gamma-Secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of beta-carboxyl terminal fragment.
about
Gamma-secretase activating protein is a therapeutic target for Alzheimer's diseaseA comparative analysis of the aggregation behavior of amyloid-β peptide variantsThe amyloid hypothesis of Alzheimer's disease at 25 yearsNeuronal response in Alzheimer's and Parkinson's disease: the effect of toxic proteins on intracellular pathwaysTransient dynamics of Aβ contribute to toxicity in Alzheimer's diseaseγ-Secretase inhibitors and modulators.Toward the structure of presenilin/γ-secretase and presenilin homologsAxonal transport of APP and the spatial regulation of APP cleavage and function in neuronal cellsStructural biology of presenilin 1 complexesThe Amyloid Precursor Protein Has a Flexible Transmembrane Domain and Binds CholesterolFamilial Alzheimer’s mutations within APPTM increase Aβ42 production by enhancing accessibility of ε-cleavage siteCurrent and future implications of basic and translational research on amyloid-β peptide production and removal pathwaysTrafficking and proteolytic processing of APPModulators of γ-secretase activity can facilitate the toxic side-effects and pathogenesis of Alzheimer's diseaseDifferential Inhibition of Signal Peptide Peptidase Family Members by Established γ-Secretase InhibitorsAftins increase amyloid-β42, lower amyloid-β38, and do not alter amyloid-β40 extracellular production in vitro: toward a chemical model of Alzheimer's disease?Changed 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.Beta-amyloid precursor protein mutants respond to gamma-secretase modulatorsIdentification and Preclinical Pharmacology of the γ-Secretase Modulator BMS-869780.Allosteric regulation of γ-secretase activity by a phenylimidazole-type γ-secretase modulator.Amyloid beta 42 peptide (Abeta42)-lowering compounds directly bind to Abeta and interfere with amyloid precursor protein (APP) transmembrane dimerization.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 diseaseLowering of amyloid beta peptide production with a small molecule inhibitor of amyloid-β precursor protein dimerizationCharacterization of intermediate steps in amyloid beta (Aβ) production under near-native conditions.And four equals one: presenilin takes the gamma-secretase role by itself.Alzheimer presenilin-1 mutations dramatically reduce trimming of long amyloid β-peptides (Aβ) by γ-secretase to increase 42-to-40-residue Aβ.Differential regulation of amyloid precursor protein/presenilin 1 interaction during Aβ40/42 [corrected] production detected using fusion constructs.The pathogenic aβ43 is enriched in familial and sporadic Alzheimer diseaseThe γ-secretase complex: from structure to function.Mechanism of intramembrane cleavage of alcadeins by γ-secretase.Targets for AD treatment: conflicting messages from γ-secretase inhibitorsOCIAD2 activates γ-secretase to enhance amyloid β production by interacting with nicastrin.γ-Secretase processing and effects of γ-secretase inhibitors and modulators on long Aβ peptides in cells.Presenilin transmembrane domain 8 conserved AXXXAXXXG motifs are required for the activity of the γ-secretase complexEffect of potent γ-secretase modulator in human neurons derived from multiple presenilin 1-induced pluripotent stem cell mutant carriers.Independent relationship between amyloid precursor protein (APP) dimerization and γ-secretase processivity.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 re
P2860
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P2860
gamma-Secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of beta-carboxyl terminal fragment.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh-hant
name
gamma-Secretase: successive tr ...... ta-carboxyl terminal fragment.
@en
gamma-Secretase: successive tr ...... ta-carboxyl terminal fragment.
@nl
type
label
gamma-Secretase: successive tr ...... ta-carboxyl terminal fragment.
@en
gamma-Secretase: successive tr ...... ta-carboxyl terminal fragment.
@nl
prefLabel
gamma-Secretase: successive tr ...... ta-carboxyl terminal fragment.
@en
gamma-Secretase: successive tr ...... ta-carboxyl terminal fragment.
@nl
P2093
P1476
gamma-Secretase: successive tr ...... ta-carboxyl terminal fragment.
@en
P2093
Maho Morishima-Kawashima
Mako Takami
Satoru Funamoto
Seiko Ishihara
Yasuo Ihara
Yoshihisa Sano
Yu Nagashima
P304
13042-13052
P356
10.1523/JNEUROSCI.2362-09.2009
P407
P577
2009-10-01T00:00:00Z