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A camelid anti-PrP antibody abrogates PrP replication in prion-permissive neuroblastoma cell linesPrion-induced neurotoxicity: Possible role for cell cycle activity and DNA damage responseExpression of mutant or cytosolic PrP in transgenic mice and cells is not associated with endoplasmic reticulum stress or proteasome dysfunctionMutant PrP suppresses glutamatergic neurotransmission in cerebellar granule neurons by impairing membrane delivery of VGCC α(2)δ-1 SubunitFull-length prion protein aggregates to amyloid fibrils and spherical particles by distinct pathways.Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions.Squalestatin alters the intracellular trafficking of a neurotoxic prion peptide.Molecular distinction between pathogenic and infectious properties of the prion protein.Fishing for prion protein functionImmunopurification of pathological prion protein aggregatesMutant prion protein expression is associated with an alteration of the Rab GDP dissociation inhibitor alpha (GDI)/Rab11 pathwayRedox control of prion and disease pathogenesis.Biological characteristics of Chinese hamster ovary cells transfected with bovine PrnpNeurotoxic mutants of the prion protein induce spontaneous ionic currents in cultured cellsA newly identified type of scrapie agent can naturally infect sheep with resistant PrP genotypes.A common BACE1 polymorphism is a risk factor for sporadic Creutzfeldt-Jakob diseaseHigh titers of transmissible spongiform encephalopathy infectivity associated with extremely low levels of PrPSc in vivo.Human PrP90-231-induced cell death is associated with intracellular accumulation of insoluble and protease-resistant macroaggregates and lysosomal dysfunction.Structural diversity and initial oligomerization of PrP106-126 studied by replica-exchange and conventional molecular dynamics simulationsTransgenic fatal familial insomnia mice indicate prion infectivity-independent mechanisms of pathogenesis and phenotypic expression of disease.A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formation.Modulation of proteinase K-resistant prion protein in cells and infectious brain homogenate by redox iron: implications for prion replication and disease pathogenesisHuman prion protein-induced autophagy flux governs neuron cell damage in primary neuron cells.The cellular prion protein (PrP(C)): its physiological function and role in diseaseNormal cellular prion protein protects against manganese-induced oxidative stress and apoptotic cell death.The N-terminal, polybasic region of PrP(C) dictates the efficiency of prion propagation by binding to PrP(Sc).Prion neurotoxicity: insights from prion protein mutantsBranched chain mechanism of polymerization and ultrastructure of prion protein amyloid fibrils.Opposing roles of prion protein in oxidative stress- and ER stress-induced apoptotic signaling.Prion diseases: from protein to cell pathology.Aggregated, wild-type prion protein causes neurological dysfunction and synaptic abnormalities.Prions: Beyond a Single Protein.Prion protein with an insertional mutation accumulates on axonal and dendritic plasmalemma and is associated with distinctive ultrastructural changes.Synaptic dysfunction in prion diseases: a trafficking problem?Protection from cytosolic prion protein toxicity by modulation of protein translocation.Myelin damage due to local quantitative abnormalities in normal prion levels: evidence from subacute combined degeneration and multiple sclerosis.The hydrophobic core region governs mutant prion protein aggregation and intracellular retention.Subclinical prion disease induced by oral inoculation.Intracellular accumulation of a mild-denatured monomer of the human PrP fragment 90-231, as possible mechanism of its neurotoxic effects.Conformation dependent pro-apoptotic activity of the recombinant human prion protein fragment 90-231.
P2860
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P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Prion diseases: what is the neurotoxic molecule?
@ast
Prion diseases: what is the neurotoxic molecule?
@en
Prion diseases: what is the neurotoxic molecule?
@nl
type
label
Prion diseases: what is the neurotoxic molecule?
@ast
Prion diseases: what is the neurotoxic molecule?
@en
Prion diseases: what is the neurotoxic molecule?
@nl
prefLabel
Prion diseases: what is the neurotoxic molecule?
@ast
Prion diseases: what is the neurotoxic molecule?
@en
Prion diseases: what is the neurotoxic molecule?
@nl
P356
P1476
Prion diseases: what is the neurotoxic molecule?
@en
P2093
P304
P356
10.1006/NBDI.2001.0433
P577
2001-10-01T00:00:00Z