| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Xuesong Wang, Bingbing Zhang, Cong Zhao, Yanli Wang, Lei He, Menghan Cui, Xiaotong Zhu, Weihong D. Inhibition of human prion neuropeptide PrP106-126 aggregation by hexacoordinated ruthenium complexes. Journal of inorganic biochemistry. vol 128. 2014-06-07. PMID:23911565. |
the neuropeptide prp106-126 has been widely used as a suitable model to study the biological and physiochemical properties of prp(sc). |
2014-06-07 |
2023-08-12 |
human |
| Xuesong Wang, Bingbing Zhang, Cong Zhao, Yanli Wang, Lei He, Menghan Cui, Xiaotong Zhu, Weihong D. Inhibition of human prion neuropeptide PrP106-126 aggregation by hexacoordinated ruthenium complexes. Journal of inorganic biochemistry. vol 128. 2014-06-07. PMID:23911565. |
prp106-126 shares several physicochemical and biological properties with prp(sc), including cellular toxicity, fibrillogenesis, and membrane-binding affinity. |
2014-06-07 |
2023-08-12 |
human |
| Florent Laferrière, Philippe Tixador, Mohammed Moudjou, Jérôme Chapuis, Pierre Sibille, Laetitia Herzog, Fabienne Reine, Emilie Jaumain, Hubert Laude, Human Rezaei, Vincent Béringu. Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics. PLoS pathogens. vol 9. issue 10. 2014-05-26. PMID:24130496. |
they are essentially composed of prp(sc), an aggregated, misfolded conformer of the ubiquitously expressed host-encoded prion protein (prp(c)). |
2014-05-26 |
2023-08-12 |
mouse |
| Florent Laferrière, Philippe Tixador, Mohammed Moudjou, Jérôme Chapuis, Pierre Sibille, Laetitia Herzog, Fabienne Reine, Emilie Jaumain, Hubert Laude, Human Rezaei, Vincent Béringu. Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics. PLoS pathogens. vol 9. issue 10. 2014-05-26. PMID:24130496. |
stable variations in prp(sc) conformation are assumed to encode the phenotypically tangible prion strains diversity. |
2014-05-26 |
2023-08-12 |
mouse |
| Florent Laferrière, Philippe Tixador, Mohammed Moudjou, Jérôme Chapuis, Pierre Sibille, Laetitia Herzog, Fabienne Reine, Emilie Jaumain, Hubert Laude, Human Rezaei, Vincent Béringu. Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics. PLoS pathogens. vol 9. issue 10. 2014-05-26. PMID:24130496. |
however the direct contribution of prp(sc) quaternary structure to the strain biological information remains mostly unknown. |
2014-05-26 |
2023-08-12 |
mouse |
| Florent Laferrière, Philippe Tixador, Mohammed Moudjou, Jérôme Chapuis, Pierre Sibille, Laetitia Herzog, Fabienne Reine, Emilie Jaumain, Hubert Laude, Human Rezaei, Vincent Béringu. Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics. PLoS pathogens. vol 9. issue 10. 2014-05-26. PMID:24130496. |
applying a sedimentation velocity fractionation technique to a panel of ovine prion strains, classified as fast and slow according to their incubation time in ovine prp transgenic mice, has previously led to the observation that the relationship between prion infectivity and prp(sc) quaternary structure was not univocal. |
2014-05-26 |
2023-08-12 |
mouse |
| Florent Laferrière, Philippe Tixador, Mohammed Moudjou, Jérôme Chapuis, Pierre Sibille, Laetitia Herzog, Fabienne Reine, Emilie Jaumain, Hubert Laude, Human Rezaei, Vincent Béringu. Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics. PLoS pathogens. vol 9. issue 10. 2014-05-26. PMID:24130496. |
for the fast strains specifically, infectivity sedimented slowly and segregated from the bulk of proteinase-k resistant prp(sc). |
2014-05-26 |
2023-08-12 |
mouse |
| Florent Laferrière, Philippe Tixador, Mohammed Moudjou, Jérôme Chapuis, Pierre Sibille, Laetitia Herzog, Fabienne Reine, Emilie Jaumain, Hubert Laude, Human Rezaei, Vincent Béringu. Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics. PLoS pathogens. vol 9. issue 10. 2014-05-26. PMID:24130496. |
the density profile of prion infectivity and proteinase-k resistant prp(sc) tended to overlap whatever the strain, fast or slow, leaving only size as the main responsible factor for the specific velocity properties of the fast strain most infectious component. |
2014-05-26 |
2023-08-12 |
mouse |
| Florent Laferrière, Philippe Tixador, Mohammed Moudjou, Jérôme Chapuis, Pierre Sibille, Laetitia Herzog, Fabienne Reine, Emilie Jaumain, Hubert Laude, Human Rezaei, Vincent Béringu. Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics. PLoS pathogens. vol 9. issue 10. 2014-05-26. PMID:24130496. |
we further show that this velocity-isolable population of discrete assemblies perfectly resists limited proteolysis and that its templating activity, as assessed by protein misfolding cyclic amplification outcompetes by several orders of magnitude that of the bulk of larger size prp(sc) aggregates. |
2014-05-26 |
2023-08-12 |
mouse |
| Florent Laferrière, Philippe Tixador, Mohammed Moudjou, Jérôme Chapuis, Pierre Sibille, Laetitia Herzog, Fabienne Reine, Emilie Jaumain, Hubert Laude, Human Rezaei, Vincent Béringu. Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics. PLoS pathogens. vol 9. issue 10. 2014-05-26. PMID:24130496. |
together, the tight correlation between small size, conversion efficiency and duration of disease establishes prp(sc) quaternary structure as a determining factor of prion replication dynamics. |
2014-05-26 |
2023-08-12 |
mouse |
| Qingzhong Kong, Jeffrey L Mills, Bishwajit Kundu, Xinyi Li, Liuting Qing, Krystyna Surewicz, Ignazio Cali, Shenghai Huang, Mengjie Zheng, Wieslaw Swietnicki, Frank D Sönnichsen, Pierluigi Gambetti, Witold K Surewic. Thermodynamic stabilization of the folded domain of prion protein inhibits prion infection in vivo. Cell reports. vol 4. issue 2. 2014-05-16. PMID:23871665. |
prion diseases, or transmissible spongiform encephalopathies (tses), are associated with the conformational conversion of the cellular prion protein, prp(c), into a protease-resistant form, prp(sc). |
2014-05-16 |
2023-08-12 |
mouse |
| Qingzhong Kong, Jeffrey L Mills, Bishwajit Kundu, Xinyi Li, Liuting Qing, Krystyna Surewicz, Ignazio Cali, Shenghai Huang, Mengjie Zheng, Wieslaw Swietnicki, Frank D Sönnichsen, Pierluigi Gambetti, Witold K Surewic. Thermodynamic stabilization of the folded domain of prion protein inhibits prion infection in vivo. Cell reports. vol 4. issue 2. 2014-05-16. PMID:23871665. |
these findings not only provide a line of evidence in support of the protein-only model of tses but also yield insight into the molecular nature of the prp(c)→prp(sc) conformational transition, and they suggest an approach to the treatment of prion diseases. |
2014-05-16 |
2023-08-12 |
mouse |
| Thorsten Kuczius, Reinhard Kelsc. Effects of metal binding on solubility and resistance of physiological prions depend on tissues and glycotypes. Journal of cellular biochemistry. vol 114. issue 12. 2014-05-06. PMID:23794222. |
prion diseases entail the conversion of a normal host-encoded prion protein (prp(c)) into an infectious isoform (prp(sc)). |
2014-05-06 |
2023-08-12 |
human |
| Thorsten Kuczius, Reinhard Kelsc. Effects of metal binding on solubility and resistance of physiological prions depend on tissues and glycotypes. Journal of cellular biochemistry. vol 114. issue 12. 2014-05-06. PMID:23794222. |
various prp(c) types differing in banding profiles and detergent solubility are present in different tissues, but only few prp(sc) types have been generated although prp(c) acts as substrate. |
2014-05-06 |
2023-08-12 |
human |
| Thorsten Kuczius, Reinhard Kelsc. Effects of metal binding on solubility and resistance of physiological prions depend on tissues and glycotypes. Journal of cellular biochemistry. vol 114. issue 12. 2014-05-06. PMID:23794222. |
we hypothesize that distinct prp(c) subtypes may be converted more efficiently to prp(sc) than others. |
2014-05-06 |
2023-08-12 |
human |
| Thorsten Kuczius, Reinhard Kelsc. Effects of metal binding on solubility and resistance of physiological prions depend on tissues and glycotypes. Journal of cellular biochemistry. vol 114. issue 12. 2014-05-06. PMID:23794222. |
the differentiation of high and low soluble metal bound prp(c) offers precious information about prp(c) protein composition and provides approaches for analyzing the transformation efficiency to prp(sc). |
2014-05-06 |
2023-08-12 |
human |
| Caroline Hinton, Helma Antony, Saeed M Hashimi, Alan Munn, Ming Q We. Significance of prion and prion-like proteins in cancer development, progression and multi-drug resistance. Current cancer drug targets. vol 13. issue 8. 2014-05-06. PMID:24015988. |
these are manifested as transmissible spongiform encephalopathies (tses) that result from the conversion of the normal glycosylphosphatidylinositol (gpi) anchored cellular prion protein (prp(c)) to a misfolded, aggregated and pathogenic form, prion protein scrapie (prp(sc)) via a post-translational process followed by the accumulation of prp(sc) within the central nervous system. |
2014-05-06 |
2023-08-12 |
Not clear |
| Fabienne Leidel, Martin Eiden, Markus Geissen, Thomas Hirschberger, Paul Tavan, Armin Giese, Hans A Kretzschmar, Hermann Schätzl, Martin H Groschu. Piperazine derivatives inhibit PrP/PrP(res) propagation in vitro and in vivo. Biochemical and biophysical research communications. vol 445. issue 1. 2014-05-02. PMID:24502948. |
the major neuropathological change in diseased brains is the conversion of the normal cellular form of the prion protein prpc(c) into a disease-associated isoform prp(sc). |
2014-05-02 |
2023-08-12 |
mouse |
| Fabienne Leidel, Martin Eiden, Markus Geissen, Thomas Hirschberger, Paul Tavan, Armin Giese, Hans A Kretzschmar, Hermann Schätzl, Martin H Groschu. Piperazine derivatives inhibit PrP/PrP(res) propagation in vitro and in vivo. Biochemical and biophysical research communications. vol 445. issue 1. 2014-05-02. PMID:24502948. |
prp(sc) accumulates into multimeres and fibrillar aggregates, which leads to the formation of amyloid plaques. |
2014-05-02 |
2023-08-12 |
mouse |
| Fabienne Leidel, Martin Eiden, Markus Geissen, Thomas Hirschberger, Paul Tavan, Armin Giese, Hans A Kretzschmar, Hermann Schätzl, Martin H Groschu. Piperazine derivatives inhibit PrP/PrP(res) propagation in vitro and in vivo. Biochemical and biophysical research communications. vol 445. issue 1. 2014-05-02. PMID:24502948. |
increasing evidence indicates a fundamental role of prp(sc) species and its aggregation in the pathogenesis of prion diseases, which initiates the pathological cascade and leads to neurodegeneration accompanied by spongiform changes. |
2014-05-02 |
2023-08-12 |
mouse |