| Year |
Citation |
Score |
| 2024 |
Shoup D, Priola SA. Grp78 destabilization of infectious prions is strain specific and modified by multiple factors including accessory chaperones and pH. The Journal of Biological Chemistry. 107346. PMID 38718859 DOI: 10.1016/j.jbc.2024.107346 |
0.488 |
|
| 2024 |
Ward A, Jessop F, Faris R, Hollister J, Shoup D, Race B, Bosio CM, Priola SA. The PINK1/Parkin pathway of mitophagy exerts a protective effect during prion disease. Plos One. 19: e0298095. PMID 38394123 DOI: 10.1371/journal.pone.0298095 |
0.413 |
|
| 2023 |
Baune C, Groveman BR, Hughson AG, Thomas T, Twardoski B, Priola S, Chesebro B, Race B. Efficacy of Wex-cide 128 disinfectant against multiple prion strains. Plos One. 18: e0290325. PMID 37616303 DOI: 10.1371/journal.pone.0290325 |
0.48 |
|
| 2023 |
Shoup D, Priola SA. Full-length prion protein incorporated into prion aggregates is a marker for prion strain specific destabilization of aggregate structure following cellular uptake. Journal of Biochemistry. PMID 37099550 DOI: 10.1093/jb/mvad032 |
0.462 |
|
| 2022 |
Shoup D, Priola SA. Cell biology of prion strains in vivo and in vitro. Cell and Tissue Research. PMID 35107622 DOI: 10.1007/s00441-021-03572-y |
0.542 |
|
| 2021 |
Shoup D, Priola SA. The Size and Stability of Infectious Prion Aggregates Fluctuate Dynamically during Cellular Uptake and Disaggregation. Biochemistry. PMID 33497187 DOI: 10.1021/acs.biochem.0c00923 |
0.597 |
|
| 2020 |
Ward A, Hollister JR, McNally K, Ritchie DL, Zanusso G, Priola SA. Transmission characteristics of heterozygous cases of Creutzfeldt-Jakob disease with variable abnormal prion protein allotypes. Acta Neuropathologica Communications. 8: 83. PMID 32517816 DOI: 10.1186/S40478-020-00958-X |
0.574 |
|
| 2019 |
Ward A, Hollister JR, Choi YP, Race B, Williams K, Shoup DW, Moore RA, Priola SA. Altered distribution, aggregation, and protease resistance of cellular prion protein following intracranial inoculation. Plos One. 14: e0219457. PMID 31291644 DOI: 10.1371/Journal.Pone.0219457 |
0.562 |
|
| 2018 |
Moore RA, Ward A, Race B, Priola SA. Processing of high-titer prions for mass spectrometry inactivates prion infectivity. Biochimica Et Biophysica Acta. Proteins and Proteomics. 1866: 1174-1180. PMID 30282615 DOI: 10.1016/J.Bbapap.2018.08.004 |
0.477 |
|
| 2018 |
Priola SA. Cell biology of prion infection. Handbook of Clinical Neurology. 153: 45-68. PMID 29887152 DOI: 10.1016/B978-0-444-63945-5.00003-9 |
0.429 |
|
| 2017 |
Priola SA. Cell Biology Approaches to Studying Prion Diseases. Methods in Molecular Biology (Clifton, N.J.). 1658: 83-94. PMID 28861784 DOI: 10.1007/978-1-4939-7244-9_7 |
0.641 |
|
| 2017 |
Fehlinger A, Wolf H, Hossinger A, Duernberger Y, Pleschka C, Riemschoss K, Liu S, Bester R, Paulsen L, Priola SA, Groschup MH, Schätzl HM, Vorberg IM. Prion strains depend on different endocytic routes for productive infection. Scientific Reports. 7: 6923. PMID 28761068 DOI: 10.1038/S41598-017-07260-2 |
0.551 |
|
| 2017 |
Wang F, Wang X, Orrú CD, Groveman BR, Surewicz K, Abskharon R, Imamura M, Yokoyama T, Kim YS, Vander Stel KJ, Sinniah K, Priola SA, Surewicz WK, Caughey B, Ma J. Self-propagating, protease-resistant, recombinant prion protein conformers with or without in vivo pathogenicity. Plos Pathogens. 13: e1006491. PMID 28704563 DOI: 10.1371/Journal.Ppat.1006491 |
0.552 |
|
| 2017 |
Faris R, Moore RA, Ward A, Sturdevant DE, Priola SA. Mitochondrial respiration is impaired during late stage hamster prion infection. Journal of Virology. PMID 28659480 DOI: 10.1128/Jvi.00524-17 |
0.397 |
|
| 2017 |
Faris R, Moore RA, Ward A, Race B, Dorward DW, Hollister JR, Fischer ER, Priola SA. Cellular prion protein is present in mitochondria of healthy mice. Scientific Reports. 7: 41556. PMID 28148964 DOI: 10.1038/Srep41556 |
0.444 |
|
| 2016 |
Marshall KE, Hughson A, Vascellari S, Priola SA, Sakudo A, Onodera T, Baron GS. PrP knockout cells expressing transmembrane PrP resist prion infection. Journal of Virology. PMID 27847358 DOI: 10.1128/Jvi.01686-16 |
0.59 |
|
| 2016 |
Moore RA, Choi YP, Head MW, Ironside JW, Faris R, Ritchie DL, Zanusso G, Priola SA. THE RELATIVE ABUNDANCE OF APOE AND Aβ1-42 ASSOCIATED WITH ABNORMAL PRION PROTEIN DIFFERS BETWEEN CREUTZFELDT-JAKOB DISEASE SUBTYPES. Journal of Proteome Research. PMID 27597180 DOI: 10.1021/Acs.Jproteome.6B00633 |
0.467 |
|
| 2016 |
Moore RA, Head MW, Ironside JW, Ritchie DL, Zanusso G, Choi YP, Priola SA. Correction: The Distribution of Prion Protein Allotypes Differs Between Sporadic and Iatrogenic Creutzfeldt-Jakob Disease Patients. Plos Pathogens. 12: e1005496. PMID 26954665 DOI: 10.1371/journal.ppat.1005496 |
0.322 |
|
| 2016 |
Moore RA, Head MW, Ironside JW, Ritchie DL, Zanusso G, Pyo Choi Y, Priola SA. The Distribution of Prion Protein Allotypes Differs Between Sporadic and Iatrogenic Creutzfeldt-Jakob Disease Patients. Plos Pathogens. 12: e1005416. PMID 26840342 DOI: 10.1371/Journal.Ppat.1005416 |
0.451 |
|
| 2015 |
Skinner PJ, Kim HO, Bryant D, Kinzel NJ, Reilly C, Priola SA, Ward AE, Goodman PA, Olson K, Seelig DM. Treatment of Prion Disease with Heterologous Prion Proteins. Plos One. 10: e0131993. PMID 26134409 DOI: 10.1371/Journal.Pone.0131993 |
0.576 |
|
| 2015 |
Moore RA, Faris R, Priola SA. Proteomics applications in prion biology and structure. Expert Review of Proteomics. 12: 171-84. PMID 25795148 DOI: 10.1586/14789450.2015.1019481 |
0.507 |
|
| 2014 |
Choi YP, Head MW, Ironside JW, Priola SA. Uptake and degradation of protease-sensitive and -resistant forms of abnormal human prion protein aggregates by human astrocytes. The American Journal of Pathology. 184: 3299-307. PMID 25280631 DOI: 10.1016/J.Ajpath.2014.08.005 |
0.64 |
|
| 2014 |
Moore RA, Sturdevant DE, Chesebro B, Priola SA. Proteomics analysis of amyloid and nonamyloid prion disease phenotypes reveals both common and divergent mechanisms of neuropathogenesis. Journal of Proteome Research. 13: 4620-34. PMID 25140793 DOI: 10.1021/Pr500329W |
0.558 |
|
| 2013 |
Choi YP, Priola SA. A specific population of abnormal prion protein aggregates is preferentially taken up by cells and disaggregated in a strain-dependent manner. Journal of Virology. 87: 11552-61. PMID 23966386 DOI: 10.1128/Jvi.01484-13 |
0.655 |
|
| 2013 |
Timmes AG, Moore RA, Fischer ER, Priola SA. Recombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivity. Plos One. 8: e71081. PMID 23936256 DOI: 10.1371/Journal.Pone.0071081 |
0.489 |
|
| 2013 |
Priola SA, Ward AE, McCall SA, Trifilo M, Choi YP, Solforosi L, Williamson RA, Cruite JT, Oldstone MB. Lack of prion infectivity in fixed heart tissue from patients with Creutzfeldt-Jakob disease or amyloid heart disease. Journal of Virology. 87: 9501-10. PMID 23785217 DOI: 10.1128/Jvi.00692-13 |
0.425 |
|
| 2012 |
Chianini F, Fernández-Borges N, Vidal E, Gibbard L, Pintado B, de Castro J, Priola SA, Hamilton S, Eaton SL, Finlayson J, Pang Y, Steele P, Reid HW, Dagleish MP, Castilla J. Rabbits are not resistant to prion infection. Proceedings of the National Academy of Sciences of the United States of America. 109: 5080-5. PMID 22416127 DOI: 10.1073/Pnas.1120076109 |
0.52 |
|
| 2012 |
Leblanc P, Hasenkrug K, Ward A, Myers L, Messer RJ, Alais S, Timmes A, Priola SA, Priola S. Co-infection with the friend retrovirus and mouse scrapie does not alter prion disease pathogenesis in susceptible mice. Plos One. 7: e30872. PMID 22295118 DOI: 10.1371/Journal.Pone.0030872 |
0.6 |
|
| 2011 |
Moore RA, Timmes AG, Wilmarth PA, Safronetz D, Priola SA. Identification and removal of proteins that co-purify with infectious prion protein improves the analysis of its secondary structure. Proteomics. 11: 3853-65. PMID 21805638 DOI: 10.1002/Pmic.201100253 |
0.463 |
|
| 2010 |
Moore RA, Timmes A, Wilmarth PA, Priola SA. Comparative profiling of highly enriched 22L and Chandler mouse scrapie prion protein preparations. Proteomics. 10: 2858-69. PMID 20518029 DOI: 10.1002/Pmic.201000104 |
0.521 |
|
| 2009 |
Race B, Meade-White KD, Miller MW, Barbian KD, Rubenstein R, LaFauci G, Cervenakova L, Favara C, Gardner D, Long D, Parnell M, Striebel J, Priola SA, Ward A, Williams ES, et al. Susceptibilities of nonhuman primates to chronic wasting disease. Emerging Infectious Diseases. 15: 1366-76. PMID 19788803 DOI: 10.3201/Eid1509.090253 |
0.463 |
|
| 2009 |
Priola SA, McNally KL. The role of the prion protein membrane anchor in prion infection. Prion. 3: 134-8. PMID 19786843 DOI: 10.4161/Pri.3.3.9771 |
0.579 |
|
| 2009 |
McNally KL, Ward AE, Priola SA. Cells expressing anchorless prion protein are resistant to scrapie infection. Journal of Virology. 83: 4469-75. PMID 19225008 DOI: 10.1128/Jvi.02412-08 |
0.64 |
|
| 2009 |
Moore RA, Taubner LM, Priola SA. Prion protein misfolding and disease. Current Opinion in Structural Biology. 19: 14-22. PMID 19157856 DOI: 10.1016/J.Sbi.2008.12.007 |
0.577 |
|
| 2008 |
Greil CS, Vorberg IM, Ward AE, Meade-White KD, Harris DA, Priola SA. Acute cellular uptake of abnormal prion protein is cell type and scrapie-strain independent. Virology. 379: 284-93. PMID 18692214 DOI: 10.1016/J.Virol.2008.07.006 |
0.509 |
|
| 2008 |
Caetano FA, Lopes MH, Hajj GN, Machado CF, Pinto Arantes C, Magalhães AC, Vieira Mde P, Américo TA, Massensini AR, Priola SA, Vorberg I, Gomez MV, Linden R, Prado VF, Martins VR, et al. Endocytosis of prion protein is required for ERK1/2 signaling induced by stress-inducible protein 1. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 28: 6691-702. PMID 18579743 DOI: 10.1523/Jneurosci.1701-08.2008 |
0.434 |
|
| 2008 |
Atarashi R, Wilham JM, Christensen L, Hughson AG, Moore RA, Johnson LM, Onwubiko HA, Priola SA, Caughey B. Simplified ultrasensitive prion detection by recombinant PrP conversion with shaking. Nature Methods. 5: 211-2. PMID 18309304 DOI: 10.1038/Nmeth0308-211 |
0.344 |
|
| 2007 |
Dirikoc S, Priola SA, Marella M, Zsürger N, Chabry J. Nonpsychoactive cannabidiol prevents prion accumulation and protects neurons against prion toxicity. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 27: 9537-44. PMID 17804615 DOI: 10.1523/Jneurosci.1942-07.2007 |
0.562 |
|
| 2007 |
Caughey WS, Priola SA, Kocisko DA, Raymond LD, Ward A, Caughey B. Cyclic tetrapyrrole sulfonation, metals, and oligomerization in antiprion activity. Antimicrobial Agents and Chemotherapy. 51: 3887-94. PMID 17709470 DOI: 10.1128/Aac.01599-06 |
0.404 |
|
| 2007 |
Atarashi R, Moore RA, Sim VL, Hughson AG, Dorward DW, Onwubiko HA, Priola SA, Caughey B. Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. Nature Methods. 4: 645-50. PMID 17643109 DOI: 10.1038/Nmeth1066 |
0.51 |
|
| 2007 |
Moore RA, Hayes SF, Fischer ER, Priola SA. Amyloid formation via supramolecular peptide assemblies. Biochemistry. 46: 7079-87. PMID 17521170 DOI: 10.1021/Bi700247Y |
0.334 |
|
| 2006 |
Priola SA, Vorberg I. Molecular aspects of disease pathogenesis in the transmissible spongiform encephalopathies. Molecular Biotechnology. 33: 71-88. PMID 16691009 DOI: 10.1385/Mb:33:1:71 |
0.445 |
|
| 2006 |
Moore RA, Herzog C, Errett J, Kocisko DA, Arnold KM, Hayes SF, Priola SA. Octapeptide repeat insertions increase the rate of protease-resistant prion protein formation. Protein Science : a Publication of the Protein Society. 15: 609-19. PMID 16452616 DOI: 10.1110/Ps.051822606 |
0.563 |
|
| 2006 |
Takemura K, Wang P, Vorberg I, Surewicz W, Priola SA, Kanthasamy A, Pottathil R, Chen SG, Sreevatsan S. DNA aptamers that bind to PrP(C) and not PrP(Sc) show sequence and structure specificity. Experimental Biology and Medicine (Maywood, N.J.). 231: 204-14. PMID 16446497 DOI: 10.1177/153537020623100211 |
0.385 |
|
| 2005 |
Moore RA, Vorberg I, Priola SA. Species barriers in prion diseases--brief review. Archives of Virology. Supplementum. 187-202. PMID 16355873 DOI: 10.1007/3-211-29981-5_15 |
0.524 |
|
| 2005 |
Chesebro B, Trifilo M, Race R, Meade-White K, Teng C, LaCasse R, Raymond L, Favara C, Baron G, Priola S, Caughey B, Masliah E, Oldstone M. Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science (New York, N.Y.). 308: 1435-9. PMID 15933194 DOI: 10.1126/Science.1110837 |
0.525 |
|
| 2004 |
Priola SA, Vorberg I. Identification of possible animal origins of prion disease in human beings. Lancet (London, England). 363: 2013-4. PMID 15207949 DOI: 10.1016/S0140-6736(04)16487-8 |
0.372 |
|
| 2004 |
Priola SA, Vorberg I. Molecular aspects of disease pathogenesis in the transmissible spongiform encephalopathies. Methods in Molecular Biology (Clifton, N.J.). 268: 517-40. PMID 15156065 DOI: 10.1385/1-59259-766-1:517 |
0.445 |
|
| 2004 |
Vorberg I, Raines A, Priola SA. Acute formation of protease-resistant prion protein does not always lead to persistent scrapie infection in vitro. The Journal of Biological Chemistry. 279: 29218-25. PMID 15133048 DOI: 10.1074/Jbc.M402576200 |
0.666 |
|
| 2004 |
Vorberg I, Raines A, Story B, Priola SA. Susceptibility of common fibroblast cell lines to transmissible spongiform encephalopathy agents. The Journal of Infectious Diseases. 189: 431-9. PMID 14745700 DOI: 10.1086/381166 |
0.484 |
|
| 2004 |
Lawson VA, Priola SA, Meade-White K, Lawson M, Chesebro B. Flexible N-terminal region of prion protein influences conformation of protease-resistant prion protein isoforms associated with cross-species scrapie infection in vivo and in vitro. The Journal of Biological Chemistry. 279: 13689-95. PMID 14736880 DOI: 10.1074/Jbc.M303697200 |
0.577 |
|
| 2003 |
Priola SA, Raines A, Caughey W. Prophylactic and therapeutic effects of phthalocyanine tetrasulfonate in scrapie-infected mice Journal of Infectious Diseases. 188: 699-705. PMID 12934186 DOI: 10.1086/377310 |
0.466 |
|
| 2003 |
Priola SA, Chesebro B, Caughey B. Biomedicine. A view from the top--prion diseases from 10,000 feet. Science (New York, N.Y.). 300: 917-9. PMID 12738843 DOI: 10.1126/Science.1085920 |
0.461 |
|
| 2003 |
Vorberg I, Groschup MH, Pfaff E, Priola SA. Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform. Journal of Virology. 77: 2003-9. PMID 12525634 DOI: 10.1128/Jvi.77.3.2003-2009.2003 |
0.531 |
|
| 2002 |
Vorberg I, Priola SA. Molecular basis of scrapie strain glycoform variation. The Journal of Biological Chemistry. 277: 36775-81. PMID 12138171 DOI: 10.1074/Jbc.M206865200 |
0.614 |
|
| 2002 |
Priola SA. Therapeutic Potential of Prion Protein Peptides in the Transmissible Spongiform Encephalopathies Labmedicine. 33: 369-373. DOI: 10.1309/J7Yv-8Va1-R6Yc-0T5Q |
0.531 |
|
| 2001 |
Hanan E, Priola SA, Solomon B. Antiaggregating antibody raised against human PrP 106-126 recognizes pathological and normal isoforms of the whole prion protein. Cellular and Molecular Neurobiology. 21: 693-703. PMID 12043842 DOI: 10.1023/A:1015199904354 |
0.473 |
|
| 2001 |
Priola SA, Lawson VA. Glycosylation influences cross-species formation of protease-resistant prion protein Embo Journal. 20: 6692-6699. PMID 11726505 DOI: 10.1093/Emboj/20.23.6692 |
0.584 |
|
| 2001 |
Vorberg I, Chan K, Priola SA. Deletion of β-Strand and α-Helix Secondary Structure in Normal Prion Protein Inhibits Formation of Its Protease-Resistant Isoform Journal of Virology. 75: 10024-10032. PMID 11581371 DOI: 10.1128/Jvi.75.21.10024-10032.2001 |
0.527 |
|
| 2001 |
Lawson VA, Priola SA, Wehrly K, Chesebro B. N-terminal Truncation of Prion Protein Affects Both Formation and Conformation of Abnormal Protease-resistant Prion Protein Generated in Vitro Journal of Biological Chemistry. 276: 35265-35271. PMID 11466311 DOI: 10.1074/Jbc.M103799200 |
0.589 |
|
| 2001 |
Priola SA, Chabry J, Chan K. Efficient Conversion of Normal Prion Protein (PrP) by Abnormal Hamster PrP Is Determined by Homology at Amino Acid Residue 155 Journal of Virology. 75: 4673-4680. PMID 11312338 DOI: 10.1128/Jvi.75.10.4673-4680.2001 |
0.567 |
|
| 2000 |
Horiuchi M, Priola SA, Chabry J, Caughey B. Interactions between heterologous forms of prion protein: binding, inhibition of conversion, and species barriers. Proceedings of the National Academy of Sciences of the United States of America. 97: 5836-41. PMID 10811921 DOI: 10.1073/Pnas.110523897 |
0.546 |
|
| 2000 |
Priola SA, Raines A, Caughey WS. Porphyrin and phthalocyanine antiscrapie compounds Science. 287: 1503-1506. PMID 10688802 DOI: 10.1126/Science.287.5457.1503 |
0.431 |
|
| 1999 |
Caughey B, Raymond GJ, Priola SA, Kocisko DA, Race RE, Bessen RA, Lansbury PT, Chesebro B. Methods for studying prion protein (PrP) metabolism and the formation of protease-resistant PrP in cell culture and cell-free systems. An update. Molecular Biotechnology. 13: 45-55. PMID 10934521 DOI: 10.1385/Mb:13:1:45 |
0.654 |
|
| 1999 |
Priola SA, Caughey B, Caughey WS. Novel therapeutic uses for porphyrins and phthalocyanines in the transmissible spongiform encephalopathies: Commentary Current Opinion in Microbiology. 2: 563-566. PMID 10617376 DOI: 10.1016/S1369-5274(99)00020-X |
0.3 |
|
| 1999 |
Chabry J, Priola SA, Wehrly K, Nishio J, Hope J, Chesebro B. Species-independent inhibition of abnormal prion protein (PrP) formation by a peptide containing a conserved PrP sequence. Journal of Virology. 73: 6245-50. PMID 10400714 DOI: 10.1128/Jvi.73.8.6245-6250.1999 |
0.589 |
|
| 1998 |
Priola SA, Chesebro B. Abnormal properties of prion protein with insertional mutations in different cell types. The Journal of Biological Chemistry. 273: 11980-5. PMID 9565627 DOI: 10.1074/Jbc.273.19.11980 |
0.592 |
|
| 1997 |
Raeber AJ, Race RE, Brandner S, Priola SA, Sailer A, Bessen RA, Mucke L, Manson J, Aguzzi A, Oldstone MB, Weissmann C, Chesebro B. Astrocyte-specific expression of hamster prion protein (PrP) renders PrP knockout mice susceptible to hamster scrapie. The Embo Journal. 16: 6057-65. PMID 9321385 DOI: 10.1093/Emboj/16.20.6057 |
0.532 |
|
| 1997 |
Raymond GJ, Hope J, Kocisko DA, Priola SA, Raymond LD, Bossers A, Ironside J, Will RG, Chen SG, Petersen RB, Gambetti P, Rubenstein R, Smits MA, Lansbury PT, Caughey B. Molecular assessment of the potential transmissibilities of BSE and scrapie to humans. Nature. 388: 285-8. PMID 9230438 DOI: 10.1038/40876 |
0.553 |
|
| 1996 |
Priola SA. Similar protein signatures for BSE and vCJD Nature Medicine. 2: 1303-1304. PMID 8946821 DOI: 10.1038/Nm1296-1303 |
0.409 |
|
| 1995 |
Priola SA, Caughey B. Inhibition of scrapie-associated PrP accumulation. Probing the role of glycosaminoglycans in amyloidogenesis. Molecular Neurobiology. 8: 113-20. PMID 7999307 DOI: 10.1007/Bf02780661 |
0.568 |
|
| 1995 |
Priola SA, Caughey B, Wehrly K, Chesebro B. A 60-kDa prion protein (PrP) with properties of both the normal and scrapie-associated forms of PrP. The Journal of Biological Chemistry. 270: 3299-305. PMID 7852415 DOI: 10.1074/Jbc.270.7.3299 |
0.65 |
|
| 1995 |
Kocisko DA, Priola SA, Raymond GJ, Chesebro B, Lansbury PT, Caughey B. Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier. Proceedings of the National Academy of Sciences of the United States of America. 92: 3923-7. PMID 7732006 DOI: 10.1073/Pnas.92.9.3923 |
0.514 |
|
| 1995 |
Race RE, Priola SA, Bessen RA, Ernst D, Dockter J, Rall GF, Mucke L, Chesebro B, Oldstone MB. Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent. Neuron. 15: 1183-91. PMID 7576660 DOI: 10.1016/0896-6273(95)90105-1 |
0.412 |
|
| 1995 |
Priola SA, Chesebro B. A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells. Journal of Virology. 69: 7754-8. PMID 7494285 DOI: 10.1128/Jvi.69.12.7754-7758.1995 |
0.62 |
|
| 1994 |
Kocisko DA, Come JH, Priola SA, Chesebro B, Raymond GJ, Lansbury PT, Caughey B. Cell-free formation of protease-resistant prion protein. Nature. 370: 471-4. PMID 7913989 DOI: 10.1038/370471A0 |
0.556 |
|
| 1994 |
Priola SA, Caughey B, Race RE, Chesebro B. Heterologous PrP molecules interfere with accumulation of protease-resistant PrP in scrapie-infected murine neuroblastoma cells. Journal of Virology. 68: 4873-8. PMID 7913509 DOI: 10.1128/Jvi.68.8.4873-4878.1994 |
0.645 |
|
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