Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo. - Wikidata - awgldk - TriplyDB

Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

http://www.wikidata.org/entity/Q44102933

about

α-Cleavage of cellular prion protein Protease resistant protein cellular isoform (PrP(c)) as a biomarker: clues into the pathogenesis of HAND Loss of Cellular Sialidases Does Not Affect the Sialylation Status of the Prion Protein but Increases the Amounts of Its Proteolytic Fragment C1 Effects of FlAsH/tetracysteine (TC) Tag on PrP proteolysis and PrPres formation by TC-scanning.Medulla oblongata transcriptome changes during presymptomatic natural scrapie and their association with prion-related lesions.A common BACE1 polymorphism is a risk factor for sporadic Creutzfeldt-Jakob disease Amyloid precursor protein (APP) processing genes and cerebrospinal fluid APP cleavage product levels in Alzheimer's disease The sheddase ADAM10 is a potent modulator of prion disease.Role of lipid rafts and GM1 in the segregation and processing of prion protein The extracellular regulated kinase-1 (ERK1) controls regulated alpha-secretase-mediated processing, promoter transactivation, and mRNA levels of the cellular prion protein.Cellular prion protein regulates its own α-cleavage through ADAM8 in skeletal muscle.Separate mechanisms act concurrently to shed and release the prion protein from the cell.The Soluble Form of the Cellular Prion Protein Enhances Phagocytic Activity and Cytokine Production by Human Monocytes Via Activation of ERK and NF-κB.The P's and Q's of cellular PrP-Aβ interactions Proteolytic processing of the prion protein in health and disease.Roles of endoproteolytic α-cleavage and shedding of the prion protein in neurodegeneration.Apparent reduction of ADAM10 in scrapie-infected cultured cells and in the brains of scrapie-infected rodents.Endoproteolytic processing of the mammalian prion glycoprotein family.Lack of a-disintegrin-and-metalloproteinase ADAM10 leads to intracellular accumulation and loss of shedding of the cellular prion protein in vivo.Shedding light on prion disease.Analysis of Cellular Prion Protein Endoproteolytic Processing.Interaction of Peptide Aptamers with Prion Protein Central Domain Promotes α-Cleavage of PrPC.Structural and mechanistic aspects influencing the ADAM10-mediated shedding of the prion protein.

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P2860

Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

http://www.wikidata.org/entity/Q44102933

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年学术文章

@wuu

2009年学术文章

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2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

2009年學術文章

@zh-hant

name

Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

@en

Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

@nl

type

label

Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

@en

Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

@nl

prefLabel

Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

@en

Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

@nl

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J.NBD.2009.07.015

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Neurobiology of Disease

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Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

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Elzbieta Kojro

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Falk Fahrenholz

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Gerda Mitteregger

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10.1016/J.NBD.2009.07.015

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2

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Prion protein family