| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Jie Chen, D Thirumala. Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition. Biochemistry. vol 52. issue 2. 2013-03-07. PMID:23256626. |
helices 2 and 3 are the initiation sites in the prp(c) → prp(sc) transition. |
2013-03-07 |
2023-08-12 |
mouse |
| Jie Chen, D Thirumala. Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition. Biochemistry. vol 52. issue 2. 2013-03-07. PMID:23256626. |
both sca and single-molecule force simulations show that in the conversion from prp(c) to prp(sc) major conformational changes occur (at least initially) in h2 and h3, which because of their sequence compositions are frustrated in the helical state. |
2013-03-07 |
2023-08-12 |
mouse |
| Gantsetseg Dorj, Hiroyuki Okada, Kohtaro Miyazawa, Kentaro Masujin, Kumiko Kimura, Shirou Mohri, Takashi Yokoyam. Retrospective analysis of sheep scrapie by western blotting with formalin-fixed paraffin-embedded (FFPE) tissues. The Journal of veterinary medical science. vol 74. issue 9. 2013-03-06. PMID:22673495. |
an abnormal isoform of prion protein (prp(sc)) was extracted from formalin-fixed paraffin-embedded (ffpe) tissues from sheep and analyzed by western blotting. |
2013-03-06 |
2023-08-12 |
Not clear |
| Gantsetseg Dorj, Hiroyuki Okada, Kohtaro Miyazawa, Kentaro Masujin, Kumiko Kimura, Shirou Mohri, Takashi Yokoyam. Retrospective analysis of sheep scrapie by western blotting with formalin-fixed paraffin-embedded (FFPE) tissues. The Journal of veterinary medical science. vol 74. issue 9. 2013-03-06. PMID:22673495. |
prp(sc) immunoreactivity against anti-prp monoclonal antibody t2, which recognizes discontinuous prp sequences, differed amongst individual scrapie sheep cases. |
2013-03-06 |
2023-08-12 |
Not clear |
| Gantsetseg Dorj, Hiroyuki Okada, Kohtaro Miyazawa, Kentaro Masujin, Kumiko Kimura, Shirou Mohri, Takashi Yokoyam. Retrospective analysis of sheep scrapie by western blotting with formalin-fixed paraffin-embedded (FFPE) tissues. The Journal of veterinary medical science. vol 74. issue 9. 2013-03-06. PMID:22673495. |
this may reflect structural differences in prp(sc) that have been formalin-fixed prior to their extraction. |
2013-03-06 |
2023-08-12 |
Not clear |
| Pravas Kumar Baral, Barbara Wieland, Mridula Swayampakula, Magdalini Polymenidou, Muhammad Hafiz Rahman, Nat N V Kav, Adriano Aguzzi, Michael N G Jame. Structural studies on the folded domain of the human prion protein bound to the Fab fragment of the antibody POM1. Acta crystallographica. Section D, Biological crystallography. vol 68. issue Pt 11. 2013-03-01. PMID:23090399. |
prion diseases are neurodegenerative diseases characterized by the conversion of the cellular prion protein prp(c) into a pathogenic isoform prp(sc). |
2013-03-01 |
2023-08-12 |
human |
| Natallia Makarava, Regina Savtchenko, Ilia V Baskako. Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification. The Journal of biological chemistry. vol 288. issue 1. 2013-02-28. PMID:23168413. |
here we show that by subjecting brain material of a synthetic strain consisting of a mixture of self-replicating states to pmcab, selective amplification of prp(sc) could be achieved, and that pmcab mimicked the evolutionary trend observed during serial transmission in animals. |
2013-02-28 |
2023-08-12 |
Not clear |
| Natallia Makarava, Regina Savtchenko, Ilia V Baskako. Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification. The Journal of biological chemistry. vol 288. issue 1. 2013-02-28. PMID:23168413. |
surprisingly, when hamster-adapted strains (263k and hyper) were subjected to dgpmcab, their proteinase k digestion profile underwent a dramatic transformation, suggesting that a mixture of atypical prpres and prp(sc) might be present in brain-derived materials. |
2013-02-28 |
2023-08-12 |
Not clear |
| Natallia Makarava, Regina Savtchenko, Ilia V Baskako. Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification. The Journal of biological chemistry. vol 288. issue 1. 2013-02-28. PMID:23168413. |
however, detailed analysis revealed that the proteinase k-resistant profile of prp(sc) changed in response to dgpmcab. |
2013-02-28 |
2023-08-12 |
Not clear |
| Natallia Makarava, Regina Savtchenko, Ilia V Baskako. Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification. The Journal of biological chemistry. vol 288. issue 1. 2013-02-28. PMID:23168413. |
this study revealed that the change in prp(sc) biochemical phenotype does not always represent an irreversible transformation of a strain, but rather demonstrated the existence of a wide range of variation for strain-specific physical features in response to a change in prion replication environment. |
2013-02-28 |
2023-08-12 |
Not clear |
| Maria E Herva, Charles Weissma. Cell-specific susceptibility to prion strains is a property of the intact cell. Prion. vol 6. issue 4. 2013-02-27. PMID:22561192. |
prions consist of prp (sc), a misfolded version of the cellular protein prp (c). |
2013-02-27 |
2023-08-12 |
Not clear |
| Maria E Herva, Charles Weissma. Cell-specific susceptibility to prion strains is a property of the intact cell. Prion. vol 6. issue 4. 2013-02-27. PMID:22561192. |
they occur in a variety of strains that share the amino acid sequence of prp but differ in phenotypic properties, such as cell tropism and pathogenicity; strain-ness is attributed to the conformation of prp (sc). |
2013-02-27 |
2023-08-12 |
Not clear |
| Maria E Herva, Charles Weissma. Cell-specific susceptibility to prion strains is a property of the intact cell. Prion. vol 6. issue 4. 2013-02-27. PMID:22561192. |
we found that both lysates supported amplification of rml prp (sc) equally well, despite a 280-fold difference in the susceptibility of the cells from which they were derived. |
2013-02-27 |
2023-08-12 |
Not clear |
| Fabio Moda, Chiara Vimercati, Ilaria Campagnani, Margherita Ruggerone, Giorgio Giaccone, Michela Morbin, Lorena Zentilin, Mauro Giacca, Ileana Zucca, Giuseppe Legname, Fabrizio Tagliavin. Brain delivery of AAV9 expressing an anti-PrP monovalent antibody delays prion disease in mice. Prion. vol 6. issue 4. 2013-02-27. PMID:22842862. |
prion diseases are caused by a conformational modification of the cellular prion protein (prp (c)) into disease-specific forms, termed prp (sc), that have the ability to interact with prp (c) promoting its conversion to prp (sc). |
2013-02-27 |
2023-08-12 |
mouse |
| Fabio Moda, Chiara Vimercati, Ilaria Campagnani, Margherita Ruggerone, Giorgio Giaccone, Michela Morbin, Lorena Zentilin, Mauro Giacca, Ileana Zucca, Giuseppe Legname, Fabrizio Tagliavin. Brain delivery of AAV9 expressing an anti-PrP monovalent antibody delays prion disease in mice. Prion. vol 6. issue 4. 2013-02-27. PMID:22842862. |
this molecule binds the prp (c) region involved in the interaction with prp (sc) thus halting further prion formation. |
2013-02-27 |
2023-08-12 |
mouse |
| Fabio Moda, Chiara Vimercati, Ilaria Campagnani, Margherita Ruggerone, Giorgio Giaccone, Michela Morbin, Lorena Zentilin, Mauro Giacca, Ileana Zucca, Giuseppe Legname, Fabrizio Tagliavin. Brain delivery of AAV9 expressing an anti-PrP monovalent antibody delays prion disease in mice. Prion. vol 6. issue 4. 2013-02-27. PMID:22842862. |
we found that the treatment was safe, prolonged the incubation time of scrapie-infected animals and decreased the burden of total proteinase-resistant prp (sc) in the brain, suggesting that scfvd18 interferes with prion replication in vivo. |
2013-02-27 |
2023-08-12 |
mouse |
| Jin Zhang, Xiao-Ping Don. Dysfunction of microtubule-associated proteins of MAP2/tau family in Prion disease. Prion. vol 6. issue 4. 2013-02-27. PMID:22874672. |
the aggregation of prp (sc) is thought to be crucial for the neuropathology of prion diseases. |
2013-02-27 |
2023-08-12 |
human |
| Jin Zhang, Xiao-Ping Don. Dysfunction of microtubule-associated proteins of MAP2/tau family in Prion disease. Prion. vol 6. issue 4. 2013-02-27. PMID:22874672. |
a growing body of evidence demonstrates that the perturbation of the microtubule network contributes to prp (sc) -mediated neurodegeneration. |
2013-02-27 |
2023-08-12 |
human |
| David Westaway, Jack H Jhamanda. The P's and Q's of cellular PrP-Aβ interactions. Prion. vol 6. issue 4. 2013-02-27. PMID:22874673. |
prion disease research has opened up the "black-box" of neurodegeneration, defining a key role for protein misfolding wherein a predominantly alpha-helical precursor protein, prp (c), is converted to a disease-associated, β-sheet enriched isoform called prp (sc). |
2013-02-27 |
2023-08-12 |
Not clear |
| David Westaway, Jack H Jhamanda. The P's and Q's of cellular PrP-Aβ interactions. Prion. vol 6. issue 4. 2013-02-27. PMID:22874673. |
early thoughts along the lines of overlap may have been on target, (1) but were eclipsed by a simultaneous (but now anachronistic) controversy over the role of prp (sc) in prion diseases. |
2013-02-27 |
2023-08-12 |
Not clear |