Binding of N- and C-terminal anti-prion protein antibodies generates distinct phenotypes of cellular prion proteins (PrPC) obtained from human, sheep, cattle and mouse (Q57374337)

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English	Binding of N- and C-terminal anti-prion protein antibodies generates distinct phenotypes of cellular prion proteins (PrPC) obtained from human, sheep, cattle and mouse	article

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Binding of N- and C-terminal anti-prion protein antibodies generates distinct phenotypes of cellular prion proteins (PrPC) obtained from human, sheep, cattle and mouse (English)

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Martin H Groschup

4

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Martin H Groschup

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3

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Helge Karch

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author name string

Thorsten Kuczius

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Jacques Grassi

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publication date

14 February 2007

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274

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6

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1492-1502

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Molecular biology of prion diseases

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Effects of different experimental conditions on the PrPSc core generated by protease digestion: implications for strain typing and molecular classification of CJD.

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A journey through the species barrier

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Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier

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

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Nearly ubiquitous tissue distribution of the scrapie agent precursor protein

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Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein

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Scrapie associated PrP accumulation and its prevention: insights from cell culture

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Putative functions of PrPC

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Hippocampal synaptic plasticity in mice devoid of cellular prion protein

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Signal transduction through prion protein

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The cellular prion protein binds copper in vivo

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Truncated forms of the human prion protein in normal brain and in prion diseases

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Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues

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Truncated PrP(c) in mammalian brain: interspecies variation and location in membrane rafts

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Proteolytic processing and glycosylation influence formation of porcine prion protein complexes.

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Proteolytic cleavage and shedding of the bovine prion protein in two cell culture systems

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Regional heterogeneity of cellular prion protein isoforms in the mouse brain

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Cases of scrapie with unusual features in Norway and designation of a new type, Nor98.

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Atypical scrapie cases in Germany and France are identified by discrepant reaction patterns in BSE rapid tests

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Molecular analysis of bovine spongiform encephalopathy and scrapie strain variation

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Comparative molecular analysis of the abnormal prion protein in field scrapie cases and experimental bovine spongiform encephalopathy in sheep by use of Western blotting and immunohistochemical methods

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The N-terminal cleavage site of PrPSc from BSE differs from that of PrPSc from scrapie

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Genetic influence on the structural variations of the abnormal prion protein

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Crystal structure of the human prion protein reveals a mechanism for oligomerization

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NMR solution structure of the human prion protein

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Selective and efficient immunoprecipitation of the disease-associated form of the prion protein can be mediated by nonspecific interactions between monoclonal antibodies and scrapie-associated fibrils

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Prion (PrPSc)-specific epitope defined by a monoclonal antibody

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Generation of monoclonal antibodies against prion proteins with an unconventional nucleic acid-based immunization strategy.

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Discrimination between scrapie and bovine spongiform encephalopathy in sheep by molecular size, immunoreactivity, and glycoprofile of prion protein

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Cellular prion protein acquires resistance to proteolytic degradation following copper ion binding

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Screening of 145 anti-PrP monoclonal antibodies for their capacity to inhibit PrPSc replication in infected cells.

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10.1111/J.1742-4658.2007.05691.X

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