Normal prion protein has an activity like that of superoxide dismutase. - Wikidata - awgldk - TriplyDB

Normal prion protein has an activity like that of superoxide dismutase.

Normal prion protein has an activity like that of superoxide dismutase.

http://www.wikidata.org/entity/Q34505606

about

Molecular features of the copper binding sites in the octarepeat domain of the prion protein Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection.Ionic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone protein Activation of microglial NADPH oxidase is synergistic with glial iNOS expression in inducing neuronal death: a dual-key mechanism of inflammatory neurodegeneration.Quantum dots and prion proteins: is this a new challenge for neurodegenerative diseases imaging?Unique Structural Characteristics of the Rabbit Prion Protein Post-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivo Disruption of copper homeostasis due to a mutation of Atp7a delays the onset of prion disease Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form.Electron paramagnetic resonance evidence for binding of Cu(2+) to the C-terminal domain of the murine prion protein Metals in obex and retropharyngeal lymph nodes of Illinois white-tailed deer and their variations associated with CWD status Comparative analysis of the human and chicken prion protein copper binding regions at pH 6.5.Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.Spectroscopic and Theoretical Study of Cu(I) Binding to His111 in the Human Prion Protein Fragment 106-115.Cleavage of the amino terminus of the prion protein by reactive oxygen species.Copper(II) binding to the human Doppel protein may mark its functional diversity from the prion protein.The biological function of the cellular prion protein: an update Increased expression and local accumulation of the prion protein, Alzheimer Aβ peptides, superoxide dismutase 1, and nitric oxide synthases 1 & 2 in muscle in a rabbit model of diabetes.Insights into prion protein function from atomistic simulations.Redox control of prion and disease pathogenesis.Evolutionary implications of metal binding features in different species' prion protein: an inorganic point of view.Copper redox cycling in the prion protein depends critically on binding mode Copper binding extrinsic to the octarepeat region in the prion protein Na+/K+-ATPase is present in scrapie-associated fibrils, modulates PrP misfolding in vitro and links PrP function and dysfunction.Deficiency of prion protein induces impaired autophagic flux in neurons.Prion and doppel proteins bind to granule cells of the cerebellum Epigenetic control of aging The Functional Role of Prion Protein (PrPC) on Autophagy.PrP(c) expression influences the establishment of herpes simplex virus type 1 latency.Infectious prion protein alters manganese transport and neurotoxicity in a cell culture model of prion disease.Prion infection impairs the cellular response to oxidative stress Prion diseases: from molecular biology to intervention strategies.Copper binding in the prion protein Immunization delays the onset of prion disease in mice.Prion Protein Protects against Renal Ischemia/Reperfusion Injury Prion Protein Does Not Confer Resistance to Hippocampus-Derived Zpl Cells against the Toxic Effects of Cu2+, Mn2+, Zn2+ and Co2+ Not Supporting a General Protective Role for PrP in Transition Metal Induced Toxicity.Antiprion immunotherapy: to suppress or to stimulate?Recent advances in prion chemotherapeutics.Copper and Zinc Interactions with Cellular Prion Proteins Change Solubility of Full-Length Glycosylated Isoforms and Induce the Occurrence of Heterogeneous Phenotypes The cellular prion protein (PrP(C)): its physiological function and role in disease

P2860

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P2860

Normal prion protein has an activity like that of superoxide dismutase.

http://www.wikidata.org/entity/Q34505606

description

1999 nî lūn-bûn

@nan

1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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name

Normal prion protein has an activity like that of superoxide dismutase.

@ast

Normal prion protein has an activity like that of superoxide dismutase.

@en

Normal prion protein has an activity like that of superoxide dismutase.

@nl

type

label

Normal prion protein has an activity like that of superoxide dismutase.

@ast

Normal prion protein has an activity like that of superoxide dismutase.

@en

Normal prion protein has an activity like that of superoxide dismutase.

@nl

prefLabel

Normal prion protein has an activity like that of superoxide dismutase.

@ast

Normal prion protein has an activity like that of superoxide dismutase.

@en

Normal prion protein has an activity like that of superoxide dismutase.

@nl

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P1433

Biochemical Journal

P1476

Normal prion protein has an activity like that of superoxide dismutase

@en

P2093

Brown DR

http://www.w3.org/2001/XMLSchema#string

Clive C

http://www.w3.org/2001/XMLSchema#string

Hafiz F

http://www.w3.org/2001/XMLSchema#string

Haswell SJ

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Jones IM

http://www.w3.org/2001/XMLSchema#string

P2860

Copper stimulates endocytosis of the prion protein

Copper binding to the prion protein: structural implications of four identical cooperative binding sites

Molecular cloning of a candidate chicken prion protein.

The cellular prion protein binds copper in vivo.

Molecular biology of prion diseases.

Scrapie prion proteins are synthesized in neurons

Prion protein NMR structure and species barrier for prion diseases

Spectrophotometric study of spontaneous disproportionation of superoxide anion radical and sensitive direct assay for superoxide dismutase.

Prion protein expression in muscle cells and toxicity of a prion protein fragment.

Prion protein expression and superoxide dismutase activity.

P304

1-5

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scholarly article

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10.1042/0264-6021:3440001

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10.1042/BJ3440001

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344 Pt 1

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1999-11-01T00:00:00Z

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12751411

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10548526

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Prion protein family

P932

1220606

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