Results 321 to 330 of about 5,604,422 (355)

Therapeutic targeting of cellular prion protein: toward the development of dual mechanism anti-prion compounds. [PDF]

Neural Regen Res
Masone A, Zucchelli C, Caruso E, Musco G, Chiesa R.   +4 more
europepmc   +1 more source

Update on a brain-penetrant cardiac glycoside that can lower cellular prion protein levels in human and guinea pig paradigms. [PDF]

PLoS One
Eid S, Zhao W, Williams D, Nasser Z, Griffin J, Nagorny P, Schmitt-Ulms G.   +6 more
europepmc   +1 more source

Cellular prion protein acts as mediator of amyloid beta uptake by caveolin-1 causing cellular dysfunctions in vitro and in vivo. [PDF]

Alzheimers Dement
da Silva Correia A, Schmitz M, Fischer AL, da Silva Correia S, Simonetti FL, Saher G, Goya-Maldonado R, Arora AS, Fischer A, Outeiro TF, Zerr I.   +10 more
europepmc   +1 more source

Conformational dynamics as an intrinsic determinant of prion protein misfolding and neurotoxicity. [PDF]

Neural Regen Res
Cembran A, Fernandez-Funez P.
europepmc   +1 more source

Sensitive detection of pathological seeds of α-synuclein, tau and prion protein on solid surfaces. [PDF]

PLoS Pathog
Orrú CD, Groveman BR, Hughson AG, Barrio T, Isiofia K, Race B, Ferreira NC, Gambetti P, Schneider DA, Masujin K, Miyazawa K, Ghetti B, Zanusso G, Caughey B.   +13 more
europepmc   +1 more source

Copper binding alters the core structure of amyloid fibrils formed by Y145Stop human prion protein.

Phys Chem Chem Phys
Sridharan V, George T, Conroy DW, Shaffer Z, Surewicz WK, Jaroniec CP.   +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 ...
Hermann M. Schätzl, Sabine Gilch
openaire   +3 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   +2 more sources

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., Marchal, Stéphane, Rezaei, Human, Kornblatt, M. Judith, Balny, Claude, Lange, Reinhard, Debey, Marie-Pascale, Hui Bon Hoa, Gaston, Marden, Michael C., Grosclaude, Jeanne   +9 more
openaire   +4 more sources

Molecular Mechanism of the Misfolding and Oligomerization of the Prion Protein: Current Understanding and Its Implications.

Biochemistry, 2015
Prion diseases, also known as transmissible spongiform encephalopathies, make up a group of fatal neurodegenerative disorders linked with the misfolding and aggregation of the prion protein (PrP).
Jogender Singh, J. Udgaonkar
semanticscholar   +1 more source