| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Baian Chen, Claudio Soto, Rodrigo Morale. Peripherally administrated prions reach the brain at sub-infectious quantities in experimental hamsters. FEBS letters. vol 588. issue 5. 2014-04-14. PMID:24492001. |
for this purpose we utilized the pmca technology which permits to detect as little as few prp(sc) molecules. |
2014-04-14 |
2023-08-12 |
Not clear |
| Baian Chen, Claudio Soto, Rodrigo Morale. Peripherally administrated prions reach the brain at sub-infectious quantities in experimental hamsters. FEBS letters. vol 588. issue 5. 2014-04-14. PMID:24492001. |
prp(sc) remains in the brain several days after administration suggesting inefficient clearance or early replication. |
2014-04-14 |
2023-08-12 |
Not clear |
| Luis Concha-Marambio, Rodrigo Diaz-Espinoza, Claudio Sot. The extent of protease resistance of misfolded prion protein is highly dependent on the salt concentration. The Journal of biological chemistry. vol 289. issue 5. 2014-04-10. PMID:24338008. |
an aberrantly folded protein (prp(sc)) is the main component of these proteinaceous infectious particles. |
2014-04-10 |
2023-08-12 |
Not clear |
| Luis Concha-Marambio, Rodrigo Diaz-Espinoza, Claudio Sot. The extent of protease resistance of misfolded prion protein is highly dependent on the salt concentration. The Journal of biological chemistry. vol 289. issue 5. 2014-04-10. PMID:24338008. |
this classical feature has been partially challenged by the isolation of sizeable amounts of protease-sensitive prp(sc) isoforms that self-propagate in vivo. |
2014-04-10 |
2023-08-12 |
Not clear |
| Luis Concha-Marambio, Rodrigo Diaz-Espinoza, Claudio Sot. The extent of protease resistance of misfolded prion protein is highly dependent on the salt concentration. The Journal of biological chemistry. vol 289. issue 5. 2014-04-10. PMID:24338008. |
here, we report that the degree of prp(sc) protease resistance is highly dependent on the concentration of salt in the solution. |
2014-04-10 |
2023-08-12 |
Not clear |
| Luis Concha-Marambio, Rodrigo Diaz-Espinoza, Claudio Sot. The extent of protease resistance of misfolded prion protein is highly dependent on the salt concentration. The Journal of biological chemistry. vol 289. issue 5. 2014-04-10. PMID:24338008. |
similar changes were observed in prp(sc) obtained from different strains and species. |
2014-04-10 |
2023-08-12 |
Not clear |
| Luis Concha-Marambio, Rodrigo Diaz-Espinoza, Claudio Sot. The extent of protease resistance of misfolded prion protein is highly dependent on the salt concentration. The Journal of biological chemistry. vol 289. issue 5. 2014-04-10. PMID:24338008. |
strikingly, the effect of salt is reversible and is associated with changes on the size of prp(sc) particles, but surprisingly, the more protease-sensitive species consists of a larger size. |
2014-04-10 |
2023-08-12 |
Not clear |
| Nathan J Cobb, Marcin I Apostol, Shugui Chen, Vytautas Smirnovas, Witold K Surewic. Conformational stability of mammalian prion protein amyloid fibrils is dictated by a packing polymorphism within the core region. The Journal of biological chemistry. vol 289. issue 5. 2014-04-10. PMID:24338015. |
mammalian prion strains are believed to arise from the propagation of distinct conformations of the misfolded prion protein prp(sc). |
2014-04-10 |
2023-08-12 |
human |
| Nathan J Cobb, Marcin I Apostol, Shugui Chen, Vytautas Smirnovas, Witold K Surewic. Conformational stability of mammalian prion protein amyloid fibrils is dictated by a packing polymorphism within the core region. The Journal of biological chemistry. vol 289. issue 5. 2014-04-10. PMID:24338015. |
one key operational parameter used to define differences between strains has been conformational stability of prp(sc) as defined by resistance to thermal and/or chemical denaturation. |
2014-04-10 |
2023-08-12 |
human |
| Nathan J Cobb, Marcin I Apostol, Shugui Chen, Vytautas Smirnovas, Witold K Surewic. Conformational stability of mammalian prion protein amyloid fibrils is dictated by a packing polymorphism within the core region. The Journal of biological chemistry. vol 289. issue 5. 2014-04-10. PMID:24338015. |
although this study was limited to synthetic prion protein amyloid fibrils, a similar structural basis for strain-dependent conformational stability may apply to brain-derived prp(sc), especially because large strain-specific differences in prp(sc) stability are often observed despite a similar size of the prp(sc) core region. |
2014-04-10 |
2023-08-12 |
human |
| Huanhuan L Cui, Belinda Guo, Benjamin Scicluna, Bradley M Coleman, Victoria A Lawson, Laura Ellett, Peter J Meikle, Michael Bukrinsky, Nigora Mukhamedova, Dmitri Sviridov, Andrew F Hil. Prion infection impairs cholesterol metabolism in neuronal cells. The Journal of biological chemistry. vol 289. issue 2. 2014-04-08. PMID:24280226. |
conversion of prion protein (prp(c)) into a pathological isoform (prp(sc)) during prion infection occurs in lipid rafts and is dependent on cholesterol. |
2014-04-08 |
2023-08-12 |
mouse |
| Huanhuan L Cui, Belinda Guo, Benjamin Scicluna, Bradley M Coleman, Victoria A Lawson, Laura Ellett, Peter J Meikle, Michael Bukrinsky, Nigora Mukhamedova, Dmitri Sviridov, Andrew F Hil. Prion infection impairs cholesterol metabolism in neuronal cells. The Journal of biological chemistry. vol 289. issue 2. 2014-04-08. PMID:24280226. |
mechanistically, conversion of prp(c) to the pathological isoform led to prp(sc) accumulation in rafts, displacement of abca1 from rafts and the cell surface, and enhanced internalization of abca1. |
2014-04-08 |
2023-08-12 |
mouse |
| Bradley M Coleman, Christopher F Harrison, Belinda Guo, Colin L Masters, Kevin J Barnham, Victoria A Lawson, Andrew F Hil. Pathogenic mutations within the hydrophobic domain of the prion protein lead to the formation of protease-sensitive prion species with increased lethality. Journal of virology. vol 88. issue 5. 2014-04-08. PMID:24352465. |
the principal mechanism of these diseases involves the misfolding the host-encoded cellular prion protein, prp(c), into the disease-associated isoform, prp(sc). |
2014-04-08 |
2023-08-12 |
mouse |
| Bradley M Coleman, Christopher F Harrison, Belinda Guo, Colin L Masters, Kevin J Barnham, Victoria A Lawson, Andrew F Hil. Pathogenic mutations within the hydrophobic domain of the prion protein lead to the formation of protease-sensitive prion species with increased lethality. Journal of virology. vol 88. issue 5. 2014-04-08. PMID:24352465. |
however, upon exposure of susceptible cell lines expressing these mutants to infectious prions, very low levels of protease-resistant aggregated prp(sc) are formed. |
2014-04-08 |
2023-08-12 |
mouse |
| Bradley M Coleman, Christopher F Harrison, Belinda Guo, Colin L Masters, Kevin J Barnham, Victoria A Lawson, Andrew F Hil. Pathogenic mutations within the hydrophobic domain of the prion protein lead to the formation of protease-sensitive prion species with increased lethality. Journal of virology. vol 88. issue 5. 2014-04-08. PMID:24352465. |
thus, these mutations appear to limit the formation of aggregated prp(sc), giving rise to the accumulation of a relatively soluble, protease sensitive, prion species that is highly neurotoxic. |
2014-04-08 |
2023-08-12 |
mouse |
| Alexander Rouvinski, Sharon Karniely, Maria Kounin, Sanaa Moussa, Miri D Goldberg, Gabriela Warburg, Roman Lyakhovetsky, Dulce Papy-Garcia, Janine Kutzsche, Carsten Korth, George A Carlson, Susan F Godsave, Peter J Peters, Katarina Luhr, Krister Kristensson, Albert Taraboulo. Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs. The Journal of cell biology. vol 204. issue 3. 2014-04-08. PMID:24493590. |
mammalian prions refold host glycosylphosphatidylinositol-anchored prp(c) into β-sheet-rich prp(sc). |
2014-04-08 |
2023-08-12 |
Not clear |
| Alexander Rouvinski, Sharon Karniely, Maria Kounin, Sanaa Moussa, Miri D Goldberg, Gabriela Warburg, Roman Lyakhovetsky, Dulce Papy-Garcia, Janine Kutzsche, Carsten Korth, George A Carlson, Susan F Godsave, Peter J Peters, Katarina Luhr, Krister Kristensson, Albert Taraboulo. Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs. The Journal of cell biology. vol 204. issue 3. 2014-04-08. PMID:24493590. |
prp(sc) is rapidly truncated into a c-terminal prp27-30 core that is stable for days in endolysosomes. |
2014-04-08 |
2023-08-12 |
Not clear |
| Alexander Rouvinski, Sharon Karniely, Maria Kounin, Sanaa Moussa, Miri D Goldberg, Gabriela Warburg, Roman Lyakhovetsky, Dulce Papy-Garcia, Janine Kutzsche, Carsten Korth, George A Carlson, Susan F Godsave, Peter J Peters, Katarina Luhr, Krister Kristensson, Albert Taraboulo. Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs. The Journal of cell biology. vol 204. issue 3. 2014-04-08. PMID:24493590. |
we overcame this hurdle by focusing on nascent full-length prp(sc) rather than on its truncated prp27-30 product. |
2014-04-08 |
2023-08-12 |
Not clear |
| Alexander Rouvinski, Sharon Karniely, Maria Kounin, Sanaa Moussa, Miri D Goldberg, Gabriela Warburg, Roman Lyakhovetsky, Dulce Papy-Garcia, Janine Kutzsche, Carsten Korth, George A Carlson, Susan F Godsave, Peter J Peters, Katarina Luhr, Krister Kristensson, Albert Taraboulo. Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs. The Journal of cell biology. vol 204. issue 3. 2014-04-08. PMID:24493590. |
we show that n-terminal prp(sc) epitopes are exposed in their physiological context and visualize, for the first time, prp(sc) in living cells. |
2014-04-08 |
2023-08-12 |
Not clear |
| Alexander Rouvinski, Sharon Karniely, Maria Kounin, Sanaa Moussa, Miri D Goldberg, Gabriela Warburg, Roman Lyakhovetsky, Dulce Papy-Garcia, Janine Kutzsche, Carsten Korth, George A Carlson, Susan F Godsave, Peter J Peters, Katarina Luhr, Krister Kristensson, Albert Taraboulo. Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs. The Journal of cell biology. vol 204. issue 3. 2014-04-08. PMID:24493590. |
prp(sc) resides for hours in unexpected cell-surface, slow moving strings and webs, sheltered from endocytosis. |
2014-04-08 |
2023-08-12 |
Not clear |