in Alzheimer's disease.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 reSubstrate sequence influences γ-secretase modulator activity, role of the transmembrane domain of the amyloid precursor proteinElevated abeta42 in skeletal muscle of Alzheimer disease patients suggests peripheral alterations of AbetaPP metabolism.A notable cleavage: winding up with beta-amyloidSubstrate recruitment of γ-secretase and mechanism of clinical presenilin mutations revealed by photoaffinity mapping.Chemical Biology, Molecular Mechanism and Clinical Perspective of γ-Secretase Modulators in Alzheimer's DiseaseIn search of gamma-secretase: presenilin at the cutting edgeProteolytic cleavage, trafficking, and functions of nuclear receptor tyrosine kinases.Effects of gamma-secretase cleavage-region mutations on APP processing and Abeta formation: interpretation with sequential cleavage and alpha-helical modelResidues at P2-P1 positions of epsilon- and zeta-cleavage sites are important in formation of beta-amyloid peptide.
P2860
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P2860
Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein.
description
1999 nî lūn-bûn
@nan
1999 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մարտին հրատարակված գիտական հոդված
@hy
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
name
Mechanism of the cleavage spec ...... the amyloid precursor protein.
@ast
Mechanism of the cleavage spec ...... the amyloid precursor protein.
@en
type
label
Mechanism of the cleavage spec ...... the amyloid precursor protein.
@ast
Mechanism of the cleavage spec ...... the amyloid precursor protein.
@en
prefLabel
Mechanism of the cleavage spec ...... the amyloid precursor protein.
@ast
Mechanism of the cleavage spec ...... the amyloid precursor protein.
@en
P2093
P2860
P356
P1476
Mechanism of the cleavage spec ...... the amyloid precursor protein.
@en
P2093
C L Masters
K Beyreuther
S F Lichtenthaler
P2860
P304
P356
10.1073/PNAS.96.6.3053
P407
P577
1999-03-01T00:00:00Z