| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Jing Wang, Jin Zhang, Qi Shi, Bao-Yun Zhang, Cao Chen, Li-Na Chen, Jing Sun, Hui Wang, Kang Xiao, Xiao-Ping Don. Scrapie infection in experimental rodents and SMB-S15 cells decreased the brain endogenous levels and activities of Sirt1. Journal of molecular neuroscience : MN. vol 55. issue 4. 2015-11-27. PMID:25391763. |
prion diseases are composed of a group of fatal neurodegenerative disorders resulting from misfolding of cellular prion (prp(c)) into scrapie prion (prp(sc)). |
2015-11-27 |
2023-08-13 |
mouse |
| Jing Wang, Jin Zhang, Qi Shi, Bao-Yun Zhang, Cao Chen, Li-Na Chen, Jing Sun, Hui Wang, Kang Xiao, Xiao-Ping Don. Scrapie infection in experimental rodents and SMB-S15 cells decreased the brain endogenous levels and activities of Sirt1. Journal of molecular neuroscience : MN. vol 55. issue 4. 2015-11-27. PMID:25391763. |
moreover, accompanying with increase of sirt1 level and decrease of acetyl-p53 level, treatments with sirt1 activators srt1720 and resveratrol in smb-s15 cells significantly reduced prp(sc); at the same time, the cellular distribution of prp proteins became normal, and the cell proliferating state was slightly improved. |
2015-11-27 |
2023-08-13 |
mouse |
| Jing Wang, Jin Zhang, Qi Shi, Bao-Yun Zhang, Cao Chen, Li-Na Chen, Jing Sun, Hui Wang, Kang Xiao, Xiao-Ping Don. Scrapie infection in experimental rodents and SMB-S15 cells decreased the brain endogenous levels and activities of Sirt1. Journal of molecular neuroscience : MN. vol 55. issue 4. 2015-11-27. PMID:25391763. |
sensitivity of the prp(sc) to sirt1 activators highlights a potential role of sirt1 in prion therapeutics. |
2015-11-27 |
2023-08-13 |
mouse |
| Roger A Moore, Robert Faris, Suzette A Priol. Proteomics applications in prion biology and structure. Expert review of proteomics. vol 12. issue 2. 2015-11-26. PMID:25795148. |
prion diseases are a heterogeneous class of fatal neurodegenerative disorders associated with misfolding of host cellular prion protein (prp(c)) into a pathological isoform, termed prp(sc). |
2015-11-26 |
2023-08-13 |
Not clear |
| Roger A Moore, Robert Faris, Suzette A Priol. Proteomics applications in prion biology and structure. Expert review of proteomics. vol 12. issue 2. 2015-11-26. PMID:25795148. |
various proteomics techniques have been instrumental in early prp(sc) detection, biomarker discovery, elucidation of prp(sc) structure and mapping of biochemical pathways affected by pathogenesis. |
2015-11-26 |
2023-08-13 |
Not clear |
| Kevin C Gough, Helen C Rees, Sarah E Ives, Ben C Maddiso. Methods for Differentiating Prion Types in Food-Producing Animals. Biology. vol 4. issue 4. 2015-11-20. PMID:26580664. |
prions are an enigma amongst infectious disease agents as they lack a genome yet confer specific pathologies thought to be dictated mainly, if not solely, by the conformation of the disease form of the prion protein (prp(sc)). |
2015-11-20 |
2023-08-13 |
cattle |
| Yraima Cordeiro, Natalia C Ferreir. New approaches for the selection and evaluation of anti-prion organic compounds. Mini reviews in medicinal chemistry. vol 15. issue 2. 2015-11-17. PMID:25723455. |
tses arise as a consequence of the conversion of soluble cellular prion protein (prp(c)) into the scrapie isoform (prp(sc)), which aggregates and accumulates in the central nervous system. |
2015-11-17 |
2023-08-13 |
Not clear |
| Yraima Cordeiro, Natalia C Ferreir. New approaches for the selection and evaluation of anti-prion organic compounds. Mini reviews in medicinal chemistry. vol 15. issue 2. 2015-11-17. PMID:25723455. |
proposed drugs against tses range from small organic compounds to antibodies; various therapeutic strategies have been proposed, including blocking the conversion of prp(c) to prp(sc), increasing prp(sc) clearance, and/or stabilizing prp(c). |
2015-11-17 |
2023-08-13 |
Not clear |
| Kevin C Gough, Claire A Baker, Hugh A Simmons, Steve A Hawkins, Ben C Maddiso. Circulation of prions within dust on a scrapie affected farm. Veterinary research. vol 46. 2015-11-17. PMID:25889731. |
using protein misfolding cyclic amplification we demonstrate that scrapie prp(sc) can be detected within circulating dusts that are present on a farm that is naturally contaminated with sheep scrapie. |
2015-11-17 |
2023-08-13 |
Not clear |
| Kurt Giles, David B Berry, Carlo Condello, Ronald C Hawley, Alejandra Gallardo-Godoy, Clifford Bryant, Abby Oehler, Manuel Elepano, Sumita Bhardwaj, Smita Patel, B Michael Silber, Shenheng Guan, Stephen J DeArmond, Adam R Renslo, Stanley B Prusine. Different 2-Aminothiazole Therapeutics Produce Distinct Patterns of Scrapie Prion Neuropathology in Mouse Brains. The Journal of pharmacology and experimental therapeutics. vol 355. issue 1. 2015-11-17. PMID:26224882. |
neuropathological examination of the brains from untreated controls showed a widespread deposition of self-propagating, β-sheet-rich "scrapie" isoform (prp(sc)) prions accompanied by a profound astrocytic gliosis. |
2015-11-17 |
2023-08-13 |
mouse |
| Kurt Giles, David B Berry, Carlo Condello, Ronald C Hawley, Alejandra Gallardo-Godoy, Clifford Bryant, Abby Oehler, Manuel Elepano, Sumita Bhardwaj, Smita Patel, B Michael Silber, Shenheng Guan, Stephen J DeArmond, Adam R Renslo, Stanley B Prusine. Different 2-Aminothiazole Therapeutics Produce Distinct Patterns of Scrapie Prion Neuropathology in Mouse Brains. The Journal of pharmacology and experimental therapeutics. vol 355. issue 1. 2015-11-17. PMID:26224882. |
in contrast, mice treated with 2-amts had lower levels of prp(sc) and associated astrocytic gliosis, with each compound resulting in a distinct pattern of deposition. |
2015-11-17 |
2023-08-13 |
mouse |
| Kurt Giles, David B Berry, Carlo Condello, Ronald C Hawley, Alejandra Gallardo-Godoy, Clifford Bryant, Abby Oehler, Manuel Elepano, Sumita Bhardwaj, Smita Patel, B Michael Silber, Shenheng Guan, Stephen J DeArmond, Adam R Renslo, Stanley B Prusine. Different 2-Aminothiazole Therapeutics Produce Distinct Patterns of Scrapie Prion Neuropathology in Mouse Brains. The Journal of pharmacology and experimental therapeutics. vol 355. issue 1. 2015-11-17. PMID:26224882. |
notably, ind125 prevented both prp(sc) accumulation and astrocytic gliosis in the cerebrum. |
2015-11-17 |
2023-08-13 |
mouse |
| Kurt Giles, David B Berry, Carlo Condello, Ronald C Hawley, Alejandra Gallardo-Godoy, Clifford Bryant, Abby Oehler, Manuel Elepano, Sumita Bhardwaj, Smita Patel, B Michael Silber, Shenheng Guan, Stephen J DeArmond, Adam R Renslo, Stanley B Prusine. Different 2-Aminothiazole Therapeutics Produce Distinct Patterns of Scrapie Prion Neuropathology in Mouse Brains. The Journal of pharmacology and experimental therapeutics. vol 355. issue 1. 2015-11-17. PMID:26224882. |
progressive central nervous system dysfunction in the ind125-treated mice was presumably due to the prp(sc) that accumulated in their brainstems. |
2015-11-17 |
2023-08-13 |
mouse |
| Malin K Sandberg, Huda Al-Doujaily, Bernadette Sharps, Michael Wiggins De Oliveira, Christian Schmidt, Angela Richard-Londt, Sarah Lyall, Jacqueline M Linehan, Sebastian Brandner, Jonathan D F Wadsworth, Anthony R Clarke, John Colling. Prion neuropathology follows the accumulation of alternate prion protein isoforms after infective titre has peaked. Nature communications. vol 5. 2015-11-16. PMID:25005024. |
prions are lethal infectious agents thought to consist of multi-chain forms (prp(sc)) of misfolded cellular prion protein (prp(c)). |
2015-11-16 |
2023-08-13 |
Not clear |
| Malin K Sandberg, Huda Al-Doujaily, Bernadette Sharps, Michael Wiggins De Oliveira, Christian Schmidt, Angela Richard-Londt, Sarah Lyall, Jacqueline M Linehan, Sebastian Brandner, Jonathan D F Wadsworth, Anthony R Clarke, John Colling. Prion neuropathology follows the accumulation of alternate prion protein isoforms after infective titre has peaked. Nature communications. vol 5. 2015-11-16. PMID:25005024. |
here we show a linear increase of proteinase k-sensitive prp isoforms distinct from classical prp(sc) at a rate proportional to prp(c) concentration, commencing at the phase transition and rising until clinical onset. |
2015-11-16 |
2023-08-13 |
Not clear |
| Hanin Abdel-Ha. Detection of water-soluble disease-associated PrP species in blood and brain of scrapie-infected hamster. Archives of virology. vol 160. issue 9. 2015-11-10. PMID:26105967. |
prp(sc) is essential in prion disease pathogenesis, but little to nothing is known about the prp(sc) species that may be associated with this form of prion infectivity. |
2015-11-10 |
2023-08-13 |
Not clear |
| Hanin Abdel-Ha. Detection of water-soluble disease-associated PrP species in blood and brain of scrapie-infected hamster. Archives of virology. vol 160. issue 9. 2015-11-10. PMID:26105967. |
scrapie-infected hamster plasma and s(hs) were subjected to biochemical analysis, and the results demonstrate for the first time that soluble infectivity is associated with a water-soluble prp(sc) species with substantially different properties from classical prp(sc), the concentration of which seems to correlate with the magnitude and efficiency of the soluble infectivity. |
2015-11-10 |
2023-08-13 |
Not clear |
| O Kovalchuk Ben-Zaken, I Nissan, S Tzaban, A Taraboulos, E Zcharia, S Matzger, I Shafat, I Vlodavsky, Y Ta. Transgenic over-expression of mammalian heparanase delays prion disease onset and progression. Biochemical and biophysical research communications. vol 464. issue 3. 2015-11-09. PMID:26168721. |
cellular heparan sulfate (hs) has a dual role in scrapie pathogenesis; it is required for prp(sc) (scrapie prion protein) formation and facilitates infection of cells, mediating cellular uptake of prions. |
2015-11-09 |
2023-08-13 |
mouse |
| O Kovalchuk Ben-Zaken, I Nissan, S Tzaban, A Taraboulos, E Zcharia, S Matzger, I Shafat, I Vlodavsky, Y Ta. Transgenic over-expression of mammalian heparanase delays prion disease onset and progression. Biochemical and biophysical research communications. vol 464. issue 3. 2015-11-09. PMID:26168721. |
in cultured cells, heparanase treatment or over-expression resulted in a profound decrease in prp(sc). |
2015-11-09 |
2023-08-13 |
mouse |
| Giuseppe Di Natale, Ildikó Turi, Giuseppe Pappalardo, Imre Sóvágó, Enrico Rizzarell. Cross-talk between the octarepeat domain and the fifth binding site of prion protein driven by the interaction of copper(II) with the N-terminus. Chemistry (Weinheim an der Bergstrasse, Germany). vol 21. issue 10. 2015-11-05. PMID:25649151. |
prion diseases are a group of neurodegenerative diseases based on the conformational conversion of the normal form of the prion protein (prp(c)) to the disease-related scrapie isoform (prp(sc)). |
2015-11-05 |
2023-08-13 |
Not clear |