منابع مشابه
The prion protein knockout mouse: a phenotype under challenge.
The key pathogenic event in prion disease involves misfolding and aggregation of the cellular prion protein (PrP). Beyond this fundamental observation, the mechanism by which PrP misfolding in neurons leads to injury and death remains enigmatic. Prion toxicity may come about by perverting the normal function of PrP. If so, understanding the normal function of PrP may help to elucidate the molec...
متن کاملB lymphocyte-restricted expression of prion protein does not enable prion replication in prion protein knockout mice.
Prion replication in spleen and neuroinvasion after i.p. inoculation of mice is impaired in forms of immunodeficiency where mature B lymphocytes are lacking. In spleens of wild-type mice, infectivity is associated with B and T lymphocytes and stroma but not with circulating lymphocytes. We generated transgenic prion protein knockout mice overexpressing prion protein in B lymphocytes and found t...
متن کاملGlycidol degrades scrapie mouse prion protein.
Agents of transmissible spongiform encephalopathy (prion) are known to be extremely resistant to physicochemical inactivation procedures such as heat, radiation, chemical disinfectants such as detergents, alcohols, glutaraldehyde, formalin, and so on. Because of its remarkable resistance, it is difficult to inactivate prion. Chemical inactivation seems to be a practical method because it is app...
متن کاملMRS of the mouse lacking prion protein (Prnp-/-) at 14.1T
Introduction: The prion diseases form a group of fatal neurodegenerative diseases, also described as transmissible spongiform encephalopathies (TSEs), which are caused by abnormal conformational isomers (PrP) of the host-encoded prion proteins (PrP) (1). The mechanism by which prions elicit brain damage and the relative contributions of PrP accumulation and PrP depletion to the prion replicatio...
متن کاملCRISPR-Cas9-Based Knockout of the Prion Protein and Its Effect on the Proteome
The molecular function of the cellular prion protein (PrPC) and the mechanism by which it may contribute to neurotoxicity in prion diseases and Alzheimer's disease are only partially understood. Mouse neuroblastoma Neuro2a cells and, more recently, C2C12 myocytes and myotubes have emerged as popular models for investigating the cellular biology of PrP. Mouse epithelial NMuMG cells might become ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Prion
سال: 2007
ISSN: 1933-6896,1933-690X
DOI: 10.4161/pri.1.2.4346