WordNet

any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
the 16th letter of the Roman alphabet (同)p

PrepTutorEJDIC

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

Quantitative Real-Time Quaking-Induced Conversion Allows Monitoring of Disease-Modifying Therapy in the Urine of Prion-Infected Mice.

Shi S1, Wagner J, Mitteregger-Kretzschmar G, Ryazanov S, Leonov A, Griesinger C, Giese A.
Journal of neuropathology and experimental neurology.J Neuropathol Exp Neurol.2015 Sep;74(9):924-33. doi: 10.1097/NEN.0000000000000233.
Prion diseases are fatal neurodegenerative diseases characterized by accumulation of the pathogenic prion protein PrP in the brain. We established quantitative real-time quaking-induced conversion for the measurement of minute amounts of PrP in body fluids such as urine. Using this approach, we moni
PMID 26247395

Mutant PrPCJD prevails over wild-type PrPCJD in the brain of V210I and R208H genetic Creutzfeldt-Jakob disease patients.

Cardone F1, Principe S2, Schininà ME3, Maras B3, Capellari S4, Parchi P4, Notari S5, Di Francesco L3, Poleggi A2, Galeno R2, Vinci R2, Mellina V2, Almonti S2, Ladogana A2, Pocchiari M2.
Biochemical and biophysical research communications.Biochem Biophys Res Commun.2014 Nov 14;454(2):289-94. doi: 10.1016/j.bbrc.2014.10.051. Epub 2014 Oct 19.
Creutzfeldt-Jakob disease (CJD) is a neurodegenerative disorder characterized by the deposition of the pathological conformer (PrP(CJD)) of the host encoded cellular prion protein (PrP(C)). In genetic CJD associated with V210I or R208H PrP substitutions, the pathogenic role of mutant residues is sti
PMID 25450391

The structure of the infectious prion protein: experimental data and molecular models.

Requena JR, Wille H.
Prion.Prion.2014 Jan-Feb;8(1):60-6.
The structures of the infectious prion protein, PrP(Sc), and that of its proteolytically truncated variant, PrP 27-30, have evaded experimental determination due to their insolubility and propensity to aggregate. Molecular modeling has been used to fill this void and to predict their structures, but
PMID 24583975