Results 221 to 230 of about 50,704 (271)

Brainwide silencing of prion protein by AAV-mediated delivery of an engineered compact epigenetic editor. [PDF]

Science
Neumann EN, Bertozzi TM, Wu E, Serack F, Harvey JW, Brauer PP, Pirtle CP, Coffey A, Howard M, Kamath N, Lenz K, Guzman K, Raymond MH, Khalil AS, Deverman BE, Minikel EV, Vallabh SM, Weissman JS.   +17 more
europepmc   +1 more source

Prion protein alters viral control and enhances pathology after perinatal cytomegalovirus infection. [PDF]

Nat Commun
Karner D, Kvestak D, Kucan Brlic P, Cokaric Brdovcak M, Lisnic B, Brizic I, Juranic Lisnic V, Golemac M, Tomac J, Krmpotic A, Karkeni E, Libri V, Mella S, Legname G, Altmeppen HC, Hasan M, Jonjic S, Lenac Rovis T.   +17 more
europepmc   +1 more source

X-Ray Photon Correlation Spectroscopy, Microscopy, and Fluorescence Recovery After Photobleaching to Study Phase Separation and Liquid-to-Solid Transition of Prion Protein Condensates. [PDF]

Bio Protoc
do Amaral MJ, Passos AR, Mohapatra S, Freire MH, Wegmann S, Cordeiro Y.   +5 more
europepmc   +1 more source

Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer's Disease, Parkinson's Disease and Prionopathies. [PDF]

Int J Mol Sci
Cehlar O, Njemoga S, Horvath M, Cizmazia E, Bednarikova Z, Barrera EE.   +5 more
europepmc   +1 more source

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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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