| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Lars Luers, Oliver Bannach, Jan Stöhr, Michael Marius Wördehoff, Martin Wolff, Luitgard Nagel-Steger, Detlev Riesner, Dieter Willbold, Eva Birkman. Seeded fibrillation as molecular basis of the species barrier in human prion diseases. PloS one. vol 8. issue 8. 2015-01-22. PMID:23977331. |
we therefore hypothesise, that the species barrier is based on the interaction of prp(c) and prp(sc). |
2015-01-22 |
2023-08-12 |
human |
| Lars Luers, Oliver Bannach, Jan Stöhr, Michael Marius Wördehoff, Martin Wolff, Luitgard Nagel-Steger, Detlev Riesner, Dieter Willbold, Eva Birkman. Seeded fibrillation as molecular basis of the species barrier in human prion diseases. PloS one. vol 8. issue 8. 2015-01-22. PMID:23977331. |
we could show that the seeding activity and therewith the molecular interaction of prp as substrate and prp(sc) as seed is sufficient to explain the phenomenon of species barriers. |
2015-01-22 |
2023-08-12 |
human |
| Bradley R Groveman, Michael A Dolan, Lara M Taubner, Allison Kraus, Reed B Wickner, Byron Caughe. Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids. The Journal of biological chemistry. vol 289. issue 35. 2015-01-22. PMID:25028516. |
prp(sc) or prp-scrapie) remain poorly defined. |
2015-01-22 |
2023-08-13 |
Not clear |
| Bradley R Groveman, Michael A Dolan, Lara M Taubner, Allison Kraus, Reed B Wickner, Byron Caughe. Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids. The Journal of biological chemistry. vol 289. issue 35. 2015-01-22. PMID:25028516. |
the prevalent structural models of prp(sc) retain most of the native α-helices of the normal, noninfectious prion protein, cellular prion protein (prp(c)), but evidence is accumulating that these helices are absent in prp(sc) amyloid. |
2015-01-22 |
2023-08-13 |
Not clear |
| Bradley R Groveman, Michael A Dolan, Lara M Taubner, Allison Kraus, Reed B Wickner, Byron Caughe. Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids. The Journal of biological chemistry. vol 289. issue 35. 2015-01-22. PMID:25028516. |
molecular dynamics simulations of prp(90-231) octameric segments suggested that such linear fibrils, which are consistent with many features of prp(sc) fibrils, can have stable parallel in-register β-sheet cores. |
2015-01-22 |
2023-08-13 |
Not clear |
| Byung-Hoon Jeong, Yong-Sun Ki. Genetic studies in human prion diseases. Journal of Korean medical science. vol 29. issue 5. 2015-01-10. PMID:24851016. |
human prion diseases are fatal neurodegenerative disorders that are characterized by spongiform changes, astrogliosis, and the accumulation of an abnormal prion protein (prp(sc)). |
2015-01-10 |
2023-08-13 |
human |
| Caterina Migliorini, Adalgisa Sinicropi, Henryk Kozlowski, Marek Luczkowski, Daniela Valensi. Copper-induced structural propensities of the amyloidogenic region of human prion protein. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. vol 19. issue 4-5. 2015-01-09. PMID:24737041. |
transmissible spongiform encephalopathies are associated with the misfolding of the cellular prion protein (prp(c)) to an abnormal protein isoform, called scrapie prion protein (prp(sc)). |
2015-01-09 |
2023-08-13 |
human |
| Ryo P Honda, Kei-Ichi Yamaguchi, Kazuo Kuwat. Acid-induced molten globule state of a prion protein: crucial role of Strand 1-Helix 1-Strand 2 segment. The Journal of biological chemistry. vol 289. issue 44. 2014-12-31. PMID:25217639. |
the conversion of a cellular prion protein (prp(c)) to its pathogenic isoform (prp(sc)) is a critical event in the pathogenesis of prion diseases. |
2014-12-31 |
2023-08-13 |
Not clear |
| Peter Rehbein, Krishna Saxena, Kai Schlepckow, Harald Schwalb. Protocol for aerosol-free recombinant production and NMR analysis of prion proteins. Journal of biomolecular NMR. vol 59. issue 2. 2014-12-30. PMID:24771297. |
the central hallmark of prion diseases is the misfolding of cellular prion protein (prp(c)) into a disease-associated aggregated isoform known as scrapie prion protein (prp(sc)). |
2014-12-30 |
2023-08-13 |
Not clear |
| F Morine. Prions: a model of conformational disease? Pathologie-biologie. vol 62. issue 2. 2014-12-11. PMID:24656441. |
the prion diseases are characterized by the conformational conversion of prp(c) to prp(sc), the fundamental even underlying prion diseases. |
2014-12-11 |
2023-08-12 |
Not clear |
| Jason J Serpa, Karl A T Makepeace, Tristan H Borchers, David S Wishart, Evgeniy V Petrotchenko, Christoph H Borcher. Using isotopically-coded hydrogen peroxide as a surface modification reagent for the structural characterization of prion protein aggregates. Journal of proteomics. vol 100. 2014-12-03. PMID:24316355. |
the conversion of the cellular prion protein (prp(c)) into aggregated ß-oligomeric (prp(ß)) and fibril (prp(sc)) forms is the central element in the development of prion diseases. |
2014-12-03 |
2023-08-12 |
Not clear |
| B Michael Silber, Joel R Gever, Satish Rao, Zhe Li, Adam R Renslo, Kartika Widjaja, Casper Wong, Kurt Giles, Yevgeniy Freyman, Manuel Elepano, John J Irwin, Matthew P Jacobson, Stanley B Prusine. Novel compounds lowering the cellular isoform of the human prion protein in cultured human cells. Bioorganic & medicinal chemistry. vol 22. issue 6. 2014-11-25. PMID:24530226. |
previous studies showed that lowering prp(c) concomitantly reduced prp(sc) in the brains of mice inoculated with prions. |
2014-11-25 |
2023-08-12 |
mouse |
| Tsuyoshi Shirai, Mihoko Saito, Atsushi Kobayashi, Masahiro Asano, Masaki Hizume, Shino Ikeda, Kenta Teruya, Masanori Morita, Tetsuyuki Kitamot. Evaluating prion models based on comprehensive mutation data of mouse PrP. Structure (London, England : 1993). vol 22. issue 4. 2014-11-25. PMID:24560805. |
the structural details of the essential entity of prion disease, fibril prion protein (prp(sc)), are still elusive despite the large body of evidence supporting the prion hypothesis. |
2014-11-25 |
2023-08-12 |
mouse |
| Tsuyoshi Shirai, Mihoko Saito, Atsushi Kobayashi, Masahiro Asano, Masaki Hizume, Shino Ikeda, Kenta Teruya, Masanori Morita, Tetsuyuki Kitamot. Evaluating prion models based on comprehensive mutation data of mouse PrP. Structure (London, England : 1993). vol 22. issue 4. 2014-11-25. PMID:24560805. |
five major working models of prp(sc) structure, which are not compatible with each other, have been proposed. |
2014-11-25 |
2023-08-12 |
mouse |
| Tsuyoshi Shirai, Mihoko Saito, Atsushi Kobayashi, Masahiro Asano, Masaki Hizume, Shino Ikeda, Kenta Teruya, Masanori Morita, Tetsuyuki Kitamot. Evaluating prion models based on comprehensive mutation data of mouse PrP. Structure (London, England : 1993). vol 22. issue 4. 2014-11-25. PMID:24560805. |
a comprehensive mutation experiment was performed on mouse prion protein, and the prp(sc) conversion efficiency of each mutant was examined. |
2014-11-25 |
2023-08-12 |
mouse |
| Kazunori Sano, Ryuichiro Atarashi, Daisuke Ishibashi, Takehiro Nakagaki, Katsuya Satoh, Noriyuki Nishid. Conformational properties of prion strains can be transmitted to recombinant prion protein fibrils in real-time quaking-induced conversion. Journal of virology. vol 88. issue 20. 2014-11-25. PMID:25078700. |
the phenomenon of prion strains with distinct biological characteristics has been hypothesized to be involved in the structural diversity of abnormal prion protein (prp(sc)). |
2014-11-25 |
2023-08-13 |
mouse |
| Kazunori Sano, Ryuichiro Atarashi, Daisuke Ishibashi, Takehiro Nakagaki, Katsuya Satoh, Noriyuki Nishid. Conformational properties of prion strains can be transmitted to recombinant prion protein fibrils in real-time quaking-induced conversion. Journal of virology. vol 88. issue 20. 2014-11-25. PMID:25078700. |
real-time quaking-induced conversion (rt-quic) is a cell-free system that uses escherichia coli-derived recombinant prp (rprp) for the sensitive detection of prp(sc). |
2014-11-25 |
2023-08-13 |
mouse |
| Kazunori Sano, Ryuichiro Atarashi, Daisuke Ishibashi, Takehiro Nakagaki, Katsuya Satoh, Noriyuki Nishid. Conformational properties of prion strains can be transmitted to recombinant prion protein fibrils in real-time quaking-induced conversion. Journal of virology. vol 88. issue 20. 2014-11-25. PMID:25078700. |
to investigate whether the properties of various prion strains can be transmitted to amyloid fibrils consisting of rprp (rprp fibrils) using rt-quic, we examined the secondary structure, conformational stability, and infectivity of rprp fibrils seeded with prp(sc) derived from either the chandler or the 22l strain. |
2014-11-25 |
2023-08-13 |
mouse |
| Kazunori Sano, Ryuichiro Atarashi, Daisuke Ishibashi, Takehiro Nakagaki, Katsuya Satoh, Noriyuki Nishid. Conformational properties of prion strains can be transmitted to recombinant prion protein fibrils in real-time quaking-induced conversion. Journal of virology. vol 88. issue 20. 2014-11-25. PMID:25078700. |
of note, specific identifying characteristics of the two rprp fibril types seen in the β-sheets resembled those of the original prp(sc). |
2014-11-25 |
2023-08-13 |
mouse |
| Kazunori Sano, Ryuichiro Atarashi, Daisuke Ishibashi, Takehiro Nakagaki, Katsuya Satoh, Noriyuki Nishid. Conformational properties of prion strains can be transmitted to recombinant prion protein fibrils in real-time quaking-induced conversion. Journal of virology. vol 88. issue 20. 2014-11-25. PMID:25078700. |
furthermore, the conformational stability of 1st-rprp-fib(ch) was significantly higher than that of 1st-rprp-fib(22l), as with chandler and 22l prp(sc). |
2014-11-25 |
2023-08-13 |
mouse |