The CNS glycoprotein Shadoo has PrP(C)-like protective properties and displays reduced levels in prion infections. - Wikidata - thesis-toulmin - TriplyDB

The CNS glycoprotein Shadoo has PrP(C)-like protective properties and displays reduced levels in prion infections.

The CNS glycoprotein Shadoo has PrP(C)-like protective properties and displays reduced levels in prion infections.

http://www.wikidata.org/entity/Q40093030

about

A systems approach to prion disease Progress on low susceptibility mechanisms of transmissible spongiform encephalopathies Shadoo/PrP (Sprn(0/0) /Prnp(0/0) ) double knockout mice: more than zeroes Evolutionary descent of prion genes from the ZIP family of metal ion transporters Interactome analyses identify ties of PrP and its mammalian paralogs to oligomannosidic N-glycans and endoplasmic reticulum-derived chaperones Knockout of the prion protein (PrP)-like Sprn gene does not produce embryonic lethality in combination with PrP(C)-deficiency Prion Protein Deficiency Causes Diverse Proteome Shifts in Cell Models That Escape Detection in Brain Tissue Genomic and post-genomic analyses of human prion diseases Prion strain discrimination based on rapid in vivo amplification and analysis by the cell panel assay Frequent missense and insertion/deletion polymorphisms in the ovine Shadoo gene parallel species-specific variation in PrP.A novel, drug-based, cellular assay for the activity of neurotoxic mutants of the prion protein.Agent-specific Shadoo responses in transmissible encephalopathies.Voluntary wheel running reverses age-induced changes in hippocampal gene expression Down-regulation of Shadoo in prion infections traces a pre-clinical event inversely related to PrP(Sc) accumulation.Protease-resistant prions selectively decrease Shadoo protein.PrionHome: a database of prions and other sequences relevant to prion phenomena.Prion protein and Shadoo are involved in overlapping embryonic pathways and trophoblastic development Comparative analysis of the Shadoo gene between cattle and buffalo reveals significant differences.Review: contribution of transgenic models to understanding human prion disease.Biochemical insight into the prion protein family.Structural studies of truncated forms of the prion protein PrP.Interaction between Shadoo and PrP Affects the PrP-Folding Pathway Unchanged survival rates of Shadoo knockout mice after infection with mouse-adapted scrapie Prion Infectivity Plateaus and Conversion to Symptomatic Disease Originate from Falling Precursor Levels and Increased Levels of Oligomeric PrPSc Species.Cellular prion protein: from physiology to pathology.A specific role for PRND in goat foetal Leydig cells is suggested by prion family gene expression during gonad development in goats and mice The ZIP-prion connection The prion protein family: looking outside the central nervous system.Expression of the Prion Protein Family Member Shadoo Causes Drug Hypersensitivity That Is Diminished by the Coexpression of the Wild Type Prion Protein.Prion neurotoxicity: insights from prion protein mutants Association of a null allele of SPRN with variant Creutzfeldt-Jakob disease.A structural overview of the vertebrate prion proteins.Neuroprotective properties of the PrP-like Shadoo glycoprotein assessed in the middle cerebral artery occlusion model of ischemia Prion protein on astrocytes or in extracellular fluid impedes neurodegeneration induced by truncated prion protein Identification of the RGG box motif in Shadoo: RNA-binding and signaling roles?The prion protein family member Shadoo induces spontaneous ionic currents in cultured cells.Prion disease tempo determined by host-dependent substrate reduction.Physiological Functions of the Cellular Prion Protein.Prion protein and cancers.Prion protein (PrP) gene-knockout cell lines: insight into functions of the PrP.

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The CNS glycoprotein Shadoo has PrP(C)-like protective properties and displays reduced levels in prion infections.

http://www.wikidata.org/entity/Q40093030

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年论文

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The CNS glycoprotein Shadoo ha ...... ed levels in prion infections.

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The CNS glycoprotein Shadoo ha ...... ed levels in prion infections.

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The CNS glycoprotein Shadoo ha ...... ed levels in prion infections.

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SJ.EMBOJ.7601830

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The EMBO Journal

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The CNS glycoprotein Shadoo ha ...... ed levels in prion infections.

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P2093

Bettina Drisaldi

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

Bob Strome

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

Catherine Bergeron

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

David Westaway

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

George A Carlson

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

Gerold Schmitt-Ulms

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

Howard T J Mount

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

Jing Yang

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Joel C Watts

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Larry Yoong

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P2860

Doppel-induced cerebellar degeneration in transgenic mice

Two different neurodegenerative diseases caused by proteins with similar structures

NMR structure of the mouse prion protein domain PrP(121-231)

Genomic characterization of the human prion protein (PrP) gene locus

Mice devoid of PrP are resistant to scrapie

Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein

Lethal recessive myelin toxicity of prion protein lacking its central domain.

Doppel is an N-glycosylated, glycosylphosphatidylinositol-anchored protein. Expression in testis and ectopic production in the brains of Prnp(0/0) mice predisposed to Purkinje cell loss.

Early loss of dendritic spines in murine scrapie revealed by confocal analysis.

Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible

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4038-4050

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17

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26

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2007-08-16T00:00:00Z

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6136974

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17703189

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Prion protein family

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1950727

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