Scrapie
Mostrando 13-24 de 300 artigos, teses e dissertações.
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13. INDEL de 12 e 23 pares de bases no gene da PRÍON bovina na raça Caracu.
A Encefalopatia Espongiforme Bovina (EEB) é uma zoonose que faz parte do grupo das Encefalopatias Espongiformes Transmissíveis (EETs). O agente etiológico é denominado de príon scrapie (PrPSc), que é uma proteína anormal. A proteína normal é a príon celular (PrPC), sintetizada a partir do gene prnp. Uma das mudanças que ocorrem no gene prnp em bov
JORNADA CIENTÍFICA DA EMBRAPA GADO DE CORTE. Publicado em: 2011
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14. Biopsia da mucosa retal e terceira pálpebra de ovinos e otimizaçao do protocolo de imuno-histoquímica para diagnóstico de PrPsc em ruminantes.
As encefalopatias espongiformes transmissíveis (EETs), também conhecidas como doenças do príon, ocorrem tanto nos animais como no homem, são responsáveis por doenças transmissíveis e hereditárias e provocam lesões degenerativas no cérebro. A presença de uma forma anormal da proteína (PrPsc) no tecido encefálico e linforreticular é característ
Publicado em: 2009
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15. Volume and energy folding landscape of prion protein revealed by pressure
The main hypothesis for prion diseases proposes that the cellular protein (PrP C) can be altered into a misfolded, ß-sheet-rich isoform, the PrP Sc (from scrapie). The formation of this abnormal isoform then triggers the transmissible spongiform encephalopathies. Here, we discuss the use of high pressure as a tool to investigate this structural transition a
Brazilian Journal of Medical and Biological Research. Publicado em: 2005-08
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16. Some physico-chemical parameters that influence proteinase K resistance and the infectivity of PrP Sc after high pressure treatment
Crude brain homogenates of terminally diseased hamsters infected with the 263 K strain of scrapie (PrP Sc) were heated and/or pressurized at 800 MPa at 60ºC for different times (a few seconds or 5, 30, 120 min) in phosphate-buffered saline (PBS) of different pH and concentration. Prion proteins were analyzed on immunoblots for their proteinase K (PK) resist
Brazilian Journal of Medical and Biological Research. Publicado em: 2005-08
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17. Insights into the physiological function of cellular prion protein
Prions have been extensively studied since they represent a new class of infectious agents in which a protein, PrPsc (prion scrapie), appears to be the sole component of the infectious particle. They are responsible for transmissible spongiform encephalopathies, which affect both humans and animals. The mechanism of disease propagation is well understood and
Brazilian Journal of Medical and Biological Research. Publicado em: 2001-05
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18. Characterization and physiological roles of interactions between the cellular prion protein and two ligands: its putative 60-66 kDa receptor and laminin / Caracterização e implicações fisiológicas das interações da proteína prion celular com o seu receptor de 60-66 kDa e com a laminina
Prions are defined as proteinaceous infectious particles that mediate the pathogenesis of certain neurodegenerative diseases, in humans and in animals. The prion particle is composed largely, if not entirely, by PrPsc (prion scrapie), a posttranslationaly modified isoform of the cellular host-encoded prion protein (PrPc). PrPc is a glycosylphosphatidylinosit
Publicado em: 2000
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19. Caracterização de um receptor para o prion atraves da teoria da hidropaticidade complementar dos amino acidos : evidencias da inteprion-laminina
Prions are slow infectious pathogens which cause transmissible neurodegenerative Jackob disease, diseases in both humans (kuru, Creutzfeldt-Gerstmann-Straussler-Scheinker syndrome and familial fatal insomnia) and animals (scrapie, bovine spongiform encephalopaty, transmissible mink encephalopaty and chronic wasting disease). The infectious prion protein (Prp
Publicado em: 1996
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20. Evidence for Normal Cell-Mediated Immunity in Scrapie-Infected Mice
Comparisons between mixed lymphocyte cultures of splenocytes from scrapie-infected and normal mouse brain-inoculated control mice did not reveal any evidence of an impaired cell-mediated immune response in scrapie-infected mice. Likewise, mixed lymphocyte cultures of splenocytes from scrapie-infected and normal mice demonstrated that infected spleen cells ha
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21. Scrapie-associated prion protein accumulates in astrocytes during scrapie infection.
In the course of scrapie, a transmissible spongiform encephalopathy caused by an unconventional agent, a normal cellular protein is converted to an abnormal form that copurifies with infectivity and aggregates to form deposits of amyloid. We have used immunocytochemistry and methods that enhance detection of amyloidogenic proteins to investigate the types of
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22. Immunoaffinity purification and neutralization of scrapie prion infectivity.
Prions are unusual infectious pathogens causing scrapie of sheep and goats as well as Creutzfeldt-Jakob disease of humans. Biochemical and genetic studies contend that the scrapie isoform of the prion protein (PrPSc) is a major component of the prion. Limited proteinase K digestion of PrPSc produced a protein of 27-30 kDa. After dispersion of brain microsome
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23. Immunological comparison of scrapie-associated fibrils isolated from animals infected with four different scrapie strains.
Scrapie-associated fibrils (SAFs) are abnormal filamentous structures that are uniquely associated with unconventional slow virus diseases. The antigenic relationships of SAFs from animals infected with four biologically distinct scrapie strains were investigated by using antisera raised to purified SAF proteins. Rabbit antisera were raised to SAFs isolated
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24. A 54-kDa normal cellular protein may be the precursor of the scrapie agent protease-resistant protein.
Scrapie is the best understood of the transmissible spongiform encephalopathies. These neurologic disorders include the human diseases kuru and Creutzfeldt-Jakob disease and are caused by pathogens with unique biological and molecular properties. One major protein, protease-resistant protein (PrP)-27-30, is present in fractions isolated from scrapie-infected