Biophysical Studies on Structure Structural Transitions and Infectivity of the Prion Protein

Autor:	Stanley B. Prusiner, Darlene Groth, Holger Wille, Hana Serban, Martin Pitschke, Detlev Riesner, Michael A. Baldwin, Karin Post, K. Kellings
Rok vydání:	1998
Předmět:	Infectivity Gene isoform medicine.diagnostic_test Chemistry animal diseases Proteolysis Scrapie agent Virology nervous system diseases Cell biology nervous system Protease resistant medicine Sucrose gradient centrifugation Prion protein Gene
Zdroj:	Prions and Brain Diseases in Animals and Humans ISBN: 9781489918987
Popis:	Prions are composed largely, if not entirely, of an abnormal isoform of the prion protein (PrP) designated PrPSc. A protease resistant polypeptide, PrP 27–30, can be derived from PrPSc by limited proteolysis with retention of infectivity. Both PrPSc and the cellular isoform PrPC are encoded by a chromosomal gene; PrPSc is produced from the cellular isoform by a posttranslational process (for review see Prusiner, 1991).
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::7b98ae9342573d6ae2e46a768a9fdc32 https://doi.org/10.1007/978-1-4899-1896-3_23 Zobrazit plný text záznamu