Relevant bibliographies by topics / Prion, copper, Transmissible spongiform encephalopathy

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Reports

Academic literature on the topic 'Prion, copper, Transmissible spongiform encephalopathy'

Author: Grafiati
Published: 14 March 2023
Last updated: 31 July 2025

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Journal articles on the topic "Prion, copper, Transmissible spongiform encephalopathy"

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Nishida, Yuzo. "Elucidation of Endemic Neurodegenerative Diseases - a Commentary." Zeitschrift für Naturforschung C 58, no. 9-10 (2003): 752–58. http://dx.doi.org/10.1515/znc-2003-9-1028.

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AbstractRecent investigations of scrapie, Creutzfeldt-Jakob disease (CJD), and chronic wasting disease (CWD) clusters in Iceland, Slovakia and Colorado, respectively, have indicated that the soil in these regions is low in copper and higher in manganese, and it has been well-known that patients of ALS or Parkinson’s disease were collectively found in the New Guinea and Papua islands, where the subterranean water (drinking water) contains much Al3+ and Mn2+ ions. Above facts suggest that these neurodegenerative diseases are closely related with the function of a metal ion.We have investigated t
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Imran, M., and S. Mahmood. "An overview of animal prion diseases." Virology journal 8, Journal Article (2011): 493–22. https://doi.org/10.5281/zenodo.13525469.

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(Uploaded by Plazi for the Bat Literature Project) Prion diseases are transmissible neurodegenerative conditions affecting human and a wide range of animal species. The pathogenesis of prion diseases is associated with the accumulation of aggregates of misfolded conformers of host-encoded cellular prion protein (PrPC). Animal prion diseases include scrapie of sheep and goats, bovine spongiform encephalopathy (BSE) or mad cow disease, transmissible mink encephalopathy, feline spongiform encephalopathy, exotic ungulate spongiform encephalopathy, chronic wasting disease of cervids and spongiform
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Imran, M., and S. Mahmood. "An overview of animal prion diseases." Virology journal 8, Journal Article (2011): 493–22. https://doi.org/10.5281/zenodo.13525469.

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(Uploaded by Plazi for the Bat Literature Project) Prion diseases are transmissible neurodegenerative conditions affecting human and a wide range of animal species. The pathogenesis of prion diseases is associated with the accumulation of aggregates of misfolded conformers of host-encoded cellular prion protein (PrPC). Animal prion diseases include scrapie of sheep and goats, bovine spongiform encephalopathy (BSE) or mad cow disease, transmissible mink encephalopathy, feline spongiform encephalopathy, exotic ungulate spongiform encephalopathy, chronic wasting disease of cervids and spongiform
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Imran, M., and S. Mahmood. "An overview of animal prion diseases." Virology journal 8, Journal Article (2011): 493–22. https://doi.org/10.5281/zenodo.13525469.

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(Uploaded by Plazi for the Bat Literature Project) Prion diseases are transmissible neurodegenerative conditions affecting human and a wide range of animal species. The pathogenesis of prion diseases is associated with the accumulation of aggregates of misfolded conformers of host-encoded cellular prion protein (PrPC). Animal prion diseases include scrapie of sheep and goats, bovine spongiform encephalopathy (BSE) or mad cow disease, transmissible mink encephalopathy, feline spongiform encephalopathy, exotic ungulate spongiform encephalopathy, chronic wasting disease of cervids and spongiform
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Imran, M., and S. Mahmood. "An overview of animal prion diseases." Virology journal 8, Journal Article (2011): 493–22. https://doi.org/10.5281/zenodo.13525469.

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(Uploaded by Plazi for the Bat Literature Project) Prion diseases are transmissible neurodegenerative conditions affecting human and a wide range of animal species. The pathogenesis of prion diseases is associated with the accumulation of aggregates of misfolded conformers of host-encoded cellular prion protein (PrPC). Animal prion diseases include scrapie of sheep and goats, bovine spongiform encephalopathy (BSE) or mad cow disease, transmissible mink encephalopathy, feline spongiform encephalopathy, exotic ungulate spongiform encephalopathy, chronic wasting disease of cervids and spongiform
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Eduardo, Salcedo. "Prion Diseases in Animals." Transactions of the National Academy of Science and Technology 24, no. 2 (2002): 1–12. https://doi.org/10.57043/transnastphl.2002.5088.

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Prion diseases refer to a group of invariably neurodegenerative diseases in humans and animals, collectively known as transmissible spongiform encephalopathies (TSEs). These diseases are caused by proteinaceous infectious particles that lack nucleic acid, called prions. This paper reviews prion diseases occurring in animals, excluding human spongiform encephalopathies. Prions in animals include scrapie or ovine spongiform encephalopathy, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), chronic wasting disease (CWD) of mule deer and elk, and feline spongiform enc
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Race, Richard E., Anne Raines, Thierry G. M. Baron, Michael W. Miller, Allen Jenny, and Elizabeth S. Williams. "Comparison of Abnormal Prion Protein Glycoform Patterns from Transmissible Spongiform Encephalopathy Agent-Infected Deer, Elk, Sheep, and Cattle." Journal of Virology 76, no. 23 (2002): 12365–68. http://dx.doi.org/10.1128/jvi.76.23.12365-12368.2002.

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ABSTRACT Analysis of abnormal prion protein glycoform patterns from chronic wasting disease (CWD)-affected deer and elk, scrapie-affected sheep and cattle, and cattle with bovine spongiform encephalopathy failed to identify patterns capable of reliably distinguishing these transmissible spongiform encephalopathy diseases. However, PrP-res patterns sometimes differed among individual animals, suggesting infection by different or multiple CWD strains in some species.
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Chesebro, Bruce. "Prion Protein and the Transmissible Spongiform Encephalopathy Diseases." Neuron 24, no. 3 (1999): 503–6. http://dx.doi.org/10.1016/s0896-6273(00)81105-8.

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Murdoch, Brenda M., and Gordon K. Murdoch. "Genetics of Prion Disease in Cattle." Bioinformatics and Biology Insights 9S4 (January 2015): BBI.S29678. http://dx.doi.org/10.4137/bbi.s29678.

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Bovine spongiform encephalopathy (BSE) is a prion disease that is invariably fatal in cattle and has been implicated as a significant human health risk. As a transmissible disease of livestock, it has impacted food safety, production practices, global trade, and profitability. Genetic polymorphisms that alter the prion protein in humans and sheep are associated with transmissible spongiform encephalopathy susceptibility or resistance. In contrast, there is no strong evidence that nonsynonymous mutations in the bovine prion gene (PRNP) are associated with classical BSE (C-BSE) disease susceptib
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Williams, J. L. "Genetics of transmissible spongiform encephalopathy susceptibility and the search for surrogate markers for infection." Australian Journal of Experimental Agriculture 44, no. 11 (2004): 1119. http://dx.doi.org/10.1071/ea03235.

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The transmissible spongiform encephalopathy diseases are unusual in that they can be sporadic or infectious, and that the infectious agent does not contain nucleic acids. Instead, infectivity is associated with a modified host-encoded protein referred to as a prion. During the course of disease, host encoded prion protein (PrP) is converted from the normal cellular form, PrPC, to a disease form, PrPSC/BSE, which is highly resistant to degradation by heat or proteinases. The occurrence of the sporadic form of transmissible spongiform encephalopathy disease in humans, as well as susceptibility t
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Dissertations / Theses on the topic "Prion, copper, Transmissible spongiform encephalopathy"

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Tran, Thanh Hoa. "The non-octarepeat copper-binding site of the prion protein and its potential role in prion conversion." Doctoral thesis, SISSA, 2016. http://hdl.handle.net/20.500.11767/4870.

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Transmissible spongiform encephalopathy (TSE) or prion diseases are fatal neurodegenerative disorders caused by a change in conformation of the prion protein from the normal cellular form (PrPC) to a misfolded form (PrPSc). Prion protein has long been known as a copper binding protein. Although the functional implication of copper binding to PrP is not yet clear, it is believed that copper is an important cofactor in prion disease. Therefore, the aim of this work is to determine the potential role of copper in prion conversion. Copper can effectively bind to PrPC via histidine residues in the
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Dobie, Karen Louise. "Investigating the relationship between abnormal prion protein (PrPSc) and the transmissible spongiform encephalopathy (TSE) infectious agent." Thesis, University of Edinburgh, 2013. http://hdl.handle.net/1842/8107.

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Transmissible spongiform encephalopathies (TSEs) are a group of fatal, neurodegenerative diseases that can affect both humans and animals. TSEs can be sporadic, familial, or acquired diseases. The prion hypothesis states that a misfolded form of the host glycoprotein, PrPC, acts as the infectious agent in TSE disease. The misfolded form, PrPSc, is increased in β-sheet content, detergent insoluble and partially resistant to proteinase K (PK) digestion. Based on the prion hypothesis, most current post-mortem diagnostic tests rely on the presence of PrPSc as indicative of TSE disease. However, re
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Bishop, Matthew T. "Role of PRNP codon 129 genotype in defining strain transmission properties of human transmissible spongiform encephalopathy." Thesis, University of Edinburgh, 2009. http://hdl.handle.net/1842/4236.

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The human prion protein (PrP) gene (PRNP) codon 129 (M/V) polymorphism is a susceptibility factor for variant Creutzfeldt-Jakob Disease (vCJD) and a major determinant of clinico-pathological phenotype in sporadic CJD. The role of codon 129 in defining susceptibility and strain transmission properties has been investigated in three lines of transgenic mice that express human PrP. The human PRNP gene has directly replaced the murine version, by gene targeting, and variation at codon 129 has given the three genotype lines (HuMM, HuMV, and HuVV). The genetics of these three mouse lines are otherwi
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CORDA, ERICA. "TRANSMISSIBLE SPONGIFORM ENCEPHALOPATHIES (TSES): EXPERIMENTAL APPROACHES TO PATHOGENESIS, THERAPY AND PREVENTION IN ANIMAL MODELS." Doctoral thesis, Università degli Studi di Milano, 2012. http://hdl.handle.net/2434/169556.

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Prion diseases are perhaps the most mysterious and peculiar diseases in nature. These diseases do not rely on the general dogmas of modern biology, seen in other infectious diseases caused by conventional pathogens, such as viruses and bacteria. On the contrary, their infectious agent is an unconventional proteinaceous pathogen, termed prion, that lacks functional nucleic acids. Prion diseases are also known as Transmissible Spongiform Encephalopathies (TSEs), since the diseases are transmissible from one host to another and manifest a spongiform appearance as result of the destruction of brai
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Brown, Karen L. "Influence of the immune system on peripherally acquired transmissible spongiform encephalopathy infection with special reference to the role of the follicular dendritic cell." Thesis, University of Edinburgh, 2009. http://hdl.handle.net/1842/4376.

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The Transmissible Spongiform Encephalopathies (TSEs) or “prion” diseases are a group of fatal neurodegenerative diseases the aetiology of which is not fully understood. These diseases are characterised by a number of pathological changes in the central nervous system (CNS) including; vacuolation of the neuropil, gliosis and deposition of PrPSc; the abnormal form of the host glycoprotein PrP. Although the major pathology in these diseases is associated with the CNS the immune system is central to the pathogenesis of many natural and experimental TSEs including natural scrapie in sheep, chronic
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Boerner, Susann. "Probing reaction conditions and cofactors of conformational prion protein changes underlying the autocatalytic self-propagation of different prion strains." Doctoral thesis, Humboldt-Universität zu Berlin, Lebenswissenschaftliche Fakultät, 2014. http://dx.doi.org/10.18452/17003.

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Prionen sind das infektiöse Agens transmissibler spongiformer Enzephalopathien von Tieren und Menschen. Prionen bestehen hauptsächlich aus einer abnormal gefalteten und aggregierten Isoform des zellulären Prionproteins (PrP). Die Replikation von Prionen findet mutmaßlich durch keiminduzierte Polymerisation des Prionproteins statt. Es existieren verschiedene Prionstämme, die unterschiedliche Eigenschaften aufweisen, aber vom selben zellulären Prionprotein abstammen können. Neben PrP scheinen Kofaktormoleküle an der Prionreplikation beteiligt zu sein. Weiterhin wird angenommen, dass Kofaktoren b
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Borges, Álvarez Marta. "Establiment de metodologia analítica per a la purificació, separació i caracterització de biomarcadors proteics de malalties neurodegeneratives." Doctoral thesis, Universitat de Barcelona, 2012. http://hdl.handle.net/10803/119540.

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En aquesta tesi doctoral, s’ha desenvolupat metodologia analítica per a la purificació, separació i caracterització de prió cel•lular (PrPC) i superòxid dismutasa (SOD-1), dues proteïnes relacionades amb les Encefalopaties Espongiformes Transmissibles (TSEs) i l’Esclerosi Lateral Amiotròfica (ALS), respectivament. Les TSEs es caracteritzen per l’acumulació de la forma patològica del PrPC (PrPSc) al cervell dels animals afectats, mentre que a l’ALS s’observa la formació d’agregats de SOD-1. Avui dia, encara es desconeixen els factors que inicien i regulen les interaccions que condueixen a la fo
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Legleiter, Leon R. "The relationship between copper, manganese, and bovine brain prion proteins: implications for trace mineral nutrition and bovine spongiform encephalopathy /." 2006. http://www.lib.ncsu.edu/theses/available/etd-11032006-085510/unrestricted/etd.pdf.

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Spassov, Sashko G. [Verfasser]. "Investigation of scrapie associated prion protein PrP27-30 and strain differentiation of transmissible spongiform encephalopathy by Fourier transform infrared spectroscopy techniques / vorgelegt von Sashko Georgiev Spassov." 2006. http://d-nb.info/980867703/34.

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Books on the topic "Prion, copper, Transmissible spongiform encephalopathy"

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International Symposium on Transmissible Subacute Spongiform Encephalopathies: Prion Diseases (3rd 1996 Paris, France). Transmissible subacute spongiform encephalopathies: Prion diseases : IIIrd International Symposium on Transmissible Subacute Spongiform Encephalopathies: Prion Diseases, 18-20 March 1996, Val-de-Grâce, Paris, France. Elsevier, 1996.

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Great Britain. Advisory Committee on Dangerous Pathogens., ed. Precautions for work with human and animal transmissible spongiform encephalopathies. HMSO, 1994.

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Ministry of Agriculture, Fisheries and Food. Strategy for research and development relating to the animal health aspects of transmissible spongiform encephalopathies. GB MAFF, 1998.

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International Meeting on Transmissible Spongiform Encephalopathies - Impact on Animal and Human Health. International Meeting on Transmissible Spongiform Encephalopathies - Impact on Animal and Human Health: Proceedings of a meeting held at the Kongresshaus, Stadthalle, Heidelberg (Germany), June 23-24, 1992. Karger, 1993.

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Kate, Brown. Meeting of the OIE Ad Hoc Research Group on Transmissible Spongiform Encephalopathies, Paris, 8-10 October, 1996: United Kingdom research review. Great Britain, Ministry of Agriculture, Fisheries and Food, 1996.

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World Health Organization (WHO). Report of a WHO consultation on medicinal and other products in relation to human and other animal transmissible spongiform encephalopathies, with the participation of the Office International des Epizooties (OIE), Geneva, Switzerland, 24-26 March, 1997. WHO, 1997.

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F, Brown, and International Association of Biological Standardization., eds. Transmissible spongiform encephalopathies: Impact on animal and human health : proceedings of a meeting held at the Kongresshaus, Stadthalle, Heidelberg (Germany), June 23-24, 1992. Karger, 1993.

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Transmissible Spongiform Enecephalopathies: Impact on Animal and Human Health (Developments in Biologicals). S. Karger AG (Switzerland), 1993.

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WHO Guidelines on Tissue Infectivity Distribution in Transmissible Spongiform Encephalopathies. World Health Organization, 2006.

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Hope, James, and Mark P. Dagleish. Prion-protein-related diseases of animals and man. Oxford University Press, 2011. http://dx.doi.org/10.1093/med/9780198570028.003.0041.

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Scrapie, bovine spongiform encephalopathy (BSE), Creutzfeldt–Jakob disease (CJD), and related diseases of mink (transmissible mink encephalopathy), mule deer and elk (chronic wasting disease) are the founder members of a group of diseases called the transmissible degenerative (or spongiform) encephalopathies (TSE). These diseases can be transmitted by prions from affected to healthy animals by inoculation or by feeding diseased tissues. Prions are cellular proteins that can transfer metabolic and pathological phenotypes vertically from parent to progeny or horizontally between cells and animal
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Book chapters on the topic "Prion, copper, Transmissible spongiform encephalopathy"

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Silveira, J. R., B. Caughey, and G. S. Baron. "Prion Protein and the Molecular Features of Transmissible Spongiform Encephalopathy Agents." In Current Topics in Microbiology and Immunology. Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-662-08441-0_1.

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Raymond, Gregory J., and Joëlle Chabry. "Purification of the Pathological Isoform of Prion Protein (PrPSc or PrPres) from Transmissible Spongiform Encephalopathy-affected Brain Tissue." In Techniques in Prion Research. Birkhäuser Basel, 2004. http://dx.doi.org/10.1007/978-3-0348-7949-1_3.

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Brown, P. "Transmissible spongiform encephalopathy (prion disease)." In Foodborne Pathogens. Elsevier, 2009. http://dx.doi.org/10.1533/9781845696337.3.1119.

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Hope, James. "Prion Protein-Related Diseases Of Man And Animals." In Zoonoses. Oxford University PressNew York, NY, 1998. http://dx.doi.org/10.1093/oso/9780192623805.003.0036.

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Abstract Scrapie, Creutzfeldt-Jakob disease (CJD), Gerstmann- Straussler-Sheinker (GSS) syndrome and related diseases of mink (transmissible mink encephalopathy), mule deer, and elk (chronic wasting disease) are the founder members of a group of diseases called the transmissible degenerative (or spongiform) encephalopathies (TSE); the range of species affected by these disorders has grown in recent years to include cattle (bovine spongiform encephalopathy), cats (feline spongiform encephalopathy), and a variety of captive zoo antelope, such as the kudu and African oryx.
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Singh, Sujatha, and Mahendra Pal. "Bovine Spongiform Encephalopathy—A Transmissible Prion Based Disease." In Reference Module in Food Science. Elsevier, 2023. http://dx.doi.org/10.1016/b978-0-12-822521-9.00083-6.

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Ironside, James W., Matthew P. Frosch, and Bernardino Ghetti. "Human Prion Diseases." In Escourolle and Poirier's Manual of Basic Neuropathology. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199929054.003.0006.

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This chapter describes and illustrates the neuropathology of prion diseases, also known as transmissible spongiform encephalopathies. These diseases are characterized pathologically by varying combinations of spongiform change, neuronal loss, reactive gliosis, and prion protein (PrP) deposition. The morphologic pattern depends on the etiology of the disease and the genotype of the patient. Different clinicopathological phenotypes of sporadic Creutzfeldt-Jakob disease (CJD) have been described depending on the PRNP codon 129 genotype and the PrP isotype. A novel form known as variably protease-
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Mead, Simon, and R. G. Will. "Human prion diseases." In Oxford Textbook of Medicine, edited by Christopher Kennard. Oxford University Press, 2020. http://dx.doi.org/10.1093/med/9780198746690.003.0599.

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Prion protein (for proteinacious infectious particle) is a membrane-associated glycoprotein present in all mammalian species. Its normal function is unknown, but in prion diseases (also known as transmissible spongiform encephalopathies) a misfolded polymer form of the protein, partially resistant to protease digestion, is deposited in the brain and associated—typically after long incubation periods—with neuronal dysfunction and death. Prion diseases have become the subject of intense scientific and public interest because they are caused by a biologically distinct disease mechanism and becaus
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Collinge, John. "Prion disease." In New Oxford Textbook of Psychiatry. Oxford University Press, 2012. http://dx.doi.org/10.1093/med/9780199696758.003.0044.

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The human prion diseases, also known as the subacute spongiform encephalopathies, have been traditionally classified into Creutzfeldt–Jakob disease (CJD), Gerstmann–Sträussler syndrome (GSS) (also known as Gerstmann–Sträussler–Scheinker disease), and kuru. Although rare, affecting about 1–2 per million worldwide per annum, remarkable attention has been recently focused on these diseases. This is because of the unique biology of the transmissible agent or prion, and also because bovine spongiform encephalopathy (BSE), an epidemic bovine prion disease, appears to have transmitted to humans as va
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Reports on the topic "Prion, copper, Transmissible spongiform encephalopathy"

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จันทร์ประทีป, พีระศักดิ์, สุมลยา กาญจนะพังคะ, ประโยชน์ ตันติเจริญยศ та กัลยาณี ตันศฤงฆาร. ความเป็นมาและสถานภาพปัจจุบันของโรคสมองฟ่ามในโค (โคบ้า) : รายงานการวิจัย. จุฬาลงกรณ์มหาวิทยาลัย, 1998. https://doi.org/10.58837/chula.res.1998.81.

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โรคสมองฟ่ามหรือโคบ้า (Bovine Spongiform Encephalopathy, BSE) เป็นโรคระบาดร้ายแรงที่เกิดขึ้น.ในสหราชอาณาจักรเป็นส่วนใหญ่ ทำความเสียหายทางเศรษฐกิจอย่างมหาศาล จำเป็นต้องกำจัดโคถึง 1 ล้านตัวเพื่อกำจัด BSE ให้หมดไป ยิ่งไปกว่านั้น BSE อาจเป็นอันตรายแก่สุขภาพและชีวิตมนุษย์ด้วย BSE เป็นโรคหนึ่งใน transmissible spongiform encephalopathies (TSEs) โดยมี prion protein เป็นสารก่อโรคที่ทำความเสียหายแก่ระบบประสาท และทำให้คนหรือสัตว์ตายในที่สุด พบเนื้อสมองทั้งส่วน cerebrum และ cerebellum เป็นรูพรุน และอาจพบ plaques และ scrapie-associated fibrils (SAF) ในเนื้อสมองด้วย การศึกษาทางระบาดวิทยาชี้แนะว่าการแพร่ของ B
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