| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| James M McCarthy, Dietmar Appelhans, Jörg Tatzelt, Mark S Roger. Nanomedicine for prion disease treatment: new insights into the role of dendrimers. Prion. vol 7. issue 3. 2014-01-08. PMID:23764833. |
studies with cell culture models of prion disease and prion infected brain homogenate have demonstrated that numerous species of dendrimers eliminate prp (sc) in a dose and time dependent fashion and specific glycodendrimers are capable of crossing the cns. |
2014-01-08 |
2023-08-12 |
Not clear |
| James M McCarthy, Dietmar Appelhans, Jörg Tatzelt, Mark S Roger. Nanomedicine for prion disease treatment: new insights into the role of dendrimers. Prion. vol 7. issue 3. 2014-01-08. PMID:23764833. |
in a number of recent studies we have tackled these questions and revealed for the first time that a specific dendrimer can inhibit the intracellular conversion of prp (c) to prp (sc) and that a high density of surface reactive groups is a necessity for dendrimers in vitro anti-prion activity. |
2014-01-08 |
2023-08-12 |
Not clear |
| Theodore R John, Hermann M Schätzl, Sabine Gilc. Early detection of chronic wasting disease prions in urine of pre-symptomatic deer by real-time quaking-induced conversion assay. Prion. vol 7. issue 3. 2014-01-08. PMID:23764839. |
to date, cwd ante-mortem diagnosis is only possible by immunohistochemical detection of protease resistant prion protein (prp (sc) ) in tonsil or recto-anal mucosa-associated lymphoid tissue (ramalt) biopsies, which requires anesthesia of animals. |
2014-01-08 |
2023-08-12 |
Not clear |
| Muhammad Khalid Salamat, Carola Munoz-Montesino, Mohammed Moudjou, Human Rezaei, Hubert Laude, Vincent Béringue, Michel Dro. Mammalian prions: tolerance to sequence changes-how far? Prion. vol 7. issue 2. 2013-12-30. PMID:23232499. |
upon prion infection, abnormal prion protein (prp (sc) ) self-perpetuate by conformational conversion of α-helix-rich prp (c) into β sheet enriched form, leading to formation and deposition of prp (sc) aggregates in affected brains. |
2013-12-30 |
2023-08-12 |
Not clear |
| Muhammad Khalid Salamat, Carola Munoz-Montesino, Mohammed Moudjou, Human Rezaei, Hubert Laude, Vincent Béringue, Michel Dro. Mammalian prions: tolerance to sequence changes-how far? Prion. vol 7. issue 2. 2013-12-30. PMID:23232499. |
we discuss the implications of our findings according to different structural models proposed for prp (sc) and questioned the postulated existence of an n- or c-terminal prion domain in the protease-resistant region. |
2013-12-30 |
2023-08-12 |
Not clear |
| Laura Solforosi, Michela Milani, Nicasio Mancini, Massimo Clementi, Roberto Burion. A closer look at prion strains: characterization and important implications. Prion. vol 7. issue 2. 2013-12-30. PMID:23357828. |
prions are infectious proteins that are responsible for transmissible spongiform encephalopathies (tses) and consist primarily of scrapie prion protein (prp (sc) ), a pathogenic isoform of the host-encoded cellular prion protein (prp (c) ). |
2013-12-30 |
2023-08-12 |
Not clear |
| Laura Solforosi, Michela Milani, Nicasio Mancini, Massimo Clementi, Roberto Burion. A closer look at prion strains: characterization and important implications. Prion. vol 7. issue 2. 2013-12-30. PMID:23357828. |
mounting evidence suggests that prion-strain-specific features segregate with different prp (sc) conformational and aggregation states. |
2013-12-30 |
2023-08-12 |
Not clear |
| Laura Solforosi, Michela Milani, Nicasio Mancini, Massimo Clementi, Roberto Burion. A closer look at prion strains: characterization and important implications. Prion. vol 7. issue 2. 2013-12-30. PMID:23357828. |
strains are of practical relevance in prion diseases as they can drastically differ in many aspects, such as incubation period, prp (sc) biochemical profile (e.g., electrophoretic mobility and glycoform ratio) and distribution of brain lesions. |
2013-12-30 |
2023-08-12 |
Not clear |
| Keiji Uchiyama, Naomi Muramatsu, Masashi Yano, Takeshi Usui, Hironori Miyata, Suehiro Sakaguch. Prions disturb post-Golgi trafficking of membrane proteins. Nature communications. vol 4. 2013-12-30. PMID:23673631. |
conformational conversion of normal cellular prion protein prp(c) into pathogenic prp(sc) is central to the pathogenesis of prion diseases. |
2013-12-30 |
2023-08-12 |
mouse |
| Keiji Uchiyama, Naomi Muramatsu, Masashi Yano, Takeshi Usui, Hironori Miyata, Suehiro Sakaguch. Prions disturb post-Golgi trafficking of membrane proteins. Nature communications. vol 4. 2013-12-30. PMID:23673631. |
prp(sc) is detected throughout endosomal compartments, being particularly abundant in recycling endosome. |
2013-12-30 |
2023-08-12 |
mouse |
| Keiji Uchiyama, Naomi Muramatsu, Masashi Yano, Takeshi Usui, Hironori Miyata, Suehiro Sakaguch. Prions disturb post-Golgi trafficking of membrane proteins. Nature communications. vol 4. 2013-12-30. PMID:23673631. |
these results suggest that prion infection might impair post-golgi trafficking of membrane proteins to the cell surface in neurons via prp(sc) accumulated in recycling endosome, and eventually induce neuronal dysfunctions associated with prion diseases. |
2013-12-30 |
2023-08-12 |
mouse |
| Daniela Saverioni, Silvio Notari, Sabina Capellari, Ilaria Poggiolini, Armin Giese, Hans A Kretzschmar, Piero Parch. Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prions. The Journal of biological chemistry. vol 288. issue 39. 2013-12-24. PMID:23897825. |
prion diseases are characterized by tissue accumulation of a misfolded, β-sheet-enriched isoform (scrapie prion protein (prp(sc))) of the cellular prion protein (prp(c)). |
2013-12-24 |
2023-08-12 |
human |
| Daniela Saverioni, Silvio Notari, Sabina Capellari, Ilaria Poggiolini, Armin Giese, Hans A Kretzschmar, Piero Parch. Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prions. The Journal of biological chemistry. vol 288. issue 39. 2013-12-24. PMID:23897825. |
at variance with prp(c), prp(sc) shows a partial resistance to protease digestion and forms highly aggregated and detergent-insoluble polymers, two properties that have been consistently used to distinguish the two proteins. |
2013-12-24 |
2023-08-12 |
human |
| Daniela Saverioni, Silvio Notari, Sabina Capellari, Ilaria Poggiolini, Armin Giese, Hans A Kretzschmar, Piero Parch. Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prions. The Journal of biological chemistry. vol 288. issue 39. 2013-12-24. PMID:23897825. |
in recent years, however, the idea that prp(sc) itself comprises heterogeneous species has grown. |
2013-12-24 |
2023-08-12 |
human |
| Daniela Saverioni, Silvio Notari, Sabina Capellari, Ilaria Poggiolini, Armin Giese, Hans A Kretzschmar, Piero Parch. Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prions. The Journal of biological chemistry. vol 288. issue 39. 2013-12-24. PMID:23897825. |
most importantly, a putative proteinase k (pk)-sensitive form of prp(sc) (sprp(sc)) is being increasingly investigated for its possible role in prion infectivity, neurotoxicity, and strain variability. |
2013-12-24 |
2023-08-12 |
human |
| Daniela Saverioni, Silvio Notari, Sabina Capellari, Ilaria Poggiolini, Armin Giese, Hans A Kretzschmar, Piero Parch. Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prions. The Journal of biological chemistry. vol 288. issue 39. 2013-12-24. PMID:23897825. |
the study of sprp(sc), however, remains technically challenging because of the need of separating it from prp(c) without using proteases. |
2013-12-24 |
2023-08-12 |
human |
| Daniela Saverioni, Silvio Notari, Sabina Capellari, Ilaria Poggiolini, Armin Giese, Hans A Kretzschmar, Piero Parch. Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prions. The Journal of biological chemistry. vol 288. issue 39. 2013-12-24. PMID:23897825. |
in this study, we have systematically analyzed both pk resistance and the aggregation state of purified prp(sc) across the whole spectrum of the currently characterized human prion strains. |
2013-12-24 |
2023-08-12 |
human |
| Daniela Saverioni, Silvio Notari, Sabina Capellari, Ilaria Poggiolini, Armin Giese, Hans A Kretzschmar, Piero Parch. Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prions. The Journal of biological chemistry. vol 288. issue 39. 2013-12-24. PMID:23897825. |
the results show that prp(sc) isolates manifest significant strain-specific differences in their pk digestion profile that are only partially explained by differences in the size of aggregates, suggesting that other factors, likely acting on prp(sc) aggregate stability, determine its resistance to proteolysis. |
2013-12-24 |
2023-08-12 |
human |
| Daniela Saverioni, Silvio Notari, Sabina Capellari, Ilaria Poggiolini, Armin Giese, Hans A Kretzschmar, Piero Parch. Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prions. The Journal of biological chemistry. vol 288. issue 39. 2013-12-24. PMID:23897825. |
fully protease-sensitive low molecular weight aggregates were detected in all isolates but in a limited proportion of the overall prp(sc) (i.e. |
2013-12-24 |
2023-08-12 |
human |
| Daniela Saverioni, Silvio Notari, Sabina Capellari, Ilaria Poggiolini, Armin Giese, Hans A Kretzschmar, Piero Parch. Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prions. The Journal of biological chemistry. vol 288. issue 39. 2013-12-24. PMID:23897825. |
<10%), arguing against a significant role of slowly sedimenting pk-sensitive prp(sc) in the biogenesis of prion strains. |
2013-12-24 |
2023-08-12 |
human |