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Science 24 December 1982:
Vol. 218. no. 4579, pp. 1309 - 1311
DOI: 10.1126/science.6815801

Articles

Science, Vol 218, Issue 4579, 1309-1311
Copyright © 1982 by American Association for the Advancement of Science


articles

Identification of a protein that purifies with the scrapie prion

DC Bolton, MP McKinley, and SB Prusiner

Purification of prions from scrapie-infected hamster brain yielded a protein that was not found in a similar fraction from uninfected brain. The protein migrated with an apparent molecular size of 27,000 to 30,000 daltons in sodium dodecyl sulfate polyacrylamide gels. The resistance of this protein to digestion by proteinase K distinguished it from proteins of similar molecular weight found in normal hamster brain. Initial results suggest that the amount of this protein correlates with the titer of the agent.


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The Effects of Host Age on Follicular Dendritic Cell Status Dramatically Impair Scrapie Agent Neuroinvasion in Aged Mice.
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J. Immunol. 183, 5199-5207
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Prions: Protein Aggregation and Infectious Diseases.
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Physiol Rev 89, 1105-1152
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Measuring prions by bioluminescence imaging.
G. Tamguney, K. P. Francis, K. Giles, A. Lemus, S. J. DeArmond, and S. B. Prusiner (2009)
PNAS 106, 15002-15006
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Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein.
C. Wolschner, A. Giese, H. A. Kretzschmar, R. Huber, L. Moroder, and N. Budisa (2009)
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Folding kinetics of the human prion protein probed by temperature jump.
T. Hart, L. L. P. Hosszu, C. R. Trevitt, G. S. Jackson, J. P. Waltho, J. Collinge, and A. R. Clarke (2009)
PNAS 106, 5651-5656
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Prion Variants and Species Barriers Among Saccharomyces Ure2 Proteins.
H. K. Edskes, L. M. McCann, A. M. Hebert, and R. B. Wickner (2009)
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Pathogenic prion protein is degraded by a manganese oxide mineral found in soils.
F. Russo, C. J. Johnson, C. J. Johnson, D. McKenzie, J. M. Aiken, and J. A. Pedersen (2009)
J. Gen. Virol. 90, 275-280
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Characterization of Truncated Forms of Abnormal Prion Protein in Creutzfeldt-Jakob Disease.
S. Notari, R. Strammiello, S. Capellari, A. Giese, M. Cescatti, J. Grassi, B. Ghetti, J. P. M. Langeveld, W.-Q. Zou, P. Gambetti, et al. (2008)
J. Biol. Chem. 283, 30557-30565
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Binding of Recombinant but Not Endogenous Prion Protein to DNA Causes DNA Internalization and Expression in Mammalian Cells.
S. Yin, X. Fan, S. Yu, C. Li, and M.-S. Sy (2008)
J. Biol. Chem. 283, 25446-25454
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Protein Misfolding and Neurodegeneration.
C. Soto and L. D. Estrada (2008)
Arch Neurol 65, 184-189
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In Vivo Depletion of CD11c+ Cells Impairs Scrapie Agent Neuroinvasion from the Intestine.
C. R. Raymond, P. Aucouturier, and N. A. Mabbott (2007)
J. Immunol. 179, 7758-7766
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Ser170 controls the conformational multiplicity of the loop 166 175 in prion proteins: implication for conversion and species barrier.
A. A. Gorfe and A. Caflisch (2007)
FASEB J 21, 3279-3287
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Efficient In Vitro Amplification of Chronic Wasting Disease PrPRES.
T. D. Kurt, M. R. Perrott, C. J. Wilusz, J. Wilusz, S. Supattapone, G. C. Telling, M. D. Zabel, and E. A. Hoover (2007)
J. Virol. 81, 9605-9608
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Prions in the peripheral nerves of bovine spongiform encephalopathy-affected cattle.
K. Masujin, D. Matthews, G. A. H. Wells, S. Mohri, and T. Yokoyama (2007)
J. Gen. Virol. 88, 1850-1858
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Role of the GALT in Scrapie Agent Neuroinvasion from the Intestine.
B. R. Glaysher and N. A. Mabbott (2007)
J. Immunol. 178, 3757-3766
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Test for Detection of Disease-Associated Prion Aggregate in the Blood of Infected but Asymptomatic Animals.
B. Chang, X. Cheng, S. Yin, T. Pan, H. Zhang, P. Wong, S.-C. Kang, F. Xiao, H. Yan, C. Li, et al. (2007)
Clin. Vaccine Immunol. 14, 36-43
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Insoluble Aggregates and Protease-resistant Conformers of Prion Protein in Uninfected Human Brains.
J. Yuan, X. Xiao, J. McGeehan, Z. Dong, I. Cali, H. Fujioka, Q. Kong, G. Kneale, P. Gambetti, and W.-Q. Zou (2006)
J. Biol. Chem. 281, 34848-34858
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Prion Protein Expression by Mouse Dendritic Cells Is Restricted to the Nonplasmacytoid Subsets and Correlates with the Maturation State.
G. Martinez del Hoyo, M. Lopez-Bravo, P. Metharom, C. Ardavin, and P. Aucouturier (2006)
J. Immunol. 177, 6137-6142
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PET-blot Analysis Contributes to BSE Strain Recognition in C57Bl/6 Mice.
S. Lezmi, A. Bencsik, and T. Baron (2006)
J. Histochem. Cytochem. 54, 1087-1094
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A systematic review of prion therapeutics in experimental models.
C. R Trevitt and J. Collinge (2006)
Brain 129, 2241-2265
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Amplified Immunohistochemical Detection of PrPsc in Animal Transmissible Spongiform Encephalopathies Using Streptomycin.
A. A. Bencsik, A. W. Coleman, S. O.S. Debeer, H. Perron, and A. Moussa (2006)
J. Histochem. Cytochem. 54, 849-853
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Characterization and Application of a Novel RNA Aptamer against the Mouse Prion Protein..
S. Sekiya, K. Noda, F. Nishikawa, T. Yokoyama, P. K.R. Kumar, and S. Nishikawa (2006)
J. Biochem. 139, 383-390
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Atypical prion protein in sheep brain collected during the British scrapie-surveillance programme.
S. J. Everest, L. Thorne, D. A. Barnicle, J. C. Edwards, H. Elliott, R. Jackman, and J. Hope (2006)
J. Gen. Virol. 87, 471-477
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Potential Role of Soil in the Transmission of Prion Disease.
P. T. Schramm, C. J. Johnson, N. E. Mathews, D. McKenzie, J. M. Aiken, and J. A. Pedersen (2006)
Reviews in Mineralogy and Geochemistry 64, 135-152
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Computerized Morphometric Analysis of Pathological Prion Protein Deposition in Scrapie-Infected Hamster Brain.
O. A. Maximova, R. E. Taffs, K. L. Pomeroy, P. Piccardo, and D. M. Asher (2006)
J. Histochem. Cytochem. 54, 97-107
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A newly identified type of scrapie agent can naturally infect sheep with resistant PrP genotypes.
A. Le Dur, V. Beringue, O. Andreoletti, F. Reine, T. L. Lai, T. Baron, B. Bratberg, J.-L. Vilotte, P. Sarradin, S. L. Benestad, et al. (2005)
PNAS 102, 16031-16036
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An Aggregation-Specific Enzyme-Linked Immunosorbent Assay: Detection of Conformational Differences between Recombinant PrP Protein Dimers and PrPSc Aggregates.
T. Pan, B. Chang, P. Wong, C. Li, R. Li, S.-C. Kang, J. D. Robinson, A. R. Thompsett, P. Tein, S. Yin, et al. (2005)
J. Virol. 79, 12355-12364
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An Alternative Pretreatment Procedure in Animal Transmissible Spongiform Encephalopathies Diagnosis Using PrPsc Immunohistochemistry.
A. A. Bencsik, S. O.S. Debeer, and T. G.M. Baron (2005)
J. Histochem. Cytochem. 53, 1199-1202
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Overexpression of PrPC by Adenovirus-Mediated Gene Targeting Reduces Ischemic Injury in a Stroke Rat Model.
W.-C. Shyu, S.-Z. Lin, M.-F. Chiang, D.-C. Ding, K.-W. Li, S.-F. Chen, H.-I Yang, and H. Li (2005)
J. Neurosci. 25, 8967-8977
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Protease-resistant Prion Protein Amplification Reconstituted with Partially Purified Substrates and Synthetic Polyanions.
N. R. Deleault, J. C. Geoghegan, K. Nishina, R. Kascsak, R. A. Williamson, and S. Supattapone (2005)
J. Biol. Chem. 280, 26873-26879
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Amyloid Formation Modulates the Biological Activity of a Bacterial Protein.
S. Bieler, L. Estrada, R. Lagos, M. Baeza, J. Castilla, and C. Soto (2005)
J. Biol. Chem. 280, 26880-26885
   Abstract »    Full Text »    PDF »
High Incidence of Scrapie Induced by Repeated Injections of Subinfectious Prion Doses.
C. Jacquemot, C. Cuche, D. Dormont, and F. Lazarini (2005)
J. Virol. 79, 8904-8908
   Abstract »    Full Text »    PDF »
Molecular neurology of prion disease.
J Collinge (2005)
J. Neurol. Neurosurg. Psychiatry 76, 906-919
   Abstract »    Full Text »    PDF »
Expression of PrPC on cellular components of sheep blood.
S. Halliday, F. Houston, and N. Hunter (2005)
J. Gen. Virol. 86, 1571-1579
   Abstract »    Full Text »    PDF »
Comparative Analysis of the Human and Chicken Prion Protein Copper Binding Regions at pH 6.5.
L. Redecke, W. Meyer-Klaucke, M. Koker, J. Clos, D. Georgieva, N. Genov, H. Echner, H. Kalbacher, M. Perbandt, R. Bredehorst, et al. (2005)
J. Biol. Chem. 280, 13987-13992
   Abstract »    Full Text »    PDF »
Novel Antibody-Lectin Enzyme-Linked Immunosorbent Assay That Distinguishes Prion Proteins in Sporadic and Variant Cases of Creutzfeldt-Jakob Disease.
T. Pan, R. Li, B.-S. Wong, S.-C. Kang, J. Ironside, and M.-S. Sy (2005)
J. Clin. Microbiol. 43, 1118-1126
   Abstract »    Full Text »    PDF »
Biochemical Fingerprints of Prion Infection: Accumulations of Aberrant Full-Length and N-Terminally Truncated PrP Species Are Common Features in Mouse Prion Disease.
T. Pan, P. Wong, B. Chang, C. Li, R. Li, S.-C. Kang, T. Wisniewski, and M.-S. Sy (2005)
J. Virol. 79, 934-943
   Abstract »    Full Text »    PDF »
Glycosylation Deficiency at Either One of the Two Glycan Attachment Sites of Cellular Prion Protein Preserves Susceptibility to Bovine Spongiform Encephalopathy and Scrapie Infections.
E. Neuendorf, A. Weber, A. Saalmueller, H. Schatzl, K. Reifenberg, E. Pfaff, and M. H. Groschup (2004)
J. Biol. Chem. 279, 53306-53316
   Abstract »    Full Text »    PDF »
Ionic Strength and Transition Metals Control PrPSc Protease Resistance and Conversion-inducing Activity.
K. Nishina, S. Jenks, and S. Supattapone (2004)
J. Biol. Chem. 279, 40788-40794
   Abstract »    Full Text »    PDF »
Acute Formation of Protease-resistant Prion Protein Does Not Always Lead to Persistent Scrapie Infection in Vitro.
I. Vorberg, A. Raines, and S. A. Priola (2004)
J. Biol. Chem. 279, 29218-29225
   Abstract »    Full Text »    PDF »
Effects of Different Experimental Conditions on the PrPSc Core Generated by Protease Digestion: IMPLICATIONS FOR STRAIN TYPING AND MOLECULAR CLASSIFICATION OF CJD.
S. Notari, S. Capellari, A. Giese, I. Westner, A. Baruzzi, B. Ghetti, P. Gambetti, H. A. Kretzschmar, and P. Parchi (2004)
J. Biol. Chem. 279, 16797-16804
   Abstract »    Full Text »    PDF »
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.
S. Lezmi, S. Martin, S. Simon, E. Comoy, A. Bencsik, J.-P. Deslys, J. Grassi, M. Jeffrey, and T. Baron (2004)
J. Virol. 78, 3654-3662
   Abstract »    Full Text »    PDF »
Prions: proteins as genes and infectious entities.
R. B. Wickner, H. K. Edskes, B. T. Roberts, U. Baxa, M. M. Pierce, E. D. Ross, and A. Brachmann (2004)
Genes & Dev. 18, 470-485
   Full Text »    PDF »
Mutant PrPSc Conformers Induced by a Synthetic Peptide and Several Prion Strains.
P. Tremblay, H. L. Ball, K. Kaneko, D. Groth, R. S. Hegde, F. E. Cohen, S. J. DeArmond, S. B. Prusiner, and J. G. Safar (2004)
J. Virol. 78, 2088-2099
   Abstract »    Full Text »    PDF »
Games Played by Rogue Proteins in Prion Disorders and Alzheimer's Disease.
A. Aguzzi and C. Haass (2003)
Science 302, 814-818
   Abstract »    Full Text »    PDF »
Identification of Novel Proteinase K-resistant C-terminal Fragments of PrP in Creutzfeldt-Jakob Disease.
W.-Q. Zou, S. Capellari, P. Parchi, M.-S. Sy, P. Gambetti, and S. G. Chen (2003)
J. Biol. Chem. 278, 40429-40436
   Abstract »    Full Text »    PDF »
Prions and the Oral Cavity.
A.J. Smith, J. Bagg, J.W. Ironside, R.G. Will, and C. Scully (2003)
Journal of Dental Research 82, 769-775
   Abstract »    Full Text »    PDF »
Influence of pH on NMR Structure and Stability of the Human Prion Protein Globular Domain.
L. Calzolai and R. Zahn (2003)
J. Biol. Chem. 278, 35592-35596
   Abstract »    Full Text »    PDF »
A novel generation of heparan sulfate mimetics for the treatment of prion diseases.
K. T. Adjou, S. Simoneau, N. Sales, F. Lamoury, D. Dormont, D. Papy-Garcia, D. Barritault, J.-P. Deslys, and C. I. Lasmezas (2003)
J. Gen. Virol. 84, 2595-2603
   Abstract »    Full Text »    PDF »
Variant Creutzfeldt-Jakob disease: pathology, epidemiology, and public health implications.
C. R Trevitt and P. N Singh (2003)
Am. J. Clinical Nutrition 78, 651S-656
   Abstract »    Full Text »    PDF »
Evaluation of Quinacrine Treatment for Prion Diseases.
A. Barret, F. Tagliavini, G. Forloni, C. Bate, M. Salmona, L. Colombo, A. De Luigi, L. Limido, S. Suardi, G. Rossi, et al. (2003)
J. Virol. 77, 8462-8469
   Abstract »    Full Text »    PDF »
Follicular Dendritic Cell Dedifferentiation by Treatment with an Inhibitor of the Lymphotoxin Pathway Dramatically Reduces Scrapie Susceptibility.
N. A. Mabbott, J. Young, I. McConnell, and M. E. Bruce (2003)
J. Virol. 77, 6845-6854
   Abstract »    Full Text »    PDF »
Introduction to the transmissible spongiform encephalopathies or prion diseases.
B. Chesebro (2003)
Br. Med. Bull. 66, 1-20
   Abstract »    Full Text »    PDF »
Sporadic and familial CJD: classification and characterisation.
P. Gambetti, Q. Kong, W. Zou, P. Parchi, and S. G Chen (2003)
Br. Med. Bull. 66, 213-239
   Abstract »    Full Text »    PDF »
Diagnosis of prion diseases.
E. Kubler, B. Oesch, and A. J Raeber (2003)
Br. Med. Bull. 66, 267-279
   Abstract »    Full Text »    PDF »
CD21-Positive Follicular Dendritic Cells: A Possible Source of PrPSc in Lymph Node Macrophages of Scrapie-Infected Sheep.
L. M. Herrmann, W. P. Cheevers, W. C. Davis, D. P. Knowles, and K. I. O'Rourke (2003)
Am. J. Pathol. 162, 1075-1081
   Abstract »    Full Text »    PDF »
Accumulation of Pathogenic Prion Protein (PrPSc) in Nervous and Lymphoid Tissues of Sheep with Subclinical Scrapie.
C. Ersdal, M. J. Ulvund, S. L. Benestad, and M. A. Tranulis (2003)
Vet. Pathol. 40, 164-174
   Abstract »    Full Text »    PDF »
Detection of PrPsc in Samples Presenting a Very Advanced Degree of Autolysis (BSE Liquid State) by Immunocytochemistry.
E. Monleon, M. Monzon, P. Hortells, A. Vargas, and J. J. Badiola (2003)
J. Histochem. Cytochem. 51, 15-18
   Abstract »    Full Text »    PDF »
Drug therapy in human and experimental transmissible spongiform encephalopathy.
P. Brown (2002)
Neurology 58, 1720-1725
   Abstract »    Full Text »    PDF »
Temporary Blockade of the Tumor Necrosis Factor Receptor Signaling Pathway Impedes the Spread of Scrapie to the Brain.
N. A. Mabbott, G. McGovern, M. Jeffrey, and M. E. Bruce (2002)
J. Virol. 76, 5131-5139
   Abstract »    Full Text »    PDF »
Transmissible Spongiform Encephalopathy Diagnosis Using PrPsc Immunohistochemistry on Fixed but Previously Frozen Brain Samples.
S. O.S. Debeer, T. G.M. Baron, and A. A. Bencsik (2002)
J. Histochem. Cytochem. 50, 611-616
   Abstract »    Full Text »    PDF »
Inaugural Article: Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein.
U. Baxa, V. Speransky, A. C. Steven, and R. B. Wickner (2002)
PNAS 99, 5253-5260
   Abstract »    Full Text »    PDF »
PrPSc Is Not Detected in Peripheral Blood Leukocytes of Scrapie-Infected Sheep: Determining the Limit of Sensitivity by Immunohistochemistry.
L. M. Herrmann, T. V. Baszler, D. P. Knowles, and W. P. Cheevers (2002)
Clin. Vaccine Immunol. 9, 499-502
   Abstract »    Full Text »    PDF »
Distribution and accumulation of PrP in gut-associated and peripheral lymphoid tissue of scrapie-affected Suffolk sheep.
R. Heggebo, C. McL. Press, G. Gunnes, L. Gonzalez, and M. Jeffrey (2002)
J. Gen. Virol. 83, 479-489
   Abstract »    Full Text »    PDF »
Migrating intestinal dendritic cells transport PrPSc from the gut.
F.-P. Huang, C. F. Farquhar, N. A. Mabbott, M. E. Bruce, and G. G. MacPherson (2002)
J. Gen. Virol. 83, 267-271
   Abstract »    Full Text »    PDF »
A Critical Review of the Nature of the Spongiform Encephalopathy Agent: Protein Theory Versus Virus Theory.
H. Narang (2002)
Experimental Biology and Medicine 227, 4-19
   Abstract »    Full Text »    PDF »
Comparison of Histological Lesions and Immunohistochemical Staining of Proteinase-resistant Prion Protein in a Naturally Occurring Spongiform Encephalopathy of Free-ranging Mule Deer (Odocoileus hemionus) with Those of Chronic Wasting Disease of Captive Mule Deer.
T. R. Spraker, R. R. Zink, B. A. Cummings, M. A. Wild, M. W. Miller, and K. I. O'Rourke (2002)
Vet. Pathol. 39, 110-119
   Abstract »    Full Text »    PDF »
Immunohistochemistry of PrPsc Within Bovine Spongiform Encephalopathy Brain Samples with Graded Autolysis.
S. O.S. Debeer, T. G.M. Baron, and A. A. Bencsik (2001)
J. Histochem. Cytochem. 49, 1519-1524
   Abstract »    Full Text »    PDF »
The molecular pathology of CJD: old and new variants.
G S Jackson and J Collinge (2001)
Mol. Pathol. 54, 393-399
   Abstract »    Full Text »    PDF »
Deletion of {beta}-Strand and {alpha}-Helix Secondary Structure in Normal Prion Protein Inhibits Formation of Its Protease-Resistant Isoform.
I. Vorberg, K. Chan, and S. A. Priola (2001)
J. Virol. 75, 10024-10032
   Abstract »    Full Text »    PDF »
Early Spread of Scrapie from the Gastrointestinal Tract to the Central Nervous System Involves Autonomic Fibers of the Splanchnic and Vagus Nerves.
P. A. McBride, W. J. Schulz-Schaeffer, M. Donaldson, M. Bruce, H. Diringer, H. A. Kretzschmar, and M. Beekes (2001)
J. Virol. 75, 9320-9327
   Abstract »    Full Text »    PDF »
The immunobiology of TSE diseases.
N. A. Mabbott and M. E. Bruce (2001)
J. Gen. Virol. 82, 2307-2318
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Prion Filament Networks in [Ure3] Cells of Saccharomyces cerevisiae.
V. V. Speransky, K. L. Taylor, H. K. Edskes, R. B. Wickner, and A. C. Steven (2001)
J. Cell Biol. 153, 1327-1336
   Abstract »    Full Text »    PDF »
Prion Proteins with Different Conformations Accumulate in Gerstmann-Straussler-Scheinker Disease Caused by A117V and F198S Mutations.
P. Piccardo, J. J. Liepnieks, A. William, S. R. Dlouhy, M. R. Farlow, K. Young, D. Nochlin, T. D. Bird, R. R. Nixon, M. J. Ball, et al. (2001)
Am. J. Pathol. 158, 2201-2207
   Abstract »    Full Text »    PDF »
Partial dissociation of PrPSc deposition and vacuolation in the brains of scrapie and BSE experimentally affected goats.
J. Foster, W. Goldmann, D. Parnham, A. Chong, and N. Hunter (2001)
J. Gen. Virol. 82, 267-273
   Abstract »    Full Text »
Distribution of prion protein in the ileal Peyer's patch of scrapie-free lambs and lambs naturally and experimentally exposed to the scrapie agent.
R. Heggebø, C. McL. Press, G. Gunnes, K. Inge Lie, M. A. Tranulis, M. Ulvund, M. H. Groschup, and T. Landsverk (2000)
J. Gen. Virol. 81, 2327-2337
   Abstract »    Full Text »
Opposite Effects of Dextran Sulfate 500, the Polyene Antibiotic MS-8209, and Congo Red on Accumulation of the Protease-Resistant Isoform of PrP in the Spleens of Mice Inoculated Intraperitoneally with the Scrapie Agent.
V. Beringue, K. T. Adjou, F. Lamoury, T. Maignien, J.-P. Deslys, R. Race, and D. Dormont (2000)
J. Virol. 74, 5432-5440
   Abstract »    Full Text »    PDF »
Ultrasensitive detection of pathological prion protein aggregates by dual-color scanning for intensely fluorescent targets.
J. Bieschke, A. Giese, W. Schulz-Schaeffer, I. Zerr, S. Poser, M. Eigen, and H. Kretzschmar (2000)
PNAS 97, 5468-5473
   Abstract »    Full Text »    PDF »
Tumor Necrosis Factor Alpha-Deficient, but Not Interleukin-6-Deficient, Mice Resist Peripheral Infection with Scrapie.
N. A. Mabbott, A. Williams, C. F. Farquhar, M. Pasparakis, G. Kollias, and M. E. Bruce (2000)
J. Virol. 74, 3338-3344
   Abstract »    Full Text »    PDF »
Prions in Saccharomyces and Podospora spp.: Protein-Based Inheritance.
R. B. Wickner, K. L. Taylor, H. K. Edskes, M.-L. Maddelein, H. Moriyama, and B. T. Roberts (1999)
Microbiol. Mol. Biol. Rev. 63, 844-861
   Abstract »    Full Text »    PDF »
Pathogenesis of the oral route of infection of mice with scrapie and bovine spongiform encephalopathy agents.
T. Maignien, C. I. Lasmé zas, V. Beringue, D. Dormont, and J.-P. Deslys (1999)
J. Gen. Virol. 80, 3035-3042
   Abstract »    Full Text »
PrP genotypes of captive and free-ranging Rocky Mountain elk (Cervus elaphus nelsoni) with chronic wasting disease.
K. I. O'Rourke, T. E. Besser, M. W. Miller, T. F. Cline, T. R. Spraker, A. L. Jenny, M. A. Wild, G. L. Zebarth, and E. S. Williams (1999)
J. Gen. Virol. 80, 2765-2679
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Two Prion-Inducing Regions of Ure2p Are Nonoverlapping.
M.-L. Maddelein and R. B. Wickner (1999)
Mol. Cell. Biol. 19, 4516-4524
   Abstract »    Full Text »    PDF »
Effectiveness of Polyene Antibiotics in Treatment of Transmissible Spongiform Encephalopathy in Transgenic Mice Expressing Syrian Hamster PrP Only in Neurons.
R. Demaimay, R. Race, and B. Chesebro (1999)
J. Virol. 73, 3511-3513
   Abstract »    Full Text »    PDF »
The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments.
H. K. Edskes, V. T. Gray, and R. B. Wickner (1999)
PNAS 96, 1498-1503
   Abstract »    Full Text »    PDF »
1755 and all that: a historical primer of transmissible spongiform encephalopathy.
P. Brown and R. Bradley (1998)
BMJ 317, 1688-1692
   Full Text »
Prions.
S. B. Prusiner (1998)
PNAS 95, 13363-13383
   Abstract »    Full Text »    PDF »
Endogenous Proteolytic Cleavage of Normal and Disease-Associated Isoforms of the Human Prion Protein in Neural and Non-Neural Tissues.
A. Jimenez-Huete, P. M. J. Lievens, R. Vidal, P. Piccardo, B. Ghetti, F. Tagliavini, B. Frangione, and F. Prelli (1998)
Am. J. Pathol. 153, 1561-1572
   Abstract »    Full Text »    PDF »
Reversibility of Scrapie Inactivation Is Enhanced by Copper.
D. McKenzie, J. Bartz, J. Mirwald, D. Olander, R. Marsh, and J. Aiken (1998)
J. Biol. Chem. 273, 25545-25547
   Abstract »    Full Text »    PDF »
Monoclonal Antibody F89/160.1.5 Defines a Conserved Epitope on the Ruminant Prion Protein.
K. I. O'Rourke, T. V. Baszler, J. M. Miller, T. R. Spraker, I. Sadler-Riggleman, and D. P. Knowles (1998)
J. Clin. Microbiol. 36, 1750-1755
   Abstract »    Full Text »    PDF »
Prion Protein Expression in Human Leukocyte Differentiation.
V. C. Dodelet and N. R. Cashman (1998)
Blood 91, 1556-1561
   Abstract »    Full Text »    PDF »
Transmissible Spongiform Encephalopathies.
A. M. Haywood (1997)
N. Engl. J. Med. 337, 1821-1828
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Commentary Review: Prion Diseases.
A. K. Shetty and R. W. Steele (1997)
Clinical Pediatrics 36, 1-7
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Molecular Biology and Genetics of Prion Diseases.
S.B. Prusiner (1996)
Cold Spring Harb Symp Quant Biol 61, 473-493
   Abstract »    PDF »
Prions of Yeast, [PSI] and [URE3], as Models for Neurodegenerative Diseases.
R.B. Wickner, D.C. Masison, H.K. Edskes, and M.-L. Maddelein (1996)
Cold Spring Harb Symp Quant Biol 61, 541-550
   Abstract »    PDF »
Prion-Inducing Domain of Yeast Ure2p and Protease Resistance of Ure2p in Prion-Containing Cells.
D. C. Masison and R. B. Wickner (1995)
Science 270, 93-95
   Abstract »    PDF »
Prion Protein Isoforms, a Convergence of Biological and Structural Investigations.
M. A. Baldwin, F. E. Cohen, and S. B. Prusiner (1995)
J. Biol. Chem. 270, 19197-19200
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A 60-kDa Prion Protein (PrP) with Properties of Both the Normal and Scrapie-associated Forms of PrP.
S. A. Priola, B. Caughey, K. Wehrly, and B. Chesebro (1995)
J. Biol. Chem. 270, 3299-3305
   Abstract »    Full Text »    PDF »
Genetic and Infectious Prion Diseases.
S. B. Prusiner (1993)
Arch Neurol 50, 1129-1153
   Abstract »    PDF »



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