| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Xuesong Wang, Menghan Cui, Cong Zhao, Lei He, Dengsen Zhu, Baohuai Wang, Weihong D. Regulation of aggregation behavior and neurotoxicity of prion neuropeptides by platinum complexes. Inorganic chemistry. vol 53. issue 10. 2015-05-12. PMID:24787240. |
the conformational conversion of a cellular prion protein (prp(c)) into an abnormal misfolded isoform (prp(sc)) is the key event in prion disease pathology. |
2015-05-12 |
2023-08-13 |
Not clear |
| Xuesong Wang, Menghan Cui, Cong Zhao, Lei He, Dengsen Zhu, Baohuai Wang, Weihong D. Regulation of aggregation behavior and neurotoxicity of prion neuropeptides by platinum complexes. Inorganic chemistry. vol 53. issue 10. 2015-05-12. PMID:24787240. |
prp106-126 resembles prp(sc) in some physicochemical and biological characteristics, such as apoptosis induction in neurons, fibrillar formation, and mediation of the conversion of native cellular prp(c) to prp(sc). |
2015-05-12 |
2023-08-13 |
Not clear |
| Yves Chapron, Laurent Charlet, Nita Saha. Fate of pathological prion (PrP(sc)92-138) in soil and water: prion-clay nanoparticle molecular dynamics. Journal of biomolecular structure & dynamics. vol 32. issue 11. 2015-05-11. PMID:24152238. |
fate of pathological prion (prp(sc)92-138) in soil and water: prion-clay nanoparticle molecular dynamics. |
2015-05-11 |
2023-08-12 |
Not clear |
| Yves Chapron, Laurent Charlet, Nita Saha. Fate of pathological prion (PrP(sc)92-138) in soil and water: prion-clay nanoparticle molecular dynamics. Journal of biomolecular structure & dynamics. vol 32. issue 11. 2015-05-11. PMID:24152238. |
pathogenic prion protein scrapie (prp(sc)) may contaminate soils for decades and remain in water in colloidal suspension, providing infection pathways for animals through the inhalation of ingested dust and soil particles, and drinking water. |
2015-05-11 |
2023-08-12 |
Not clear |
| Yves Chapron, Laurent Charlet, Nita Saha. Fate of pathological prion (PrP(sc)92-138) in soil and water: prion-clay nanoparticle molecular dynamics. Journal of biomolecular structure & dynamics. vol 32. issue 11. 2015-05-11. PMID:24152238. |
we restricted our model to the moiety prp(92-138), which is a portion of the whole prp(sc) molecule responsible for infectivity and modeled it using explicit solvating water molecules in contact with a pyrophyllite cleavage plane. |
2015-05-11 |
2023-08-12 |
Not clear |
| Yves Chapron, Laurent Charlet, Nita Saha. Fate of pathological prion (PrP(sc)92-138) in soil and water: prion-clay nanoparticle molecular dynamics. Journal of biomolecular structure & dynamics. vol 32. issue 11. 2015-05-11. PMID:24152238. |
our results provide insight to the mechanism responsible for the strong association between the prp(sc) peptide and clay nanoparticles and the associations present in contaminated soil and water which may lead to the infection of animals. |
2015-05-11 |
2023-08-12 |
Not clear |
| Swati Haldar, Ajai Tripathi, Juan Qian, Amber Beserra, Srinivas Suda, Matthew McElwee, Jerrold Turner, Ulrich Hopfer, Neena Sing. Prion protein promotes kidney iron uptake via its ferrireductase activity. The Journal of biological chemistry. vol 290. issue 9. 2015-05-11. PMID:25572394. |
brain iron-dyshomeostasis is an important cause of neurotoxicity in prion disorders, a group of neurodegenerative conditions associated with the conversion of prion protein (prp(c)) from its normal conformation to an aggregated, prp-scrapie (prp(sc)) isoform. |
2015-05-11 |
2023-08-13 |
mouse |
| Belinda B Guo, Shayne A Bellingham, Andrew F Hil. The neutral sphingomyelinase pathway regulates packaging of the prion protein into exosomes. The Journal of biological chemistry. vol 290. issue 6. 2015-05-05. PMID:25505180. |
prion diseases are a group of transmissible, fatal neurodegenerative disorders associated with the misfolding of the host-encoded prion protein, prp(c), into a disease-associated form, prp(sc). |
2015-05-05 |
2023-08-13 |
mouse |
| Belinda B Guo, Shayne A Bellingham, Andrew F Hil. The neutral sphingomyelinase pathway regulates packaging of the prion protein into exosomes. The Journal of biological chemistry. vol 290. issue 6. 2015-05-05. PMID:25505180. |
the transmissible prion agent is principally formed of prp(sc) itself and is associated with extracellular vesicles known as exosomes. |
2015-05-05 |
2023-08-13 |
mouse |
| Belinda B Guo, Shayne A Bellingham, Andrew F Hil. The neutral sphingomyelinase pathway regulates packaging of the prion protein into exosomes. The Journal of biological chemistry. vol 290. issue 6. 2015-05-05. PMID:25505180. |
we also demonstrate that prp(c) packaging is dependent on nsmase2, whereas the packaging of disease-associated prp(sc) into exosomes occurs independently of nsmase2. |
2015-05-05 |
2023-08-13 |
mouse |
| Takeshi Yamasaki, Akio Suzuki, Rie Hasebe, Motohiro Horiuch. Comparison of the anti-prion mechanism of four different anti-prion compounds, anti-PrP monoclonal antibody 44B1, pentosan polysulfate, chlorpromazine, and U18666A, in prion-infected mouse neuroblastoma cells. PloS one. vol 9. issue 9. 2015-04-27. PMID:25181483. |
molecules that inhibit the formation of an abnormal isoform of prion protein (prp(sc)) in prion-infected cells are candidate therapeutic agents for prion diseases. |
2015-04-27 |
2023-08-13 |
mouse |
| Takeshi Yamasaki, Akio Suzuki, Rie Hasebe, Motohiro Horiuch. Comparison of the anti-prion mechanism of four different anti-prion compounds, anti-PrP monoclonal antibody 44B1, pentosan polysulfate, chlorpromazine, and U18666A, in prion-infected mouse neuroblastoma cells. PloS one. vol 9. issue 9. 2015-04-27. PMID:25181483. |
understanding how these molecules inhibit prp(sc) formation provides logical basis for proper evaluation of their therapeutic potential. |
2015-04-27 |
2023-08-13 |
mouse |
| Takeshi Yamasaki, Akio Suzuki, Rie Hasebe, Motohiro Horiuch. Comparison of the anti-prion mechanism of four different anti-prion compounds, anti-PrP monoclonal antibody 44B1, pentosan polysulfate, chlorpromazine, and U18666A, in prion-infected mouse neuroblastoma cells. PloS one. vol 9. issue 9. 2015-04-27. PMID:25181483. |
in this study, we extensively analyzed the effects of the anti-prp monoclonal antibody (mab) 44b1, pentosan polysulfate (pps), chlorpromazine (cpz) and u18666a on the intracellular dynamics of a cellular isoform of prion protein (prp(c)) and prp(sc) in prion-infected mouse neuroblastoma cells to re-evaluate the effects of those agents. |
2015-04-27 |
2023-08-13 |
mouse |
| Takeshi Yamasaki, Akio Suzuki, Rie Hasebe, Motohiro Horiuch. Comparison of the anti-prion mechanism of four different anti-prion compounds, anti-PrP monoclonal antibody 44B1, pentosan polysulfate, chlorpromazine, and U18666A, in prion-infected mouse neuroblastoma cells. PloS one. vol 9. issue 9. 2015-04-27. PMID:25181483. |
mab 44b1 and pps rapidly reduced prp(sc) levels without altering intracellular distribution of prp(sc). |
2015-04-27 |
2023-08-13 |
mouse |
| Takeshi Yamasaki, Akio Suzuki, Rie Hasebe, Motohiro Horiuch. Comparison of the anti-prion mechanism of four different anti-prion compounds, anti-PrP monoclonal antibody 44B1, pentosan polysulfate, chlorpromazine, and U18666A, in prion-infected mouse neuroblastoma cells. PloS one. vol 9. issue 9. 2015-04-27. PMID:25181483. |
pps did not change the distribution and levels of prp(c), whereas mab 44b1 appeared to inhibit the trafficking of cell surface prp(c) to organelles in the endocytic-recycling pathway that are thought to be one of the sites for prp(sc) formation. |
2015-04-27 |
2023-08-13 |
mouse |
| Takeshi Yamasaki, Akio Suzuki, Rie Hasebe, Motohiro Horiuch. Comparison of the anti-prion mechanism of four different anti-prion compounds, anti-PrP monoclonal antibody 44B1, pentosan polysulfate, chlorpromazine, and U18666A, in prion-infected mouse neuroblastoma cells. PloS one. vol 9. issue 9. 2015-04-27. PMID:25181483. |
in contrast, cpz and u18666a initiated the redistribution of prp(sc) from organelles in the endocytic-recycling pathway to late endosomes/lysosomes without apparent changes in the distribution of prp(c). |
2015-04-27 |
2023-08-13 |
mouse |
| Takeshi Yamasaki, Akio Suzuki, Rie Hasebe, Motohiro Horiuch. Comparison of the anti-prion mechanism of four different anti-prion compounds, anti-PrP monoclonal antibody 44B1, pentosan polysulfate, chlorpromazine, and U18666A, in prion-infected mouse neuroblastoma cells. PloS one. vol 9. issue 9. 2015-04-27. PMID:25181483. |
the inhibition of lysosomal function by monensin or bafilomycin a1 after the occurrence of prp(sc) redistribution by cpz or u18666a partly antagonized prp(sc) degradation, suggesting that the transfer of prp(sc) to late endosomes/lysosomes, possibly via alteration of the membrane trafficking machinery of cells, leads to prp(sc) degradation. |
2015-04-27 |
2023-08-13 |
mouse |
| Takeshi Yamasaki, Akio Suzuki, Rie Hasebe, Motohiro Horiuch. Comparison of the anti-prion mechanism of four different anti-prion compounds, anti-PrP monoclonal antibody 44B1, pentosan polysulfate, chlorpromazine, and U18666A, in prion-infected mouse neuroblastoma cells. PloS one. vol 9. issue 9. 2015-04-27. PMID:25181483. |
this study revealed that precise analysis of the intracellular dynamics of prp(c) and prp(sc) provides important information for understanding the mechanism of anti-prion agents. |
2015-04-27 |
2023-08-13 |
mouse |
| Bradley R Groveman, Allison Kraus, Lynne D Raymond, Michael A Dolan, Kelsie J Anson, David W Dorward, Byron Caughe. Charge neutralization of the central lysine cluster in prion protein (PrP) promotes PrP(Sc)-like folding of recombinant PrP amyloids. The Journal of biological chemistry. vol 290. issue 2. 2015-04-21. PMID:25416779. |
charge neutralization of the central lysine cluster in prion protein (prp) promotes prp(sc)-like folding of recombinant prp amyloids. |
2015-04-21 |
2023-08-13 |
Not clear |
| Bradley R Groveman, Allison Kraus, Lynne D Raymond, Michael A Dolan, Kelsie J Anson, David W Dorward, Byron Caughe. Charge neutralization of the central lysine cluster in prion protein (PrP) promotes PrP(Sc)-like folding of recombinant PrP amyloids. The Journal of biological chemistry. vol 290. issue 2. 2015-04-21. PMID:25416779. |
the structure of the infectious form of prion protein, prp(sc), remains unclear. |
2015-04-21 |
2023-08-13 |
Not clear |