| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| 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. |
most pure recombinant prion protein (prp) amyloids generated in vitro are not infectious and lack the extent of the protease-resistant core and solvent exclusion of infectious prp(sc), especially within residues ∼90-160. |
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. |
polyanionic cofactors can enhance infectivity and prp(sc)-like characteristics of such fibrils, but the mechanism of this enhancement is unknown. |
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. |
in considering structural models of prp(sc) multimers, we identified an obstacle to tight packing that might be overcome with polyanionic cofactors, namely, electrostatic repulsion between four closely spaced cationic lysines within a central lysine cluster of residues 101-110. |
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. |
for example, in our parallel in-register intermolecular β-sheet model of prp(sc), not only would these lysines be clustered within the 101-110 region of the primary sequence, but they would have intermolecular spacings of only ∼4.8 Å between stacked β-strands. |
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. |
we also show empirically that substitution of these clustered lysine residues with alanines or asparagines results in recombinant prp amyloid fibrils with extended proteinase-k resistant β-sheet cores and infrared spectra that are more reminiscent of bona fide prp(sc). |
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. |
this charge neutralization may be a key aspect of the mechanism by which anionic cofactors promote prp(sc) formation. |
2015-04-21 |
2023-08-13 |
Not clear |
| Kenichi Takahashi, Yasuo Inoshima, Naotaka Ishigur. Role of cell death in the propagation of PrP(Sc) in immune cells. Archives of virology. vol 160. issue 3. 2015-04-21. PMID:25559669. |
role of cell death in the propagation of prp(sc) in immune cells. |
2015-04-21 |
2023-08-13 |
Not clear |
| Kenichi Takahashi, Yasuo Inoshima, Naotaka Ishigur. Role of cell death in the propagation of PrP(Sc) in immune cells. Archives of virology. vol 160. issue 3. 2015-04-21. PMID:25559669. |
a number of studies have suggested that macrophages, dendritic cells, and follicular dendritic cells play an important role in the propagation of prp(sc). |
2015-04-21 |
2023-08-13 |
Not clear |
| Kenichi Takahashi, Yasuo Inoshima, Naotaka Ishigur. Role of cell death in the propagation of PrP(Sc) in immune cells. Archives of virology. vol 160. issue 3. 2015-04-21. PMID:25559669. |
both accumulation and proteolysis of prp(sc) have been demonstrated in peripheral macrophages. |
2015-04-21 |
2023-08-13 |
Not clear |
| Kenichi Takahashi, Yasuo Inoshima, Naotaka Ishigur. Role of cell death in the propagation of PrP(Sc) in immune cells. Archives of virology. vol 160. issue 3. 2015-04-21. PMID:25559669. |
macrophages may act as reservoirs for prp(sc) particles if the cells die during transient prp(sc) propagation. |
2015-04-21 |
2023-08-13 |
Not clear |
| Kenichi Takahashi, Yasuo Inoshima, Naotaka Ishigur. Role of cell death in the propagation of PrP(Sc) in immune cells. Archives of virology. vol 160. issue 3. 2015-04-21. PMID:25559669. |
however, whether cell death plays a role in prp(sc) propagation in macrophages remains unclear. |
2015-04-21 |
2023-08-13 |
Not clear |
| Kenichi Takahashi, Yasuo Inoshima, Naotaka Ishigur. Role of cell death in the propagation of PrP(Sc) in immune cells. Archives of virology. vol 160. issue 3. 2015-04-21. PMID:25559669. |
in this study, we investigated the possibility of propagation and transmission of prp(sc) between dead immune cells and living neural cells. |
2015-04-21 |
2023-08-13 |
Not clear |
| Kenichi Takahashi, Yasuo Inoshima, Naotaka Ishigur. Role of cell death in the propagation of PrP(Sc) in immune cells. Archives of virology. vol 160. issue 3. 2015-04-21. PMID:25559669. |
we found that under specific conditions, transient prp(sc) propagation occurs in dead cells, indicating that interaction between prp(c) and prp(sc) on plasma membrane lipid rafts might be important for prp(sc) propagation. |
2015-04-21 |
2023-08-13 |
Not clear |
| Kenichi Takahashi, Yasuo Inoshima, Naotaka Ishigur. Role of cell death in the propagation of PrP(Sc) in immune cells. Archives of virology. vol 160. issue 3. 2015-04-21. PMID:25559669. |
co-culturing of killed donor prp(sc)-infected macrophages with recipient n2a-3 neuroblastoma cells accelerated prp(sc) transmission. |
2015-04-21 |
2023-08-13 |
Not clear |
| Kenichi Takahashi, Yasuo Inoshima, Naotaka Ishigur. Role of cell death in the propagation of PrP(Sc) in immune cells. Archives of virology. vol 160. issue 3. 2015-04-21. PMID:25559669. |
our results suggest that cell death may play an important role in prp(sc) propagation, whereas transient prp(sc) propagation in macrophages has little effect on prp(sc) transmission. |
2015-04-21 |
2023-08-13 |
Not clear |
| Ilia V Baskako. The many shades of prion strain adaptation. Prion. vol 8. issue 2. 2015-04-15. PMID:24518385. |
gradual transformation of disease phenotypes and prp(sc) properties was observed during serial transmission of synthetic prions, a process that resembled the phenomenon of prion strain adaptation. |
2015-04-15 |
2023-08-12 |
Not clear |
| Allen Herbst, Judd M Aiken, Debbie McKenzi. Replication of prions in differentiated muscle cells. Prion. vol 8. issue 2. 2015-04-15. PMID:24518642. |
(1) we confirmed that observation and demonstrated, for the first time, that while replicative myoblasts do not accumulate prp(sc), differentiated post-mitotic myotube cultures replicate prions robustly. |
2015-04-15 |
2023-08-12 |
Not clear |
| Anja Lukan, Maja Černilec, Tanja Vranac, Mara Popović, Vladka Čurin Šerbe. Regional distribution of anchorless prion protein, PrP226*, in the human brain. Prion. vol 8. issue 2. 2015-04-15. PMID:24584121. |
its distribution correlates with the distribution of prp(sc). |
2015-04-15 |
2023-08-12 |
human |
| Fozia Saleem, Trent C Bjorndahl, Carol L Ladner, Rolando Perez-Pineiro, Burim N Ametaj, David S Wishar. Lipopolysaccharide induced conversion of recombinant prion protein. Prion. vol 8. issue 2. 2015-04-15. PMID:24819168. |
the conformational conversion of the cellular prion protein (prp(c)) to the β-rich infectious isoform prp(sc) is considered a critical and central feature in prion pathology. |
2015-04-15 |
2023-08-13 |
Not clear |
| Fozia Saleem, Trent C Bjorndahl, Carol L Ladner, Rolando Perez-Pineiro, Burim N Ametaj, David S Wishar. Lipopolysaccharide induced conversion of recombinant prion protein. Prion. vol 8. issue 2. 2015-04-15. PMID:24819168. |
although prp(sc) is the critical component of the infectious agent, as proposed in the "protein-only" prion hypothesis, cellular components have been identified as important cofactors in triggering and enhancing the conversion of prp(c) to proteinase k resistant prp(sc). |
2015-04-15 |
2023-08-13 |
Not clear |