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A receptor for infectious and cellular prion protein BJMBR
Martins,V.R..
Prions are an unconventional form of infectious agents composed only of protein and involved in transmissible spongiform encephalopathies in humans and animals. The infectious particle is composed by PrPsc which is an isoform of a normal cellular glycosyl-phosphatidylinositol (GPI) anchored protein, PrPc, of unknown function. The two proteins differ only in conformation, PrPc is composed of 40% <FONT FACE="Symbol">a</FONT> helix while PrPsc has 60% ß-sheet and 20% <FONT FACE="Symbol">a</FONT> helix structure. The infection mechanism is trigged by interaction of PrPsc with cellular prion protein causing conversion of the latter's conformation. Therefore, the infection spreads because new PrPsc molecules are generated exponentially...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Prion; Transmissible spongiform encephalopathies; PrPc; Receptor.
Ano: 1999 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000700009
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Insights into the physiological function of cellular prion protein BJMBR
Martins,V.R.; Mercadante,A.F.; Cabral,A.L.B.; Freitas,A.R.O.; Castro,R.M.R.P.S..
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 involves the interaction of PrPsc with its cellular isoform (PrPc) and subsequently abnormal structural conversion of the latter. PrPc is a glycoprotein anchored on the cell surface by a glycosylphosphatidylinositol moiety and expressed in most cell types but mainly in neurons. Prion diseases have been associated with the accumulation of the abnormally folded protein and its neurotoxic effects;...
Tipo: Info:eu-repo/semantics/article Palavras-chave: PrPc; Cellular function; Transmissible spongiform encephalopathies; Laminin; Signal transduction; Copper.
Ano: 2001 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001000500005
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