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Cellular prion protein in ovine milk
Biochemical and Biophysical Research Communications, 2007Cellular prion protein, PrP(C), is essential for the development of prion diseases where it is considered to be a substrate for the formation of the disease-associated conformer, PrP(Sc). In sheep, PrP(C) is abundant in neuronal tissue and is also found at lower concentrations in a range of non-neuronal tissues, including mammary gland.
Ben C, Maddison +2 more
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The biology of the cellular prion protein
Neurochemistry International, 2002Prions are the etiological agents for infectious degenerative encephalopaties acting by inducing conformational changes in the cellular prion protein (PrPc), which is a cell membrane GPI anchored glycoprotein. Besides its conservation among species and expression in most tissues, and in particular, in high levels in the nervous system, the role for ...
Vilma Regina, Martins +1 more
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The cellular and pathologic prion protein
2018The cellular prion protein, PrPC, is a small, cell surface glycoprotein with a function that is currently somewhat ill defined. It is also the key molecule involved in the family of neurodegenerative disorders called transmissible spongiform encephalopathies, which are also known as prion diseases.
Andrew Gill, Andrew R. Castle
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Nonneuronal cellular prion protein
2001The normal cellular prion protein (PrP(c)) is a membrane sialoglycoprotein of unknown function having the unique property of adopting an abnormal tertiary conformation. The pathological conformer PrP(sc) would be the agent of transmissible spongiform encephalopathies or prion diseases.
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Alzheimer's disease, cellular prion protein, and dolphins
Alzheimer's & Dementia, 2018The present Letter comments the fascinating article by Dr Gunn-Moore and coworkers, reporting for the first time Alzheimer’s disease (AD)-related pathological findings in the brain tissue from two wild dolphin species. In this respect, based upon the crucial role played by the cellular prion protein (PrPC) in AD pathogenesis, characterizing the ...
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NMR Structural Studies of Human Cellular Prion Proteins
Current Topics in Medicinal Chemistry, 2013Prion diseases or transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative disorders associated with the conformational conversion of the cellular prion protein, PrP(C), into a pathological form known as prion or PrP(Sc). They can be classified into sporadic, inherited and infectious forms.
Biljan, I. +4 more
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Cellular prion protein and GABAA receptors: no physical association?
NeuroReport, 1995The so-called prion diseases are probably caused by the conformational conversion of the cellular prion protein (PrPc) into an abnormal, pathological form (PrPsc). PrPc is widely expressed in neuronal tissues, but its function is not known. From electrophysiological measurements in prion-less mice it was proposed that PrPc may contribute to the ...
K, Kannenberg, M H, Groschup, E, Sigel
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Cellular Prion Protein and Cancers
2012Prion was first identified as the infectious agent of prion disease, since then the biological functions of PrP have been extensively studied. One of the functions of this glycosylphosphatidylinositol (GPI)-anchored protein is to act as an apoptotic regulator. Studies have shown that prion protein (PrP) is upregulated in some cancers including gastric,
Wei Xin, Man-sun Sy, Chaoyang Li
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Insoluble Cellular Prion Protein
2012The detergent-soluble cellular prion protein (PrPC) and its detergent-insoluble infectious isoform (PrPSc) are two major conformers of the prion protein. Soluble PrPC has been the only isoform detected in the normal mammalian brain. In 2006, however, we identified an insoluble PrPC conformer (termed iPrPC) in uninfected human and animal brains.
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Scrapie and Cellular Prion Proteins Share Polypeptide Epitopes
Journal of Infectious Diseases, 1986Purified preparations of scrapie prions contain one major protein, PrP 27-30, and aggregates of rod-shaped structures. On the basis of the NH2-terminal amino acid sequence of PrP 27-30, a synthetic peptide (PrP-P1) was constructed. Monospecific rabbit antisera to PrP-P1 were found by immunoblotting to react with PrP 27-30 and its precursor (PrP 33-35Sc)
R A, Barry +6 more
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