| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Fabio Moda, Thanh-Nhat T Le, Suzana Aulić, Edoardo Bistaffa, Ilaria Campagnani, Tommaso Virgilio, Antonio Indaco, Luisa Palamara, Olivier Andréoletti, Fabrizio Tagliavini, Giuseppe Legnam. Synthetic prions with novel strain-specified properties. PLoS pathogens. vol 11. issue 12. 2016-05-10. PMID:26720726. |
the information for strains and structural specific barriers appears to be contained exclusively in the folding of the pathological isoform, prp(sc). |
2016-05-10 |
2023-08-13 |
mouse |
| Fabio Moda, Thanh-Nhat T Le, Suzana Aulić, Edoardo Bistaffa, Ilaria Campagnani, Tommaso Virgilio, Antonio Indaco, Luisa Palamara, Olivier Andréoletti, Fabrizio Tagliavini, Giuseppe Legnam. Synthetic prions with novel strain-specified properties. PLoS pathogens. vol 11. issue 12. 2016-05-10. PMID:26720726. |
neither infected brain extracts nor amplified prp(sc) were used. |
2016-05-10 |
2023-08-13 |
mouse |
| William Wan, Holger Wille, Jan Stöhr, Amy Kendall, Wen Bian, Michele McDonald, Sarah Tiggelaar, Joel C Watts, Stanley B Prusiner, Gerald Stubb. Structural studies of truncated forms of the prion protein PrP. Biophysical journal. vol 108. issue 6. 2016-05-05. PMID:25809267. |
even these larger fragments did not adopt the prion structure itself with detailed fidelity, and in some cases their structures were radically different from that of pathogenic prp(sc). |
2016-05-05 |
2023-08-13 |
Not clear |
| Takujiro Homma, Daisuke Ishibashi, Takehiro Nakagaki, Takayuki Fuse, Tsuyoshi Mori, Katsuya Satoh, Ryuichiro Atarashi, Noriyuki Nishid. Ubiquitin-specific protease 14 modulates degradation of cellular prion protein. Scientific reports. vol 5. 2016-05-05. PMID:26061634. |
the accumulated prp, termed prp(sc), forms amyloid fibrils and could be infectious. |
2016-05-05 |
2023-08-13 |
Not clear |
| Takujiro Homma, Daisuke Ishibashi, Takehiro Nakagaki, Takayuki Fuse, Tsuyoshi Mori, Katsuya Satoh, Ryuichiro Atarashi, Noriyuki Nishid. Ubiquitin-specific protease 14 modulates degradation of cellular prion protein. Scientific reports. vol 5. 2016-05-05. PMID:26061634. |
it has been suggested that prp(sc) is abnormally folded and resistant to proteolytic degradation, and also inhibits proteasomal functions in infected cells, thereby inducing neuronal death. |
2016-05-05 |
2023-08-13 |
Not clear |
| Takujiro Homma, Daisuke Ishibashi, Takehiro Nakagaki, Takayuki Fuse, Tsuyoshi Mori, Katsuya Satoh, Ryuichiro Atarashi, Noriyuki Nishid. Ubiquitin-specific protease 14 modulates degradation of cellular prion protein. Scientific reports. vol 5. 2016-05-05. PMID:26061634. |
results from the present study showed that treatment with a selective inhibitor of usp14 reduced prp(c), as well as prp(sc), levels in prion-infected neuronal cells. |
2016-05-05 |
2023-08-13 |
Not clear |
| Takujiro Homma, Daisuke Ishibashi, Takehiro Nakagaki, Takayuki Fuse, Tsuyoshi Mori, Katsuya Satoh, Ryuichiro Atarashi, Noriyuki Nishid. Ubiquitin-specific protease 14 modulates degradation of cellular prion protein. Scientific reports. vol 5. 2016-05-05. PMID:26061634. |
overexpression of the dominant negative mutant form of usp14 reduced prp(sc), whereas wildtype usp14 increased prp(sc) in prion-infected cells. |
2016-05-05 |
2023-08-13 |
Not clear |
| Takujiro Homma, Daisuke Ishibashi, Takehiro Nakagaki, Takayuki Fuse, Tsuyoshi Mori, Katsuya Satoh, Ryuichiro Atarashi, Noriyuki Nishid. Ubiquitin-specific protease 14 modulates degradation of cellular prion protein. Scientific reports. vol 5. 2016-05-05. PMID:26061634. |
collectively, a better understanding about the regulation of prp(sc) clearance caused by usp14 might contribute greatly to the development of therapeutic strategies for prion diseases. |
2016-05-05 |
2023-08-13 |
Not clear |
| Nina Klimova, Natallia Makarava, Ilia V Baskako. The diversity and relationship of prion protein self-replicating states. Virus research. vol 207. 2016-05-02. PMID:25312451. |
it has become evident that the prion protein (prp) can form a diverse range of self-replicating structures in addition to bona fide prp(sc) or strain-specific prp(sc) variants. |
2016-05-02 |
2023-08-13 |
Not clear |
| Nina Klimova, Natallia Makarava, Ilia V Baskako. The diversity and relationship of prion protein self-replicating states. Virus research. vol 207. 2016-05-02. PMID:25312451. |
we also discuss the possibility of the transformation of self-replicating states and triggering of prp(sc) formation within the frame of the deformed templating model. |
2016-05-02 |
2023-08-13 |
Not clear |
| Nhat Tran Thanh Le, Joanna Narkiewicz, Suzana Aulić, Giulia Salzano, Hoa Thanh Tran, Denis Scaini, Fabio Moda, Gabriele Giachin, Giuseppe Legnam. Synthetic prions and other human neurodegenerative proteinopathies. Virus research. vol 207. 2016-05-02. PMID:25449570. |
the common feature of these diseases is the pathological conversion of the normal cellular prion protein (prp(c)) into a β-structure-rich conformer-termed prp(sc). |
2016-05-02 |
2023-08-13 |
human |
| Nhat Tran Thanh Le, Joanna Narkiewicz, Suzana Aulić, Giulia Salzano, Hoa Thanh Tran, Denis Scaini, Fabio Moda, Gabriele Giachin, Giuseppe Legnam. Synthetic prions and other human neurodegenerative proteinopathies. Virus research. vol 207. 2016-05-02. PMID:25449570. |
much evidence suggests that prp(sc) itself is able to recruit and misfold prp(c) into the pathological conformation. |
2016-05-02 |
2023-08-13 |
human |
| Nhat Tran Thanh Le, Joanna Narkiewicz, Suzana Aulić, Giulia Salzano, Hoa Thanh Tran, Denis Scaini, Fabio Moda, Gabriele Giachin, Giuseppe Legnam. Synthetic prions and other human neurodegenerative proteinopathies. Virus research. vol 207. 2016-05-02. PMID:25449570. |
recent data have shown that recombinant prp(c) can be misfolded in vitro and the resulting synthetic conformers are able to induce the conversion of prp(c) into prp(sc)in vivo. |
2016-05-02 |
2023-08-13 |
human |
| Susan F Godsave, Peter J Peters, Holger Will. Subcellular distribution of the prion protein in sickness and in health. Virus research. vol 207. 2016-05-02. PMID:25683509. |
these protein misfolding diseases can be sporadic, acquired, or genetic and are caused by refolding of endogenous prp(c) into a beta sheet-rich, pathogenic form, prp(sc). |
2016-05-02 |
2023-08-13 |
cattle |
| Susan F Godsave, Peter J Peters, Holger Will. Subcellular distribution of the prion protein in sickness and in health. Virus research. vol 207. 2016-05-02. PMID:25683509. |
prp molecules can be broadly categorized as either 'good' (cellular) prp(c) or 'bad' (scrapie prion-type) prp(sc), but both populations are heterogeneous and different forms of prp(c) may influence various cellular activities. |
2016-05-02 |
2023-08-13 |
cattle |
| Susan F Godsave, Peter J Peters, Holger Will. Subcellular distribution of the prion protein in sickness and in health. Virus research. vol 207. 2016-05-02. PMID:25683509. |
both prp(c) and prp(sc) are localized predominantly at the cell surface, with the c-terminus attached to the plasma membrane via a glycosyl-phosphatidylinositol (gpi) anchor and both can exist in cleaved forms. |
2016-05-02 |
2023-08-13 |
cattle |
| Susan F Godsave, Peter J Peters, Holger Will. Subcellular distribution of the prion protein in sickness and in health. Virus research. vol 207. 2016-05-02. PMID:25683509. |
prp(c) also has cytosolic and transmembrane forms, and prp(sc) is known to exist in a variety of conformations and aggregation states. |
2016-05-02 |
2023-08-13 |
cattle |
| Susan F Godsave, Peter J Peters, Holger Will. Subcellular distribution of the prion protein in sickness and in health. Virus research. vol 207. 2016-05-02. PMID:25683509. |
here, we discuss the roles of different prp isoforms in sickness and in health, and show the subcellular distributions of several forms of prp that are particularly relevant for prp(c) to prp(sc) conversion and prion-induced pathology in the hippocampus. |
2016-05-02 |
2023-08-13 |
cattle |
| Christopher J Silva, Ester Vázquez-Fernández, Bruce Onisko, Jesús R Requen. Proteinase K and the structure of PrPSc: The good, the bad and the ugly. Virus research. vol 207. 2016-05-02. PMID:25816779. |
a defining characteristic of the transmissible isoform of the prion protein (prp(sc)) is its partial resistance to proteinase k (pk) digestion. |
2016-05-02 |
2023-08-13 |
Not clear |
| Christopher J Silva, Ester Vázquez-Fernández, Bruce Onisko, Jesús R Requen. Proteinase K and the structure of PrPSc: The good, the bad and the ugly. Virus research. vol 207. 2016-05-02. PMID:25816779. |
diagnosis of prion disease typically relies upon immunodetection of pk-digested prp(sc) by western blot, elisa or immunohistochemical detection. |
2016-05-02 |
2023-08-13 |
Not clear |