Nonspecific interaction of prefibrillar amyloid aggregates with glutamatergic receptors results in Ca2+ increase in primary neuronal cells.

Nonspecific interaction of prefibrillar amyloid aggregates with glutamatergic receptors results in Ca2+ increase in primary neuronal cells.

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http://www.wikidata.org/entity/Q43154901
Amyloid-β acts as a regulator of neurotransmitter release disrupting the interaction between synaptophysin and VAMP2Amyloid oligomer neurotoxicity, calcium dysregulation, and lipid raftsCopper-triggered aggregation of ubiquitin.β-Amyloid (1-40) peptide interactions with supported phospholipid membranes: a single-molecule studyProtein folding and aggregation into amyloid: the interference by natural phenolic compoundsSoluble oligomeric amyloid-β induces calcium dyshomeostasis that precedes synapse loss in the living mouse brain.Amyloid toxicity and platelet-activating factor signaling.Beneficial properties of natural phenols: highlight on protection against pathological conditions associated with amyloid aggregation.Misfolding of amyloidogenic proteins and their interactions with membranes.Different Molecular Mechanisms Mediate Direct or Glia-Dependent Prion Protein Fragment 90-231 Neurotoxic Effects in Cerebellar Granule Neurons.Interaction of toxic and non-toxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy.Peptide-lipid interactions: experiments and applications.Protein folding and misfolding on surfaces.Calcium dysregulation in relation to Alzheimer-type pathology in the ageing brain.Abnormal dendritic calcium activity and synaptic depotentiation occur early in a mouse model of Alzheimer's disease.Excitotoxicity through NMDA receptors mediates cerebellar granule neuron apoptosis induced by prion protein 90-231 fragment.Epigallocatechin-3-gallate and related phenol compounds redirect the amyloidogenic aggregation pathway of ataxin-3 towards non-toxic aggregates and prevent toxicity in neural cells and Caenorhabditis elegans animal model.
P2860

Nonspecific interaction of prefibrillar amyloid aggregates with glutamatergic receptors results in Ca2+ increase in primary neuronal cells.

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http://www.wikidata.org/entity/Q43154901
description
2008 nî lūn-bûn
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2008年の論文
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2008年学术文章
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2008年学术文章
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name
Nonspecific interaction of pre ...... ase in primary neuronal cells.
@en
Nonspecific interaction of pre ...... ase in primary neuronal cells.
@nl
type
label
Nonspecific interaction of pre ...... ase in primary neuronal cells.
@en
Nonspecific interaction of pre ...... ase in primary neuronal cells.
@nl
prefLabel
Nonspecific interaction of pre ...... ase in primary neuronal cells.
@en
Nonspecific interaction of pre ...... ase in primary neuronal cells.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P932
P356
P1433
P1476
Nonspecific interaction of pre ...... ease in primary neuronal cells
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P932