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| FIGUEIREDO,CLAUDIA P.; FERREIRA,NATALIA C.; PASSOS,GISELLE F.; COSTA,ROBSON DA; NEVES,FERNANDA S.; MACHADO,CLARICE S.C.; MASCARELLO,ALESSANDRA; CHIARADIA-DELATORRE,LOUISE D.; NEUENFELDT,PATRÍCIA D.; NUNES,RICARDO J.; CORDEIRO,YRAIMA. |
| An altered form of the cellular prion protein, the PrPScor PrPRes, is implicated in the occurrence of the still untreatable transmissible spongiform encephalopathies. We have previously synthesized and characterized aromatic compounds that inhibit protease-resistant prion protein (PrPRes) accumulation in scrapie-infected cells. These compounds belong to different chemical classes, including acylhydrazones, chalcones and oxadiazoles. Some of the active compounds were non-toxic to neuroblastoma cells in culture and seem to possess drugable properties, since they are in agreement with the Lipinski´s rule of 5 and present desirable pharmacokinetic profiles as predicted in silico. Before the evaluation of the in vivo efficacy of the aromatic compounds in... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Prion; Acute toxicity; Organic compound; Drug safety; Scrapie; Pharmacokinetics. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000301421 |
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| Mokry,David Z.; Abrahão,Josielle; Ramos,Carlos H.I.. |
| The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Amyloid; Disaggregase; Shock protein; Molecular chaperones; Prion; Protein folding. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000301273 |
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| Leal,J.S.; Correa,G.L.F.; Boos,G.S.; Bianchi,M.V.; Boabaid,F.M.; Lopes,R.F.F.; Driemeier,D.. |
| Scrapie is a fatal and progressive transmissible spongiform encephalopathy (TSE) of natural occurrence in sheep and goats. The suspicion of scrapie may be based on clinical signs; however, the detection of pathological features of the prionic protein (PrP) in target tissues is necessary to diagnose the disease. The presence of an abnormal protein form (PrPSc) in lymphoreticular and nervous tissues is an important characteristic in diagnosis. This paper reports a case of scrapie in a flock of 55 Suffolk crossbred sheep, 19 Santa Inês sheep and 21 goats in the Mato Grosso state, midwestern Brazil. The animals were euthanized after the confirmation of a scrapie case with clinical signs in a Suffolk sheep in the same farm. Samples of brainstem at the level of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Scrapie; Prion; Diseases of small ruminants; Immunohistochemistry; Lymphoid tissues. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0102-09352015000601625 |
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| 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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