| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Daniela Saverioni, Silvio Notari, Sabina Capellari, Ilaria Poggiolini, Armin Giese, Hans A Kretzschmar, Piero Parch. Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prions. The Journal of biological chemistry. vol 288. issue 39. 2013-12-24. PMID:23897825. |
finally, we highlight the limitations of current operational definitions of sprp(sc) and of the quantitative analytical measurements that are not based on the isolation of a fully pk-sensitive prp(sc) form. |
2013-12-24 |
2023-08-12 |
human |
| Stefano Thellung, Elena Gatta, Francesca Pellistri, Alessandro Corsaro, Valentina Villa, Massimo Vassalli, Mauro Robello, Tullio Flori. Excitotoxicity through NMDA receptors mediates cerebellar granule neuron apoptosis induced by prion protein 90-231 fragment. Neurotoxicity research. vol 23. issue 4. 2013-12-23. PMID:22855343. |
prion diseases recognize, as a unique molecular trait, the misfolding of cns-enriched prion protein (prp(c)) into an aberrant isoform (prp(sc)). |
2013-12-23 |
2023-08-12 |
rat |
| Stefano Thellung, Elena Gatta, Francesca Pellistri, Alessandro Corsaro, Valentina Villa, Massimo Vassalli, Mauro Robello, Tullio Flori. Excitotoxicity through NMDA receptors mediates cerebellar granule neuron apoptosis induced by prion protein 90-231 fragment. Neurotoxicity research. vol 23. issue 4. 2013-12-23. PMID:22855343. |
this recombinant fragment assumes a toxic conformation (prp90-231(tox)) after controlled thermal denaturation (1 h at 53 °c) acquiring structural characteristics identified in prp(sc) (enrichment in β-structures, increased hydrophobicity, partial resistance to proteinase k, and aggregation in amyloid fibrils). |
2013-12-23 |
2023-08-12 |
rat |
| Ludovica Marzo, Zrinka Marijanovic, Duncan Browman, Zeina Chamoun, Anna Caputo, Chiara Zurzol. 4-hydroxytamoxifen leads to PrPSc clearance by conveying both PrPC and PrPSc to lysosomes independently of autophagy. Journal of cell science. vol 126. issue Pt 6. 2013-12-17. PMID:23418355. |
prion diseases are fatal neurodegenerative disorders involving the abnormal folding of a native cellular protein, named prp(c), to a malconformed aggregation-prone state, enriched in beta sheet secondary structure, denoted prp(sc). |
2013-12-17 |
2023-08-12 |
mouse |
| Ludovica Marzo, Zrinka Marijanovic, Duncan Browman, Zeina Chamoun, Anna Caputo, Chiara Zurzol. 4-hydroxytamoxifen leads to PrPSc clearance by conveying both PrPC and PrPSc to lysosomes independently of autophagy. Journal of cell science. vol 126. issue Pt 6. 2013-12-17. PMID:23418355. |
stimulation of autophagy by chemical compounds has also been shown to reduce prp(sc) in infected neuronal cells and prolong survival times in mouse models. |
2013-12-17 |
2023-08-12 |
mouse |
| Ludovica Marzo, Zrinka Marijanovic, Duncan Browman, Zeina Chamoun, Anna Caputo, Chiara Zurzol. 4-hydroxytamoxifen leads to PrPSc clearance by conveying both PrPC and PrPSc to lysosomes independently of autophagy. Journal of cell science. vol 126. issue Pt 6. 2013-12-17. PMID:23418355. |
we report that in infected neuronal cells different compounds known to stimulate autophagy are ineffective in increasing autophagic flux and in reducing prp(sc). |
2013-12-17 |
2023-08-12 |
mouse |
| Peter C Griffiths, Jane M Plater, Alun Chave, Dhanushka Jayasena, Anna C Tout, Paul B Rice, Christopher M Vickery, John Spiropoulos, Michael J Stack, Otto Wind. Overexpression of chimaeric murine/ovine PrP (A136H154Q171) in transgenic mice facilitates transmission and differentiation of ruminant prions. The Journal of general virology. vol 94. issue Pt 11. 2013-12-13. PMID:23761404. |
), 100% disease penetrance and early western blot detection of protease-resistant fragments (prp(res)) of the disease-associated isoform, prp(sc), in em16 brain from 110 days p.i. |
2013-12-13 |
2023-08-12 |
mouse |
| Peter C Griffiths, Jane M Plater, Alun Chave, Dhanushka Jayasena, Anna C Tout, Paul B Rice, Christopher M Vickery, John Spiropoulos, Michael J Stack, Otto Wind. Overexpression of chimaeric murine/ovine PrP (A136H154Q171) in transgenic mice facilitates transmission and differentiation of ruminant prions. The Journal of general virology. vol 94. issue Pt 11. 2013-12-13. PMID:23761404. |
immunohistochemistry was used to confirm prp(sc) deposition in brain sections from terminal phase transmissible spongiform encephalopathy-challenged em16 mice. |
2013-12-13 |
2023-08-12 |
mouse |
| Susan F Godsave, Holger Wille, Jason Pierson, Stanley B Prusiner, Peter J Peter. Plasma membrane invaginations containing clusters of full-length PrPSc are an early form of prion-associated neuropathology in vivo. Neurobiology of aging. vol 34. issue 6. 2013-12-11. PMID:23481568. |
during prion disease, cellular prion protein (prp(c)) is refolded into a pathogenic isoform (prp(sc)) that accumulates in the central nervous system and causes neurodegeneration and death. |
2013-12-11 |
2023-08-12 |
mouse |
| Susan F Godsave, Holger Wille, Jason Pierson, Stanley B Prusiner, Peter J Peter. Plasma membrane invaginations containing clusters of full-length PrPSc are an early form of prion-associated neuropathology in vivo. Neurobiology of aging. vol 34. issue 6. 2013-12-11. PMID:23481568. |
we used immunofluorescence, quantitative cryo-immunogold em, and tomography to detect nascent, full-length prp(sc) in the hippocampus of prion-infected mice from early preclinical disease stages onward. |
2013-12-11 |
2023-08-12 |
mouse |
| Susan F Godsave, Holger Wille, Jason Pierson, Stanley B Prusiner, Peter J Peter. Plasma membrane invaginations containing clusters of full-length PrPSc are an early form of prion-associated neuropathology in vivo. Neurobiology of aging. vol 34. issue 6. 2013-12-11. PMID:23481568. |
comparison of uninfected and infected brains showed that sites containing full-length prp(sc) could be recognized in the neuropil by bright spots and streaks of immunofluorescence on semi-thin (200-nm) sections, and by clusters of cryo-immunogold em labeling. |
2013-12-11 |
2023-08-12 |
mouse |
| Susan F Godsave, Holger Wille, Jason Pierson, Stanley B Prusiner, Peter J Peter. Plasma membrane invaginations containing clusters of full-length PrPSc are an early form of prion-associated neuropathology in vivo. Neurobiology of aging. vol 34. issue 6. 2013-12-11. PMID:23481568. |
prp(sc) was found mainly on neuronal plasma membranes, most strikingly on membrane invaginations and sites of cell-to-cell contact, and was evident by 65 days postinoculation, or 54% of the incubation period to terminal disease. |
2013-12-11 |
2023-08-12 |
mouse |
| Tracy Haldiman, Chae Kim, Yvonne Cohen, Wei Chen, Janis Blevins, Liuting Qing, Mark L Cohen, Jan Langeveld, Glenn C Telling, Qingzhong Kong, Jiri G Safa. Co-existence of distinct prion types enables conformational evolution of human PrPSc by competitive selection. The Journal of biological chemistry. vol 288. issue 41. 2013-12-11. PMID:23974118. |
the unique phenotypic characteristics of mammalian prions are thought to be encoded in the conformation of pathogenic prion proteins (prp(sc)). |
2013-12-11 |
2023-08-12 |
human |
| Tracy Haldiman, Chae Kim, Yvonne Cohen, Wei Chen, Janis Blevins, Liuting Qing, Mark L Cohen, Jan Langeveld, Glenn C Telling, Qingzhong Kong, Jiri G Safa. Co-existence of distinct prion types enables conformational evolution of human PrPSc by competitive selection. The Journal of biological chemistry. vol 288. issue 41. 2013-12-11. PMID:23974118. |
using biophysical techniques and conformation-dependent immunoassays in tandem, we isolated two distinct populations of prp(sc) particles with different conformational stabilities and aggregate sizes, which frequently co-exist in the most common human prion disease, sporadic creutzfeldt-jakob disease. |
2013-12-11 |
2023-08-12 |
human |
| Tracy Haldiman, Chae Kim, Yvonne Cohen, Wei Chen, Janis Blevins, Liuting Qing, Mark L Cohen, Jan Langeveld, Glenn C Telling, Qingzhong Kong, Jiri G Safa. Co-existence of distinct prion types enables conformational evolution of human PrPSc by competitive selection. The Journal of biological chemistry. vol 288. issue 41. 2013-12-11. PMID:23974118. |
the protein misfolding cyclic amplification replicates each of the prp(sc) particle types independently and leads to the competitive selection of those with lower initial conformational stability. |
2013-12-11 |
2023-08-12 |
human |
| Tracy Haldiman, Chae Kim, Yvonne Cohen, Wei Chen, Janis Blevins, Liuting Qing, Mark L Cohen, Jan Langeveld, Glenn C Telling, Qingzhong Kong, Jiri G Safa. Co-existence of distinct prion types enables conformational evolution of human PrPSc by competitive selection. The Journal of biological chemistry. vol 288. issue 41. 2013-12-11. PMID:23974118. |
in serial propagation with a nonglycosylated mutant prp(c) substrate, the dominant prp(sc) conformers are subject to further evolution by natural selection of the subpopulation with the highest replication rate due to its lowest stability. |
2013-12-11 |
2023-08-12 |
human |
| Tracy Haldiman, Chae Kim, Yvonne Cohen, Wei Chen, Janis Blevins, Liuting Qing, Mark L Cohen, Jan Langeveld, Glenn C Telling, Qingzhong Kong, Jiri G Safa. Co-existence of distinct prion types enables conformational evolution of human PrPSc by competitive selection. The Journal of biological chemistry. vol 288. issue 41. 2013-12-11. PMID:23974118. |
cumulatively, the data show that sporadic creutzfeldt-jakob disease prp(sc) is not a single conformational entity but a dynamic collection of two distinct populations of particles. |
2013-12-11 |
2023-08-12 |
human |
| Tracy Haldiman, Chae Kim, Yvonne Cohen, Wei Chen, Janis Blevins, Liuting Qing, Mark L Cohen, Jan Langeveld, Glenn C Telling, Qingzhong Kong, Jiri G Safa. Co-existence of distinct prion types enables conformational evolution of human PrPSc by competitive selection. The Journal of biological chemistry. vol 288. issue 41. 2013-12-11. PMID:23974118. |
this implies the co-existence of different prions, whose adaptation and evolution are governed by the selection of progressively less stable, faster replicating prp(sc) conformers. |
2013-12-11 |
2023-08-12 |
human |
| Rohana P Dassanayake, Thomas C Truscott, M Özgür Özyiğit, Dongyue Zhuang, David A Schneider, Katherine I O'Rourk. Accumulation profiles of PrP(Sc) in hemal nodes of naturally and experimentally scrapie-infected sheep. BMC veterinary research. vol 9. 2013-12-10. PMID:23601183. |
accumulation profiles of prp(sc) in hemal nodes of naturally and experimentally scrapie-infected sheep. |
2013-12-10 |
2023-08-12 |
Not clear |
| Rohana P Dassanayake, Thomas C Truscott, M Özgür Özyiğit, Dongyue Zhuang, David A Schneider, Katherine I O'Rourk. Accumulation profiles of PrP(Sc) in hemal nodes of naturally and experimentally scrapie-infected sheep. BMC veterinary research. vol 9. 2013-12-10. PMID:23601183. |
in classical scrapie, the disease-associated abnormal isoform (prp(sc)) of normal prion protein accumulates principally in the nervous system and lymphoid tissues of small ruminants. |
2013-12-10 |
2023-08-12 |
Not clear |