"Hub\u00E1lek, Jarom\u00EDr" . . . "H\u00FAska, Dalibor" . "Beklov\u00E1, Miroslava" . "978-80-7375-514-0" . . . "43210" . "Electrochemical behaviuor of (PRPC) and changed (PRPSC) prion protein" . . "Electrochemical behaviuor of (PRPC) and changed (PRPSC) prion protein" . . . "Mendelova zem\u011Bd\u011Blsk\u00E1 a lesnick\u00E1 univerzita v Brn\u011B" . "P(GA102/08/1546), P(KAN208130801)" . "Electrochemical behaviuor of (PRPC) and changed (PRPSC) prion protein"@en . . "prion protein; infectious diseases; nerve cells"@en . "[91EE1FC85653]" . "Adam, Vojt\u011Bch" . "Majzl\u00EDk, Petr" . "2011-01-01+01:00"^^ . . "XI. pracovn\u00ED setk\u00E1n\u00ED fyzik\u00E1ln\u00EDch chemik\u016F a elektrochemik\u016F" . "7"^^ . . "3"^^ . . . . . "Brno" . "Kizek, Ren\u00E9" . . . . "MENDELU" . "197025" . "\u0160obrov\u00E1, Pavl\u00EDna" . "7"^^ . . "Prion diseases are fatal neurodegenerative and infectious disorders of humans and animals, characterized by structural transition of the host-encoded cellular prion protein (PrPC) into the aberrantly folded pathologic isoform PrPSc. Prion protein is a biomolecule naturally occurring in the animal cells. This protein is present in all mammal cells and occurs primarily in neural cells and immune system cells. The main aim of this study was to optimize electrochemical methods for the detection of natural (PrPC) and changed (PrPSC) prion protein. To carry out the main objective a complex study of the electrochemical behaviour of both proteins was required. For this purpose fundamental electrochemical techniques were used. Both of the prions were characterized using different techniques, their limits of detection were found at pM levels and possible ability to change the structure of alpha-helix of natural prion (PrPC) to beta-sheet of the infectious prion (PrPSc) were monitored." . . "RIV/62156489:43210/11:00173966!RIV12-AV0-43210___" . "Electrochemical behaviuor of (PRPC) and changed (PRPSC) prion protein"@en . . . . "RIV/62156489:43210/11:00173966" . . "Prion diseases are fatal neurodegenerative and infectious disorders of humans and animals, characterized by structural transition of the host-encoded cellular prion protein (PrPC) into the aberrantly folded pathologic isoform PrPSc. Prion protein is a biomolecule naturally occurring in the animal cells. This protein is present in all mammal cells and occurs primarily in neural cells and immune system cells. The main aim of this study was to optimize electrochemical methods for the detection of natural (PrPC) and changed (PrPSC) prion protein. To carry out the main objective a complex study of the electrochemical behaviour of both proteins was required. For this purpose fundamental electrochemical techniques were used. Both of the prions were characterized using different techniques, their limits of detection were found at pM levels and possible ability to change the structure of alpha-helix of natural prion (PrPC) to beta-sheet of the infectious prion (PrPSc) were monitored."@en . .