| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Justin J Greenlee, Eric M Nicholson, Jodi D Smith, Robert A Kunkle, Amir N Hami. Susceptibility of cattle to the agent of chronic wasting disease from elk after intracranial inoculation. Journal of veterinary diagnostic investigation : official publication of the American Association of Veterinary Laboratory Diagnosticians, Inc. vol 24. issue 6. 2013-04-18. PMID:22991389. |
accumulation of abnormal prion protein (prp(sc)) occurred in only the 2 clinically affected cattle and was confined to the central nervous system, with the most prominent immunoreactivity in midbrain, brainstem, and hippocampus with lesser immunoreactivity in the cervical spinal cord. |
2013-04-18 |
2023-08-12 |
cattle |
| Justin J Greenlee, Eric M Nicholson, Jodi D Smith, Robert A Kunkle, Amir N Hami. Susceptibility of cattle to the agent of chronic wasting disease from elk after intracranial inoculation. Journal of veterinary diagnostic investigation : official publication of the American Association of Veterinary Laboratory Diagnosticians, Inc. vol 24. issue 6. 2013-04-18. PMID:22991389. |
a critical finding is that if cwd did transmit to exposed cattle, currently used diagnostic techniques would detect and differentiate it from other prion diseases in cattle based on absence of spongiform change, distinct pattern of prp(sc) deposition, and unique molecular profile. |
2013-04-18 |
2023-08-12 |
cattle |
| Piero Parchi, Laura de Boni, Daniela Saverioni, Mark L Cohen, Isidro Ferrer, Pierluigi Gambetti, Ellen Gelpi, Giorgio Giaccone, Jean-Jacques Hauw, Romana Höftberger, James W Ironside, Casper Jansen, Gabor G Kovacs, Annemieke Rozemuller, Danielle Seilhean, Fabrizio Tagliavini, Armin Giese, Hans A Kretzschma. Consensus classification of human prion disease histotypes allows reliable identification of molecular subtypes: an inter-rater study among surveillance centres in Europe and USA. Acta neuropathologica. vol 124. issue 4. 2013-04-15. PMID:22744790. |
the current classification of human sporadic prion diseases recognizes six major phenotypic subtypes with distinctive clinicopathological features, which largely correlate at the molecular level with the genotype at the polymorphic codon 129 (methionine, m, or valine, v) in the prion protein gene and with the size of the protease-resistant core of the abnormal prion protein, prp(sc) (i.e. |
2013-04-15 |
2023-08-12 |
human |
| Piero Parchi, Laura de Boni, Daniela Saverioni, Mark L Cohen, Isidro Ferrer, Pierluigi Gambetti, Ellen Gelpi, Giorgio Giaccone, Jean-Jacques Hauw, Romana Höftberger, James W Ironside, Casper Jansen, Gabor G Kovacs, Annemieke Rozemuller, Danielle Seilhean, Fabrizio Tagliavini, Armin Giese, Hans A Kretzschma. Consensus classification of human prion disease histotypes allows reliable identification of molecular subtypes: an inter-rater study among surveillance centres in Europe and USA. Acta neuropathologica. vol 124. issue 4. 2013-04-15. PMID:22744790. |
we previously demonstrated that prp(sc) typing by western blotting is a reliable means of strain typing and disease classification. |
2013-04-15 |
2023-08-12 |
human |
| Piero Parchi, Laura de Boni, Daniela Saverioni, Mark L Cohen, Isidro Ferrer, Pierluigi Gambetti, Ellen Gelpi, Giorgio Giaccone, Jean-Jacques Hauw, Romana Höftberger, James W Ironside, Casper Jansen, Gabor G Kovacs, Annemieke Rozemuller, Danielle Seilhean, Fabrizio Tagliavini, Armin Giese, Hans A Kretzschma. Consensus classification of human prion disease histotypes allows reliable identification of molecular subtypes: an inter-rater study among surveillance centres in Europe and USA. Acta neuropathologica. vol 124. issue 4. 2013-04-15. PMID:22744790. |
limitations of this approach, however, particularly in the interlaboratory setting, are the association of prp(sc) types 1 or 2 with more than one clinicopathological phenotype, which precludes definitive case classification if not supported by further analysis, and the difficulty of fully recognizing cases with mixed phenotypic features. |
2013-04-15 |
2023-08-12 |
human |
| Piero Parchi, Laura de Boni, Daniela Saverioni, Mark L Cohen, Isidro Ferrer, Pierluigi Gambetti, Ellen Gelpi, Giorgio Giaccone, Jean-Jacques Hauw, Romana Höftberger, James W Ironside, Casper Jansen, Gabor G Kovacs, Annemieke Rozemuller, Danielle Seilhean, Fabrizio Tagliavini, Armin Giese, Hans A Kretzschma. Consensus classification of human prion disease histotypes allows reliable identification of molecular subtypes: an inter-rater study among surveillance centres in Europe and USA. Acta neuropathologica. vol 124. issue 4. 2013-04-15. PMID:22744790. |
the present data fully support the basis for the current classification of sporadic human prion diseases and indicate that, besides molecular prp(sc) typing, histopathological analysis permits reliable disease classification with high interlaboratory accuracy. |
2013-04-15 |
2023-08-12 |
human |
| Nam Ky Chu, Christian F W Becke. Recombinant expression of soluble murine prion protein for C-terminal modification. FEBS letters. vol 587. issue 5. 2013-04-12. PMID:23337878. |
membrane attachment of prion protein (prp) via its glycosylphosphatidylinositol (gpi) anchor plays a key role during conversion of cellular prp(c) into its pathogenic isoform prp(sc). |
2013-04-12 |
2023-08-12 |
Not clear |
| Hyo-Jin Kim, Dong-Seob Tark, Yoon-Hee Lee, Min-Jeong Kim, Won-Yong Lee, In-Soo Cho, Hyun-Joo Sohn, Takashi Yokoyam. Establishment of a cell line persistently infected with chronic wasting disease prions. The Journal of veterinary medical science. vol 74. issue 10. 2013-04-11. PMID:22673102. |
the elkrk13 cells have been shown to be permissive to accumulation of abnormal isoforms of prion protein (prp(sc)) resulting from cwd prions up to 97 serial passages thus far. |
2013-04-11 |
2023-08-12 |
rabbit |
| Maddalena D Caiati, Victoria F Safiulina, Giorgia Fattorini, Sudhir Sivakumaran, Giuseppe Legname, Enrico Cherubin. PrPC controls via protein kinase A the direction of synaptic plasticity in the immature hippocampus. The Journal of neuroscience : the official journal of the Society for Neuroscience. vol 33. issue 7. 2013-04-11. PMID:23407955. |
the cellular form of prion protein prp(c) is highly expressed in the brain, where it can be converted into its abnormally folded isoform prp(sc) to cause neurodegenerative diseases. |
2013-04-11 |
2023-08-12 |
mouse |
| Qi Shi, Xiao-Ping Don. (Ctm)PrP and ER stress: a neurotoxic mechanism of some special PrP mutants. Prion. vol 5. issue 3. 2013-04-11. PMID:21795854. |
the pathogenic agent is hypothesized to be prp(sc) in prion diseases. |
2013-04-11 |
2023-08-12 |
mouse |
| Qi Shi, Xiao-Ping Don. (Ctm)PrP and ER stress: a neurotoxic mechanism of some special PrP mutants. Prion. vol 5. issue 3. 2013-04-11. PMID:21795854. |
in conclusion, some kinds of intermediate forms of prp(sc) , including (ctm)prp, may work as the ultimate cause of neurodegeneration. |
2013-04-11 |
2023-08-12 |
mouse |
| Alberto Miranda, Eva Pericuesta, Miguel Ángel Ramírez, Alfonso Gutiérrez-Adá. Prion protein in ESC regulation. Prion. vol 5. issue 3. 2013-04-11. PMID:21814032. |
a reduction in brain stem cells pluripotency after prp(c) is misfolded into the pathological conformation (prp(sc)) could lead to a delay or a disappearance of the normal brain damage recovery. |
2013-04-11 |
2023-08-12 |
Not clear |
| Wen-Quan Zou, Xiaochen Zhou, Jue Yuan, Xiangzhu Xia. Insoluble cellular prion protein and its association with prion and Alzheimer diseases. Prion. vol 5. issue 3. 2013-04-11. PMID:21847014. |
the soluble cellular prion protein (prp(c)) is best known for its association with prion disease (prd) through its conversion to a pathogenic insoluble isoform (prp(sc)). |
2013-04-11 |
2023-08-12 |
human |
| Wen-Quan Zou, Xiaochen Zhou, Jue Yuan, Xiangzhu Xia. Insoluble cellular prion protein and its association with prion and Alzheimer diseases. Prion. vol 5. issue 3. 2013-04-11. PMID:21847014. |
however, its deleterious effects independent of prp(sc) have recently been observed not only in prd but also in alzheimer disease (ad), two diseases which mainly affect cognition. |
2013-04-11 |
2023-08-12 |
human |
| Wen-Quan Zou, Xiaochen Zhou, Jue Yuan, Xiangzhu Xia. Insoluble cellular prion protein and its association with prion and Alzheimer diseases. Prion. vol 5. issue 3. 2013-04-11. PMID:21847014. |
remarkably, the prp(sc) -like iprpc shares the immunoreactivity behavior and fragmentation with a newly-identified prp(sc) species in a novel human prd termed variably protease-sensitive prionopathy. |
2013-04-11 |
2023-08-12 |
human |
| Binggong Chang, Robert Petersen, Thomas Wisniewski, Richard Rubenstei. Influence of Mabs on PrP(Sc) formation using in vitro and cell-free systems. PloS one. vol 7. issue 7. 2013-04-09. PMID:22848548. |
influence of mabs on prp(sc) formation using in vitro and cell-free systems. |
2013-04-09 |
2023-08-12 |
Not clear |
| Binggong Chang, Robert Petersen, Thomas Wisniewski, Richard Rubenstei. Influence of Mabs on PrP(Sc) formation using in vitro and cell-free systems. PloS one. vol 7. issue 7. 2013-04-09. PMID:22848548. |
prp(sc) is believed to serve as a template for the conversion of prp(c) to the abnormal isoform. |
2013-04-09 |
2023-08-12 |
Not clear |
| Binggong Chang, Robert Petersen, Thomas Wisniewski, Richard Rubenstei. Influence of Mabs on PrP(Sc) formation using in vitro and cell-free systems. PloS one. vol 7. issue 7. 2013-04-09. PMID:22848548. |
we hypothesized that antibodies binding to either prp(c)or prp(sc) would hinder or prevent the formation of the prp(c)-prp(sc) complex and thus slow down or prevent the conversion process. |
2013-04-09 |
2023-08-12 |
Not clear |
| Binggong Chang, Robert Petersen, Thomas Wisniewski, Richard Rubenstei. Influence of Mabs on PrP(Sc) formation using in vitro and cell-free systems. PloS one. vol 7. issue 7. 2013-04-09. PMID:22848548. |
two systems were used to analyze the effect of different antibodies on prp(sc) formation: (i) neuroblastoma cells persistently infected with the 22l mouse-adapted scrapie stain, and (ii) protein misfolding cyclic amplification (pmca), which uses prp(sc) as a template or seed, and a series of incubations and sonications, to convert prp(c) to prp(sc). |
2013-04-09 |
2023-08-12 |
Not clear |
| Binggong Chang, Robert Petersen, Thomas Wisniewski, Richard Rubenstei. Influence of Mabs on PrP(Sc) formation using in vitro and cell-free systems. PloS one. vol 7. issue 7. 2013-04-09. PMID:22848548. |
the two systems yielded similar results, in most cases, and demonstrate that prp-specific monoclonal antibodies (mabs) vary in their ability to inhibit the prp(c)-prp(sc) conversion process. |
2013-04-09 |
2023-08-12 |
Not clear |