| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Charles E Mays, Jacques van der Merwe, Chae Kim, Tracy Haldiman, Debbie McKenzie, Jiri G Safar, David Westawa. Prion Infectivity Plateaus and Conversion to Symptomatic Disease Originate from Falling Precursor Levels and Increased Levels of Oligomeric PrPSc Species. Journal of virology. vol 89. issue 24. 2016-02-25. PMID:26423957. |
in lethal prion neurodegenerative diseases, misfolded prion proteins (prp(sc)) replicate by redirecting the folding of the cellular prion glycoprotein (prp(c)). |
2016-02-25 |
2023-08-13 |
Not clear |
| Charles E Mays, Jacques van der Merwe, Chae Kim, Tracy Haldiman, Debbie McKenzie, Jiri G Safar, David Westawa. Prion Infectivity Plateaus and Conversion to Symptomatic Disease Originate from Falling Precursor Levels and Increased Levels of Oligomeric PrPSc Species. Journal of virology. vol 89. issue 24. 2016-02-25. PMID:26423957. |
although a hypothetical lethal isoform of prp cannot be excluded, our data argue that diminishing residual prp(c) levels and continuously increasing levels of oprp(sc) are crucial determinants in the transition from presymptomatic to symptomatic prion disease. |
2016-02-25 |
2023-08-13 |
Not clear |
| Dana J Levine, Jan Stöhr, Lillian E Falese, Julian Ollesch, Holger Wille, Stanley B Prusiner, Jeffrey R Lon. Mechanism of scrapie prion precipitation with phosphotungstate anions. ACS chemical biology. vol 10. issue 5. 2016-02-22. PMID:25695325. |
the phosphotungstate anion (pta) is widely used to facilitate the precipitation of disease-causing prion protein (prp(sc)) from infected tissue for applications in structural studies and diagnostic approaches. |
2016-02-22 |
2023-08-13 |
mouse |
| Dana J Levine, Jan Stöhr, Lillian E Falese, Julian Ollesch, Holger Wille, Stanley B Prusiner, Jeffrey R Lon. Mechanism of scrapie prion precipitation with phosphotungstate anions. ACS chemical biology. vol 10. issue 5. 2016-02-22. PMID:25695325. |
in order to elucidate the nature of the pta interaction with prp(sc) under physiological conditions, solutions of pta were characterized by nmr spectroscopy at varying ph. |
2016-02-22 |
2023-08-13 |
mouse |
| Dana J Levine, Jan Stöhr, Lillian E Falese, Julian Ollesch, Holger Wille, Stanley B Prusiner, Jeffrey R Lon. Mechanism of scrapie prion precipitation with phosphotungstate anions. ACS chemical biology. vol 10. issue 5. 2016-02-22. PMID:25695325. |
to measure the efficacy of each component of pta, increasing concentrations of pw11, wo4, and mixtures thereof were used to precipitate prp(sc) from brain homogenates of scrapie prion-infected mice. |
2016-02-22 |
2023-08-13 |
mouse |
| Dana J Levine, Jan Stöhr, Lillian E Falese, Julian Ollesch, Holger Wille, Stanley B Prusiner, Jeffrey R Lon. Mechanism of scrapie prion precipitation with phosphotungstate anions. ACS chemical biology. vol 10. issue 5. 2016-02-22. PMID:25695325. |
the amount of prp(sc) isolated, quantified by elisa and immunoblotting, revealed that both pw11 and wo4 contribute to prp(sc) precipitation. |
2016-02-22 |
2023-08-13 |
mouse |
| Dana J Levine, Jan Stöhr, Lillian E Falese, Julian Ollesch, Holger Wille, Stanley B Prusiner, Jeffrey R Lon. Mechanism of scrapie prion precipitation with phosphotungstate anions. ACS chemical biology. vol 10. issue 5. 2016-02-22. PMID:25695325. |
these experiments revealed that yield and purity of prp(sc) were greater with polyoxometalates (poms), which substantially supported the separation of lipids from prp(sc) in the samples. |
2016-02-22 |
2023-08-13 |
mouse |
| Dana J Levine, Jan Stöhr, Lillian E Falese, Julian Ollesch, Holger Wille, Stanley B Prusiner, Jeffrey R Lon. Mechanism of scrapie prion precipitation with phosphotungstate anions. ACS chemical biology. vol 10. issue 5. 2016-02-22. PMID:25695325. |
interaction of poms and sarkosyl with brain homogenates promoted the formation of fibrillar prp(sc) aggregates prior to centrifugation, likely through the separation of lipids like gm1 from prp(sc). |
2016-02-22 |
2023-08-13 |
mouse |
| Dana J Levine, Jan Stöhr, Lillian E Falese, Julian Ollesch, Holger Wille, Stanley B Prusiner, Jeffrey R Lon. Mechanism of scrapie prion precipitation with phosphotungstate anions. ACS chemical biology. vol 10. issue 5. 2016-02-22. PMID:25695325. |
we propose that this separation of lipids from prp is a major factor governing the facile precipitation of prp(sc) by pta from tissue and might be optimized further for the detection of prions. |
2016-02-22 |
2023-08-13 |
mouse |
| Rob Goold, Chris McKinnon, Sarah J Tabriz. Prion degradation pathways: Potential for therapeutic intervention. Molecular and cellular neurosciences. vol 66. issue Pt A. 2016-02-17. PMID:25584786. |
pathology is closely linked to the misfolding of native cellular prp(c) into the disease-associated form prp(sc) that accumulates in the brain as disease progresses. |
2016-02-17 |
2023-08-13 |
Not clear |
| Rob Goold, Chris McKinnon, Sarah J Tabriz. Prion degradation pathways: Potential for therapeutic intervention. Molecular and cellular neurosciences. vol 66. issue Pt A. 2016-02-17. PMID:25584786. |
although treatments have yet to be developed, strategies aimed at stimulating the degradation of prp(sc) have shown efficacy in experimental models of prion disease. |
2016-02-17 |
2023-08-13 |
Not clear |
| Rob Goold, Chris McKinnon, Sarah J Tabriz. Prion degradation pathways: Potential for therapeutic intervention. Molecular and cellular neurosciences. vol 66. issue Pt A. 2016-02-17. PMID:25584786. |
here, we describe the cellular pathways that mediate prp(sc) degradation and review possible targets for therapeutic intervention. |
2016-02-17 |
2023-08-13 |
Not clear |
| Seng Zhu, Guiliana Soraya Victoria, Ludovica Marzo, Rupam Ghosh, Chiara Zurzol. Prion aggregates transfer through tunneling nanotubes in endocytic vesicles. Prion. vol 9. issue 2. 2016-02-10. PMID:25996400. |
transmissible spongiform encephalopathies (tses) are a group of neurodegenerative diseases caused by the misfolding of the cellular prion protein to an infectious form prp(sc). |
2016-02-10 |
2023-08-13 |
Not clear |
| Seng Zhu, Guiliana Soraya Victoria, Ludovica Marzo, Rupam Ghosh, Chiara Zurzol. Prion aggregates transfer through tunneling nanotubes in endocytic vesicles. Prion. vol 9. issue 2. 2016-02-10. PMID:25996400. |
the intercellular transfer of prp(sc) is a question of immediate interest as the cell-to-cell movement of the infectious particle causes the inexorable propagation of disease. |
2016-02-10 |
2023-08-13 |
Not clear |
| Seng Zhu, Guiliana Soraya Victoria, Ludovica Marzo, Rupam Ghosh, Chiara Zurzol. Prion aggregates transfer through tunneling nanotubes in endocytic vesicles. Prion. vol 9. issue 2. 2016-02-10. PMID:25996400. |
we have previously identified tunneling nanotubes (tnts) as one mechanism by which prp(sc) can move between cells. |
2016-02-10 |
2023-08-13 |
Not clear |
| Seng Zhu, Guiliana Soraya Victoria, Ludovica Marzo, Rupam Ghosh, Chiara Zurzol. Prion aggregates transfer through tunneling nanotubes in endocytic vesicles. Prion. vol 9. issue 2. 2016-02-10. PMID:25996400. |
here we investigate further the details of this mechanism and show that prp(sc) travels within tnts in endolysosomal vesicles. |
2016-02-10 |
2023-08-13 |
Not clear |
| Xuesong Wang, Dengsen Zhu, Cong Zhao, Lei He, Weihong D. Inhibitory effects of NAMI-A-like ruthenium complexes on prion neuropeptide fibril formation. Metallomics : integrated biometal science. vol 7. issue 5. 2016-02-08. PMID:25856332. |
prion diseases are a group of infectious and fatal neurodegenerative disorders caused by the conformational conversion of a cellular prion protein (prp) into its abnormal isoform prp(sc). |
2016-02-08 |
2023-08-13 |
Not clear |
| Xuesong Wang, Dengsen Zhu, Cong Zhao, Lei He, Weihong D. Inhibitory effects of NAMI-A-like ruthenium complexes on prion neuropeptide fibril formation. Metallomics : integrated biometal science. vol 7. issue 5. 2016-02-08. PMID:25856332. |
prp106-126 resembles prp(sc) in terms of physicochemical and biological characteristics and is used as a common model for the treatment of prion diseases. |
2016-02-08 |
2023-08-13 |
Not clear |
| Roumita Moulick, Ranabir Das, Jayant B Udgaonka. Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR. The Journal of biological chemistry. vol 290. issue 42. 2016-02-08. PMID:26306043. |
the susceptibility of the cellular prion protein (prp(c)) to convert to an alternative misfolded conformation (prp(sc)), which is the key event in the pathogenesis of prion diseases, is indicative of a conformationally flexible native (n) state. |
2016-02-08 |
2023-08-13 |
mouse |
| Ben C Maddison, John Spiropoulos, Christopher M Vickery, Richard Lockey, Jonathan P Owen, Keith Bishop, Claire A Baker, Kevin C Goug. Incubation of ovine scrapie with environmental matrix results in biological and biochemical changes of PrP(Sc) over time. Veterinary research. vol 46. 2016-02-04. PMID:25928902. |
incubation of ovine scrapie with environmental matrix results in biological and biochemical changes of prp(sc) over time. |
2016-02-04 |
2023-08-13 |
mouse |