| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Kazuyuki Akasaka, Akihiro Maeno, Taichi Murayama, Hideki Tachibana, Yuzo Fujita, Hitoki Yamanaka, Noriyuki Nishida, Ryuichiro Atarash. Pressure-assisted dissociation and degradation of "proteinase K-resistant" fibrils prepared by seeding with scrapie-infected hamster prion protein. Prion. vol 8. issue 4. 2015-10-30. PMID:25482603. |
the crucial step for the fatal neurodegenerative prion diseases involves the conversion of a normal cellular protein, prp(c), into a fibrous pathogenic form, prp(sc), which has an unusual stability against heat and resistance against proteinase k digestion. |
2015-10-30 |
2023-08-13 |
Not clear |
| Kazuyuki Akasaka, Akihiro Maeno, Taichi Murayama, Hideki Tachibana, Yuzo Fujita, Hitoki Yamanaka, Noriyuki Nishida, Ryuichiro Atarash. Pressure-assisted dissociation and degradation of "proteinase K-resistant" fibrils prepared by seeding with scrapie-infected hamster prion protein. Prion. vol 8. issue 4. 2015-10-30. PMID:25482603. |
a successful challenge to reverse the reaction from prp(sc) into prp(c) is considered valuable, as it would give a key to dissolving the complex molecular events into thermodynamic and kinetic analyses and may also provide a means to prevent the formation of prp(sc) from prp(c) eventually in vivo. |
2015-10-30 |
2023-08-13 |
Not clear |
| Kazuyuki Akasaka, Akihiro Maeno, Taichi Murayama, Hideki Tachibana, Yuzo Fujita, Hitoki Yamanaka, Noriyuki Nishida, Ryuichiro Atarash. Pressure-assisted dissociation and degradation of "proteinase K-resistant" fibrils prepared by seeding with scrapie-infected hamster prion protein. Prion. vol 8. issue 4. 2015-10-30. PMID:25482603. |
the result is consistent with the notion that rhaprp(res) fibrils are dissociated into rhaprp monomers under pressure and that the formation of prp(sc) from prp(c) is thermodynamically controlled. |
2015-10-30 |
2023-08-13 |
Not clear |
| Kazuyuki Akasaka, Akihiro Maeno, Taichi Murayama, Hideki Tachibana, Yuzo Fujita, Hitoki Yamanaka, Noriyuki Nishida, Ryuichiro Atarash. Pressure-assisted dissociation and degradation of "proteinase K-resistant" fibrils prepared by seeding with scrapie-infected hamster prion protein. Prion. vol 8. issue 4. 2015-10-30. PMID:25482603. |
moreover, the efficient degradation of prion fibrils under pressure provides a novel means of eliminating infectious prp(sc) from various systems of pathogenic concern. |
2015-10-30 |
2023-08-13 |
Not clear |
| Abigail B Diack, Mark W Head, Sandra McCutcheon, Aileen Boyle, Richard Knight, James W Ironside, Jean C Manson, Robert G Wil. Variant CJD. 18 years of research and surveillance. Prion. vol 8. issue 4. 2015-10-30. PMID:25495404. |
importantly, we recently established that a prnp 129mv patient blood recipient with an asymptomatic infection and limited prp(sc) deposition in the spleen could readily transmit disease into mice, demonstrating the potential for peripheral infection in the absence of clinical disease. |
2015-10-30 |
2023-08-13 |
mouse |
| Julia Hernandez-Rapp, Séverine Martin-Lannerée, Théo Z Hirsch, Elodie Pradines, Aurélie Alleaume-Butaux, Benoît Schneider, Anne Baudry, Jean-Marie Launay, Sophie Mouillet-Richar. A PrP(C)-caveolin-Lyn complex negatively controls neuronal GSK3β and serotonin 1B receptor. Scientific reports. vol 4. 2015-10-22. PMID:24810941. |
while prp(c) is much studied for its involvement under its abnormal prp(sc) isoform in transmissible spongiform encephalopathies, its physiological role remains unclear. |
2015-10-22 |
2023-08-13 |
mouse |
| Takujiro Homma, Daisuke Ishibashi, Takehiro Nakagaki, Katsuya Satoh, Kazunori Sano, Ryuichiro Atarashi, Noriyuki Nishid. Increased expression of p62/SQSTM1 in prion diseases and its association with pathogenic prion protein. Scientific reports. vol 4. 2015-10-21. PMID:24675871. |
prion diseases are neurodegenerative disorders characterized by the aggregation of abnormally folded prion protein (prp(sc)). |
2015-10-21 |
2023-08-12 |
Not clear |
| Takujiro Homma, Daisuke Ishibashi, Takehiro Nakagaki, Katsuya Satoh, Kazunori Sano, Ryuichiro Atarashi, Noriyuki Nishid. Increased expression of p62/SQSTM1 in prion diseases and its association with pathogenic prion protein. Scientific reports. vol 4. 2015-10-21. PMID:24675871. |
in this study, we focused on the mechanism of clearance of prp(sc), which remains unclear. |
2015-10-21 |
2023-08-12 |
Not clear |
| Takujiro Homma, Daisuke Ishibashi, Takehiro Nakagaki, Katsuya Satoh, Kazunori Sano, Ryuichiro Atarashi, Noriyuki Nishid. Increased expression of p62/SQSTM1 in prion diseases and its association with pathogenic prion protein. Scientific reports. vol 4. 2015-10-21. PMID:24675871. |
upon proteasome inhibition, p62 co-localized with prp(sc), forming a large aggregate in the perinuclear region, hereafter referred to as prp(sc)-aggresome. |
2015-10-21 |
2023-08-12 |
Not clear |
| Takujiro Homma, Daisuke Ishibashi, Takehiro Nakagaki, Katsuya Satoh, Kazunori Sano, Ryuichiro Atarashi, Noriyuki Nishid. Increased expression of p62/SQSTM1 in prion diseases and its association with pathogenic prion protein. Scientific reports. vol 4. 2015-10-21. PMID:24675871. |
moreover, transient expression of the phosphomimic form of p62, which has enhanced ubiquitin-binding activity, reduced the amount of prp(sc) in prion-infected cells, indicating that the activation of p62 could accelerate the clearance of prp(sc). |
2015-10-21 |
2023-08-12 |
Not clear |
| Maria Cramm, Matthias Schmitz, André Karch, Saima Zafar, Daniela Varges, Eva Mitrova, Bjoern Schroeder, Alex Raeber, Franziska Kuhn, Inga Zer. Characteristic CSF prion seeding efficiency in humans with prion diseases. Molecular neurobiology. vol 51. issue 1. 2015-10-20. PMID:24809690. |
the development of in vitro amplification systems allows detecting femtomolar amounts of prion protein scrapie (prp(sc)) in human cerebrospinal fluid (csf). |
2015-10-20 |
2023-08-13 |
human |
| Maria Cramm, Matthias Schmitz, André Karch, Saima Zafar, Daniela Varges, Eva Mitrova, Bjoern Schroeder, Alex Raeber, Franziska Kuhn, Inga Zer. Characteristic CSF prion seeding efficiency in humans with prion diseases. Molecular neurobiology. vol 51. issue 1. 2015-10-20. PMID:24809690. |
we performed a csf study to determine the effects of prion disease type, codon 129 genotype, prp(sc) type, and other disease-related factors on the real-time quaking-induced conversion (rt-quic) response. |
2015-10-20 |
2023-08-13 |
human |
| Maria Cramm, Matthias Schmitz, André Karch, Saima Zafar, Daniela Varges, Eva Mitrova, Bjoern Schroeder, Alex Raeber, Franziska Kuhn, Inga Zer. Characteristic CSF prion seeding efficiency in humans with prion diseases. Molecular neurobiology. vol 51. issue 1. 2015-10-20. PMID:24809690. |
interestingly, type of prion disease (sporadic vs. genetic) and the prnp mutation (e200k vs. v210i and ffi), codon 129 genotype, and prp(sc) type affected rt-quic response. |
2015-10-20 |
2023-08-13 |
human |
| Maria Cramm, Matthias Schmitz, André Karch, Saima Zafar, Daniela Varges, Eva Mitrova, Bjoern Schroeder, Alex Raeber, Franziska Kuhn, Inga Zer. Characteristic CSF prion seeding efficiency in humans with prion diseases. Molecular neurobiology. vol 51. issue 1. 2015-10-20. PMID:24809690. |
this study demonstrated that prp(sc) characteristics in the csf of human prion disease patients are associated with disease subtypes and rate of decline as defined by disease duration. |
2015-10-20 |
2023-08-13 |
human |
| Evgenia Salta, Eirini Kanata, Christos A Ouzounis, Sabine Gilch, Hermann Schätzl, Theodoros Sklaviadi. Assessing proteinase K resistance of fish prion proteins in a scrapie-infected mouse neuroblastoma cell line. Viruses. vol 6. issue 11. 2015-10-19. PMID:25402173. |
the key event in prion pathogenesis is the structural conversion of the normal cellular protein, prp(c), into an aberrant and partially proteinase k resistant isoform, prp(sc). |
2015-10-19 |
2023-08-13 |
mouse |
| Jue Yuan, Yi-An Zhan, Romany Abskharon, Xiangzhu Xiao, Manuel Camacho Martinez, Xiaochen Zhou, Geoff Kneale, Jacqueline Mikol, Sylvain Lehmann, Witold K Surewicz, Joaquín Castilla, Jan Steyaert, Shulin Zhang, Qingzhong Kong, Robert B Petersen, Alexandre Wohlkonig, Wen-Quan Zo. Recombinant human prion protein inhibits prion propagation in vitro. Scientific reports. vol 3. 2015-10-15. PMID:24105336. |
prion diseases are associated with the conformational conversion of the cellular prion protein (prp(c)) into the pathological scrapie isoform (prp(sc)) in the brain. |
2015-10-15 |
2023-08-12 |
mouse |
| Jue Yuan, Yi-An Zhan, Romany Abskharon, Xiangzhu Xiao, Manuel Camacho Martinez, Xiaochen Zhou, Geoff Kneale, Jacqueline Mikol, Sylvain Lehmann, Witold K Surewicz, Joaquín Castilla, Jan Steyaert, Shulin Zhang, Qingzhong Kong, Robert B Petersen, Alexandre Wohlkonig, Wen-Quan Zo. Recombinant human prion protein inhibits prion propagation in vitro. Scientific reports. vol 3. 2015-10-15. PMID:24105336. |
both the in vivo and in vitro conversion of prp(c) into prp(sc) is significantly inhibited by differences in amino acid sequence between the two molecules. |
2015-10-15 |
2023-08-12 |
mouse |
| Jue Yuan, Yi-An Zhan, Romany Abskharon, Xiangzhu Xiao, Manuel Camacho Martinez, Xiaochen Zhou, Geoff Kneale, Jacqueline Mikol, Sylvain Lehmann, Witold K Surewicz, Joaquín Castilla, Jan Steyaert, Shulin Zhang, Qingzhong Kong, Robert B Petersen, Alexandre Wohlkonig, Wen-Quan Zo. Recombinant human prion protein inhibits prion propagation in vitro. Scientific reports. vol 3. 2015-10-15. PMID:24105336. |
notably, it binds to prp(sc), but not prp(c), suggesting that the inhibitory effect of recombinant prp results from blocking the interaction of brain prp(c) with prp(sc). |
2015-10-15 |
2023-08-12 |
mouse |
| Jue Yuan, Yi-An Zhan, Romany Abskharon, Xiangzhu Xiao, Manuel Camacho Martinez, Xiaochen Zhou, Geoff Kneale, Jacqueline Mikol, Sylvain Lehmann, Witold K Surewicz, Joaquín Castilla, Jan Steyaert, Shulin Zhang, Qingzhong Kong, Robert B Petersen, Alexandre Wohlkonig, Wen-Quan Zo. Recombinant human prion protein inhibits prion propagation in vitro. Scientific reports. vol 3. 2015-10-15. PMID:24105336. |
our findings suggest a new avenue for treating prion diseases, in which a patient's own unglycosylated and anchorless prp is used to inhibit prp(sc) propagation without inducing immune response side effects. |
2015-10-15 |
2023-08-12 |
mouse |
| O O Nwankiti, E I Ikeh, O A Arowolo, A J Nwankiti, M O Odugbo, T Seuberlic. A Targeted Survey for Scrapie in Jos Plateau State, Nigeria. Journal of veterinary medicine. vol 2013. 2015-10-14. PMID:26464913. |
caudal brainstem tissues of suspect animals collected postmortem were analyzed for the disease specific form of the prion protein, prp(sc), using bio-rad's tesee elisa rapid test kit. |
2015-10-14 |
2023-08-13 |
Not clear |