Differential solubility of prions is associated in manifold phenotypes
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[1] J. Hauw,et al. Correction: Regulating Factors of PrPres Glycosylation in Creutzfeldt-Jakob Disease - Implications for the Dissemination and the Diagnosis of Human Prion Strains , 2008, PLoS ONE.
[2] J. Hauw,et al. Regulating Factors of PrPres Glycosylation in Creutzfeldt-Jakob Disease - Implications for the Dissemination and the Diagnosis of Human Prion Strains , 2008, PloS one.
[3] J. Manson,et al. Host PrP Glycosylation: A Major Factor Determining the Outcome of Prion Infection , 2008, PLoS biology.
[4] I. Izquierdo,et al. Physiology of the prion protein. , 2008, Physiological reviews.
[5] H. Karch,et al. Regional and phenotype heterogeneity of cellular prion proteins in the human brain , 2007, The European journal of neuroscience.
[6] H. Karch,et al. 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 , 2007, The FEBS journal.
[7] J. Grassi,et al. Immunoreactivity enhancement with chelators for increasing the detection sensitivity of human PrPSc by Western blotting , 2007, Neurochemistry International.
[8] J. Launay,et al. Cellular Prion Protein Signaling in Serotonergic Neuronal Cells , 2007, Annals of the New York Academy of Sciences.
[9] J. McGeehan,et al. Insoluble Aggregates and Protease-resistant Conformers of Prion Protein in Uninfected Human Brains* , 2006, Journal of Biological Chemistry.
[10] C. Fonta,et al. Truncated PrPc in mammalian brain: interspecies variation and location in membrane rafts , 2006, Biological chemistry.
[11] H. Kretzschmar,et al. Prion protein induced signaling cascades in monocytes. , 2006, Biochemical and biophysical research communications.
[12] J. Langeveld,et al. Immunopathology and Infectious Diseases Detection of Type 1 Prion Protein in Variant Creutzfeldt-Jakob Disease , 2005 .
[13] A. Aguzzi,et al. Coexistence of multiple PrPSc types in individuals with Creutzfeldt-Jakob disease , 2005, The Lancet Neurology.
[14] S. Prusiner,et al. Recombinant prion protein induces rapid polarization and development of synapses in embryonic rat hippocampal neurons in vitro , 2005, Journal of neurochemistry.
[15] J. Ironside,et al. Prion protein heterogeneity in sporadic but not variant Creutzfeldt–Jakob disease: U.K. cases 1991–2002 , 2004, Annals of neurology.
[16] A. Buschmann,et al. Atypical scrapie cases in Germany and France are identified by discrepant reaction patterns in BSE rapid tests. , 2004, Journal of virological methods.
[17] F. Tagliavini,et al. Identification of a second bovine amyloidotic spongiform encephalopathy: molecular similarities with sporadic Creutzfeldt-Jakob disease. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[18] V. Mutel,et al. NADPH oxidase and extracellular regulated kinases 1/2 are targets of prion protein signaling in neuronal and nonneuronal cells , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[19] J. Collinge,et al. Regional heterogeneity of cellular prion protein isoforms in the mouse brain. , 2003, Brain : a journal of neurology.
[20] P. Sarradin,et al. Cases of scrapie with unusual features in Norway and designation of a new type, Nor98 , 2003, Veterinary Record.
[21] H. Budka,et al. Molecular classification of sporadic Creutzfeldt-Jakob disease. , 2003, Brain : a journal of neurology.
[22] Shu G. Chen,et al. Sporadic and familial CJD: classification and characterisation. , 2003, British medical bulletin.
[23] I. Vorberg,et al. Molecular Basis of Scrapie Strain Glycoform Variation* , 2002, The Journal of Biological Chemistry.
[24] C. Soto,et al. Cyclic amplification of protein misfolding: application to prion-related disorders and beyond , 2002, Trends in Neurosciences.
[25] Tong Liu,et al. Heterogeneity of normal prion protein in two‐dimensional immunoblot: presence of various glycosylated and truncated forms , 2002, Journal of neurochemistry.
[26] G. Edelman,et al. Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein. , 2001, Journal of molecular biology.
[27] D. Dormont,et al. Identification of interaction domains of the prion protein with its 37‐kDa/67‐kDa laminin receptor , 2001, The EMBO journal.
[28] B. Strooper,et al. The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. , 2001, The Journal of biological chemistry.
[29] J. Collinge,et al. Tissue distribution of protease resistant prion protein in variant Creutzfeldt-Jakob disease using a highly sensitive immunoblotting assay , 2001, The Lancet.
[30] J. Collinge,et al. Location and properties of metal-binding sites on the human prion protein , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[31] J. Laplanche,et al. Signal transduction through prion protein. , 2000, Science.
[32] K Wüthrich,et al. NMR solution structure of the human prion protein. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[33] A. Buschmann,et al. Characterization of BSE and scrapie strains/isolates. , 2000, Archives of virology. Supplementum.
[34] D. Dormont,et al. New insight into abnormal prion protein using monoclonal antibodies. , 1999, Biochemical and biophysical research communications.
[35] S. Prusiner,et al. Glycosylation differences between the normal and pathogenic prion protein isoforms. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[36] V. Daggett,et al. PrPc glycoform heterogeneity as a function of brain region: implications for selective targeting of neurons by prion strains. , 1999, Journal of neuropathology and experimental neurology.
[37] Stanley B. Prusiner,et al. Nobel Lecture: Prions , 1998 .
[38] B. Ghetti,et al. Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues. , 1998, The American journal of pathology.
[39] F. Cohen,et al. Eight prion strains have PrPSc molecules with different conformations , 1998, Nature Medicine.
[40] M. Groschup,et al. Molecular analysis of bovine spongiform encephalopathy and scrapie strain variation. , 1998, The Journal of infectious diseases.
[41] P E Wright,et al. Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[42] F. Cohen,et al. Selective Neuronal Targeting in Prion Disease , 1997, Neuron.
[43] K Wüthrich,et al. NMR characterization of the full‐length recombinant murine prion protein, mPrP(23–231) , 1997, FEBS letters.
[44] A. Chong,et al. Biochemical typing of scrapie strains , 1997, Nature.
[45] Andrew F. Hill,et al. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD , 1996, Nature.
[46] D. Teplow,et al. Truncated Forms of the Human Prion Protein in Normal Brain and in Prion Diseases (*) , 1995, The Journal of Biological Chemistry.
[47] B. Caughey. Scrapie associated PrP accumulation and its prevention: insights from cell culture. , 1993, British medical bulletin.
[48] N. Cashman,et al. Nearly ubiquitous tissue distribution of the scrapie agent precursor protein , 1992, Neurology.
[49] S. Prusiner,et al. Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein. , 1989, Biochemistry.
[50] S. Prusiner,et al. Scrapie prion proteins are synthesized in neurons. , 1986, The American journal of pathology.