THE PUBLIC HEALTH IMPACT OF PRION DISEASES

Novel Proteinaceous Infectious Particles Cause Scrapie

Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,221

A new variant of Creutzfeldt-Jakob disease in the UK

Will, R. G., Ironside, J. W., Zeidler, M., Estibeiro, K., Cousens, S. N., Smith, P. G., Alpérovitch, A., Poser, S., Pocchiari, M., & Albert Hofman, D. (1996) · The Lancet · doi:10.1016/s0140-6736(96)91412-9 · Cited by 2,702

Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.

Pan, K. M., Baldwin, M. A., Nguyen, J. T., Gasset, M., Serban, A. V., Groth, D., Mehlhorn, I., Huang, Z., Fletterick, R. J., & Cohen, F. E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.10962 · Cited by 2,281

Mice devoid of PrP are resistant to scrapie

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A cellular gene encodes scrapie PrP 27-30 protein

Oesch, B., Westaway, D. A., Wälchli, M., McKinley, M. P., Kent, S. B. H., Aebersold, R. H., Barry, R. A., Tempst, P., Teplow, D. B., Hood, L., et al. (1985) · Cell · doi:10.1016/0092-8674(85)90333-2 · Cited by 1,532

Identification of a Protein That Purifies with the Scrapie Prion

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Nature of the Scrapie Agent: Self-replication and Scrapie

Griffith, J. S. (1967) · Nature · doi:10.1038/2151043a0 · Cited by 1,188

Possible transmission of variant Creutzfeldt-Jakob disease by blood transfusion

Llewelyn, C. A., Hewitt, P. B., Knight, R., Amar, K. A., Cousens, S., Mackenzie, J., & Will, R. G. (2004) · The Lancet · doi:10.1016/s0140-6736(04)15486-x · Cited by 1,137

Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication

Prusiner, S. B., Scott, M., FOSTER, D. B., Pan, K., Groth, D., Mirenda, C. A., Torchia, M., Yang, S.-L., Serban, D., Carlson, G. A., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90134-z · Cited by 875

Evidence for the Conformation of the Pathologic Isoform of the Prion Protein Enciphering and Propagating Prion Diversity

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2007 Guideline for Isolation Precautions: Preventing Transmission of Infectious Agents in Health Care Settings

Siegel, J. D., Rhinehart, E., Jackson, M. M., & Chiarello, L. A. (2007) · American Journal of Infection Control · doi:10.1016/j.ajic.2007.10.007 · Cited by 3,506

Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders

Jucker, M., & Walker, L. C. (2011) · Annals of Neurology · doi:10.1002/ana.22615 · Cited by 622

Emerging infectious disease agents and their potential threat to transfusion safety

Stramer, S. L., Hollinger, F. B., Katz, L. M., Kleinman, S. H., Metzel, P., Gregory, K. R., & Dodd, R. Y. (2009) · Transfusion · doi:10.1111/j.1537-2995.2009.02279.x · Cited by 438

Prions Adhere to Soil Minerals and Remain Infectious

Johnson, C. J., Phillips, K. E., Schramm, P. T., McKenzie, D. I., Aiken, J. M., & Pedersen, J. A. (2006) · PLoS Pathogens · doi:10.1371/journal.ppat.0020032 · Cited by 316

Induction of cerebral β-amyloidosis: Intracerebral versus systemic Aβ inoculation

Eisele, Y. S., Bolmont, T., Heikenwalder, M., Langer, F., Jacobson, L. H., Yan, Z.-X., Roth, K., Aguzzi, A., Staufenbiel, M., Walker, L. C., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903200106 · Cited by 279

High-Pressure Chemical Biology and Biotechnology

Silva, J. L., de Oliveira, A. C., Vieira, T. C. R. G., de Oliveira, G. A. P., Suarez, M. C., & Foguel, D. (2014) · Chemical Reviews · doi:10.1021/cr400204z · Cited by 227

Prospective 10-year surveillance of human prion diseases in Japan

Nozaki, I., Hamaguchi, T., Sanjo, N., Noguchi‐Shinohara, M., Sakai, K., Nakamura, Y., SATO, T. A., Kitamoto, T., Mizusawa, H., Moriwaka, F., et al. (2010) · Brain · doi:10.1093/brain/awq216 · Cited by 200

Humans and Cattle: A Review of Bovine Zoonoses

McDaniel, C. J., Cardwell, D. M., Moeller, R. B., & Gray, G. C. (2013) · Vector-Borne and Zoonotic Diseases · doi:10.1089/vbz.2012.1164 · Cited by 193

Cdk5: Multitasking between physiological and pathological conditions

Lopes, J. P., & Agostinho, P. M. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.03.006 · Cited by 134

Iatrogenic Creutzfeldt-Jakob disease with Amyloid-β pathology: an international study

Calì, I., Cohen, M. L., Haı̈k, S., Parchi, P., Giaccone, G., Collins, S. J., Kofskey, D., Wang, H., McLean, C., Brandel, J., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0503-z · Cited by 121

Human Prion Diseases in the United States

Holman, R. C., Belay, E. D., Christensen, K. L. Y., Maddox, R. A., Miniño, A., Folkema, A. M., Haberling, D. L., Hammett, T. A., Kochanek, K. D., Sejvar, J. J., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0008521 · Cited by 112

The role of the cellular prion protein in the immune system

Isaacs, J. D., Jackson, G. S., & Altmann, D. M. (2006) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2006.03194.x · Cited by 106

Prions in the environment

Saunders, S. E., Bartelt‐Hunt, S. L., & Bartz, J. C. (2008) · Prion · doi:10.4161/pri.2.4.7951 · Cited by 98

Sterilization and Disinfection

Mohapatra, S. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805299-0.00059-2 · Cited by 97

Diagnostic accuracy of cerebrospinal fluid protein markers for sporadic Creutzfeldt-Jakob disease in Canada: a 6-year prospective study

Coulthart, M. B., Jansen, G. H., Olsen, E., Godal, D. L., Connolly, T., Choi, B. C. K., Wang, Z., & Cashman, N. R. (2011) · BMC Neurology · doi:10.1186/1471-2377-11-133 · Cited by 73

Validation of cold plasma treatment for protein inactivation: a surface plasmon resonance-based biosensor study

Bernard, C., Leduc, A., Barbeau, J., Saoudi, B., Yahia, L., & Crescenzo, G. D. (2006) · Journal of Physics D Applied Physics · doi:10.1088/0022-3727/39/16/s04 · Cited by 54

Soil-mediated prion transmission: Is local soil-type a key determinant of prion disease incidence?

Saunders, S. E., Bartz, J. C., & Bartelt‐Hunt, S. L. (2012) · Chemosphere · doi:10.1016/j.chemosphere.2011.12.076 · Cited by 51

The inhibition of prions through blocking prion conversion by permanently charged branched polyamines of low cytotoxicity

Lim, Y., Mays, C. E., Kim, Y., Titlow, W. B., & Ryou, C. (2009) · Biomaterials · doi:10.1016/j.biomaterials.2009.11.085 · Cited by 50

Adsorption and photocatalytic degradation of human serum albumin on TiO2 and Ag–TiO2 films

Ahmed, M. H., Keyes, T. E., Byrne, J., Blackledge, C. W., & Hamilton, J. W. J. (2011) · Journal of Photochemistry and Photobiology A Chemistry · doi:10.1016/j.jphotochem.2011.05.011 · Cited by 48

Lack of evidence of transfusion transmission of Creutzfeldt‐Jakob disease in a US surveillance study

Dorsey, K. A., Zou, S., Schonberger, L. B., Sullivan, M., Kessler, D. A., Notari, E. P., Fang, C. T., & Dodd, R. Y. (2009) · Transfusion · doi:10.1111/j.1537-2995.2008.02056.x · Cited by 48

Risk of infection and tracking of work-related infectious diseases in the funeral industry

Davidson, S. S., & Benjamin, W. H. (2006) · American Journal of Infection Control · doi:10.1016/j.ajic.2006.05.290 · Cited by 44

Bovine spongiform encephalopathy

Harman, J. L., & Silva, C. J. (2009) · Journal of the American Veterinary Medical Association · doi:10.2460/javma.234.1.59 · Cited by 41

Absolute Quantification of Prion Protein (90–231) Using Stable Isotope-Labeled Chymotryptic Peptide Standards in a LC-MRM AQUA Workflow

Sturm, R. M., Sheynkman, G., Booth, C. J., Smith, L. M., Pedersen, J. A., & Li, L. (2012) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-012-0411-1 · Cited by 36

Decontamination, Disinfection, and Sterilization

Wendt, C., Frei, R., & Widmer, A. F. (2015) · ASM Press eBooks · doi:10.1128/9781555817381.ch13 · Cited by 34

Management of Neurosurgical Instruments and Patients Exposed to Creutzfeldt-Jakob Disease

Belay, E. D., Blase, J. L., Sehulster, L. M., Maddox, R. A., & Schonberger, L. B. (2013) · Infection Control and Hospital Epidemiology · doi:10.1086/673986 · Cited by 34

The clearance of misfolded proteins in neurodegenerative diseases by zinc metalloproteases: An inorganic perspective

Malgieri, G., & Grasso, G. (2013) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2013.10.008 · Cited by 33

Species barriers for chronic wasting disease by in vitro conversion of prion protein

Li, L., Coulthart, M. B., Balachandran, A., Chakrabartty, A., & Cashman, N. R. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.10.087 · Cited by 31

Ruminant organotypic brain‐slice cultures as a model for the investigation of CNS listeriosis

Guldimann, C., Lejeune, B., Höfer, S., Leib, S. L., Frey, J., Zurbriggen, A., Seuberlich, T., & Oevermann, A. (2012) · International Journal of Experimental Pathology · doi:10.1111/j.1365-2613.2012.00821.x · Cited by 30

Six-year follow-up of a point-source exposure to CWD contaminated venison in an Upstate New York community: risk behaviours and health outcomes 2005–2011

Olszowy, K. M., Lavelle, J. D., Rachfal, K., Hempstead, S., Drouin, K., D’Arcy, J., Reiber, C., & Garruto, R. M. (2014) · Public Health · doi:10.1016/j.puhe.2014.06.012 · Cited by 29

Creutzfeldt-Jakob Disease Surveillance and Diagnosis

Belay, E. D., Holman, R. C., & Schonberger, L. B. (2005) · Clinical Infectious Diseases · doi:10.1086/432726 · Cited by 29

Identification of Anti-prion Compounds using a Novel Cellular Assay

Imberdis, T., Heeres, J. T., Yueh, H., Fang, C., Zhen, J., Rich, C. B., Glicksman, M. A., Beeler, A. B., & Harris, D. A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.745612 · Cited by 28

A potential role for Transmissible Spongiform Encephalopathies in Neanderthal extinction

Underdown, S. (2008) · Medical Hypotheses · doi:10.1016/j.mehy.2007.12.014 · Cited by 28

Lower Risk of Creutzfeldt-Jakob Disease in Pituitary Growth Hormone Recipients Initiating Treatment after 1977

Abrams, J. Y., Schonberger, L. B., Belay, E. D., Maddox, R. A., Leschek, E., Mills, J. L., Wysowski, D. K., & FRADKIN, J. E. (2011) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2011-1357 · Cited by 27

Critical factors influencing prion inactivation by sodium hydroxide

Bauman, P. A., Lawrence, L. A., BIESERT, L., Dichtelmüller, H. O., Fabbrizzi, F., Gajardo, R., Gröner, A., Jorquera, J. I., Kempf, C., Kreil, T. R., et al. (2006) · Vox Sanguinis · doi:10.1111/j.1423-0410.2006.00790.x · Cited by 23

Decontamination, Disinfection, and Sterilization

Widmer, A. F., & Frei, R. (2011) · Wiley eBooks · doi:10.1128/9781555816728.ch11 · Cited by 22

Variant Creutzfeldt-Jakob Disease Death, United States

Belay, E. D., Sejvar, J. J., Shieh, W., Wiersma, S., Zou, W.-Q., Gambetti, P. L., HUNTER, S. B., Maddox, R. A., Crockett, L. K., Zaki, S. R., et al. (2005) · Emerging infectious diseases · doi:10.3201/eid1109.050371 · Cited by 22

The Challenge of Preventing a Rare but Potentially Devastating Iatrogenic Exposure to Variant Creutzfeldt-Jakob Disease: An Ambi-directional Observation with Policy Intervention

Pandey, R., Rai, D., Giles, J., Laguio-Vila, M. R., & Lesho, E. P. (2021) · Advances in Clinical Medical Research and Healthcare Delivery · doi:10.53785/2769-2779.1032 · Cited by 19

Comparative Study of Prions in Iatrogenic and Sporadic Creutzfeldt-Jakob Disease

Xiao, X. (2014) · Journal of Clinical & Cellular Immunology · doi:10.4172/2155-9899.1000240 · Cited by 19

How to Select Replacement Grafts for Various Periodontal and Implant Indications

Hsu, Y., & Wang, H. (2012) · Clinical Advances in Periodontics · doi:10.1902/cap.2012.120031 · Cited by 19

Consumption of Bovine Spongiform Encephalopathy (BSE) Contaminated Beef and the Risk of Variant Creutzfeldt‐Jakob Disease

Chen, C., Wang, Y.-F., & Wu, K. (2013) · Risk Analysis · doi:10.1111/risa.12079 · Cited by 18

Injecting human growth hormone as a performance-enhancing drug—perspectives from the United Kingdom

Evans-Brown, M. J., & McVeigh, J. (2009) · Journal of Substance Use · doi:10.3109/14659890903224383 · Cited by 18

Transmissible spongiform encephalopathies

Sejvar, J. J., Schonberger, L. B., & Belay, E. D. (2008) · Journal of the American Veterinary Medical Association · doi:10.2460/javma.233.11.1705 · Cited by 16

Meat Borne Diseases

Almashhadany, D. A. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.97391 · Cited by 16

Neuroepidemiology and the epidemiology of viral infections of the nervous system

Sejvar, J. J. (2014) · Handbook of clinical neurology · doi:10.1016/b978-0-444-53488-0.00003-1 · Cited by 16

Pastoralism

Little, M. A. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-802652-6.00024-4 · Cited by 15

Koch's postulates, carnivorous cows, and tuberculosis today.

Tabrah, F. L. (2011) · Europe PMC (PubMed Central) · Cited by 15

Risk behaviors in a rural community with a known point-source exposure to chronic wasting disease

Garruto, R. M., Reiber, C., Alfonso, M. P., Gastrich, H. J., Needham, K., Sunderman, S., Walker, S., Weeks, J., DeRosa, N., Faisst, E., et al. (2008) · Environmental Health · doi:10.1186/1476-069x-7-31 · Cited by 15

Creutzfeldt-Jakob disease mortality in Canada, 1998 to 2013

Coulthart, M. B., Jansen, G. H., Connolly, T., D’Amour, R., Kruse, J., Lynch, J., Sabourin, S., Wang, Z., Giulivi, A., Ricketts, M., et al. (2015) · Canada Communicable Disease Report · doi:10.14745/ccdr.v41i08a01 · Cited by 15

Mathematical Modeling of Prion Disease

Sindi, S. (2017) · InTech eBooks · doi:10.5772/66917 · Cited by 12

Early Noninvasive Diagnosis of Neurodegenerative Diseases

Danev, S., & Stoyanov, D. (2010) · Folia Medica · doi:10.2478/v10153-010-0041-y · Cited by 12

Defining and Assessing Analytical Performance Criteria for Transmissible Spongiform Encephalopathy–Detecting Amyloid Seeding Assays

Gray, J. G., Graham, C., Dudas, S., Paxman, E., Vuong, B., & Czub, S. (2016) · Journal of Molecular Diagnostics · doi:10.1016/j.jmoldx.2016.01.005 · Cited by 11

Functional nanofibers for filtration applications

Chase, G. G., Swaminathan, S., & Raghavan, B. K. (2012) · Elsevier eBooks · doi:10.1533/9780857095640.2.121 · Cited by 10

A Case of Creutzfeldt-Jakob Disease Associated With a Dura Mater Graft in the United States

Blossom, D. B., Maddox, R. A., Beavers, S. F., Church, K. A., Thoroughman, D., Schonberger, L. B., & Belay, E. D. (2007) · Infection Control and Hospital Epidemiology · doi:10.1086/523862 · Cited by 10

Utility of RNAi-mediated prnp gene silencing in neuroblastoma cells permanently infected by prions: Potentials and limitations

Kim, Y., Han, B., Titlow, W. B., Mays, C. E., Kwon, M., & Ryou, C. (2009) · Antiviral Research · doi:10.1016/j.antiviral.2009.09.002 · Cited by 9

Cell nutrition

Malda, J., Radisic, M., Levenberg, S., Woodfield, T. B. F., Oomens, C. W. J., Baaijens, F. F., Svalander, P. C., & Vunjak‐Novakovic, G. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-370869-4.00012-4 · Cited by 9

Interpretation of cerebrospinal fluid protein tests in the diagnosis of sporadic Creutzfeldt–Jakob disease: an evidence-based approach

Coulthart, M. B., Jansen, G. H., & Cashman, N. R. (2014) · Canadian Medical Association Journal · doi:10.1503/cmaj.130720 · Cited by 8

Blood safety and the choice of anti‐hemophilic factor concentrate

Valentino, L. A., & Oza, V. M. (2006) · Pediatric Blood & Cancer · doi:10.1002/pbc.20895 · Cited by 8

Prions and endotoxins: reprocessing strategies for reusable medical devices

Sehulster, L. M. (2012) · Elsevier eBooks · doi:10.1533/9780857096265.261 · Cited by 7

A Small‐Molecule Inhibitor of Prion Replication and Mutant Prion Protein Toxicity

Massignan, T., Sangiovanni, V., Biggi, S., Stincardini, C., Elezgarai, S. R., Maietta, G., Andreev, I. A., Ratmanova, N. K., Belov, D. S., Lukyanenko, E. R., et al. (2017) · ChemMedChem · doi:10.1002/cmdc.201700302 · Cited by 7

Strain conformation controls the specificity of cross-species prion transmission in the yeast model

Grizel, A. V., Rubel, A. A., & Chernoff, Y. O. (2016) · Prion · doi:10.1080/19336896.2016.1204060 · Cited by 7

Modelling bovine spongiform encephalopathy

Thornley, J. H. M., & France, J. (2008) · The Journal of Agricultural Science · doi:10.1017/s0021859607007629 · Cited by 6

Transmissible Spongiform Encephalopathies

Belay, E. D. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803678-5.00469-0 · Cited by 6

Zoonoses

Rabinowitz, P. M., & Conti, L. (2010) · Elsevier eBooks · doi:10.1016/b978-1-4160-6837-2.00009-9 · Cited by 5

Dynamics of prion proliferation under combined treatment of pharmacological chaperones and interferons

Garzón, D. N., Castillo, Y., Navas-Zuloaga, M. G., Darwin, L. J., Hardin, A., Culik, N., Yang, A., Castillo-Garsow, C. W., Rı́os-Soto, K. R., Arriola, L. M., et al. (2021) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2021.110797 · Cited by 5

Progress in the discovery and definition of monoclonal antibodies for use in feline research

Meister, R. K., Taglinger, K., Haverson, K., Strohminger, N., & Mathes, L. E. (2007) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2007.06.012 · Cited by 5

Endogenous Viral Etiology of Prion DiseasesPreprint

BANDEA, C. I. (2009) · Nature Precedings · doi:10.1038/npre.2009.3887.1 · Cited by 5

Comparative Hazard Characterization in Food Toxicology

Hammerling, U., Tallsjö, A., Grafström, R., & Ilbäck, N. (2009) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408390802145617 · Cited by 4

Manganese and Prion Disease

Jin, H., Harischandra, D. S., Choi, C. J., Martin, D. P., Anantharam, V., Kanthasamy, A., & Kanthasamy, A. G. (2014) · Royal Society of Chemistry eBooks · doi:10.1039/9781782622383-00574 · Cited by 4

Cell-Based Seafood Production: Regulatory Framework in the United States and Food Safety Considerations

Omidvar, R., & Farzad, R. (2024) · EDIS · doi:10.32473/edis-fs456-2024 · Cited by 4

A Potential Blood Test for Transmissible Spongiform Encephalopathies by Detecting Carbohydrate‐Dependent Aggregates of PrPres‐Like Proteins in Scrapie‐Infected Hamster Plasma

Tsukui, K., Takata, M., & Tadokoro, K. (2007) · Microbiology and Immunology · doi:10.1111/j.1348-0421.2007.tb04009.x · Cited by 4

Professionalism in Forensic Archaeology: Transitioning from “Cowboy of Science” to “Officer of the Court”

Connor, M. (2019) · Springer eBooks · doi:10.1007/978-3-030-03291-3_3 · Cited by 3

Formaldehyde-fixed arterial allograft as a novel vascular access alternative in end-stage renal disease patients

Canaud, B. (2007) · Kidney International · doi:10.1038/sj.ki.5002558 · Cited by 3

Policy and Politics of BSE in the United States

Campbell, R., & Satō, H. (2009) · Alliance for Global Sustainability bookseries · doi:10.1007/978-90-481-3028-3_10 · Cited by 3

Mapping of Nervous System Diseases via MicroRNAs

(2016) · CRC Press eBooks · doi:10.1201/b19229 · Cited by 3

Role of MFG-E8 in the Brain

Aziz, M., & Wang, P. (2014) · Springer eBooks · doi:10.1007/978-94-017-8765-9_10 · Cited by 2

Microbiology in the modern era

Cruz-Ruiz, L., & Tawil, B. J. (2023) · Journal of Applied Biotechnology & Bioengineering · doi:10.15406/jabb.2023.10.00327 · Cited by 2

Liberty to Decide on Dual Use Biomedical Research: An Acknowledged Necessity

Keuleyan, E. E. (2008) · Science and Engineering Ethics · doi:10.1007/s11948-008-9064-7 · Cited by 2

Facing up to Complexity: Implications for Our Social Experiments

Hawkins, R. Z. (2015) · Science and Engineering Ethics · doi:10.1007/s11948-015-9657-x · Cited by 2

Sterilization, disinfection and universal precautions

Patel, S. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-22273-3.00054-7 · Cited by 1

Familial Creutzfeldt-Jakob Disease Cluster Among an African American Family

Johnson, M. G., Bradley, K. K., Coffman, R. L., & Belay, E. D. (2016) · Journal of Public Health Management and Practice · doi:10.1097/phh.0000000000000464 · Cited by 1

Selling stem cell based biologics and salesforce alignment for the biomedical device industry

Jaeger, B., & Kopf, D. A. (2014) · International Journal of Pharmaceutical and Healthcare Marketing · doi:10.1108/ijphm-08-2013-0046 · Cited by 1

The Immune System in the Pathogenesis and Prevention of Prion Diseases

Furr, A. (2011) · Journal of Bioterrorism & Biodefense · doi:10.4172/2157-2526.s1-012 · Cited by 1

Prion Diseases

Belay, E. D., & Bartz, J. C. (2014) · Springer eBooks · doi:10.1007/978-1-4899-7448-8_47 · Cited by 1

Characterization of Prion Removal Devices for Blood Products

Ortolano, G. A., Wilkins, K. M., & Cervia, J. S. (2005) · Transfusion Medicine and Hemotherapy · doi:10.1159/000087373 · Cited by 1

Timing recombinant prion protein conversion as a measure of prion activity in chronic wasting disease

Gray, J. G. (2014) · Libraries and Cultural Resources (University of Calgary) · doi:10.11575/prism/28457 · Cited by 1

Transmissible Spongiform Encephalopathies

Belay, E. D., & Schonberger, L. B. (2008) · Elsevier eBooks · doi:10.1016/b978-012374410-4.00557-4 · Cited by 1

Prion Diseases

Ryou, C. (2011) · Wiley eBooks · doi:10.1002/9780470015902.a0000428.pub2 · Cited by 1

Prions: Transmissable Spongiform Encelphalopathies and Dental Transmission Risk Assessment

Hamilton, J. (2007) · Journal of the California Dental Association · doi:10.1080/19424396.2007.12221198 · Cited by 1

Emerging Infectious Diseases in Mobile Populations

Hochberg, N. S., & Franco‐Paredes, C. (2014) · ASM Press eBooks · doi:10.1128/9781555816803.ch16

Roles of manganese and protein kinase signaling in cell culture and animal models of prion disease

Martin, D. P. (2013) · Iowa State University Digital Repository (Iowa State University) · doi:10.31274/etd-180810-721

Creutzfeldt‐Jakob and Other Prion Diseases

Crichton, R. R., & Ward, R. J. (2005) · Wiley eBooks · doi:10.1002/0470022574.ch7

Proposal on iatrogenic risks of urine derived medicinal products

Amate, J. M. (2012) · European Journal of Obstetrics & Gynecology and Reproductive Biology · doi:10.1016/j.ejogrb.2012.09.022

Human Prion Diseases Now Reportable in Alaska

Butler, J. C., & McLaughlin, J. B. (2007)

The Effects of Growth Hormone and Insulin-Like Growth Factor-1 Treatments on Hepatic Gene Expression in Obese and Diabetic Mice with Nonalcoholic Fatty Liver Disease

Blischak, J. (2010) · OhioLink ETD Center (Ohio Library and Information Network)

Transmissible Spongiform Encephalopathies

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