Results 221 to 230 of about 1,598,142 (264)

Leveraging the dominant-negative effect of the kuru-protective G127V prion protein variant as a novel therapeutic strategy. [PDF]

open access: yesNeurobiol Dis
Gatdula JRP   +11 more
europepmc   +1 more source

Prion propagation is controlled by discrete structural regions of PrP rather than overall stability. [PDF]

open access: yesJ Biol Chem
Bhamra SK   +8 more
europepmc   +1 more source

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
openaire   +2 more sources

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.
openaire   +1 more source

The fate of the prion protein in the prion/plasminogen complex

Biochemical and Biophysical Research Communications, 2003
The cellular prion protein (PrP(c)) forms complexes with plasminogen. Here, we show that the PrP(c) in this complex is cleaved to yield fragments of PrP(c). The cleavage is accelerated by plasmin but does not appear to be dependent on it.
Kornblatt, Jack A.   +9 more
openaire   +3 more sources

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