| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Brendan Molloy, Hilary E M McMaho. A cell-biased effect of estrogen in prion infection. Journal of virology. vol 88. issue 2. 2014-03-10. PMID:24227845. |
tam and oht had half-maximal inhibitory concentrations for clearance of prp(sc) of 0.47 μm and 0.14 nm, respectively. |
2014-03-10 |
2023-08-12 |
Not clear |
| Brendan Molloy, Hilary E M McMaho. A cell-biased effect of estrogen in prion infection. Journal of virology. vol 88. issue 2. 2014-03-10. PMID:24227845. |
this work identifies further factors involved in the prion disease process, and through antagonism of the estrogen system, we demonstrate that the estrogen system is a target for controlling prp(sc) levels. |
2014-03-10 |
2023-08-12 |
Not clear |
| Julia Hernandez-Rapp, Séverine Martin-Lannerée, Théo Z Hirsch, Jean-Marie Launay, Sophie Mouillet-Richar. Hijacking PrP(c)-dependent signal transduction: when prions impair Aβ clearance. Frontiers in aging neuroscience. vol 6. 2014-03-10. PMID:24592237. |
the cellular prion protein prp(c) is the normal counterpart of the scrapie prion protein prp (sc), the main component of the infectious agent of transmissible spongiform encephalopathies. |
2014-03-10 |
2023-08-12 |
Not clear |
| Julia Hernandez-Rapp, Séverine Martin-Lannerée, Théo Z Hirsch, Jean-Marie Launay, Sophie Mouillet-Richar. Hijacking PrP(c)-dependent signal transduction: when prions impair Aβ clearance. Frontiers in aging neuroscience. vol 6. 2014-03-10. PMID:24592237. |
disease-associated prp (sc) shares with aβ the ability to hijack prp (c)-dependent signaling cascades, and thereby instigate pathogenic events. |
2014-03-10 |
2023-08-12 |
Not clear |
| Laura Pirisinu, Romolo Nonno, Elena Esposito, Sylvie L Benestad, Pierluigi Gambetti, Umberto Agrimi, Wen-Quan Zo. Small ruminant nor98 prions share biochemical features with human gerstmann-sträussler-scheinker disease and variably protease-sensitive prionopathy. PloS one. vol 8. issue 6. 2014-03-05. PMID:23826096. |
prion diseases are classically characterized by the accumulation of pathological prion protein (prp(sc)) with the protease resistant c-terminal fragment (prp(res)) of 27-30 kda. |
2014-03-05 |
2023-08-12 |
human |
| Laura Pirisinu, Romolo Nonno, Elena Esposito, Sylvie L Benestad, Pierluigi Gambetti, Umberto Agrimi, Wen-Quan Zo. Small ruminant nor98 prions share biochemical features with human gerstmann-sträussler-scheinker disease and variably protease-sensitive prionopathy. PloS one. vol 8. issue 6. 2014-03-05. PMID:23826096. |
in this study we performed a detailed comparison of the biochemical features of prp(sc) from atypical prion diseases including human gerstmann-sträussler-scheinker disease (gss) and variably protease-sensitive prionopathy (vpspr) and in small ruminant nor98 or atypical scrapie. |
2014-03-05 |
2023-08-12 |
human |
| Laura Pirisinu, Romolo Nonno, Elena Esposito, Sylvie L Benestad, Pierluigi Gambetti, Umberto Agrimi, Wen-Quan Zo. Small ruminant nor98 prions share biochemical features with human gerstmann-sträussler-scheinker disease and variably protease-sensitive prionopathy. PloS one. vol 8. issue 6. 2014-03-05. PMID:23826096. |
the kinetics of prp(res) production and its cleavage sites after pk digestion were analyzed, along with the prp(sc) conformational stability, using a new method able to characterize both protease-resistant and protease-sensitive prp(sc) components. |
2014-03-05 |
2023-08-12 |
human |
| Laura Pirisinu, Romolo Nonno, Elena Esposito, Sylvie L Benestad, Pierluigi Gambetti, Umberto Agrimi, Wen-Quan Zo. Small ruminant nor98 prions share biochemical features with human gerstmann-sträussler-scheinker disease and variably protease-sensitive prionopathy. PloS one. vol 8. issue 6. 2014-03-05. PMID:23826096. |
all these prp(sc) types shared common and distinctive biochemical features compared to prp(sc) from classical prion diseases such as sporadic creutzfeldt-jakob disease and scrapie. |
2014-03-05 |
2023-08-12 |
human |
| Laura Pirisinu, Romolo Nonno, Elena Esposito, Sylvie L Benestad, Pierluigi Gambetti, Umberto Agrimi, Wen-Quan Zo. Small ruminant nor98 prions share biochemical features with human gerstmann-sträussler-scheinker disease and variably protease-sensitive prionopathy. PloS one. vol 8. issue 6. 2014-03-05. PMID:23826096. |
notwithstanding, distinct biochemical signatures based on prp(res) cleavage sites and prp(sc) conformational stability were identified in gss a117v, gss f198s, gss p102l and vpspr, which allowed their specific identification. |
2014-03-05 |
2023-08-12 |
human |
| Laura Pirisinu, Romolo Nonno, Elena Esposito, Sylvie L Benestad, Pierluigi Gambetti, Umberto Agrimi, Wen-Quan Zo. Small ruminant nor98 prions share biochemical features with human gerstmann-sträussler-scheinker disease and variably protease-sensitive prionopathy. PloS one. vol 8. issue 6. 2014-03-05. PMID:23826096. |
importantly, the biochemical properties of prp(sc) from nor98 and gss p102l largely overlapped, but were distinct from the other human prions investigated. |
2014-03-05 |
2023-08-12 |
human |
| Alessandro Didonn. Prion protein and its role in signal transduction. Cellular & molecular biology letters. vol 18. issue 2. 2014-03-03. PMID:23479001. |
they are characterized by the unique nature of their etiologic agent: prions (prp(sc)). |
2014-03-03 |
2023-08-12 |
Not clear |
| Takuji Yamamoto, Yuko Ushiki-Kaku, Takashi Yokoyama, Shunji Hattor. Sensitivity and specificity of a commercial BSE kit for the detection of ovine scrapie. Animal science journal = Nihon chikusan Gakkaiho. vol 84. issue 6. 2014-02-28. PMID:23607323. |
the detection limit of the abnormal isoform of prion protein (prp(sc) ) of nippibl was examined using diluted scrapie-positive samples. |
2014-02-28 |
2023-08-12 |
cattle |
| Jan Stöh. Prion protein aggregation and fibrillogenesis in vitro. Sub-cellular biochemistry. vol 65. 2014-02-21. PMID:23225001. |
they key event in prion diseases is the conversion of the cellular prion protein (prp(c)) into its disease causing isoform prp(sc). |
2014-02-21 |
2023-08-12 |
Not clear |
| Jan Stöh. Prion protein aggregation and fibrillogenesis in vitro. Sub-cellular biochemistry. vol 65. 2014-02-21. PMID:23225001. |
this conversion is represented by a conformational change from an β-helical dominated isoform into the mostly β-sheeted prp(sc). |
2014-02-21 |
2023-08-12 |
Not clear |
| Beata Sikorska, Pawel P Libersk. Human prion diseases: from Kuru to variant Creutzfeldt-Jakob disease. Sub-cellular biochemistry. vol 65. 2014-02-21. PMID:23225013. |
more recently a novel prion disease variable protease-sensitive prionopathy (pspr) was described in humans.tses are caused by a still incompletely defined infectious agent known as a "prion" which is widely regarded to be an aggregate of a misfolded isoform (prp(sc)) of a normal cellular glycoprotein (prp(c)). |
2014-02-21 |
2023-08-12 |
human |
| Beata Sikorska, Pawel P Libersk. Human prion diseases: from Kuru to variant Creutzfeldt-Jakob disease. Sub-cellular biochemistry. vol 65. 2014-02-21. PMID:23225013. |
the conversion mechanism of prp(c) into prp(sc) is still not certain. |
2014-02-21 |
2023-08-12 |
human |
| Otto Windl, Mike Dawso. Animal prion diseases. Sub-cellular biochemistry. vol 65. 2014-02-21. PMID:23225014. |
the post-mortem diagnosis is based on the detection of this protein, prp(sc), but despite recent impressive developments a routine ante-mortem diagnostic test has proved elusive.there is no treatment for prion diseases in animals, but disease outbreaks are controlled through a mixture of movement restrictions on holdings, culling of affected animals and herds and, for classical scrapie in sheep, selective breeding for genetic resistance. |
2014-02-21 |
2023-08-12 |
mouse |
| H Okada, Y Iwamaru, M Kakizaki, K Masujin, M Imamura, S Fukuda, Y Matsuura, Y Shimizu, K Kasai, S Mohri, T Yokoyam. Properties of L-type bovine spongiform encephalopathy in intraspecies passages. Veterinary pathology. vol 49. issue 5. 2014-02-19. PMID:22081134. |
detailed immunohistochemical and neuropathologic analysis of the brains of second-passaged animals, which had developed the disease and survived for an average of 16 months after inoculation, revealed distribution of spongiform changes and disease-associated prion protein (prp(sc)) throughout the brain. |
2014-02-19 |
2023-08-12 |
cattle |
| H Okada, Y Iwamaru, M Kakizaki, K Masujin, M Imamura, S Fukuda, Y Matsuura, Y Shimizu, K Kasai, S Mohri, T Yokoyam. Properties of L-type bovine spongiform encephalopathy in intraspecies passages. Veterinary pathology. vol 49. issue 5. 2014-02-19. PMID:22081134. |
although immunolabeled prp(sc) obtained from brain tissue was characterized by the presence of prp plaques and diffuse synaptic granular accumulations, no stellate-type deposits were detected. |
2014-02-19 |
2023-08-12 |
cattle |
| H Okada, Y Iwamaru, M Kakizaki, K Masujin, M Imamura, S Fukuda, Y Matsuura, Y Shimizu, K Kasai, S Mohri, T Yokoyam. Properties of L-type bovine spongiform encephalopathy in intraspecies passages. Veterinary pathology. vol 49. issue 5. 2014-02-19. PMID:22081134. |
western blot analysis suggested no obvious differences in prp(sc) molecular mass or glycoform pattern in the brains of first- and second-passaged cattle. |
2014-02-19 |
2023-08-12 |
cattle |