| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Ryan Taschuk, Jacques Van der Merwe, Kristen Marciniuk, Andrew Potter, Neil Cashman, Philip Griebel, Scott Nappe. In vitro neutralization of prions with PrP(Sc)-specific antibodies. Prion. vol 9. issue 4. 2016-05-23. PMID:26284508. |
by targeting epitopes uniquely exposed by misfolding, our group developed prp(sc)-specific vaccines to 3 disease specific epitopes (dses). |
2016-05-23 |
2023-08-13 |
Not clear |
| Ryan Taschuk, Jacques Van der Merwe, Kristen Marciniuk, Andrew Potter, Neil Cashman, Philip Griebel, Scott Nappe. In vitro neutralization of prions with PrP(Sc)-specific antibodies. Prion. vol 9. issue 4. 2016-05-23. PMID:26284508. |
for both purified antibodies and immunoreactive sera, the prp(sc)-specific antibodies were equally effective in neutralizing prions. |
2016-05-23 |
2023-08-13 |
Not clear |
| Ryan Taschuk, Jacques Van der Merwe, Kristen Marciniuk, Andrew Potter, Neil Cashman, Philip Griebel, Scott Nappe. In vitro neutralization of prions with PrP(Sc)-specific antibodies. Prion. vol 9. issue 4. 2016-05-23. PMID:26284508. |
at a low antibody concentration, the prp(sc)-specific antibodies matched the neutralization achieved by an antibody that may act via both prp(c) and prp(sc). |
2016-05-23 |
2023-08-13 |
Not clear |
| Ryan Taschuk, Jacques Van der Merwe, Kristen Marciniuk, Andrew Potter, Neil Cashman, Philip Griebel, Scott Nappe. In vitro neutralization of prions with PrP(Sc)-specific antibodies. Prion. vol 9. issue 4. 2016-05-23. PMID:26284508. |
at higher doses, however, this pan-specific antibody was more effective, potentially due to a combined deactivation of prp(sc) and depletion of prp(c). |
2016-05-23 |
2023-08-13 |
Not clear |
| Clive Bate, William Nolan, Alun William. Glycosylphosphatidylinositols: More than just an anchor? Communicative & integrative biology. vol 9. issue 2. 2016-05-19. PMID:27195066. |
the "prion diseases" arise following the conversion of prp(c) to a disease-associated isoform called prp(sc) or "prion". |
2016-05-19 |
2023-08-13 |
Not clear |
| Clive Bate, William Nolan, Alun William. Glycosylphosphatidylinositols: More than just an anchor? Communicative & integrative biology. vol 9. issue 2. 2016-05-19. PMID:27195066. |
our paper showed that desialylated prp(c) inhibited prp(sc) formation. |
2016-05-19 |
2023-08-13 |
Not clear |
| Clive Bate, William Nolan, Alun William. Glycosylphosphatidylinositols: More than just an anchor? Communicative & integrative biology. vol 9. issue 2. 2016-05-19. PMID:27195066. |
aggregated prp(sc) creates a signaling platform in the cell membrane incorporating and activating cytoplasmic phospholipase a2 (cpla2), an enzyme that regulates prp(c) trafficking and hence prp(sc) formation. |
2016-05-19 |
2023-08-13 |
Not clear |
| Clive Bate, William Nolan, Alun William. Glycosylphosphatidylinositols: More than just an anchor? Communicative & integrative biology. vol 9. issue 2. 2016-05-19. PMID:27195066. |
the presence of desialylated prp(c) caused the dissociation of cpla2 from prp-containing platforms, reduced the activation of cpla2 and inhibited prp(sc) production. |
2016-05-19 |
2023-08-13 |
Not clear |
| Clive Bate, William Nolan, Alun William. Glycosylphosphatidylinositols: More than just an anchor? Communicative & integrative biology. vol 9. issue 2. 2016-05-19. PMID:27195066. |
we concluded that sialic acid contained within the gpi attached to prp(c) modifies local membrane microenvironments that are important in prp-mediated cell signaling and prp(sc) formation. |
2016-05-19 |
2023-08-13 |
Not clear |
| Clive Bate, William Nolan, Alun William. Sialic Acid on the Glycosylphosphatidylinositol Anchor Regulates PrP-mediated Cell Signaling and Prion Formation. The Journal of biological chemistry. vol 291. issue 1. 2016-05-17. PMID:26553874. |
the prion diseases occur following the conversion of the cellular prion protein (prp(c)) into disease-related isoforms (prp(sc)). |
2016-05-17 |
2023-08-13 |
Not clear |
| Clive Bate, William Nolan, Alun William. Sialic Acid on the Glycosylphosphatidylinositol Anchor Regulates PrP-mediated Cell Signaling and Prion Formation. The Journal of biological chemistry. vol 291. issue 1. 2016-05-17. PMID:26553874. |
prp(sc) formation in two prion-infected neuronal cell lines (scgt1 and scn2a cells) and in scrapie-infected primary cortical neurons was increased following the introduction of prp(c). |
2016-05-17 |
2023-08-13 |
Not clear |
| Clive Bate, William Nolan, Alun William. Sialic Acid on the Glycosylphosphatidylinositol Anchor Regulates PrP-mediated Cell Signaling and Prion Formation. The Journal of biological chemistry. vol 291. issue 1. 2016-05-17. PMID:26553874. |
in contrast, prp(c) containing a gpi anchor from which the sialic acid had been removed (desialylated prp(c)) was not converted to prp(sc). |
2016-05-17 |
2023-08-13 |
Not clear |
| Clive Bate, William Nolan, Alun William. Sialic Acid on the Glycosylphosphatidylinositol Anchor Regulates PrP-mediated Cell Signaling and Prion Formation. The Journal of biological chemistry. vol 291. issue 1. 2016-05-17. PMID:26553874. |
furthermore, the presence of desialylated prp(c) inhibited the production of prp(sc) within prion-infected cortical neurons and scgt1 and scn2a cells. |
2016-05-17 |
2023-08-13 |
Not clear |
| Clive Bate, William Nolan, Alun William. Sialic Acid on the Glycosylphosphatidylinositol Anchor Regulates PrP-mediated Cell Signaling and Prion Formation. The Journal of biological chemistry. vol 291. issue 1. 2016-05-17. PMID:26553874. |
these findings show that the sialic acid moiety of the gpi attached to prp(c) modifies local membrane microenvironments that are important in prp-mediated cell signaling and prp(sc) formation. |
2016-05-17 |
2023-08-13 |
Not clear |
| Christina M Carlson, Jay R Schneider, Joel A Pedersen, Dennis M Heisey, Christopher J Johnso. Experimental infection of meadow voles (Microtus pennsylvanicus) with sheep scrapie. Canadian journal of veterinary research = Revue canadienne de recherche veterinaire. vol 79. issue 1. 2016-05-15. PMID:25673912. |
vacuolization patterns and disease-associated prion protein (prp(sc)) deposition were generally similar in all scrapie-affected voles, except in the hippocampus, where prp(sc) staining varied markedly among the animals. |
2016-05-15 |
2023-08-13 |
Not clear |
| Lester Carter, Seung Joong Kim, Dina Schneidman-Duhovny, Jan Stöhr, Guillaume Poncet-Montange, Thomas M Weiss, Hiro Tsuruta, Stanley B Prusiner, Andrej Sal. Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering. Biophysical journal. vol 109. issue 4. 2016-05-12. PMID:26287631. |
in particular, misfolding of the mostly α-helical cellular prion protein (prp(c)) into a β-sheet-rich disease-causing isoform (prp(sc)) is the key molecular event in the formation of prp(sc) aggregates. |
2016-05-12 |
2023-08-13 |
mouse |
| Lester Carter, Seung Joong Kim, Dina Schneidman-Duhovny, Jan Stöhr, Guillaume Poncet-Montange, Thomas M Weiss, Hiro Tsuruta, Stanley B Prusiner, Andrej Sal. Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering. Biophysical journal. vol 109. issue 4. 2016-05-12. PMID:26287631. |
the molecular mechanisms underlying the prp(c)-to-prp(sc) conversion and subsequent aggregation remain to be elucidated. |
2016-05-12 |
2023-08-13 |
mouse |
| Lester Carter, Seung Joong Kim, Dina Schneidman-Duhovny, Jan Stöhr, Guillaume Poncet-Montange, Thomas M Weiss, Hiro Tsuruta, Stanley B Prusiner, Andrej Sal. Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering. Biophysical journal. vol 109. issue 4. 2016-05-12. PMID:26287631. |
however, in persistently prion-infected cell-culture models, it was shown that treatment with monoclonal antibodies against defined regions of the prion protein (prp) led to the clearing of prp(sc) in cultured cells. |
2016-05-12 |
2023-08-13 |
mouse |
| Lester Carter, Seung Joong Kim, Dina Schneidman-Duhovny, Jan Stöhr, Guillaume Poncet-Montange, Thomas M Weiss, Hiro Tsuruta, Stanley B Prusiner, Andrej Sal. Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering. Biophysical journal. vol 109. issue 4. 2016-05-12. PMID:26287631. |
the resulting structural models suggest two mechanisms for how these fabs may prevent the conversion of prp(c) into prp(sc). |
2016-05-12 |
2023-08-13 |
mouse |
| Uli S Herrmann, Anne K Schütz, Hamid Shirani, Danzhi Huang, Dino Saban, Mario Nuvolone, Bei Li, Boris Ballmer, Andreas K O Åslund, Jeffrey J Mason, Elisabeth Rushing, Herbert Budka, Sofie Nyström, Per Hammarström, Anja Böckmann, Amedeo Caflisch, Beat H Meier, K Peter R Nilsson, Simone Hornemann, Adriano Aguzz. Structure-based drug design identifies polythiophenes as antiprion compounds. Science translational medicine. vol 7. issue 299. 2016-05-10. PMID:26246168. |
prions consist of prp(sc), a misfolded and aggregated form of the cellular prion protein (prp(c)). |
2016-05-10 |
2023-08-13 |
mouse |