| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Jiapu Zhang, Yuanli Zhan. Molecular dynamics studies on 3D structures of the hydrophobic region PrP(109-136). Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23563221. |
these neurodegenerative diseases are caused by the conversion from a soluble normal cellular prion protein (prp(c)) into insoluble abnormally folded infectious prions (prp(sc)). |
2013-12-09 |
2023-08-12 |
cattle |
| Zheng Zhou, Gengfu Xia. Conformational conversion of prion protein in prion diseases. Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23580591. |
the conformational conversion of a cellular prion protein (prp(c)) into an abnormal misfolded isoform (prp(sc)) is the key event in prion diseases pathology. |
2013-12-09 |
2023-08-12 |
Not clear |
| Zheng Zhou, Gengfu Xia. Conformational conversion of prion protein in prion diseases. Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23580591. |
under normal conditions, the high-energy barrier separates prp(c) from prp(sc) isoform. |
2013-12-09 |
2023-08-12 |
Not clear |
| Ping Ping Hu, Cheng Zhi Huan. Prion protein: structural features and related toxicity. Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23615535. |
the conformational conversion from cellular form (prp(c)) to disease-causing isoform (prp(sc)) is considered to be the most important and remarkable event in these diseases, while accumulation of prp(sc) is thought to be the main reason for cell death, inflammation and spongiform degeneration observed in infected individuals. |
2013-12-09 |
2023-08-12 |
Not clear |
| Ping Ping Hu, Cheng Zhi Huan. Prion protein: structural features and related toxicity. Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23615535. |
in particular, most data supports the idea that the smaller oligomeric prp(sc) aggregates, rather than the mature amyloid fibers, exhibit the highest toxicity to the host. |
2013-12-09 |
2023-08-12 |
Not clear |
| Katy E Beck, Leigh Thorne, Richard Lockey, Christopher M Vickery, Linda A Terry, Raymond Bujdoso, John Spiropoulo. Strain typing of classical scrapie by transgenic mouse bioassay using protein misfolding cyclic amplification to replace primary passage. PloS one. vol 8. issue 3. 2013-12-03. PMID:23472112. |
here we sought to investigate whether protein misfolding cyclic amplification (pmca), an in-vitro method of prp(sc) replication, could be used to replace serial passage of vrq/vrq classical scrapie isolates undergoing strain typing in ovine transgenic tg338 mice. |
2013-12-03 |
2023-08-12 |
mouse |
| Jens Wagner, Sergey Ryazanov, Andrei Leonov, Johannes Levin, Song Shi, Felix Schmidt, Catharina Prix, Francisco Pan-Montojo, Uwe Bertsch, Gerda Mitteregger-Kretzschmar, Markus Geissen, Martin Eiden, Fabienne Leidel, Thomas Hirschberger, Andreas A Deeg, Julian J Krauth, Wolfgang Zinth, Paul Tavan, Jens Pilger, Markus Zweckstetter, Tobias Frank, Mathias Bähr, Jochen H Weishaupt, Manfred Uhr, Henning Urlaub, Ulrike Teichmann, Matthias Samwer, Kai Bötzel, Martin Groschup, Hans Kretzschmar, Christian Griesinger, Armin Gies. Anle138b: a novel oligomer modulator for disease-modifying therapy of neurodegenerative diseases such as prion and Parkinson's disease. Acta neuropathologica. vol 125. issue 6. 2013-12-03. PMID:23604588. |
in vitro, anle138b blocked the formation of pathological aggregates of prion protein (prp(sc)) and of α-synuclein (α-syn), which is deposited in pd and other synucleinopathies such as dementia with lewy bodies (dlb) and multiple system atrophy (msa). |
2013-12-03 |
2023-08-12 |
mouse |
| Young Pyo Choi, Suzette A Priol. A specific population of abnormal prion protein aggregates is preferentially taken up by cells and disaggregated in a strain-dependent manner. Journal of virology. vol 87. issue 21. 2013-11-27. PMID:23966386. |
prion diseases are characterized by the conversion of the soluble protease-sensitive host-encoded prion protein (prp(c)) into its aggregated, protease-resistant, and infectious isoform (prp(sc)). |
2013-11-27 |
2023-08-12 |
mouse |
| Young Pyo Choi, Suzette A Priol. A specific population of abnormal prion protein aggregates is preferentially taken up by cells and disaggregated in a strain-dependent manner. Journal of virology. vol 87. issue 21. 2013-11-27. PMID:23966386. |
one of the earliest events occurring in cells following exposure to an exogenous source of prions is the cellular uptake of prp(sc). |
2013-11-27 |
2023-08-12 |
mouse |
| Young Pyo Choi, Suzette A Priol. A specific population of abnormal prion protein aggregates is preferentially taken up by cells and disaggregated in a strain-dependent manner. Journal of virology. vol 87. issue 21. 2013-11-27. PMID:23966386. |
it is unclear how the biochemical properties of prp(sc) influence its uptake, although aggregate size is thought to be important. |
2013-11-27 |
2023-08-12 |
mouse |
| Young Pyo Choi, Suzette A Priol. A specific population of abnormal prion protein aggregates is preferentially taken up by cells and disaggregated in a strain-dependent manner. Journal of virology. vol 87. issue 21. 2013-11-27. PMID:23966386. |
here we show that for two different strains of mouse prions, one that infects cells (22l) and one that does not (87v), a fraction of prp(sc) associated with distinct sedimentation properties is preferentially taken up by the cells. |
2013-11-27 |
2023-08-12 |
mouse |
| Young Pyo Choi, Suzette A Priol. A specific population of abnormal prion protein aggregates is preferentially taken up by cells and disaggregated in a strain-dependent manner. Journal of virology. vol 87. issue 21. 2013-11-27. PMID:23966386. |
however, while the fraction of prp(sc) and the kinetics of uptake were similar for both strains, prp(sc) derived from the 87v strain was disaggregated more rapidly than that derived from 22l. |
2013-11-27 |
2023-08-12 |
mouse |
| Young Pyo Choi, Suzette A Priol. A specific population of abnormal prion protein aggregates is preferentially taken up by cells and disaggregated in a strain-dependent manner. Journal of virology. vol 87. issue 21. 2013-11-27. PMID:23966386. |
the increased rate of prp(sc) disaggregation did not correlate with either the conformational or aggregate stability of 87v prp(sc), both of which were greater than those of 22l prp(sc). |
2013-11-27 |
2023-08-12 |
mouse |
| Young Pyo Choi, Suzette A Priol. A specific population of abnormal prion protein aggregates is preferentially taken up by cells and disaggregated in a strain-dependent manner. Journal of virology. vol 87. issue 21. 2013-11-27. PMID:23966386. |
our data suggest that the kinetics of disaggregation of prp(sc) following cellular uptake is independent of prp(sc) stability but may be dependent upon some component of the prp(sc) aggregate other than prp. |
2013-11-27 |
2023-08-12 |
mouse |
| Young Pyo Choi, Suzette A Priol. A specific population of abnormal prion protein aggregates is preferentially taken up by cells and disaggregated in a strain-dependent manner. Journal of virology. vol 87. issue 21. 2013-11-27. PMID:23966386. |
rapid disaggregation of 87v prp(sc) by the cell may contribute, at least in part, to the inability of 87v to infect cells in vitro. |
2013-11-27 |
2023-08-12 |
mouse |
| Suzette A Priola, Anne E Ward, Sherman A McCall, Matthew Trifilo, Young Pyo Choi, Laura Solforosi, R Anthony Williamson, Justin T Cruite, Michael B A Oldston. Lack of prion infectivity in fixed heart tissue from patients with Creutzfeldt-Jakob disease or amyloid heart disease. Journal of virology. vol 87. issue 17. 2013-11-25. PMID:23785217. |
although abnormal disease-associated prion protein (prp(sc)) has not been detected in heart tissue from several amyloid heart disease patients, it has been observed in the heart tissue of a patient with sporadic creutzfeldt-jakob disease (scjd), the most common form of human prion disease. |
2013-11-25 |
2023-08-12 |
mouse |
| Suzette A Priola, Anne E Ward, Sherman A McCall, Matthew Trifilo, Young Pyo Choi, Laura Solforosi, R Anthony Williamson, Justin T Cruite, Michael B A Oldston. Lack of prion infectivity in fixed heart tissue from patients with Creutzfeldt-Jakob disease or amyloid heart disease. Journal of virology. vol 87. issue 17. 2013-11-25. PMID:23785217. |
although the scjd brain samples led to clinical or subclinical prion infection and deposition of prp(sc) in the brain, none of the inoculated heart samples resulted in disease or the accumulation of prp(sc). |
2013-11-25 |
2023-08-12 |
mouse |
| Mathéa Pietri, Caroline Dakowski, Samia Hannaoui, Aurélie Alleaume-Butaux, Julia Hernandez-Rapp, Audrey Ragagnin, Sophie Mouillet-Richard, Stéphane Haik, Yannick Bailly, Jean-Michel Peyrin, Jean-Marie Launay, Odile Kellermann, Benoit Schneide. PDK1 decreases TACE-mediated α-secretase activity and promotes disease progression in prion and Alzheimer's diseases. Nature medicine. vol 19. issue 9. 2013-11-25. PMID:23955714. |
α-secretase-mediated cleavage of amyloid precursor protein (app) precludes formation of neurotoxic amyloid-β (aβ) peptides, and α-cleavage of cellular prion protein (prp(c)) prevents its conversion into misfolded, pathogenic prions (prp(sc)). |
2013-11-25 |
2023-08-12 |
mouse |
| Mathéa Pietri, Caroline Dakowski, Samia Hannaoui, Aurélie Alleaume-Butaux, Julia Hernandez-Rapp, Audrey Ragagnin, Sophie Mouillet-Richard, Stéphane Haik, Yannick Bailly, Jean-Michel Peyrin, Jean-Marie Launay, Odile Kellermann, Benoit Schneide. PDK1 decreases TACE-mediated α-secretase activity and promotes disease progression in prion and Alzheimer's diseases. Nature medicine. vol 19. issue 9. 2013-11-25. PMID:23955714. |
here, we find that tumor necrosis factor-α-converting enzyme (tace)-mediated α-secretase activity is impaired at the surface of neurons infected with prp(sc) or isolated from app-transgenic mice with amyloid pathology. |
2013-11-25 |
2023-08-12 |
mouse |
| Mathéa Pietri, Caroline Dakowski, Samia Hannaoui, Aurélie Alleaume-Butaux, Julia Hernandez-Rapp, Audrey Ragagnin, Sophie Mouillet-Richard, Stéphane Haik, Yannick Bailly, Jean-Michel Peyrin, Jean-Marie Launay, Odile Kellermann, Benoit Schneide. PDK1 decreases TACE-mediated α-secretase activity and promotes disease progression in prion and Alzheimer's diseases. Nature medicine. vol 19. issue 9. 2013-11-25. PMID:23955714. |
this dysregulation of tace increases prp(sc) and aβ accumulation and reduces shedding of tnf-α receptor type 1 (tnfr1). |
2013-11-25 |
2023-08-12 |
mouse |