| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Alexander Rouvinski, Sharon Karniely, Maria Kounin, Sanaa Moussa, Miri D Goldberg, Gabriela Warburg, Roman Lyakhovetsky, Dulce Papy-Garcia, Janine Kutzsche, Carsten Korth, George A Carlson, Susan F Godsave, Peter J Peters, Katarina Luhr, Krister Kristensson, Albert Taraboulo. Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs. The Journal of cell biology. vol 204. issue 3. 2014-04-08. PMID:24493590. |
prion strings and webs are the first demonstration of membrane-anchored prp(sc) amyloids. |
2014-04-08 |
2023-08-12 |
Not clear |
| Andrew G Timmes, Roger A Moore, Elizabeth R Fischer, Suzette A Priol. Recombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivity. PloS one. vol 8. issue 7. 2014-04-01. PMID:23936256. |
during prion infection, the normal, protease-sensitive conformation of prion protein (prp(c)) is converted via seeded polymerization to an abnormal, infectious conformation with greatly increased protease-resistance (prp(sc)). |
2014-04-01 |
2023-08-12 |
mouse |
| Andrew G Timmes, Roger A Moore, Elizabeth R Fischer, Suzette A Priol. Recombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivity. PloS one. vol 8. issue 7. 2014-04-01. PMID:23936256. |
in vitro, protein misfolding cyclic amplification (pmca) uses prp(sc) in prion-infected brain homogenates as an initiating seed to convert prp(c) and trigger the self-propagation of prp(sc) over many cycles of amplification. |
2014-04-01 |
2023-08-12 |
mouse |
| Andrew G Timmes, Roger A Moore, Elizabeth R Fischer, Suzette A Priol. Recombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivity. PloS one. vol 8. issue 7. 2014-04-01. PMID:23936256. |
while pmca reactions produce high levels of protease-resistant prp, the infectious titer is often lower than that of brain-derived prp(sc). |
2014-04-01 |
2023-08-12 |
mouse |
| Andrew G Timmes, Roger A Moore, Elizabeth R Fischer, Suzette A Priol. Recombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivity. PloS one. vol 8. issue 7. 2014-04-01. PMID:23936256. |
more recently, pmca techniques using bacterially derived recombinant prp (rprp) in the presence of lipid and rna but in the absence of any starting prp(sc) seed have been used to generate infectious prions that cause disease in wild-type mice with relatively short incubation times. |
2014-04-01 |
2023-08-12 |
mouse |
| Andrew G Timmes, Roger A Moore, Elizabeth R Fischer, Suzette A Priol. Recombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivity. PloS one. vol 8. issue 7. 2014-04-01. PMID:23936256. |
using rprp purified by two different techniques, we generated a self-propagating protease-resistant rprp molecule that, regardless of the amount of rna and lipid used, had a molecular mass, protease resistance and insolubility similar to that of prp(sc). |
2014-04-01 |
2023-08-12 |
mouse |
| Jae-Kyo Jeong, Myung-Hee Moon, Yang-Gyu Park, Ju-Hee Lee, You-Jin Lee, Jae-Won Seol, Sang-Youel Par. Gingerol-induced hypoxia-inducible factor 1 alpha inhibits human prion peptide-mediated neurotoxicity. Phytotherapy research : PTR. vol 27. issue 8. 2014-03-28. PMID:23008012. |
prion diseases are a family member of neurodegenerative disorders caused by the accumulation of misfolded-prion proteins (scrapie form of prp, prp(sc)). |
2014-03-28 |
2023-08-12 |
human |
| Jae-Kyo Jeong, Myung-Hee Moon, Yang-Gyu Park, Ju-Hee Lee, You-Jin Lee, Jae-Won Seol, Sang-Youel Par. Gingerol-induced hypoxia-inducible factor 1 alpha inhibits human prion peptide-mediated neurotoxicity. Phytotherapy research : PTR. vol 27. issue 8. 2014-03-28. PMID:23008012. |
the accumulation of prp(sc) in the brain leads to neurotoxicity by the induction of mitochondrial-apoptotic pathways. |
2014-03-28 |
2023-08-12 |
human |
| Ji-Hae Lee, Se-Eun Bae, Sunghoon Jung, Insung Ahn, Hyeon Seok So. Discriminant analysis of prion sequences for prediction of susceptibility. Experimental & molecular medicine. vol 45. 2014-03-20. PMID:24113272. |
prion diseases, including ovine scrapie, bovine spongiform encephalopathy (bse), human kuru and creutzfeldt-jakob disease (cjd), originate from a conformational change of the normal cellular prion protein (prp(c)) into abnormal protease-resistant prion protein (prp(sc)). |
2014-03-20 |
2023-08-12 |
human |
| A Miranda, P Ramos-Ibeas, E Pericuesta, M A Ramirez, A Gutierrez-Ada. The role of prion protein in stem cell regulation. Reproduction (Cambridge, England). vol 146. issue 3. 2014-03-18. PMID:23740082. |
cellular prion protein (prp(c)) has been well described as an essential partner of prion diseases due to the existence of a pathological conformation (prp(sc)). |
2014-03-18 |
2023-08-12 |
Not clear |
| Ting Liu, Wenjing Yi, Boya Feng, Zheng Zhou, Gengfu Xia. IGF-1-induced enhancement of PRNP expression depends on the negative regulation of transcription factor FOXO3a. PloS one. vol 8. issue 8. 2014-03-18. PMID:23967259. |
the conformational conversion of the cellular prion protein (prp(c)) into its β-sheet-rich scrapie isoform (prp(sc)) causes fatal prion diseases, which are also called transmissible spongiform encephalopathies (tses). |
2014-03-18 |
2023-08-12 |
human |
| Fangzhong Yuan, Lifeng Yang, Zhuming Zhang, Wenyu Wu, Xiangmei Zhou, Xiaomin Yin, Deming Zha. Cellular prion protein (PrPC) of the neuron cell transformed to a PK-resistant protein under oxidative stress, comprising main mitochondrial damage in prion diseases. Journal of molecular neuroscience : MN. vol 51. issue 1. 2014-03-12. PMID:23715697. |
the purpose of this study was to investigate three things: the possible mechanisms of neuron cell damage, the conformation of anti-protease k (pk) prp(sc), and the role of oxidative stress in the progression of prion diseases. |
2014-03-12 |
2023-08-12 |
Not clear |
| Maria G Cancedda, Giovanni Di Guardo, Roberto Chiocchetti, Francesca Demontis, Giuseppe Marruchella, Caterina Sorteni, Caterina Maestrale, Alfio Lai, Ciriaco Ligio. Role of palatine tonsils as a prion entry site in classical and atypical experimental sheep scrapie. Journal of virology. vol 88. issue 2. 2014-03-10. PMID:24198416. |
we first detected classical prp(sc) within the inoculated tonsil and in the ipsilateral retropharyngeal lymph node at 3 months postinoculation (p.i.). |
2014-03-10 |
2023-08-12 |
Not clear |
| Maria G Cancedda, Giovanni Di Guardo, Roberto Chiocchetti, Francesca Demontis, Giuseppe Marruchella, Caterina Sorteni, Caterina Maestrale, Alfio Lai, Ciriaco Ligio. Role of palatine tonsils as a prion entry site in classical and atypical experimental sheep scrapie. Journal of virology. vol 88. issue 2. 2014-03-10. PMID:24198416. |
at 7 months p.i., prp(sc) colonized other lymphoid tissues bilaterally, including ileal peyer's patches. |
2014-03-10 |
2023-08-12 |
Not clear |
| Maria G Cancedda, Giovanni Di Guardo, Roberto Chiocchetti, Francesca Demontis, Giuseppe Marruchella, Caterina Sorteni, Caterina Maestrale, Alfio Lai, Ciriaco Ligio. Role of palatine tonsils as a prion entry site in classical and atypical experimental sheep scrapie. Journal of virology. vol 88. issue 2. 2014-03-10. PMID:24198416. |
the earliest prp(sc) deposition within the brain was ipsilaterally observed at 9 months p.i. |
2014-03-10 |
2023-08-12 |
Not clear |
| Maria G Cancedda, Giovanni Di Guardo, Roberto Chiocchetti, Francesca Demontis, Giuseppe Marruchella, Caterina Sorteni, Caterina Maestrale, Alfio Lai, Ciriaco Ligio. Role of palatine tonsils as a prion entry site in classical and atypical experimental sheep scrapie. Journal of virology. vol 88. issue 2. 2014-03-10. PMID:24198416. |
at 12 months p.i., prp(sc) deposition was present bilaterally in the nucleus parasympathicus nervi vagi, as well as in the intermediolateral cell column of the thoracolumbar spinal cord. |
2014-03-10 |
2023-08-12 |
Not clear |
| Maria G Cancedda, Giovanni Di Guardo, Roberto Chiocchetti, Francesca Demontis, Giuseppe Marruchella, Caterina Sorteni, Caterina Maestrale, Alfio Lai, Ciriaco Ligio. Role of palatine tonsils as a prion entry site in classical and atypical experimental sheep scrapie. Journal of virology. vol 88. issue 2. 2014-03-10. PMID:24198416. |
no prp(sc) was detected in the lambs inoculated with atypical scrapie. |
2014-03-10 |
2023-08-12 |
Not clear |
| Brendan Molloy, Hilary E M McMaho. A cell-biased effect of estrogen in prion infection. Journal of virology. vol 88. issue 2. 2014-03-10. PMID:24227845. |
prion disorders are associated with the accumulation of a misfolded form (prp(sc)) of the normal prion protein, prp(c). |
2014-03-10 |
2023-08-12 |
Not clear |
| Brendan Molloy, Hilary E M McMaho. A cell-biased effect of estrogen in prion infection. Journal of virology. vol 88. issue 2. 2014-03-10. PMID:24227845. |
by using specific receptor agonists, erα was found to be the main receptor active in slowing prion infection, whereas in chronically infected cells, although erα allowed partial maintenance of prp(sc) levels, erβ was the main receptor involved in maintaining prp(sc) in a treatment paradigm. |
2014-03-10 |
2023-08-12 |
Not clear |
| Brendan Molloy, Hilary E M McMaho. A cell-biased effect of estrogen in prion infection. Journal of virology. vol 88. issue 2. 2014-03-10. PMID:24227845. |
this work also identified that by targeting the estrogen receptors with the selective estrogen receptor modulators tamoxifen (tam) and 4-hydroxy-tamoxifen (oht), prp(sc) could be cleared from prion-infected cell culture. |
2014-03-10 |
2023-08-12 |
Not clear |