Alternative processing of γ-secretase substrates in common forms of mild cognitive impairment and Alzheimer's disease: evidence for γ-secretase dysfunction.
about
The specific α-neurexin interactor calsyntenin-3 promotes excitatory and inhibitory synapse developmentγ-secretase binding sites in aged and Alzheimer's disease human cerebrum: the choroid plexus as a putative origin of CSF AβLoss of c-Jun N-terminal kinase-interacting protein-1 does not affect axonal transport of the amyloid precursor protein or Aβ production.Mechanism of intramembrane cleavage of alcadeins by γ-secretase.Cytoplasmic fragment of Alcadein α generated by regulated intramembrane proteolysis enhances amyloid β-protein precursor (APP) transport into the late secretory pathway and facilitates APP cleavage.Coordinated increase of γ-secretase reaction products in the plasma of some female Japanese sporadic Alzheimer's disease patients: quantitative analysis of p3-Alcα with a new ELISA system.Multiple γ-secretase product peptides are coordinately increased in concentration in the cerebrospinal fluid of a subpopulation of sporadic Alzheimer's disease subjects.Qualitative changes in human γ-secretase underlie familial Alzheimer's disease.Amyloid plaque pathogenesis in 5XFAD mouse spinal cord: retrograde transneuronal modulation after peripheral nerve injuryDistinct patterns of APP processing in the CNS in autosomal-dominant and sporadic Alzheimer diseaseSubstrate ectodomain is critical for substrate preference and inhibition of γ-secretase.Stabilization of intracellular trafficking and metabolism of amyloid β-protein precursor and Alcadein β by apolipoprotein E.Processing of the platelet amyloid precursor protein in the mild cognitive impairment (MCI).Complexity and Selectivity of γ-Secretase Cleavage on Multiple Substrates: Consequences in Alzheimer's Disease and Cancer.Phosphorylation of multiple sites within an acidic region of Alcadein α is required for kinesin-1 association and Golgi exit of Alcadein α cargo.Trafficking in Alzheimer's Disease: Modulation of APP Transport and Processing by the Transmembrane Proteins LRP1, SorLA, SorCS1c, Sortilin, and Calsyntenin.Age-related modulation of γ-secretase activity in non-human primate brains.
P2860
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P2860
Alternative processing of γ-secretase substrates in common forms of mild cognitive impairment and Alzheimer's disease: evidence for γ-secretase dysfunction.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Alternative processing of γ-se ...... e for γ-secretase dysfunction.
@ast
Alternative processing of γ-se ...... e for γ-secretase dysfunction.
@en
type
label
Alternative processing of γ-se ...... e for γ-secretase dysfunction.
@ast
Alternative processing of γ-se ...... e for γ-secretase dysfunction.
@en
prefLabel
Alternative processing of γ-se ...... e for γ-secretase dysfunction.
@ast
Alternative processing of γ-se ...... e for γ-secretase dysfunction.
@en
P2093
P2860
P50
P356
P1433
P1476
Alternative processing of γ-se ...... e for γ-secretase dysfunction.
@en
P2093
Allan Levey
Elaine Peskind
Hiroyasu Akatsu
Kathryn A Chung
Katsuya Urakami
Kazuo Yamamoto
Masahiko Araseki
Masahiro Maeda
Masaki Nishimura
Miyako Taniguchi
P2860
P304
P356
10.1002/ANA.22343
P50
P577
2011-06-01T00:00:00Z