Prion Protein Gene
Mostrando 1-12 de 97 artigos, teses e dissertações.
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1. Calcium homeostasis modulator 1 ( CALHM1 ) polymorphisms in cattle
ABSTRACT: The calcium homeostasis modulator 1 gene (CALHM1), which is located on chromosome 10 in humans and on chromosome 26 in cattle, is a transmembrane glycoprotein that controls the cytosolic calcium concentrations. Altered calcium homeostasis has been associated with several neurodegenerative disorders, including Alzheimer’s disease (AD). In a recent
Pesq. Vet. Bras.. Publicado em: 2017-06
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2. Detecção de polimorfismos do gene da proteína priônica no rebanho ovino do Estado de São Paulo: métodos e aplicabilidade à seleção para resistência ao scrapie / Detection of Polymorphisms in the prion protein gene in Sheeps flock in the State of São Paulo: Methods and Applicability of Selection for Scrapie Resistance
Scrapie ou paraplexia enzoótica dos ovinos é uma doença neurodegenerativa fatal que acomete ovinos e raramente caprinos. A doença é influenciada por polimorfismos nos códons 136, 154 e 171 do gene prnp que codifica a proteína priônica. Os animais podem ser susceptíveis ou resistentes, de acordo com as sequências alélicas observadas nos referidos c
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 31/05/2012
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3. Poliformismos do gene da proteína príon celular em pacientes com doença de Alzheimer / Prion protein gene polymorphism in Alzheimers disease
INTRODUÇÃO: Os polimorfismos do gene da proteína priônica (PRNP) podem estar associados a doenças neurológicas não priônicas. Estudos em pacientes com doença de Alzheimer (DA) apontam para possível associação entre os polimorfismos do códon 129 do PRNP e DA. Essa associação não foi estudada na população brasileira. Neste estudo, descrevemos
Publicado em: 2011
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4. The prion protein and New World primate phylogeny
The PrP C prion protein contains 250 amino acids with some variation among species and is expressed in several cell types. PrP C is converted to PrP Sc by a post-translational process in which it acquires amino acid sequences of three-dimensional conformation of beta-sheets. Variations in the prion protein gene were observed among 16 genera of New World prim
Genetics and Molecular Biology. Publicado em: 2004
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5. 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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6. Estudo da regulação da expressão do gene da proteína prion celular / Cellular prion protein gene expression regulation
A conversão da proteína prion celular normal (PrPc), cuja função ainda esta sob investigação, para a forma infecciosa (PrPsc) é a causa de algumas doenças neurodegenerativas em humanos e animais. Vários estudos têm sido realizados e mostram que PrPc pode participar de processos normais como memória, estresse oxidativo, neuritogênese e outros. Por
Publicado em: 2001
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7. Antibody to DNA detects scrapie but not normal prion protein
Prion diseases, a group of fatal neurodegenerative disorders, are characterized by the presence of the abnormal scrapie isoform of prion protein (PrPSc) in affected brains. A conformational change is believed to convert the normal cellular prion protein into PrPSc. Detection of PrPSc for diagnosis and prophylaxis is impaired because available Abs recognizing
National Academy of Sciences.
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8. The prion protein gene is dispensable for the development of spongiform myeloencephalopathy induced by the neurovirulent Cas-Br-E murine leukemia virus.
The Cas-Br-E murine leukemia virus (MuLV) induces paralysis in susceptible mice that is accompanied by a severe spongiform myeloencephalopathy. These neurodegenerative lesions are very similar to those observed in prion diseases. To determine whether the prion protein gene (Prn-p) product was a downstream effector of this neurovirulent MuLV, we inoculated Pr
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9. Neurodegeneration in humans caused by prions.
Prion diseases include kuru, Creutzfeldt-Jakob disease, Gerstmann-Sträussler-Scheinker disease, and fatal familial insomnia of humans as well as scrapie and bovine spongiform encephalopathy of animals. For many years, the prion diseases were thought to be caused by viruses despite evidence to the contrary. The unique characteristic common to all of these di
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10. Prion-induced Activation of Cholesterogenic Gene Expression by Srebp2 in Neuronal Cells*
Prion diseases are neurodegenerative diseases associated with the accumulation of a pathogenic isoform of the host-encoded prion protein. The cellular responses to prion infection are not well defined. By performing microarray analysis on cultured neuronal cells infected with prion strain 22L, in the group of up-regulated genes we observed predominantly gene
American Society for Biochemistry and Molecular Biology.
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11. Assignment of the human and mouse prion protein genes to homologous chromosomes.
Purified preparations of scrapie prions contain one major macromolecule, designated prion protein (PrP). Genes encoding PrP are found in normal animals and humans but not within the infectious particles. The PrP gene was assigned to human chromosome 20 and the corresponding mouse chromosome 2 using somatic cell hybrids. In situ hybridization studies mapped t
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12. Medical genetics: advances in brief: Fatal familial insomnia, a prion disease with a mutation at codon 178 of the prion protein gene