| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Yuzuru Taguchi, Hermann M Schätz. Identifying critical sites of PrP(c)-PrP(Sc) interaction in prion-infected cells by dominant-negative inhibition. Prion. vol 7. issue 6. 2015-03-30. PMID:24401595. |
this showed that mutant prps with deletions in the region between first and second α-helix are involved in prp-prp interaction and conversion of prp(c) into prp(sc). |
2015-03-30 |
2023-08-12 |
Not clear |
| Yuzuru Taguchi, Hermann M Schätz. Identifying critical sites of PrP(c)-PrP(Sc) interaction in prion-infected cells by dominant-negative inhibition. Prion. vol 7. issue 6. 2015-03-30. PMID:24401595. |
although some prps did not reach the plasma membrane, they had access to the locales of prion conversion and prp(sc) recycling using autophagy pathways. |
2015-03-30 |
2023-08-12 |
Not clear |
| Claudia Avis Madampage, Kristen Marciniuk, Pekka Määttänen, Neil R Cashman, Andrew Potter, Jeremy S Lee, Scott Nappe. Nanopore analysis reveals differences in structural stability of ovine PrP(C) proteins corresponding to scrapie susceptible (VRQ) and resistance (ARR) genotypes. Prion. vol 7. issue 6. 2015-03-30. PMID:24401607. |
defining the structure-activity relationship of prp(c)/prp(sc) with respect to infectivity/susceptibility will benefit disease understanding and assessment of transmission risks. |
2015-03-30 |
2023-08-12 |
Not clear |
| Claudia Avis Madampage, Kristen Marciniuk, Pekka Määttänen, Neil R Cashman, Andrew Potter, Jeremy S Lee, Scott Nappe. Nanopore analysis reveals differences in structural stability of ovine PrP(C) proteins corresponding to scrapie susceptible (VRQ) and resistance (ARR) genotypes. Prion. vol 7. issue 6. 2015-03-30. PMID:24401607. |
addition of prp(sc)-specific polyclonal antibody (yml) to the arr variant, pre-incubated in 2m gdn-hcl, reduced the number of type ii events with no clear intercalation/translocation peak, whereas for vrq, type ii events above blockades of 90 pa bound yml. |
2015-03-30 |
2023-08-12 |
Not clear |
| Claudia Avis Madampage, Kristen Marciniuk, Pekka Määttänen, Neil R Cashman, Andrew Potter, Jeremy S Lee, Scott Nappe. Nanopore analysis reveals differences in structural stability of ovine PrP(C) proteins corresponding to scrapie susceptible (VRQ) and resistance (ARR) genotypes. Prion. vol 7. issue 6. 2015-03-30. PMID:24401607. |
a second prp(sc)-specific antibody (sn6b) to a different cryptic epitope reduced type ii events for vrq but not the arr variant. |
2015-03-30 |
2023-08-12 |
Not clear |
| Claudia Avis Madampage, Kristen Marciniuk, Pekka Määttänen, Neil R Cashman, Andrew Potter, Jeremy S Lee, Scott Nappe. Nanopore analysis reveals differences in structural stability of ovine PrP(C) proteins corresponding to scrapie susceptible (VRQ) and resistance (ARR) genotypes. Prion. vol 7. issue 6. 2015-03-30. PMID:24401607. |
collectively, the event patterns associated with sequential denaturation, as well as interactions with prp(sc)-specific antibodies, support unique patterns and/or propensities of misfolding between the genotypes. |
2015-03-30 |
2023-08-12 |
Not clear |
| Juliana A P Chaves, Carolina Sanchez-López, Mariana P B Gomes, Tháyna Sisnande, Bruno Macedo, Vanessa End de Oliveira, Carolina A C Braga, Luciana P Rangel, Jerson L Silva, Liliana Quintanar, Yraima Cordeir. Biophysical and morphological studies on the dual interaction of non-octarepeat prion protein peptides with copper and nucleic acids. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. vol 19. issue 6. 2015-03-30. PMID:24557708. |
conversion of prion protein (prp) to an altered conformer, the scrapie prp (prp(sc)), is a critical step in the development of transmissible spongiform encephalopathies. |
2015-03-30 |
2023-08-12 |
human |
| Michal Mizrahi, Yael Friedman-Levi, Liraz Larush, Kati Frid, Orli Binyamin, Dvir Dori, Nina Fainstein, Haim Ovadia, Tamir Ben-Hur, Shlomo Magdassi, Ruth Gabizo. Pomegranate seed oil nanoemulsions for the prevention and treatment of neurodegenerative diseases: the case of genetic CJD. Nanomedicine : nanotechnology, biology, and medicine. vol 10. issue 6. 2015-03-30. PMID:24704590. |
neurodegenerative diseases generate the accumulation of specific misfolded proteins, such as prp(sc) prions or a-beta in alzheimer's diseases, and share common pathological features, like neuronal death and oxidative damage. |
2015-03-30 |
2023-08-13 |
mouse |
| Michal Mizrahi, Yael Friedman-Levi, Liraz Larush, Kati Frid, Orli Binyamin, Dvir Dori, Nina Fainstein, Haim Ovadia, Tamir Ben-Hur, Shlomo Magdassi, Ruth Gabizo. Pomegranate seed oil nanoemulsions for the prevention and treatment of neurodegenerative diseases: the case of genetic CJD. Nanomedicine : nanotechnology, biology, and medicine. vol 10. issue 6. 2015-03-30. PMID:24704590. |
analysis of brain samples revealed that nano-pso treatment did not decrease prp(sc) accumulation, but rather reduced lipid oxidation and neuronal loss, indicating a strong neuroprotective effect. |
2015-03-30 |
2023-08-13 |
mouse |
| Susan W Robinson, Marie L Nugent, David Dinsdale, Joern R Steiner. Prion protein facilitates synaptic vesicle release by enhancing release probability. Human molecular genetics. vol 23. issue 17. 2015-03-30. PMID:24722203. |
in humans, prion disease occurs typically with a sporadic origin where uncharacterized mechanisms induce spontaneous prp(c) misfolding leading to neurotoxic prp-scrapie formation (prp(sc)). |
2015-03-30 |
2023-08-13 |
drosophila_melanogaster |
| Susan W Robinson, Marie L Nugent, David Dinsdale, Joern R Steiner. Prion protein facilitates synaptic vesicle release by enhancing release probability. Human molecular genetics. vol 23. issue 17. 2015-03-30. PMID:24722203. |
thus, our data present essential new information possibly related to prion pathogenesis in which a functional synaptic role of prp(c) is compromised due to its advanced conversion into prp(sc) thereby creating a lack-of-function scenario. |
2015-03-30 |
2023-08-13 |
drosophila_melanogaster |
| Phuhai Nguyen, Nassima Oumata, Flavie Soubigou, Justine Evrard, Nathalie Desban, Pascale Lemoine, Serge Bouaziz, Marc Blondel, Cécile Voisse. Evaluation of the antiprion activity of 6-aminophenanthridines and related heterocycles. European journal of medicinal chemistry. vol 82. 2015-03-30. PMID:24927056. |
the most potent derivatives were then assayed ex vivo against the mammalian prion prp(sc) in a cell-based assay. |
2015-03-30 |
2023-08-13 |
Not clear |
| Théo Z Hirsch, Julia Hernandez-Rapp, Séverine Martin-Lannerée, Jean-Marie Launay, Sophie Mouillet-Richar. PrP(C) signalling in neurons: from basics to clinical challenges. Biochimie. vol 104. 2015-03-30. PMID:24952348. |
the cellular prion protein prp(c) was identified over twenty-five years ago as the normal counterpart of the scrapie prion protein prp(sc), itself the main if not the sole component of the infectious agent at the root of transmissible spongiform encephalopathies (tses). |
2015-03-30 |
2023-08-13 |
Not clear |
| Théo Z Hirsch, Julia Hernandez-Rapp, Séverine Martin-Lannerée, Jean-Marie Launay, Sophie Mouillet-Richar. PrP(C) signalling in neurons: from basics to clinical challenges. Biochimie. vol 104. 2015-03-30. PMID:24952348. |
prp(c) is a ubiquitous cell surface protein, abundantly expressed in neurons, which constitute the targets of prp(sc)-mediated toxicity. |
2015-03-30 |
2023-08-13 |
Not clear |
| Théo Z Hirsch, Julia Hernandez-Rapp, Séverine Martin-Lannerée, Jean-Marie Launay, Sophie Mouillet-Richar. PrP(C) signalling in neurons: from basics to clinical challenges. Biochimie. vol 104. 2015-03-30. PMID:24952348. |
a diverse array of data have allowed to shed light on how this function is corrupted by prp(sc). |
2015-03-30 |
2023-08-13 |
Not clear |
| Théo Z Hirsch, Julia Hernandez-Rapp, Séverine Martin-Lannerée, Jean-Marie Launay, Sophie Mouillet-Richar. PrP(C) signalling in neurons: from basics to clinical challenges. Biochimie. vol 104. 2015-03-30. PMID:24952348. |
here, we provide an overview of the various signal transduction cascades ascribed to prp(c) in neurons, summarize how their subversion by prp(sc) or aβ oligomers contributes to tse or ad neuropathogenesis and discuss the ensuing clinical implications. |
2015-03-30 |
2023-08-13 |
Not clear |
| Alessandro Didonna, Anja Colja Venturini, Katrina Hartman, Tanja Vranac, Vladka Čurin Šerbec, Giuseppe Legnam. Characterization of four new monoclonal antibodies against the distal N-terminal region of PrP(c). PeerJ. vol 3. 2015-03-24. PMID:25802800. |
additionally, we show their ability to block prion (prp(sc)) replication at nanomolar concentrations in a cell culture model of prion infection. |
2015-03-24 |
2023-08-13 |
mouse |
| Kyle M Doolan, David W Colb. Conformation-dependent epitopes recognized by prion protein antibodies probed using mutational scanning and deep sequencing. Journal of molecular biology. vol 427. issue 2. 2015-03-19. PMID:25451031. |
prion diseases are caused by a structural rearrangement of the cellular prion protein, prp(c), into a disease-associated conformation, prp(sc), which may be distinguished from one another using conformation-specific antibodies. |
2015-03-19 |
2023-08-13 |
Not clear |
| Amely Campe, Kristin Sauter, Martin Beyerbach, Jan Schael, Thomas Selhorst, Sandra B Leo, Matthias Kramer, Lothar Kreienbroc. Case-control study on the risks of BSE infections in Northern Germany. Berliner und Munchener tierarztliche Wochenschrift. vol 126. issue 5-6. 2015-03-12. PMID:23758037. |
this study, like findings in bavaria, lower saxony and schleswig-holstein, strengthens the hypothesis that bse in germany was caused by a feed mediated ubiquitous exposure to prp(sc) during a confined time period. |
2015-03-12 |
2023-08-12 |
cattle |
| Amely Campe, Kristin Sauter, Martin Beyerbach, Jan Schael, Thomas Selhorst, Sandra B Leo, Matthias Kramer, Lothar Kreienbroc. Case-control study on the risks of BSE infections in Northern Germany. Berliner und Munchener tierarztliche Wochenschrift. vol 126. issue 5-6. 2015-03-12. PMID:23758037. |
producers, in need of buying animal derived feed components during that time slot, were more likely to spread the prp(sc) than others. |
2015-03-12 |
2023-08-12 |
cattle |