Gamma-secretase inhibition reduces spine density in vivo via an amyloid precursor protein-dependent pathway. - Wikidata - awgldk - TriplyDB

Gamma-secretase inhibition reduces spine density in vivo via an amyloid precursor protein-dependent pathway.

Gamma-secretase inhibition reduces spine density in vivo via an amyloid precursor protein-dependent pathway.

http://www.wikidata.org/entity/Q53303993

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In vivo imaging reveals sigmoidal growth kinetic of β-amyloid plaques.Role of presenilin 1 in structural plasticity of cortical dendritic spines in vivo Multiple events lead to dendritic spine loss in triple transgenic Alzheimer's disease mice A γ-secretase inhibitor, but not a γ-secretase modulator, induced defects in BDNF axonal trafficking and signaling: evidence for a role for APP Amyloid precursor protein-mediated endocytic pathway disruption induces axonal dysfunction and neurodegeneration Analyzing dendritic spine pathology in Alzheimer's disease: problems and opportunities Amyloid precursor protein (APP) regulates synaptic structure and function Allosteric modulation of PS1/gamma-secretase conformation correlates with amyloid beta(42/40) ratio.Genetic analysis reveals that amyloid precursor protein and death receptor 6 function in the same pathway to control axonal pruning independent of β-secretase.Comparative analysis of single and combined APP/APLP knockouts reveals reduced spine density in APP-KO mice that is prevented by APPsα expression.Group II metabotropic glutamate receptor stimulation triggers production and release of Alzheimer's amyloid(beta)42 from isolated intact nerve terminals Meeting at the crossroads: common mechanisms in Fragile X and Down syndrome Longitudinal in vivo two-photon fluorescence imaging.Modeling presenilin-dependent familial Alzheimer's disease: emphasis on presenilin substrate-mediated signaling and synaptic function.Deletion of the amyloid precursor-like protein 2 (APLP2) does not affect hippocampal neuron morphology or function.The FAM3 superfamily member ILEI ameliorates Alzheimer's disease-like pathology by destabilizing the penultimate amyloid-β precursor.N-{N-[2-(3,5-Difluorophenyl)acetyl]-(S)-alanyl}-(S)-phenylglycine tert-butyl ester (DAPT): an inhibitor of γ-secretase, revealing fine electronic and hydrogen-bonding features.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.In vivo multiphoton imaging reveals gradual growth of newborn amyloid plaques over weeks.Multi-target action of the novel anti-Alzheimer compound CHF5074: in vivo study of long term treatment in Tg2576 mice.Experience-dependent structural plasticity in the cortex.Intraneuronal beta-amyloid accumulation and synapse pathology in Alzheimer's disease.The crystal structure of DR6 in complex with the amyloid precursor protein provides insight into death receptor activation.Cognitive performance and cerebrospinal fluid biomarkers of neurodegeneration: a study of patients with bipolar disorder and healthy controls.Amyloid-PET predicts inhibition of de novo plaque formation upon chronic γ-secretase modulator treatment New pathway links γ-secretase to inflammation and memory while sparing notch.Transgenic APP expression during postnatal development causes persistent locomotor hyperactivity in the adult.Amyloid plaque formation precedes dendritic spine loss.Distinct patterns of APP processing in the CNS in autosomal-dominant and sporadic Alzheimer disease Intraneuronal aggregation of the β-CTF fragment of APP (C99) induces Aβ-independent lysosomal-autophagic pathology.Controlled cortical impact results in an extensive loss of dendritic spines that is not mediated by injury-induced amyloid-beta accumulation.Can BACE1 inhibition mitigate early axonal pathology in neurological diseases?An amyloid-notch hypothesis for Alzheimer's disease.The upside of APP at synapses.Therapeutic intervention for Alzheimer's disease with γ-secretase inhibitors: still a viable option?The complex world of oligodendroglial differentiation inhibitors.Biology and pathophysiology of the amyloid precursor protein.APP physiological and pathophysiological functions: insights from animal models.Presenilins in synaptic function and disease.Functions of the APP gene family in the nervous system: insights from mouse models.

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P2860

Gamma-secretase inhibition reduces spine density in vivo via an amyloid precursor protein-dependent pathway.

http://www.wikidata.org/entity/Q53303993

description

2009 nî lūn-bûn

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2009年学术文章

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Gamma-secretase inhibition red ...... sor protein-dependent pathway.

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Gamma-secretase inhibition red ...... sor protein-dependent pathway.

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Gamma-secretase inhibition red ...... sor protein-dependent pathway.

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Gamma-secretase inhibition red ...... sor protein-dependent pathway.

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Gamma-secretase inhibition red ...... sor protein-dependent pathway.

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Gamma-secretase inhibition red ...... sor protein-dependent pathway.

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JNEUROSCI.2288-09.2009

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Christian Haass

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Christian K E Jung

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Christiane Volbracht

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Gerda Mitteregger

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Harald Steiner

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10405-10409

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scholarly article

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10.1523/JNEUROSCI.2288-09.2009

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