Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain. - Wikidata - awgldk - TriplyDB

Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain.

Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain.

http://www.wikidata.org/entity/Q34868772

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A phase Ib multiple ascending dose study of the safety, tolerability, and central nervous system availability of AZD0530 (saracatinib) in Alzheimer's disease Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer aβ oligomer bound to cellular prion protein Synaptic Cell Adhesion Molecules in Alzheimer's Disease Amyloid-β induced signaling by cellular prion protein and Fyn kinase in Alzheimer disease Hijacking PrP(c)-dependent signal transduction: when prions impair Aβ clearance Insoluble cellular prion protein and its association with prion and Alzheimer diseases Alzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Therapeutic molecules and endogenous ligands regulate the interaction between brain cellular prion protein (PrPC) and metabotropic glutamate receptor 5 (mGluR5).Exosomes neutralize synaptic-plasticity-disrupting activity of Aβ assemblies in vivo.Fyn inhibition rescues established memory and synapse loss in Alzheimer mice.Synthetic Aβ peptides acquire prion-like properties in the brain.Characterization of spontaneously generated prion-like conformers in cultured cells.Cellular prion protein is essential for oligomeric amyloid-β-induced neuronal cell death.Prion-Protein-interacting Amyloid-β Oligomers of High Molecular Weight Are Tightly Correlated with Memory Impairment in Multiple Alzheimer Mouse Models.Isolation of soluble and insoluble PrP oligomers in the normal human brain.Pathogenic prions deviate PrP(C) signaling in neuronal cells and impair A-beta clearance The complex PrP(c)-Fyn couples human oligomeric Aβ with pathological tau changes in Alzheimer's disease.Metabotropic glutamate receptor 5 couples cellular prion protein to intracellular signalling in Alzheimer's disease Soluble prion protein and its N-terminal fragment prevent impairment of synaptic plasticity by Aβ oligomers: Implications for novel therapeutic strategy in Alzheimer's disease.The cellular prion protein traps Alzheimer's Aβ in an oligomeric form and disassembles amyloid fibers.Prions: Beyond a Single Protein.Quiescin-sulfhydryl oxidase inhibits prion formation in vitro.Fyn kinase inhibition as a novel therapy for Alzheimer's disease.Allosteric function and dysfunction of the prion protein.Interaction between pathogenic proteins in neurodegenerative disorders.Deregulation of excitatory neurotransmission underlying synapse failure in Alzheimer's disease.Overcoming barriers and thresholds - signaling of oligomeric Aβ through the prion protein to Fyn.Biophysical studies of the amyloid β-peptide: interactions with metal ions and small molecules.Taking advantage of physiological proteolytic processing of the prion protein for a therapeutic perspective in prion and Alzheimer diseases.The cellular prion protein (PrPC) as neuronal receptor for α-synuclein.Cross-interactions between the Alzheimer Disease Amyloid-β Peptide and Other Amyloid Proteins: A Further Aspect of the Amyloid Cascade Hypothesis.S100A6 amyloid fibril formation is calcium-modulated and enhances superoxide dismutase-1 (SOD1) aggregation.Unraveling the neuroprotective mechanisms of PrP (C) in excitotoxicity.Involvement of Cellular Prion Protein in α-Synuclein Transport in Neurons.High molecular mass assemblies of amyloid-β oligomers bind prion protein in patients with Alzheimer's disease.Liquid and Hydrogel Phases of PrP Linked to Conformation Shifts and Triggered by Alzheimer's Amyloid-β Oligomers Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification

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P2860

Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain.

http://www.wikidata.org/entity/Q34868772

description

2011 nî lūn-bûn

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2011 թուականի Մարտին հրատարակուած գիտական յօդուած

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2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain.

@ast

Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain.

@en

Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain.

@nl

type

label

Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain.

@ast

Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain.

@en

Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain.

@nl

prefLabel

Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain.

@ast

Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain.

@en

Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain.

@nl

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JBC.M110.199356

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Journal of Biological Chemistry

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Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain.

@en

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Diego E Rincon-Limas

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Geoff Kneale

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Gianfranco Puoti

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Hisashi Fujioka

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Hyoung-gon Lee

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Jian-Ping Guo

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John McGeehan

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Jue Yuan

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Patrick L McGeer

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Pedro Fernandez-Funez

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P2860

Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers

Abeta and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer's disease

Synthetic amyloid-beta oligomers impair long-term memory independently of cellular prion protein

Molecular cross talk between misfolded proteins in animal models of Alzheimer's and prion diseases

NMR solution structure of the human prion protein

The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics

A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in aplysia

Prions as adaptive conduits of memory and inheritance

A general model of prion strains and their pathogenicity

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15095-15105

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scholarly article

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10.1074/JBC.M110.199356

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17

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286

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Mark Anthony Smith

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2011-03-10T00:00:00Z

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21393248

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Alzheimer's disease

Prion protein family

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3083157

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