| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Clive Bate, Alun William. Clustering of sialylated glycosylphosphatidylinositol anchors mediates PrP-induced activation of cytoplasmic phospholipase A 2 and synapse damage. Prion. vol 6. issue 4. 2013-02-27. PMID:22895089. |
precisely how the accumulation of prp (sc) causes the neuronal degeneration that leads to the clinical symptoms of prion diseases is poorly understood. |
2013-02-27 |
2023-08-12 |
Not clear |
| Clive Bate, Alun William. Clustering of sialylated glycosylphosphatidylinositol anchors mediates PrP-induced activation of cytoplasmic phospholipase A 2 and synapse damage. Prion. vol 6. issue 4. 2013-02-27. PMID:22895089. |
first, we demonstrated that small, soluble prp (sc) oligomers caused synapse damage via a gpi-dependent process. |
2013-02-27 |
2023-08-12 |
Not clear |
| Neil A Mabbot. Prion pathogenesis and secondary lymphoid organs (SLO): tracking the SLO spread of prions to the brain. Prion. vol 6. issue 4. 2013-02-27. PMID:22895090. |
these diseases are characterized by the accumulation of prp (sc), an abnormally folded isoform of the cellular prion protein (prp (c)), in affected tissues. |
2013-02-27 |
2023-08-12 |
Not clear |
| Ulrike K Resenberger, Veronika Müller, Lisa M Munter, Michael Baier, Gerd Multhaup, Mark R Wilson, Konstanze F Winklhofer, Jörg Tatzel. The heat shock response is modulated by and interferes with toxic effects of scrapie prion protein and amyloid β. The Journal of biological chemistry. vol 287. issue 52. 2013-02-26. PMID:23115236. |
we have studied the modulation of the hsr by the scrapie prion protein (prp(sc)) and amyloid β peptide (aβ) and investigated whether an activated hsr or the ectopic expression of individual chaperones can interfere with prp(sc)- or aβ-induced toxicity. |
2013-02-26 |
2023-08-12 |
Not clear |
| Ulrike K Resenberger, Veronika Müller, Lisa M Munter, Michael Baier, Gerd Multhaup, Mark R Wilson, Konstanze F Winklhofer, Jörg Tatzel. The heat shock response is modulated by and interferes with toxic effects of scrapie prion protein and amyloid β. The Journal of biological chemistry. vol 287. issue 52. 2013-02-26. PMID:23115236. |
first, we observed different effects on the hsr under acute or chronic exposure of cells to prp(sc) or aβ. |
2013-02-26 |
2023-08-12 |
Not clear |
| Ulrike K Resenberger, Veronika Müller, Lisa M Munter, Michael Baier, Gerd Multhaup, Mark R Wilson, Konstanze F Winklhofer, Jörg Tatzel. The heat shock response is modulated by and interferes with toxic effects of scrapie prion protein and amyloid β. The Journal of biological chemistry. vol 287. issue 52. 2013-02-26. PMID:23115236. |
next, we employed models of prp(sc)- and aβ-induced toxicity to demonstrate that the induction of the hsr ameliorates the toxic effects of both prp(sc) and aβ. |
2013-02-26 |
2023-08-12 |
Not clear |
| Ulrike K Resenberger, Veronika Müller, Lisa M Munter, Michael Baier, Gerd Multhaup, Mark R Wilson, Konstanze F Winklhofer, Jörg Tatzel. The heat shock response is modulated by and interferes with toxic effects of scrapie prion protein and amyloid β. The Journal of biological chemistry. vol 287. issue 52. 2013-02-26. PMID:23115236. |
similarly, the ectopic expression of cytosolic hsp72 or the extracellular chaperone clusterin protected against prp(sc)- or aβ-induced toxicity. |
2013-02-26 |
2023-08-12 |
Not clear |
| Cleiton F Machado, Flavio H Beraldo, Tiago G Santos, Dominique Bourgeon, Michele C Landemberger, Martin Roffé, Vilma R Martin. Disease-associated mutations in the prion protein impair laminin-induced process outgrowth and survival. The Journal of biological chemistry. vol 287. issue 52. 2013-02-26. PMID:23132868. |
prp(c) is converted into an abnormal insoluble form, prp(sc), that gains neurotoxic activity. |
2013-02-26 |
2023-08-12 |
mouse |
| Cleiton F Machado, Flavio H Beraldo, Tiago G Santos, Dominique Bourgeon, Michele C Landemberger, Martin Roffé, Vilma R Martin. Disease-associated mutations in the prion protein impair laminin-induced process outgrowth and survival. The Journal of biological chemistry. vol 287. issue 52. 2013-02-26. PMID:23132868. |
conversely, clinical manifestations of prion disease may occur either before or in the absence of prp(sc) deposits, but the loss of normal prp(c) function contribution for the etiology of these diseases is still debatable. |
2013-02-26 |
2023-08-12 |
mouse |
| Yufuko Tanaka, Tetsuji Sadaike, Yasuo Inoshima, Naotaka Ishigur. Characterization of PrP(Sc) transmission from immune cells to neuronal cells. Cellular immunology. vol 279. issue 2. 2013-02-19. PMID:23246505. |
characterization of prp(sc) transmission from immune cells to neuronal cells. |
2013-02-19 |
2023-08-12 |
Not clear |
| Yufuko Tanaka, Tetsuji Sadaike, Yasuo Inoshima, Naotaka Ishigur. Characterization of PrP(Sc) transmission from immune cells to neuronal cells. Cellular immunology. vol 279. issue 2. 2013-02-19. PMID:23246505. |
we investigated prp(sc) transmission in neuronal cells, spleen cells and several immune cells using an in vitro cell-to-cell transmission system. |
2013-02-19 |
2023-08-12 |
Not clear |
| Yufuko Tanaka, Tetsuji Sadaike, Yasuo Inoshima, Naotaka Ishigur. Characterization of PrP(Sc) transmission from immune cells to neuronal cells. Cellular immunology. vol 279. issue 2. 2013-02-19. PMID:23246505. |
the transmission of prp(sc) in the supernatant of prp(sc)-infected neuronal cells was also investigated. |
2013-02-19 |
2023-08-12 |
Not clear |
| Yufuko Tanaka, Tetsuji Sadaike, Yasuo Inoshima, Naotaka Ishigur. Characterization of PrP(Sc) transmission from immune cells to neuronal cells. Cellular immunology. vol 279. issue 2. 2013-02-19. PMID:23246505. |
we found that prp(sc) transmission was more efficient in the cell-to-cell transmission system than in the supernatant-mediated system. |
2013-02-19 |
2023-08-12 |
Not clear |
| Yufuko Tanaka, Tetsuji Sadaike, Yasuo Inoshima, Naotaka Ishigur. Characterization of PrP(Sc) transmission from immune cells to neuronal cells. Cellular immunology. vol 279. issue 2. 2013-02-19. PMID:23246505. |
prp(sc) was more efficiently transmitted from adherent spleen cells to neuronal cells than from floating spleen cells. |
2013-02-19 |
2023-08-12 |
Not clear |
| Yufuko Tanaka, Tetsuji Sadaike, Yasuo Inoshima, Naotaka Ishigur. Characterization of PrP(Sc) transmission from immune cells to neuronal cells. Cellular immunology. vol 279. issue 2. 2013-02-19. PMID:23246505. |
the adherent spleen cells were composed of macrophages (80%), dendritic cells (8%) and follicular dendritic cells (3%), indicating that macrophages play an important role in prp(sc) transmission from immune cells to neuronal cells. |
2013-02-19 |
2023-08-12 |
Not clear |
| Yufuko Tanaka, Tetsuji Sadaike, Yasuo Inoshima, Naotaka Ishigur. Characterization of PrP(Sc) transmission from immune cells to neuronal cells. Cellular immunology. vol 279. issue 2. 2013-02-19. PMID:23246505. |
although prp(sc) in the immune cells used as donor cells was gradually degraded, the prp(sc) transmitted to neuronal cells was observed by western blot analysis. |
2013-02-19 |
2023-08-12 |
Not clear |
| Yufuko Tanaka, Tetsuji Sadaike, Yasuo Inoshima, Naotaka Ishigur. Characterization of PrP(Sc) transmission from immune cells to neuronal cells. Cellular immunology. vol 279. issue 2. 2013-02-19. PMID:23246505. |
investigation of the mechanism of prp(sc) transmission between cells represents an important step towards understanding the pathogenesis of prion diseases. |
2013-02-19 |
2023-08-12 |
Not clear |
| Samuel E Saunders, Jason C Bartz, Ronald A Shikiy. Protein misfolding cyclic amplification of prions. Journal of visualized experiments : JoVE. issue 69. 2013-02-15. PMID:23168797. |
the prion protein has two distinct isoforms, the non-infectious host-encoded protein (prp(c)) and the infectious protein (prp(sc)), an abnormally-folded isoform of prp(c 8). |
2013-02-15 |
2023-08-12 |
Not clear |
| Samuel E Saunders, Jason C Bartz, Ronald A Shikiy. Protein misfolding cyclic amplification of prions. Journal of visualized experiments : JoVE. issue 69. 2013-02-15. PMID:23168797. |
furthermore, the biochemical and biophysical properties of prp(sc) are poorly characterized due to their unusual conformation and aggregation states. |
2013-02-15 |
2023-08-12 |
Not clear |
| Samuel E Saunders, Jason C Bartz, Ronald A Shikiy. Protein misfolding cyclic amplification of prions. Journal of visualized experiments : JoVE. issue 69. 2013-02-15. PMID:23168797. |
prp(sc) can seed the conversion of prp(c) to prp(sc) in vitro(14). |
2013-02-15 |
2023-08-12 |
Not clear |