| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Kazunori Sano, Ryuichiro Atarashi, Daisuke Ishibashi, Takehiro Nakagaki, Katsuya Satoh, Noriyuki Nishid. Conformational properties of prion strains can be transmitted to recombinant prion protein fibrils in real-time quaking-induced conversion. Journal of virology. vol 88. issue 20. 2014-11-25. PMID:25078700. |
importance: the phenomenon of prion strains with distinct biological characteristics is assumed to result from the conformational variations in the abnormal prion protein (prp(sc)). |
2014-11-25 |
2023-08-13 |
mouse |
| Kazunori Sano, Ryuichiro Atarashi, Daisuke Ishibashi, Takehiro Nakagaki, Katsuya Satoh, Noriyuki Nishid. Conformational properties of prion strains can be transmitted to recombinant prion protein fibrils in real-time quaking-induced conversion. Journal of virology. vol 88. issue 20. 2014-11-25. PMID:25078700. |
in this study, we investigated whether the properties of diverse prion strains can be transmitted to amyloid fibrils consisting of e. coli-derived recombinant prp (rprp) generated by real-time quaking-induced conversion (rt-quic), a recently developed in vitro prp(sc) formation method. |
2014-11-25 |
2023-08-13 |
mouse |
| Kazunori Sano, Ryuichiro Atarashi, Daisuke Ishibashi, Takehiro Nakagaki, Katsuya Satoh, Noriyuki Nishid. Conformational properties of prion strains can be transmitted to recombinant prion protein fibrils in real-time quaking-induced conversion. Journal of virology. vol 88. issue 20. 2014-11-25. PMID:25078700. |
we demonstrate that at least some of the strain-specific conformational properties can be transmitted to rprp fibrils in the first round of rt-quic by examining the secondary structure, conformational stability, and infectivity of rprp fibrils seeded with prp(sc) derived from either the chandler or the 22l prion strain. |
2014-11-25 |
2023-08-13 |
mouse |
| Qi Shi, Qin-Qin Song, Peng Sun, Jin Zhang, Juan Song, Li-Na Chen, Kang Xiao, Shao-Bin Wang, Ya-Zhou Zhang, Gong-Qi Li, Lin-Jun Sheng, Bao-Dong Wang, Ming-Zhi Lu, Jun Han, Xiao-Ping Don. Infection of prions and treatment of PrP106-126 alter the endogenous status of protein 14-3-3 and trigger the mitochondrial apoptosis possibly via activating Bax pathway. Molecular neurobiology. vol 49. issue 2. 2014-11-21. PMID:24135906. |
these data illustrate that significant down-regulation of brain 14-3-3 levels during prion infection may not only be a scenario of the terminal consequence of interacting with abnormal prp(sc) but may also participate in the pathogenesis of neuronal damage. |
2014-11-21 |
2023-08-12 |
Not clear |
| Thibaut Imberdis, Adeline Ayrolles-Torro, Jean-Michel Verdier, Véronique Perrie. Thienyl pyrimidine derivatives with PrP(Sc) oligomer-inducing activity are a promising tool to study prions. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059332. |
thienyl pyrimidine derivatives with prp(sc) oligomer-inducing activity are a promising tool to study prions. |
2014-11-15 |
2023-08-12 |
cattle |
| Thibaut Imberdis, Adeline Ayrolles-Torro, Jean-Michel Verdier, Véronique Perrie. Thienyl pyrimidine derivatives with PrP(Sc) oligomer-inducing activity are a promising tool to study prions. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059332. |
a critical event in prion diseases is the accumulation in the central nervous system (cns) of the abnormally folded prp(sc) protein that is the protease-resistant isoform of a normal cellular protein encoded by the host and called prp(c). |
2014-11-15 |
2023-08-12 |
cattle |
| Thibaut Imberdis, Adeline Ayrolles-Torro, Jean-Michel Verdier, Véronique Perrie. Thienyl pyrimidine derivatives with PrP(Sc) oligomer-inducing activity are a promising tool to study prions. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059332. |
prp(sc) (also known as rprp(sc) or prp27-30) represents the main marker of prion diseases and is routinely used in the reference method for the diagnosis of prion diseases. |
2014-11-15 |
2023-08-12 |
cattle |
| Thibaut Imberdis, Adeline Ayrolles-Torro, Jean-Michel Verdier, Véronique Perrie. Thienyl pyrimidine derivatives with PrP(Sc) oligomer-inducing activity are a promising tool to study prions. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059332. |
most of the therapeutic strategies developed so far aimed at identifying compounds that diminish the levels of prp(sc), with variable success when tested in vivo. |
2014-11-15 |
2023-08-12 |
cattle |
| Thibaut Imberdis, Adeline Ayrolles-Torro, Jean-Michel Verdier, Véronique Perrie. Thienyl pyrimidine derivatives with PrP(Sc) oligomer-inducing activity are a promising tool to study prions. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059332. |
in this review, we present an alternative approach in which small molecules that induce prp(sc) oligomers are identified. |
2014-11-15 |
2023-08-12 |
cattle |
| Thibaut Imberdis, Adeline Ayrolles-Torro, Jean-Michel Verdier, Véronique Perrie. Thienyl pyrimidine derivatives with PrP(Sc) oligomer-inducing activity are a promising tool to study prions. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059332. |
by using virtual and cellular screenings, we found several thienyl pyrimidine compounds that trigger prp(sc) oligomerization and trap prion infectivity. |
2014-11-15 |
2023-08-12 |
cattle |
| Gianluigi Forloni, Vladimiro Artuso, Ignazio Roiter, Michela Morbin, Fabrizio Tagliavin. Therapy in prion diseases. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059336. |
the main target of the antiprion strategy has been the pathological form of the cellular prion protein (prp(c)) termed prp(sc), invariably associated with the diseases. |
2014-11-15 |
2023-08-12 |
Not clear |
| Gianluigi Forloni, Vladimiro Artuso, Ignazio Roiter, Michela Morbin, Fabrizio Tagliavin. Therapy in prion diseases. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059336. |
several compounds have been found to affect prp(sc) formation or enhance its clearance in in vitro models, and prolong survival in experimental animals. |
2014-11-15 |
2023-08-12 |
Not clear |
| Gianluigi Forloni, Vladimiro Artuso, Ignazio Roiter, Michela Morbin, Fabrizio Tagliavin. Therapy in prion diseases. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059336. |
furthermore, the possibility to interfere with prp(c) to prp(sc) conversion by an active control of prp(c) is another interesting approach emerging from experimental studies. |
2014-11-15 |
2023-08-12 |
Not clear |
| Ivana Biljan, Gregor Ilc, Gabriele Giachin, Giuseppe Legname, Janez Plave. NMR structural studies of human cellular prion proteins. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059340. |
prion diseases or transmissible spongiform encephalopathies (tses) are fatal neurodegenerative disorders associated with the conformational conversion of the cellular prion protein, prp(c), into a pathological form known as prion or prp(sc). |
2014-11-15 |
2023-08-12 |
human |
| Ivana Biljan, Gregor Ilc, Gabriele Giachin, Giuseppe Legname, Janez Plave. NMR structural studies of human cellular prion proteins. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059340. |
spontaneous generation of prp(sc) in inherited forms of prion diseases is caused by mutations in the human prion protein gene (prnp). |
2014-11-15 |
2023-08-12 |
human |
| Ivana Biljan, Gregor Ilc, Gabriele Giachin, Giuseppe Legname, Janez Plave. NMR structural studies of human cellular prion proteins. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059340. |
we describe subtle local differences between the three-dimensional (3d) structures of huprp mutants and the wild-type (wt) protein, providing new insights into the possible key structural determinants underlying conversion of prp(c) into prp(sc). |
2014-11-15 |
2023-08-12 |
human |
| Lakshmi Miller-Vedam, Sina Ghaemmagham. Strain specificity and drug resistance in anti-prion therapy. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059341. |
prion diseases are a group of fatal neurodegenerative diseases caused by the misfolding of cellular prion protein (prp(c)) into pathogenic conformers (prp(sc)). |
2014-11-15 |
2023-08-12 |
Not clear |
| Lakshmi Miller-Vedam, Sina Ghaemmagham. Strain specificity and drug resistance in anti-prion therapy. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059341. |
although no effective therapies for prion diseases are currently available, a number of small molecule inhibitors have been identified that are capable of reducing or eliminating prp(sc) in prion infected cells. |
2014-11-15 |
2023-08-12 |
Not clear |
| Lakshmi Miller-Vedam, Sina Ghaemmagham. Strain specificity and drug resistance in anti-prion therapy. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059341. |
these studies suggest that the mechanism of prion strain adaptation involves rare conformational conversions followed by competitive selection among the heterogeneous pool of prp(sc) conformers. |
2014-11-15 |
2023-08-12 |
Not clear |
| Lakshmi Miller-Vedam, Sina Ghaemmagham. Strain specificity and drug resistance in anti-prion therapy. Current topics in medicinal chemistry. vol 13. issue 19. 2014-11-15. PMID:24059341. |
the plasticity of prion conformers makes prp(sc) a particularly challenging drug target and suggests that combination drug therapies or targeting of prp(c) may be required for effective therapy. |
2014-11-15 |
2023-08-12 |
Not clear |