| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Sandra Pritzkow, Rodrigo Morales, Fabio Moda, Uffaf Khan, Glenn C Telling, Edward Hoover, Claudio Sot. Grass plants bind, retain, uptake, and transport infectious prions. Cell reports. vol 11. issue 8. 2016-04-05. PMID:25981035. |
furthermore, leaves contaminated by spraying with a prion-containing preparation retained prp(sc) for several weeks in the living plant. |
2016-04-05 |
2023-08-13 |
Not clear |
| Saurabh Srivastava, Natallia Makarava, Elizaveta Katorcha, Regina Savtchenko, Reinhard Brossmer, Ilia V Baskako. Post-conversion sialylation of prions in lymphoid tissues. Proceedings of the National Academy of Sciences of the United States of America. vol 112. issue 48. 2016-04-04. PMID:26627256. |
here we show that the sialylation status of the infectious, disease-associated state of the prion protein (prp(sc)) changes with colonization of secondary lymphoid organs (slos). |
2016-04-04 |
2023-08-13 |
Not clear |
| Saurabh Srivastava, Natallia Makarava, Elizaveta Katorcha, Regina Savtchenko, Reinhard Brossmer, Ilia V Baskako. Post-conversion sialylation of prions in lymphoid tissues. Proceedings of the National Academy of Sciences of the United States of America. vol 112. issue 48. 2016-04-04. PMID:26627256. |
as a result, spleen-derived prp(sc) is more sialylated than brain-derived prp(sc). |
2016-04-04 |
2023-08-13 |
Not clear |
| Saurabh Srivastava, Natallia Makarava, Elizaveta Katorcha, Regina Savtchenko, Reinhard Brossmer, Ilia V Baskako. Post-conversion sialylation of prions in lymphoid tissues. Proceedings of the National Academy of Sciences of the United States of America. vol 112. issue 48. 2016-04-04. PMID:26627256. |
enhanced sialylation of prp(sc) is recapitulated in vitro by incubating brain-derived prp(sc) with primary splenocytes or cultured macrophage raw 264.7 cells. |
2016-04-04 |
2023-08-13 |
Not clear |
| Saurabh Srivastava, Natallia Makarava, Elizaveta Katorcha, Regina Savtchenko, Reinhard Brossmer, Ilia V Baskako. Post-conversion sialylation of prions in lymphoid tissues. Proceedings of the National Academy of Sciences of the United States of America. vol 112. issue 48. 2016-04-04. PMID:26627256. |
general inhibitors of sialyltranserases (sts), the enzymes that transfer sialic acid residues onto terminal positions of glycans, suppressed extrasialylation of prp(sc). |
2016-04-04 |
2023-08-13 |
Not clear |
| Andrei Soutyrine, Nishandan Yogasingam, Hongsheng Huang, Gordon Mitchel. Effects of heme-PrP complex on cell-free conversion and peroxidase-linked immunodetection of prions in blood-based assays. Research in veterinary science. vol 101. 2016-03-28. PMID:26022071. |
this study investigated implications of this interaction in blood-based peroxidase-linked prion immunodetection and seeded conversion of cellular prion (prp(c)) into disease associated form (prp(sc)). |
2016-03-28 |
2023-08-13 |
Not clear |
| Andrei Soutyrine, Nishandan Yogasingam, Hongsheng Huang, Gordon Mitchel. Effects of heme-PrP complex on cell-free conversion and peroxidase-linked immunodetection of prions in blood-based assays. Research in veterinary science. vol 101. 2016-03-28. PMID:26022071. |
additionally, 10 μm heme inhibited (p<0.05) the seeded conversion of prp(c) to prp(sc) through the protein misfolding cycling amplification assay. |
2016-03-28 |
2023-08-13 |
Not clear |
| Andrei Soutyrine, Nishandan Yogasingam, Hongsheng Huang, Gordon Mitchel. Effects of heme-PrP complex on cell-free conversion and peroxidase-linked immunodetection of prions in blood-based assays. Research in veterinary science. vol 101. 2016-03-28. PMID:26022071. |
these results indicate that heme-prp interactions could modulate intrinsic pod and protect prp(c) from conversion into prp(sc). |
2016-03-28 |
2023-08-13 |
Not clear |
| Stéphane Haïk, Jean-Philippe Brande. Infectious prion diseases in humans: cannibalism, iatrogenicity and zoonoses. Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases. vol 26. 2016-03-24. PMID:24956437. |
the transmissible agent is thought to be solely composed of the abnormal isoform (prp(sc)) of the host-encoded prion protein that accumulated in the central nervous system of affected individuals. |
2016-03-24 |
2023-08-13 |
human |
| Stéphane Haïk, Jean-Philippe Brande. Infectious prion diseases in humans: cannibalism, iatrogenicity and zoonoses. Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases. vol 26. 2016-03-24. PMID:24956437. |
compared to its normal counterpart, prp(sc) is β-sheet enriched and aggregated and its propagation is based on an autocatalytic conversion process. |
2016-03-24 |
2023-08-13 |
human |
| Stéphane Haïk, Jean-Philippe Brande. Infectious prion diseases in humans: cannibalism, iatrogenicity and zoonoses. Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases. vol 26. 2016-03-24. PMID:24956437. |
increasing evidence supports the view that conformational variations of prp(sc) encoded the biological properties of the various prion strains that have been isolated by transmission studies in experimental models. |
2016-03-24 |
2023-08-13 |
human |
| G Scalabrino, D Veber, R De Giuseppe, F Roncarol. Low levels of cobalamin, epidermal growth factor, and normal prions in multiple sclerosis spinal cord. Neuroscience. vol 298. 2016-03-21. PMID:25888933. |
the cbl, egf, and prp(c) levels were significantly decreased in ms scs in comparison with controls and, paradoxically, the decreased cbl levels were associated with decreased sc levels of homocysteine, a biochemical marker of cbl deficiency. |
2016-03-21 |
2023-08-13 |
Not clear |
| G Scalabrino, D Veber, R De Giuseppe, F Roncarol. Low levels of cobalamin, epidermal growth factor, and normal prions in multiple sclerosis spinal cord. Neuroscience. vol 298. 2016-03-21. PMID:25888933. |
only prp(c) levels were invariably decreased in both the sc and csf regardless of the clinical course of the disease. |
2016-03-21 |
2023-08-13 |
Not clear |
| Paola Scano, Antonella Rosa, Alessandra Incani, Caterina Maestrale, Cinzia Santucciu, Daniela Perra, Sarah Vascellari, Alessandra Pani, Ciriaco Ligio. (1)H NMR brain metabonomics of scrapie exposed sheep. Molecular bioSystems. vol 11. issue 7. 2016-03-16. PMID:25959287. |
on the basis of clinical examinations and western blotting analysis for the pathological prion protein (prp(sc)) in brain tissues, sheep were catalogued as not infected (h), infected with clinical signs (s), and infected without clinical signs (a). |
2016-03-16 |
2023-08-13 |
mouse |
| Paola Scano, Antonella Rosa, Alessandra Incani, Caterina Maestrale, Cinzia Santucciu, Daniela Perra, Sarah Vascellari, Alessandra Pani, Ciriaco Ligio. (1)H NMR brain metabonomics of scrapie exposed sheep. Molecular bioSystems. vol 11. issue 7. 2016-03-16. PMID:25959287. |
by means of partial least squares regression, an excellent correlation was found between the prp(sc) amount and the (1)h nmr metabolite profile of infected (s and a) sheep, and the metabolite mostly correlated with prp(sc) was alanine. |
2016-03-16 |
2023-08-13 |
mouse |
| Paola Scano, Antonella Rosa, Alessandra Incani, Caterina Maestrale, Cinzia Santucciu, Daniela Perra, Sarah Vascellari, Alessandra Pani, Ciriaco Ligio. (1)H NMR brain metabonomics of scrapie exposed sheep. Molecular bioSystems. vol 11. issue 7. 2016-03-16. PMID:25959287. |
the overall results, obtained using different chemometric tools, were able to describe a brain metabolite profile of infected sheep with and without clinical signs, compared to healthy ones, and indicated alanine as a biomarker for prp(sc) amounts in scrapie brains. |
2016-03-16 |
2023-08-13 |
mouse |
| Justin J Greenlee, M Heather West Greenle. The transmissible spongiform encephalopathies of livestock. ILAR journal. vol 56. issue 1. 2016-03-03. PMID:25991695. |
these diseases are associated with the accumulation of a protease-resistant, disease-associated isoform of the prion protein (called prp(sc)) in the central nervous system and other tissues, depending on the host species. |
2016-03-03 |
2023-08-13 |
cattle |
| Laura J Ellett, Bradley M Coleman, Mitch C Shambrook, Vanessa A Johanssen, Steven J Collins, Colin L Masters, Andrew F Hill, Victoria A Lawso. Glycosaminoglycan sulfation determines the biochemical properties of prion protein aggregates. Glycobiology. vol 25. issue 7. 2016-03-01. PMID:25701659. |
prion diseases are transmissible neurodegenerative disorders associated with the conversion of the cellular prion protein, prp(c), to a misfolded isoform called prp(sc). |
2016-03-01 |
2023-08-13 |
Not clear |
| Laura J Ellett, Bradley M Coleman, Mitch C Shambrook, Vanessa A Johanssen, Steven J Collins, Colin L Masters, Andrew F Hill, Victoria A Lawso. Glycosaminoglycan sulfation determines the biochemical properties of prion protein aggregates. Glycobiology. vol 25. issue 7. 2016-03-01. PMID:25701659. |
although prp(sc) is a necessary component of the infectious prion, additional factors, or cofactors, have been shown to contribute to the efficient formation of transmissible prp(sc). |
2016-03-01 |
2023-08-13 |
Not clear |
| Laura J Ellett, Bradley M Coleman, Mitch C Shambrook, Vanessa A Johanssen, Steven J Collins, Colin L Masters, Andrew F Hill, Victoria A Lawso. Glycosaminoglycan sulfation determines the biochemical properties of prion protein aggregates. Glycobiology. vol 25. issue 7. 2016-03-01. PMID:25701659. |
glycosaminoglycans (gags) are attractive cofactor candidates as they can be found associated with prp(sc) deposits, have been shown to enhance prp misfolding in vitro, are found in the same cellular compartments as prp(c) and have been shown to be disease modifying in vivo. |
2016-03-01 |
2023-08-13 |
Not clear |