about
Isoprostanes and neuroprostanes as biomarkers of oxidative stress in neurodegenerative diseasesExpression patterns of antioxidant proteins in brains of patients with sporadic Creutzfeldt-Jacob disease.Redox control of prion and disease pathogenesis.Prion protein accumulation and neuroprotection in hypoxic brain damage.Prion proteins and the gut: une liaison dangereuse?Normal cellular prion protein protects against manganese-induced oxidative stress and apoptotic cell death.Methionine oxidation perturbs the structural core of the prion protein and suggests a generic misfolding pathwayBovine spongiform encephalopathy in Japan: history and recent studies on oxidative stress in prion diseases.Opposing roles of prion protein in oxidative stress- and ER stress-induced apoptotic signaling.Flotillin-1 mediates PrPc endocytosis in the cultured cells during Cu²⁺ stimulation through molecular interaction.Cellular prion protein transduces neuroprotective signals.Expression of truncated PrP targeted to Purkinje cells of PrP knockout mice causes Purkinje cell death and ataxia.Serum withdrawal-induced apoptosis in ZrchI prion protein (PrP) gene-deficient neuronal cell line is suppressed by PrP, independent of Doppel.Prion protein fragment 106-126 induces a p38 MAP kinase-dependent apoptosis in SH-SY5Y neuroblastoma cells independently from the amyloid fibril formation.Biochemical fingerprints of prion infection: accumulations of aberrant full-length and N-terminally truncated PrP species are common features in mouse prion disease.Fragmentation and dimerization of copper-loaded prion protein by copper-catalysed oxidation.Channel activity of deamidated isoforms of prion protein fragment 106-126 in planar lipid bilayers.Green fluorescent protein as a reporter of prion protein folding.Affinity, speciation, and molecular features of copper(II) complexes with a prion tetraoctarepeat domain in aqueous solution: insights into old and new results.Protective activity of aromatic amines and imines against oxidative nerve cell death.Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism.Cell surface expression of the prion protein in yeast does not alter copper utilization phenotypes.Ageing and exposure to oxidative stress in vivo differentially affect cellular levels of PrP in mouse cerebral microvessels and brain parenchyma.Preferential Cu2+ coordination by His96 and His111 induces beta-sheet formation in the unstructured amyloidogenic region of the prion protein.Expression of excitatory amino acid transporter-1 (EAAT-1) in brain macrophages and microglia of patients with prion diseases.Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides.A survey of diamagnetic probes for copper2+ binding to the prion protein. 1H NMR solution structure of the palladium2+ bound single octarepeat.
P2860
Q26822872-023C3603-FD9F-459E-AA46-D43501B817A0Q31107740-686D644C-5B16-462D-8C19-6D2C96E61800Q33830151-9C0C857E-FB42-4C88-AE63-22B4B8D269EBQ35102832-DD054A20-8EE8-4041-89A6-4985DF28C8E0Q35363050-DD00E59E-8A77-45E9-A1BB-6E0F0857A7D6Q36123408-B4CE4A8D-E507-49DF-B735-08E3114D55DEQ36217394-9AC70801-DBCD-4C6A-B910-CC833AB87E79Q36573251-DD80AD29-C839-4119-A9C4-CC248FC11BA1Q37066530-EC77E856-0375-45CE-85BA-4FF5FDBDA85AQ39159118-F37ACC7C-840B-4754-B41E-ED1AB5BFF22FQ39644937-D448F7CB-38A0-492C-A7EB-0288A6AB5684Q39777445-1267EC75-ABFD-412E-9D35-2119D13F43DCQ40143435-9069EB07-0AD4-4674-A143-3A95C8757DCEQ40576035-190D147E-C092-4A93-ABBE-88A85C1295B3Q40721456-27478B31-9F4A-45FE-A08D-0875F32007FFQ42156555-F571FDED-1B42-438B-B7E9-2DB7A44FECF8Q42661041-EE00F65D-C512-49CF-B4FE-D2A8C150764AQ43101604-D76D7768-A3B2-4993-AE68-2AE8056FC9C1Q43747316-021C0487-F123-4150-A38E-673F814E188CQ43840174-B04A7668-D351-4A53-9209-8F4B8F6AE9B9Q44231104-0F2B976A-5DB1-4432-A359-00500873A903Q44386982-13279AE1-4CC7-41B5-B512-D1E108AC7DC7Q44813964-CE241462-0A6C-4D8B-B1B1-7771BCC20C6AQ44897846-FDACA61C-8AC6-470C-864B-FFA6B47BE26EQ45145157-683A0E21-DCBE-4CC2-BCF7-C6D4271FFA61Q46782390-1817F83E-610D-496C-8204-FB220CEF0F2CQ46881301-9E65760A-2009-423A-9FC3-C7050F779B36
P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Prion disease: A loss of antioxidant function?
@ast
Prion disease: A loss of antioxidant function?
@en
Prion disease: A loss of antioxidant function?
@nl
type
label
Prion disease: A loss of antioxidant function?
@ast
Prion disease: A loss of antioxidant function?
@en
Prion disease: A loss of antioxidant function?
@nl
prefLabel
Prion disease: A loss of antioxidant function?
@ast
Prion disease: A loss of antioxidant function?
@en
Prion disease: A loss of antioxidant function?
@nl
P2093
P356
P1476
Prion disease: A loss of antioxidant function?
@en
P2093
Gambetti P
Petersen RB
P304
P356
10.1006/BBRC.2000.3158
P407
P577
2000-08-01T00:00:00Z