| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Elizaveta Katorcha, Martin L Daus, Nuria Gonzalez-Montalban, Natallia Makarava, Peter Lasch, Michael Beekes, Ilia V Baskako. Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation. Scientific reports. vol 6. 2018-05-31. PMID:27609323. |
upon intracerebral administration, all animals that received prp(sc) with original or restored sialylation levels were infected, whereas none of the animals that received prp(sc) with reduced sialylation were infected. |
2018-05-31 |
2023-08-13 |
Not clear |
| Elizaveta Katorcha, Martin L Daus, Nuria Gonzalez-Montalban, Natallia Makarava, Peter Lasch, Michael Beekes, Ilia V Baskako. Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation. Scientific reports. vol 6. 2018-05-31. PMID:27609323. |
the current work established that the ability of prions to infect the host via intracerebral administration depends on prp(sc) sialylation status. |
2018-05-31 |
2023-08-13 |
Not clear |
| Elizaveta Katorcha, Martin L Daus, Nuria Gonzalez-Montalban, Natallia Makarava, Peter Lasch, Michael Beekes, Ilia V Baskako. Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation. Scientific reports. vol 6. 2018-05-31. PMID:27609323. |
remarkably, prp(sc) infectivity could be switched off and on in a reversible manner by first removing and then restoring prp(sc) sialylation. |
2018-05-31 |
2023-08-13 |
Not clear |
| Akihiko Urayama, Luis Concha-Marambio, Uffaf Khan, Javiera Bravo-Alegria, Vineetkumar Kharat, Claudio Sot. Prions efficiently cross the intestinal barrier after oral administration: Study of the bioavailability, and cellular and tissue distribution in vivo. Scientific reports. vol 6. 2018-05-30. PMID:27573341. |
the main goal of this study was to evaluate the fate of prions after oral administration, using highly purified radiolabeled prp(sc). |
2018-05-30 |
2023-08-13 |
Not clear |
| Akihiko Urayama, Luis Concha-Marambio, Uffaf Khan, Javiera Bravo-Alegria, Vineetkumar Kharat, Claudio Sot. Prions efficiently cross the intestinal barrier after oral administration: Study of the bioavailability, and cellular and tissue distribution in vivo. Scientific reports. vol 6. 2018-05-30. PMID:27573341. |
the results showed a bi-phasic reduction of prp(sc) with time in the gi, except for the ileum and colon which showed sustained increases peaking at 3-6 hr, respectively. |
2018-05-30 |
2023-08-13 |
Not clear |
| Akihiko Urayama, Luis Concha-Marambio, Uffaf Khan, Javiera Bravo-Alegria, Vineetkumar Kharat, Claudio Sot. Prions efficiently cross the intestinal barrier after oral administration: Study of the bioavailability, and cellular and tissue distribution in vivo. Scientific reports. vol 6. 2018-05-30. PMID:27573341. |
size-exclusion chromatography revealed that oligomeric (125)i-prp(sc) were transported from the intestinal tract, and protein misfolding cyclic amplification showed that prp(sc) in organs and blood retained the typical prion self-replicating ability. |
2018-05-30 |
2023-08-13 |
Not clear |
| Mohammed Moudjou, Jérôme Chapuis, Mériem Mekrouti, Fabienne Reine, Laetitia Herzog, Pierre Sibille, Hubert Laude, Didier Vilette, Olivier Andréoletti, Human Rezaei, Michel Dron, Vincent Béringu. Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification. Scientific reports. vol 6. 2018-05-21. PMID:27384922. |
prions are formed of misfolded assemblies (prp(sc)) of the variably n-glycosylated cellular prion protein (prp(c)). |
2018-05-21 |
2023-08-13 |
Not clear |
| Mohammed Moudjou, Jérôme Chapuis, Mériem Mekrouti, Fabienne Reine, Laetitia Herzog, Pierre Sibille, Hubert Laude, Didier Vilette, Olivier Andréoletti, Human Rezaei, Michel Dron, Vincent Béringu. Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification. Scientific reports. vol 6. 2018-05-21. PMID:27384922. |
distinct prion strains can be recognized, exhibiting defined prp(sc) biochemical properties such as the glycotype and specific biological traits. |
2018-05-21 |
2023-08-13 |
Not clear |
| Mohammed Moudjou, Jérôme Chapuis, Mériem Mekrouti, Fabienne Reine, Laetitia Herzog, Pierre Sibille, Hubert Laude, Didier Vilette, Olivier Andréoletti, Human Rezaei, Michel Dron, Vincent Béringu. Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification. Scientific reports. vol 6. 2018-05-21. PMID:27384922. |
while strain information is encoded within the conformation of prp(sc) assemblies, the storage of the structural information and the molecular requirements for self-perpetuation remain uncertain. |
2018-05-21 |
2023-08-13 |
Not clear |
| Mohammed Moudjou, Jérôme Chapuis, Mériem Mekrouti, Fabienne Reine, Laetitia Herzog, Pierre Sibille, Hubert Laude, Didier Vilette, Olivier Andréoletti, Human Rezaei, Michel Dron, Vincent Béringu. Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification. Scientific reports. vol 6. 2018-05-21. PMID:27384922. |
applying the technique to prp(c) glycosylation mutants expressing cells revealed that neither prp(c) nor prp(sc) glycoform stoichiometry was instrumental to prp(sc) formation and strainness perpetuation. |
2018-05-21 |
2023-08-13 |
Not clear |
| Mohammed Moudjou, Jérôme Chapuis, Mériem Mekrouti, Fabienne Reine, Laetitia Herzog, Pierre Sibille, Hubert Laude, Didier Vilette, Olivier Andréoletti, Human Rezaei, Michel Dron, Vincent Béringu. Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification. Scientific reports. vol 6. 2018-05-21. PMID:27384922. |
our study supports the view that strain properties, including prp(sc) glycotype are enciphered within prp(sc) structural backbone, not in the attached glycans. |
2018-05-21 |
2023-08-13 |
Not clear |
| Berta Puig, Hermann C Altmeppen, Sarah Ulbrich, Luise Linsenmeier, Susanne Krasemann, Karima Chakroun, Claudia Y Acevedo-Morantes, Holger Wille, Jörg Tatzelt, Markus Glatze. Secretory pathway retention of mutant prion protein induces p38-MAPK activation and lethal disease in mice. Scientific reports. vol 6. 2018-01-25. PMID:27117504. |
the prion protein (prp(c)) is a gpi-anchored protein that resides at the plasma membrane and may be misfolded to prp(sc) leading to prion diseases. |
2018-01-25 |
2023-08-13 |
mouse |
| Jing Wang, Bao-Yun Zhang, Jin Zhang, Kang Xiao, Li-Na Chen, Hui Wang, Jing Sun, Qi Shi, Xiao-Ping Don. Treatment of SMB-S15 Cells with Resveratrol Efficiently Removes the PrP(Sc) Accumulation In Vitro and Prion Infectivity In Vivo. Molecular neurobiology. vol 53. issue 8. 2018-01-22. PMID:26440667. |
treatment of smb-s15 cells with resveratrol efficiently removes the prp(sc) accumulation in vitro and prion infectivity in vivo. |
2018-01-22 |
2023-08-13 |
mouse |
| Jing Wang, Bao-Yun Zhang, Jin Zhang, Kang Xiao, Li-Na Chen, Hui Wang, Jing Sun, Qi Shi, Xiao-Ping Don. Treatment of SMB-S15 Cells with Resveratrol Efficiently Removes the PrP(Sc) Accumulation In Vitro and Prion Infectivity In Vivo. Molecular neurobiology. vol 53. issue 8. 2018-01-22. PMID:26440667. |
our previous study has proposed that the natural phytoalexin, resveratrol, can reduce the amounts of prp(sc) in a scrapie-infected cell line smb-s15. |
2018-01-22 |
2023-08-13 |
mouse |
| Jing Wang, Bao-Yun Zhang, Jin Zhang, Kang Xiao, Li-Na Chen, Hui Wang, Jing Sun, Qi Shi, Xiao-Ping Don. Treatment of SMB-S15 Cells with Resveratrol Efficiently Removes the PrP(Sc) Accumulation In Vitro and Prion Infectivity In Vivo. Molecular neurobiology. vol 53. issue 8. 2018-01-22. PMID:26440667. |
exposure of smb-s15 cells to various concentrations of resveratrol (0.25 to 200 μm) reduced and even removed cellular prp(sc) in a dose-dependent manner, with ec50 0.61 μm. |
2018-01-22 |
2023-08-13 |
mouse |
| Jing Wang, Bao-Yun Zhang, Jin Zhang, Kang Xiao, Li-Na Chen, Hui Wang, Jing Sun, Qi Shi, Xiao-Ping Don. Treatment of SMB-S15 Cells with Resveratrol Efficiently Removes the PrP(Sc) Accumulation In Vitro and Prion Infectivity In Vivo. Molecular neurobiology. vol 53. issue 8. 2018-01-22. PMID:26440667. |
meanwhile, prp(sc) signals in smb-s15 cells treated with 5 and 10 μm resveratrol maintained undetectable after drug withdrawal, indicating that the removal of prp(sc) in smb-s15 cells by resveratrol is irreversible. |
2018-01-22 |
2023-08-13 |
mouse |
| Jing Wang, Bao-Yun Zhang, Jin Zhang, Kang Xiao, Li-Na Chen, Hui Wang, Jing Sun, Qi Shi, Xiao-Ping Don. Treatment of SMB-S15 Cells with Resveratrol Efficiently Removes the PrP(Sc) Accumulation In Vitro and Prion Infectivity In Vivo. Molecular neurobiology. vol 53. issue 8. 2018-01-22. PMID:26440667. |
prp-specific western blots and neuropathological tests did not identify prp(sc) or prion disease-associated pathological abnormality in the brains of mice inoculated with 7-day resveratrol-treated smb-s15 cells. |
2018-01-22 |
2023-08-13 |
mouse |
| Jing Wang, Bao-Yun Zhang, Jin Zhang, Kang Xiao, Li-Na Chen, Hui Wang, Jing Sun, Qi Shi, Xiao-Ping Don. Treatment of SMB-S15 Cells with Resveratrol Efficiently Removes the PrP(Sc) Accumulation In Vitro and Prion Infectivity In Vivo. Molecular neurobiology. vol 53. issue 8. 2018-01-22. PMID:26440667. |
sensitivity of prp(sc) to resveratrol highlights its potential role in prion therapeutics. |
2018-01-22 |
2023-08-13 |
mouse |
| Yeong-Gon Choi, Hae-Young Shin, Jae-Il Kim, Eun-Kyoung Choi, Richard I Carp, Yong-Sun Ki. N(ε)-Carboxymethyl Modification of Lysine Residues in Pathogenic Prion Isoforms. Molecular neurobiology. vol 53. issue 5. 2017-12-25. PMID:25983034. |
the most prominent hallmark of prion diseases is prion protein conversion and the subsequent deposition of the altered prions, prp(sc), at the pathological sites of affected individuals, particularly in the brain. |
2017-12-25 |
2023-08-13 |
Not clear |
| Yeong-Gon Choi, Hae-Young Shin, Jae-Il Kim, Eun-Kyoung Choi, Richard I Carp, Yong-Sun Ki. N(ε)-Carboxymethyl Modification of Lysine Residues in Pathogenic Prion Isoforms. Molecular neurobiology. vol 53. issue 5. 2017-12-25. PMID:25983034. |
a previous study has demonstrated that the n-terminus of the pathogenic prion isoform (prp(sc)) is modified with advanced glycation end products (ages), most likely at one or more of the three lys residues (positions 23, 24, and 27) in the n-terminus (23kkrpkp28). |
2017-12-25 |
2023-08-13 |
Not clear |