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Molecular biology of prion diseases

Prusiner, S.B. (University of California, San Francisco, CA)

Science (American Association for the Advancement of Science), 1991-06, Vol.252 (5012), p.1515-1522 [Periódico revisado por pares]

Washington, DC: American Society for the Advancement of Science

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Título:
Molecular biology of prion diseases
Autor: Prusiner, S.B. (University of California, San Francisco, CA)
Assuntos: Amino acids ; Amyloids ; Animals ; Biological and medical sciences ; Biology ; Codons ; Creutzfeldt-Jakob Syndrome - genetics ; Creutzfeldt-Jakob Syndrome - microbiology ; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases ; Disease ; EXPRESION GENICA ; EXPRESSION DES GENES ; Genes, Viral ; GENETICA MOLECULAR ; GENETIQUE MOLECULAIRE ; Gerstmann-Straussler-Scheinker Disease - genetics ; Gerstmann-Straussler-Scheinker Disease - microbiology ; Humans ; Medical research ; Medical sciences ; Mice ; Molecules ; Nervous system diseases ; Neurology ; Neurons ; Open Reading Frames ; Physiological aspects ; Prion diseases ; Prions ; Prions - genetics ; Prions - pathogenicity ; PrPSc Proteins ; Scrapie - genetics ; Scrapie - microbiology ; Transgenic animals ; TRASTORNOS DEL SISTEMA NERVIOSO ; TROUBLE DU SYSTEME NERVEUX ; Viral Proteins - genetics ; VIRUS TEMBLADERA DE LOS OVINOS ; VIRUS TREMBLANTE DU MOUTON
É parte de: Science (American Association for the Advancement of Science), 1991-06, Vol.252 (5012), p.1515-1522
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Descrição: Prions cause transmissible and genetic neurodegenerative diseases, including scrapie and bovine spongiform encephalopathy of animals and Creutzfeldt-Jakob and Gerstmann-Straussler-Scheinker diseases of humans. Infectious prion particles are composed largely, if not entirely, of an abnormal isoform of the prion protein, which is encoded by a chromosomal gene. A posttranslational process, as yet unidentified, converts the cellular prion protein into an abnormal isoform. Scrapie incubation times, neuropathology, and prion synthesis in transgenic mice are controlled by the prion protein gene. Point mutations in the prion protein genes of animals and humans are genetically linked to development of neurodegeneration. Transgenic mice expressing mutant prion proteins spontaneously develop neurologic dysfunction and spongiform neuropathology. Understanding prion diseases may advance investigations of other neurodegenerative disorders and of the processes by which neurons differentiate, function for decades, and then grow senescent
Editor: Washington, DC: American Society for the Advancement of Science
Idioma: Inglês

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Molecular biology of prion diseases

Prusiner, S.B. (University of California, San Francisco, CA)

Washington, DC: American Society for the Advancement of Science

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