Results 241 to 250 of about 3,400,014 (272)
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Physiology of the Prion Protein
Physiological Reviews, 2008Prion diseases are transmissible spongiform encephalopathies (TSEs), attributed to conformational conversion of the cellular prion protein (PrPC) into an abnormal conformer that accumulates in the brain. Understanding the pathogenesis of TSEs requires the identification of functional properties of PrPC.
Rafael, Linden +5 more
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Cellular and Molecular Life Sciences, 2007
From Creutzfeldt-Jakob disease (CJD) to variant CJD through Gerstmann-Sträussler-Scheinker syndrome, kuru and fatal familial insomnia, the journey leading to current understanding of the basic aspects of human prion diseases has been full of unexpected, but often dramatic and always fascinating twists.
W Q, Zou, P, Gambetti
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From Creutzfeldt-Jakob disease (CJD) to variant CJD through Gerstmann-Sträussler-Scheinker syndrome, kuru and fatal familial insomnia, the journey leading to current understanding of the basic aspects of human prion diseases has been full of unexpected, but often dramatic and always fascinating twists.
W Q, Zou, P, Gambetti
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Prion Protein Disease and Neuropathology of Prion Disease
Neuroimaging Clinics of North America, 2008Human prion diseases, in common with other neurodegenerative diseases, may be sporadic or inherited and are characterized by the accumulation of cellular proteins accompanied by neuronal death and synaptic loss. Prion diseases are, however, unique in being transmissible.
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Infective Proteins: The Prion Puzzle
Current Protein & Peptide Science, 2001According to the Koch postulates an infectious organism is the one that can be isolated from an host suffering from a disorder, can be propagated in laboratory, can cause the same disease when introduced in another host, and finally, can be re-isolated from the host itself.
F. Ceciliani, P. Pergami
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A Function for the Prion Protein?
2003Protein function is often observed directly following protein isolation, or is deduced by loss of function following gene knockout or by analogy with proteins of known function and similar amino acid sequence. None of these is true in the case of prion proteins because aside from the association with the pathogenesis of the spongiform encaphalopathies,
D R, Brown, I M, Jones
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Photo-induced crosslinking of prion protein oligomers and prions
Amyloid, 2006Prion diseases are caused by a unique type of infectious agent, which is thought to consist of a misfolded beta-sheeted form of the alpha-helical cellular prion protein (PrPC). This misfolded isoform (PrPSc) tends to form insoluble amyloid-like aggregates, impeding classical structural analysis by X-ray crystallography or NMR.
Niklas, Piening +5 more
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Prion Protein: The Molecule of Many Forms and Faces
International Journal of Molecular Sciences, 2022Valerija Kovac, Vladka Curin Šerbec
exaly
N-Terminal Regions of Prion Protein: Functions and Roles in Prion Diseases
International Journal of Molecular Sciences, 2020Suehiro Sakaguchi
exaly