Results 261 to 270 of about 97,377 (307)

Aptamers against prion proteins and prions

Cellular and Molecular Life Sciences, 2009
Prion diseases are fatal neurodegenerative and infectious disorders of humans and animals, characterized by structural transition of the host-encoded cellular prion protein (PrP(c)) into the aberrantly folded pathologic isoform PrP(Sc). RNA, DNA or peptide aptamers are classes of molecules which can be selected from complex combinatorial libraries for ...
Sabine, Gilch, Hermann M, Schätzl
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Mammalian prion proteins

Current Opinion in Structural Biology, 2000
The past two years have seen the extension of our knowledge on the cellular prion protein structure with new NMR data on both the hamster and human proteins. In addition, the folding dynamics of two cellular prion proteins have been elucidated. There are now several examples of recombinant prion proteins that are able to adopt different conformations ...
Jackson, GS, Clarke, AR
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Human prion diseases with variant prion protein

Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, 1994
Recent molecular genetic studies revealed that the human prion protein (PrP) gene has a large repertoire of polymorphisms and mutations. Each variant PrP seems to correspond to a distinct type of prion diseases. W e report herein that it is useful to classify prion diseases into plaque type or non-plaque type, based on the distribution of PrP in the ...
T, Kitamoto, J, Tateishi
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Prion Protein Oligomerization

Current Alzheimer Research, 2008
The PrP propensity to adopt different structures is tightly linked to transmissible spongiform encephalopathies (TSE) which include Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scjeinker (GSS) and Kuru syndrome. In most cases, TSE is associated with the accumulation in the brain of an abnormally folded protease-resistant protein, PrP Sc or ...
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Structural Studies of Prion Proteins and Prions

2011
Prion diseases are a group of fatal and incurable neurodegenerative ­disorders of mammals. They uniquely manifest as sporadic, genetic, and infectious maladies. The agent responsible for prion diseases is the prion. A prion is defined as a proteinaceous infectious particle, which is solely constituted by an alternately folded form of the prion protein (
Legname, Giuseppe, GIACHIN G, BENETTI F.
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Prions and prion proteins.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 1991
Neurodegenerative diseases of animals and humans including scrapie, bovine spongiform encephalopathy, and Creutzfeldt-Jakob disease are caused by unusual infectious pathogens called prions. There is no evidence for a nucleic acid in the prion, but diverse experimental results indicate that a host-derived protein called PrPSc is a component of the ...
N, Stahl, S B, Prusiner
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Immunology of Prion Protein and Prions

2017
Many natural prion diseases are acquired peripherally, such as following the oral consumption of contaminated food or pasture. After peripheral exposure many prion isolates initially accumulate to high levels within the host's secondary lymphoid tissues. The replication of prions within these tissues is essential for their efficient spread to the brain
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Mapping Functional Prion–Prion Protein Interaction Sites Using Prion Protein Based Peptide-Arrays

2009
Protein-protein interactions are at the basis of most if not all biological processes in living cells. Therefore, adapting existing techniques or developing new techniques to study interactions between proteins are of importance in elucidating which amino acid sequences contribute to these interactions.
Rigter, A., Priem, J., Timmers-Parohi, D., Langeveld, J., Bossers, A.   +4 more
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Prion proteins: a biological role beyond prion diseases

Acta Neurologica Scandinavica, 2007
The biological role of the scrapie isoform of prion protein (PrP(Sc)) as an infectious agent in numerous human and non-human disorders of the central nervous system is well established. In contrast, and despite decades of intensive research, the physiological function of the endogenous cellular form of the prion protein (PrP(C)) remains elusive.
W, Hu, R N, Rosenberg, O, Stüve
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