Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain. - Wikidata - awgldk - TriplyDB

Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain.

Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain.

http://www.wikidata.org/entity/Q36320330

about

The CRMP family of proteins and their role in Sema3A signaling Glycogen synthase kinase-3 (GSK3): inflammation, diseases, and therapeutics The Beta-amyloid protein of Alzheimer's disease: communication breakdown by modifying the neuronal cytoskeleton The multifaceted nature of amyloid precursor protein and its proteolytic fragments: friends and foes APP intracellular domain impairs adult neurogenesis in transgenic mice by inducing neuroinflammation Tau Protein Mediates APP Intracellular Domain (AICD)-Induced Alzheimer's-Like Pathological Features in Mice Proteolytic processing of Alzheimer's β-amyloid precursor protein The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer's Disease Transgenic expression of the amyloid-beta precursor protein-intracellular domain does not induce Alzheimer's Disease-like traits in vivo Presenilin/gamma-secretase-dependent processing of beta-amyloid precursor protein regulates EGF receptor expression Role of X11 and ubiquilin as in vivo regulators of the amyloid precursor protein in Drosophila Abnormal neuronal networks and seizure susceptibility in mice overexpressing the APP intracellular domain.GSK3beta: role in therapeutic landscape and development of modulators.Alterations of brain and cerebellar proteomes linked to Aβ and tau pathology in a female triple-transgenic murine model of Alzheimer's disease.Comparative transcriptome profiling of amyloid precursor protein family members in the adult cortex Identification and characterization of a neuronal enriched novel transcript encoding the previously described p60Fe65 isoform.Tip60 HAT activity mediates APP induced lethality and apoptotic cell death in the CNS of a Drosophila Alzheimer's disease model.Model Hirano bodies protect against tau-independent and tau-dependent cell death initiated by the amyloid precursor protein intracellular domain.The β-secretase-derived C-terminal fragment of βAPP, C99, but not Aβ, is a key contributor to early intraneuronal lesions in triple-transgenic mouse hippocampus.Epigenetic control of learning and memory in Drosophila by Tip60 HAT action.Epigenetic induction of EGR-1 expression by the amyloid precursor protein during exposure to novelty.Epigenetic regulations of immediate early genes expression involved in memory formation by the amyloid precursor protein of Alzheimer disease Manipulations of amyloid precursor protein cleavage disrupt the circadian clock in aging Drosophila.The roles of amyloid precursor protein (APP) in neurogenesis: Implications to pathogenesis and therapy of Alzheimer disease.Modulation of gene expression and cytoskeletal dynamics by the amyloid precursor protein intracellular domain (AICD)Selectively silencing GSK-3 isoforms reduces plaques and tangles in mouse models of Alzheimer's disease.Amyloid Precursor Protein (APP) Metabolites APP Intracellular Fragment (AICD), Aβ42, and Tau in Nuclear Roles.GSK3β Interactions with Amyloid Genes: An Autopsy Verification and Extension Oxidative stress-dependent phosphorylation activates ZNRF1 to induce neuronal/axonal degeneration Appoptosin is a novel pro-apoptotic protein and mediates cell death in neurodegeneration.APP Receptor? To Be or Not To Be.Evidence that the Amyloid beta Precursor Protein-intracellular domain lowers the stress threshold of neurons and has a "regulated" transcriptional role Reassessing the amyloid cascade hypothesis of Alzheimer's disease Involvement of WAVE accumulation in Abeta/APP pathology-dependent tangle modification in Alzheimer's disease.The interactome of the amyloid beta precursor protein family members is shaped by phosphorylation of their intracellular domains.Alzheimer's disease-like pathological features in transgenic mice expressing the APP intracellular domain.Interactions between GSK3β and amyloid genes explain variance in amyloid burden.Neprilysin and Aβ Clearance: Impact of the APP Intracellular Domain in NEP Regulation and Implications in Alzheimer's Disease Pharmacological targeting of the β-amyloid precursor protein intracellular domain.Amyloid-independent mechanisms in Alzheimer's disease pathogenesis

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P2860

Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain.

http://www.wikidata.org/entity/Q36320330

description

2005 nî lūn-bûn

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2005年學術文章

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Activation of GSK-3 and phosph ...... sing APP intracellular domain.

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Activation of GSK-3 and phosph ...... sing APP intracellular domain.

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Journal of Cell Biology

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Activation of GSK-3 and phosph ...... sing APP intracellular domain.

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Kathleen A Ryan

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Sanjay W Pimplikar

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P2860

PAT1, a microtubule-interacting protein, recognizes the basolateral sorting signal of amyloid precursor protein

The gamma -secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus

The amyloid precursor protein and its regulatory protein, FE65, in growth cones and synapses in vitro and in vivo

Binding of F-spondin to amyloid-beta precursor protein: a candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage

The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein

Neurofibrillary tangle-associated collapsin response mediator protein-2 (CRMP-2) is highly phosphorylated on Thr-509, Ser-518, and Ser-522

Proteolytic processing and cell biological functions of the amyloid precursor protein

Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans

A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60

CRMP-2 binds to tubulin heterodimers to promote microtubule assembly

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10.1083/JCB.200505078

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phosphorylation

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