What the evolution of the amyloid protein precursor supergene family tells us about its function.
about
Origins of amyloid-βHomo- and heterodimerization of APP family members promotes intercellular adhesion.The amyloid precursor protein: beyond amyloidAnalysis of Amyloid Precursor Protein Function in Drosophila melanogasterMulti-Target Directed Donepezil-Like Ligands for Alzheimer's DiseasePrimate aging in the mammalian scheme: the puzzle of extreme variation in brain agingGenetic heterogeneity in Alzheimer disease and implications for treatment strategiesQuantification of copper binding to amyloid precursor protein domain 2 and its Caenorhabditis elegans ortholog. Implications for biological functionAPP processing in Alzheimer's diseaseGenetic variants associated with neurodegenerative Alzheimer disease in natural modelsProteolytic processing of Alzheimer's β-amyloid precursor proteinEssential roles for the FE65 amyloid precursor protein-interacting proteins in brain developmentInteraction of Alzheimer's beta -amyloid precursor family proteins with scaffold proteins of the JNK signaling cascadeHow to innervate a simple gut: familiar themes and unique aspects in the formation of the insect enteric nervous system.Characterization of the beta amyloid precursor protein-like gene in the central nervous system of the crab Chasmagnathus. Expression during memory consolidationIdentification and comparative analysis of differentially expressed proteins in rat striatum following 6-hydroxydopamine lesions of the nigrostriatal pathway: up-regulation of amyloid precursor-like protein 2 expression.Pharmacological analysis of Drosophila melanogaster gamma-secretase with respect to differential proteolysis of Notch and APP.beta-Secretase cleavage is not required for generation of the intracellular C-terminal domain of the amyloid precursor family of proteins.The insect homologue of the amyloid precursor protein interacts with the heterotrimeric G protein Go alpha in an identified population of migratory neurons.Copper binding to the Alzheimer's disease amyloid precursor proteinThe beta-amyloid precursor protein (APP) and Alzheimer's disease: does the tail wag the dog?Deletion of the amyloid precursor-like protein 2 (APLP2) does not affect hippocampal neuron morphology or function.PAT1a modulates intracellular transport and processing of amyloid precursor protein (APP), APLP1, and APLP2.Turnover of amyloid precursor protein family members determines their nuclear signaling capabilityImplications of amyloid precursor protein and subsequent beta-amyloid production to the pharmacotherapy of Alzheimer's disease.Impact of cerebrospinal fluid shunting for idiopathic normal pressure hydrocephalus on the amyloid cascade.Neurotoxic effects induced by the Drosophila amyloid-beta peptide suggest a conserved toxic function.APL-1, a Caenorhabditis elegans protein related to the human beta-amyloid precursor protein, is essential for viability.Monocyte-to-macrophage differentiation: synthesis and secretion of a complex extracellular matrix.Lineage-specific and ubiquitous biological roles of the mammalian transcription factor LSFAlzheimer Aβ disrupts the mitotic spindle and directly inhibits mitotic microtubule motors.The 28-amino acid form of an APLP1-derived Abeta-like peptide is a surrogate marker for Abeta42 production in the central nervous system.Invertebrate models of Alzheimer's disease.Analysis by a highly sensitive split luciferase assay of the regions involved in APP dimerization and its impact on processing.ASS234, As a New Multi-Target Directed Propargylamine for Alzheimer's Disease Therapy.Effects of glucose and insulin on secretion of amyloid-β by human adipose tissue cellsAn amyloid-notch hypothesis for Alzheimer's disease.γ-Secretase-regulated mechanisms similar to notch signaling may play a role in signaling events, including APP signaling, which leads to Alzheimer's disease.Analysis of amyloid precursor protein function in Drosophila melanogaster.Proteomic analysis of the presynaptic active zone.
P2860
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P2860
What the evolution of the amyloid protein precursor supergene family tells us about its function.
description
2000 nî lūn-bûn
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2000 թուականի Մարտին հրատարակուած գիտական յօդուած
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2000 թվականի մարտին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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name
What the evolution of the amyl ...... y tells us about its function.
@ast
What the evolution of the amyl ...... y tells us about its function.
@en
type
label
What the evolution of the amyl ...... y tells us about its function.
@ast
What the evolution of the amyl ...... y tells us about its function.
@en
prefLabel
What the evolution of the amyl ...... y tells us about its function.
@ast
What the evolution of the amyl ...... y tells us about its function.
@en
P2093
P1476
What the evolution of the amyl ...... y tells us about its function.
@en
P2093
Beyreuther K
Coulson EJ
Masters CL
P304
P356
10.1016/S0197-0186(99)00125-4
P577
2000-03-01T00:00:00Z