Littérature scientifique sur le sujet « Prion, copper, Transmissible spongiform encephalopathy »
Créez une référence correcte selon les styles APA, MLA, Chicago, Harvard et plusieurs autres
Consultez les listes thématiques d’articles de revues, de livres, de thèses, de rapports de conférences et d’autres sources académiques sur le sujet « Prion, copper, Transmissible spongiform encephalopathy ».
À côté de chaque source dans la liste de références il y a un bouton « Ajouter à la bibliographie ». Cliquez sur ce bouton, et nous générerons automatiquement la référence bibliographique pour la source choisie selon votre style de citation préféré : APA, MLA, Harvard, Vancouver, Chicago, etc.
Vous pouvez aussi télécharger le texte intégral de la publication scolaire au format pdf et consulter son résumé en ligne lorsque ces informations sont inclues dans les métadonnées.
Articles de revues sur le sujet "Prion, copper, Transmissible spongiform encephalopathy"
Langeveld, J. P. M., J. G. Jacobs, N. Hunter, L. J. M. van Keulen, F. Lantier, F. G. van Zijderveld et A. Bossers. « Prion Type-Dependent Deposition ofPRNPAllelic Products in Heterozygous Sheep ». Journal of Virology 90, no 2 (28 octobre 2015) : 805–12. http://dx.doi.org/10.1128/jvi.02316-15.
Texte intégralNishida, Yuzo. « Elucidation of Endemic Neurodegenerative Diseases - a Commentary ». Zeitschrift für Naturforschung C 58, no 9-10 (1 octobre 2003) : 752–58. http://dx.doi.org/10.1515/znc-2003-9-1028.
Texte intégralChesebro, Bruce. « Prion Protein and the Transmissible Spongiform Encephalopathy Diseases ». Neuron 24, no 3 (novembre 1999) : 503–6. http://dx.doi.org/10.1016/s0896-6273(00)81105-8.
Texte intégralRace, Richard E., Anne Raines, Thierry G. M. Baron, Michael W. Miller, Allen Jenny et 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 (1 décembre 2002) : 12365–68. http://dx.doi.org/10.1128/jvi.76.23.12365-12368.2002.
Texte intégralHeumüller, Stefanie-Elisabeth, Annika C. Hornberger, Alina S. Hebestreit, André Hossinger et Ina M. Vorberg. « Propagation and Dissemination Strategies of Transmissible Spongiform Encephalopathy Agents in Mammalian Cells ». International Journal of Molecular Sciences 23, no 6 (8 mars 2022) : 2909. http://dx.doi.org/10.3390/ijms23062909.
Texte intégralMurdoch, Brenda M., et Gordon K. Murdoch. « Genetics of Prion Disease in Cattle ». Bioinformatics and Biology Insights 9S4 (janvier 2015) : BBI.S29678. http://dx.doi.org/10.4137/bbi.s29678.
Texte intégralWilliams, 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.
Texte intégralTakemura, K., M. Kahdre, D. Joseph, A. Yousef et S. Sreevatsan. « An overview of transmissible spongiform encephalopathies ». Animal Health Research Reviews 5, no 2 (décembre 2004) : 103–24. http://dx.doi.org/10.1079/ahr200494.
Texte intégralHamir, A. N., J. M. Miller, R. A. Kunkle, S. M. Hall et J. A. Richt. « Susceptibility of Cattle to First-passage Intracerebral Inoculation with Chronic Wasting Disease Agent from White-tailed Deer ». Veterinary Pathology 44, no 4 (juillet 2007) : 487–93. http://dx.doi.org/10.1354/vp.44-4-487.
Texte intégralRace, Richard E., et Gregory J. Raymond. « Inactivation of Transmissible Spongiform Encephalopathy (Prion) Agents by Environ LpH ». Journal of Virology 78, no 4 (15 février 2004) : 2164–65. http://dx.doi.org/10.1128/jvi.78.4.2164-2165.2004.
Texte intégralThèses sur le sujet "Prion, copper, Transmissible spongiform encephalopathy"
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.
Texte intégralBishop, 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.
Texte intégralCORDA, 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.
Texte intégralBrown, 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.
Texte intégralBoerner, 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.
Texte intégralPrions are the causative agent of transmissible spongiform encephalopathies in animals and humans such as scrapie, bovine spongiform encephalopathy (BSE) and Creutzfeldt-Jakob disease (CJD). Prions are thought to be composed essentially of a misfolded and aberrantly aggregated isoform of the cellular prion protein (PrP) and to replicate by seeded PrP polymerization. Prions may exist in the form of distinct strains that differ in their phenotypic characteristics although they are derived from the same cellular prion protein. Cofactor molecules other than PrP may be involved in prion replication and may be a determinant of strain properties. Furthermore, cofactors may also be required for conveying infectivity. The present study examined the effects of different cofactor molecules on the replication efficacy of four hamster adapted prion agents using the method of serial protein misfolding cyclic amplification (PMCA) as in vitro assay for PrP misfolding and aggregation. The study revealed strain dependent differences of PMCA conditions and cofactors required for efficient in vitro replication. The impact of cofactors was assessed by comparative analyses of selected biological, biochemical and biophysical properties of PMCA products (PrPres) and native prion seeds. The biological seeding activity as monitored in a primary hamster glial cell assay, and biochemical properties such as electrophoretic migration in SDS-gels, were affected differently by different cofactors. In order to define the impact of putative cofactors on the molecular conversion of PrP in more detail, changes in the spatial structure associated with different cofactor molecule conditions during amplification of PrPres in PMCA was monitored by Fourier transform-infrared (FT-IR) spectroscopic analysis. Largely preliminary data revealed spectral differences between native prion seeds and progeny PMCA generated PrPres for all prion strains, but no variations due to different cofactor conditions.
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.
Texte intégralIn this thesis, we developed an analytical method for the purification, separation and characterization of cellular prion (PrPC) and superoxide dismutase (SOD-1), two proteins related to Transmissible Spongiform Encephalopathies (TSEs) and the Amyotrophic Lateral Sclerosis (ALS), respectively. The TSEs are characterized by the accumulation of the pathological form of PrPC (PrPSc) in the brain of affected animals, whereas in ALS it is observed the formation of aggregates of SOD-1. Today, factors that initiate and regulate the interactions that lead to the formation of protein aggregates in many neurodegenerative diseases are still unknown. Some authors suggest mechanisms based on the structural changes observed between the native and the pathology protein which cold be related with the conformation, the amino acid sequence, metals or post-translational modifications. In oligomeric proteins such as SOD-1, the dissociation of oligomers to monomers before aggregation it is also considered. So, it is crucial to increase the knowledge of the structure of these proteins and the mechanisms that govern its aggregation for understanding the disease development. This paper proposes a strategy for having an efficient recovery in the purification of bovine brain PrPC using conventional purification methods that not involves immunochemical procedures. The presence of PrPC was checked at different stages by western blot (WB). Then, the separation and characterization of the SOD-1 by capillary electrophoresis coupled to mass spectrometry with ion trap and time of flight analyzers (CE-IT-MS and CE-TOF-MS), matrix-assisted laser desorption/ionization with a time of flight mass analyzer (MALDI-TOF-MS) and ion mobility mass spectrometry with power nano-electrospray ionization source (n-ESI-IM-MS) was studied. The comparison of purified SOD-1 from blood samples of healthy individuals and patients with ALS have yielded some preliminary interesting conclusions about structural changes in the protein associated with cold be related with the disease.
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.
Texte intégralSpassov, 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.
Texte intégralLivres sur le sujet "Prion, copper, Transmissible spongiform encephalopathy"
Mad cows and cannibals : A guide to the transmissible spongiform encephalopathies. Upper Saddle River, NJ : Pearson/Prentice Hall, 2004.
Trouver le texte intégralInternational 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. Amsterdam : Elsevier, 1996.
Trouver le texte intégralGreat Britain. Advisory Committee on Dangerous Pathogens., dir. Precautions for work with human and animal transmissible spongiform encephalopathies. London : HMSO, 1994.
Trouver le texte intégralMinistry of Agriculture, Fisheries and Food. Strategy for research and development relating to the animal health aspects of transmissible spongiform encephalopathies. [London] : GB MAFF, 1998.
Trouver le texte intégralInternational 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. Basel : Karger, 1993.
Trouver le texte intégralKate, Brown. Meeting of the OIE Ad Hoc Research Group on Transmissible Spongiform Encephalopathies, Paris, 8-10 October, 1996 : United Kingdom research review. London : Great Britain, Ministry of Agriculture, Fisheries and Food, 1996.
Trouver le texte intégralWorld 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. Geneva : WHO, 1997.
Trouver le texte intégralF, Brown, et International Association of Biological Standardization., dir. Transmissible spongiform encephalopathies : Impact on animal and human health : proceedings of a meeting held at the Kongresshaus, Stadthalle, Heidelberg (Germany), June 23-24, 1992. Basel : Karger, 1993.
Trouver le texte intégralTransmissible Spongiform Enecephalopathies : Impact on Animal and Human Health (Developments in Biologicals). S. Karger AG (Switzerland), 1993.
Trouver le texte intégralWHO Guidelines on Tissue Infectivity Distribution in Transmissible Spongiform Encephalopathies. World Health Organization, 2006.
Trouver le texte intégralChapitres de livres sur le sujet "Prion, copper, Transmissible spongiform encephalopathy"
Silveira, J. R., B. Caughey et G. S. Baron. « Prion Protein and the Molecular Features of Transmissible Spongiform Encephalopathy Agents ». Dans Current Topics in Microbiology and Immunology, 1–50. Berlin, Heidelberg : Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-662-08441-0_1.
Texte intégralRaymond, Gregory J., et Joëlle Chabry. « Purification of the Pathological Isoform of Prion Protein (PrPSc or PrPres) from Transmissible Spongiform Encephalopathy-affected Brain Tissue ». Dans Techniques in Prion Research, 16–26. Basel : Birkhäuser Basel, 2004. http://dx.doi.org/10.1007/978-3-0348-7949-1_3.
Texte intégralBrown, P. « Transmissible spongiform encephalopathy (prion disease) ». Dans Foodborne Pathogens, 1119–39. Elsevier, 2009. http://dx.doi.org/10.1533/9781845696337.3.1119.
Texte intégralSingh, Sujatha, et Mahendra Pal. « Bovine Spongiform Encephalopathy—A Transmissible Prion Based Disease ». Dans Reference Module in Food Science. Elsevier, 2023. http://dx.doi.org/10.1016/b978-0-12-822521-9.00083-6.
Texte intégralIronside, James W., Matthew P. Frosch et Bernardino Ghetti. « Human Prion Diseases ». Dans Escourolle and Poirier's Manual of Basic Neuropathology, 149–60. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199929054.003.0006.
Texte intégralMead, Simon, et R. G. Will. « Human prion diseases ». Dans Oxford Textbook of Medicine, sous la direction de Christopher Kennard, 6109–19. Oxford University Press, 2020. http://dx.doi.org/10.1093/med/9780198746690.003.0599.
Texte intégralCollinge, John. « Prion disease ». Dans New Oxford Textbook of Psychiatry, 351–61. Oxford University Press, 2012. http://dx.doi.org/10.1093/med/9780199696758.003.0044.
Texte intégral