| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Kevin C Gough, Keith Bishop, Ben C Maddiso. Highly sensitive detection of small ruminant bovine spongiform encephalopathy within transmissible spongiform encephalopathy mixes by serial protein misfolding cyclic amplification. Journal of clinical microbiology. vol 52. issue 11. 2015-10-12. PMID:25143565. |
here, we present a novel assay based on the specific amplification of bse prp(sc) using the serial protein misfolding cyclic amplification assay (spmca), which specifically amplified small amounts of ovine and caprine bse agent which had been mixed into a range of scrapie-positive brain homogenates. |
2015-10-12 |
2023-08-13 |
cattle |
| Kevin C Gough, Keith Bishop, Ben C Maddiso. Highly sensitive detection of small ruminant bovine spongiform encephalopathy within transmissible spongiform encephalopathy mixes by serial protein misfolding cyclic amplification. Journal of clinical microbiology. vol 52. issue 11. 2015-10-12. PMID:25143565. |
in a blind trial, this spmca-based assay specifically amplified bse prp(sc) within brain mixes with 100% specificity and 97% sensitivity when bse agent was diluted into scrapie-infected brain homogenates at 1% (vol/vol). |
2015-10-12 |
2023-08-13 |
cattle |
| Yoshio Tsubo. [Current Trends in the Treatment of Prion Disease]. Brain and nerve = Shinkei kenkyu no shinpo. vol 67. issue 7. 2015-10-09. PMID:26160821. |
the pathogenesis of prion disease is the conversion of a normal type prion protein (prp(c)) into a pathological isoform with protease resistance (prp(sc)), which accumulates in the brain. |
2015-10-09 |
2023-08-13 |
Not clear |
| Yoshio Tsubo. [Current Trends in the Treatment of Prion Disease]. Brain and nerve = Shinkei kenkyu no shinpo. vol 67. issue 7. 2015-10-09. PMID:26160821. |
a number of therapeutic agents, including quinacrine, doxycycline, and pentosan polysulphate have shown preventive effects against the conversion of prp(c) into prp(sc) in experimental studies; however, none of these agents have shown satisfactory efficacy in clinical trials. |
2015-10-09 |
2023-08-13 |
Not clear |
| Jogender Singh, Jayant B Udgaonka. Molecular Mechanism of the Misfolding and Oligomerization of the Prion Protein: Current Understanding and Its Implications. Biochemistry. vol 54. issue 29. 2015-10-08. PMID:26171558. |
although it is not yet understood how the misfolding of prp induces neurodegeneration, it is widely accepted that the formation of misfolded prion protein (termed prp(sc)) is both the triggering event in the disease and the main component of the infectious agent responsible for disease transmission. |
2015-10-08 |
2023-08-13 |
Not clear |
| Jogender Singh, Jayant B Udgaonka. Molecular Mechanism of the Misfolding and Oligomerization of the Prion Protein: Current Understanding and Its Implications. Biochemistry. vol 54. issue 29. 2015-10-08. PMID:26171558. |
despite the clear involvement of prp(sc) in prion diseases, the exact composition of prp(sc) is not yet well-known. |
2015-10-08 |
2023-08-13 |
Not clear |
| Fernando Goñi, Candace K Mathiason, Lucia Yim, Kinlung Wong, Jeanette Hayes-Klug, Amy Nalls, Daniel Peyser, Veronica Estevez, Nathaniel Denkers, Jinfeng Xu, David A Osborn, Karl V Miller, Robert J Warren, David R Brown, Jose A Chabalgoity, Edward A Hoover, Thomas Wisniewsk. Mucosal immunization with an attenuated Salmonella vaccine partially protects white-tailed deer from chronic wasting disease. Vaccine. vol 33. issue 5. 2015-10-05. PMID:25539804. |
prion disease is a unique category of illness, affecting both animals and humans, in which the underlying pathogenesis is related to a conformational change of a normal, self-protein called prp(c) (c for cellular) to a pathological and infectious conformer known as prp(sc) (sc for scrapie). |
2015-10-05 |
2023-08-13 |
mouse |
| Nataraj S Pagadala, Rolando Perez-Pineiro, David S Wishart, Jack A Tuszynsk. In silico studies and fluorescence binding assays of potential anti-prion compounds reveal an important binding site for prion inhibition from PrP(C) to PrP(Sc). European journal of medicinal chemistry. vol 91. 2015-09-30. PMID:25042003. |
in silico studies and fluorescence binding assays of potential anti-prion compounds reveal an important binding site for prion inhibition from prp(c) to prp(sc). |
2015-09-30 |
2023-08-13 |
Not clear |
| Nataraj S Pagadala, Rolando Perez-Pineiro, David S Wishart, Jack A Tuszynsk. In silico studies and fluorescence binding assays of potential anti-prion compounds reveal an important binding site for prion inhibition from PrP(C) to PrP(Sc). European journal of medicinal chemistry. vol 91. 2015-09-30. PMID:25042003. |
this high level of correlation between molecular docking and fluorescence quenching studies confirm that these five compounds are likely to act as inhibitors for prion propagation while noscapine might act as a prion accelerator from prp(c) to prp(sc). |
2015-09-30 |
2023-08-13 |
Not clear |
| Ronald A Shikiya, Thomas E Eckland, Alan J Young, Jason C Bart. Prion formation, but not clearance, is supported by protein misfolding cyclic amplification. Prion. vol 8. issue 6. 2015-09-28. PMID:25482601. |
the kinetics of prion infectivity and prp(sc) accumulation can differ between prion strains and within a single strain in different tissues. |
2015-09-28 |
2023-08-13 |
Not clear |
| Ronald A Shikiya, Thomas E Eckland, Alan J Young, Jason C Bart. Prion formation, but not clearance, is supported by protein misfolding cyclic amplification. Prion. vol 8. issue 6. 2015-09-28. PMID:25482601. |
the net accumulation of prp(sc) in animals is controlled by the relationship between the rate of prp(sc) formation and clearance. |
2015-09-28 |
2023-08-13 |
Not clear |
| Ronald A Shikiya, Thomas E Eckland, Alan J Young, Jason C Bart. Prion formation, but not clearance, is supported by protein misfolding cyclic amplification. Prion. vol 8. issue 6. 2015-09-28. PMID:25482601. |
protein misfolding cyclic amplification (pmca) is a powerful technique that faithfully recapitulates prp(sc) formation and prion infectivity in a cell-free system. |
2015-09-28 |
2023-08-13 |
Not clear |
| Ronald A Shikiya, Thomas E Eckland, Alan J Young, Jason C Bart. Prion formation, but not clearance, is supported by protein misfolding cyclic amplification. Prion. vol 8. issue 6. 2015-09-28. PMID:25482601. |
in this study we investigated if degradation of prp(sc) and/or prion infectivity occurs during pmca. |
2015-09-28 |
2023-08-13 |
Not clear |
| Ronald A Shikiya, Thomas E Eckland, Alan J Young, Jason C Bart. Prion formation, but not clearance, is supported by protein misfolding cyclic amplification. Prion. vol 8. issue 6. 2015-09-28. PMID:25482601. |
to accomplish this we performed pmca under conditions that do not support prp(sc) formation and did not observe either a reduction in prp(sc) abundance or an extension of prion incubation period, compared to untreated control samples. |
2015-09-28 |
2023-08-13 |
Not clear |
| Bonto Faburay, Dongseob Tark, Anumantha G Kanthasamy, Juergen A Rich. In vitro amplification of scrapie and chronic wasting disease PrP(res) using baculovirus-expressed recombinant PrP as substrate. Prion. vol 8. issue 6. 2015-09-28. PMID:25495764. |
protein misfolding cyclic amplification (pmca) is an in vitro simulation of prion replication, which relies on the use of normal brain homogenate derived from host species as substrate for the specific amplification of abnormal prion protein, prp(sc). |
2015-09-28 |
2023-08-13 |
Not clear |
| Bonto Faburay, Dongseob Tark, Anumantha G Kanthasamy, Juergen A Rich. In vitro amplification of scrapie and chronic wasting disease PrP(res) using baculovirus-expressed recombinant PrP as substrate. Prion. vol 8. issue 6. 2015-09-28. PMID:25495764. |
here, we report that baculovirus-expressed recombinant prp(c) shows a glycoform and gpi-anchor profile similar to mammalian brain-derived prp(c) and supports amplification of prp(sc) and prp(cwd) derived from prion-affected animals in a single round of seeded pmca in the absence of exogenous co-factors. |
2015-09-28 |
2023-08-13 |
Not clear |
| Bonto Faburay, Dongseob Tark, Anumantha G Kanthasamy, Juergen A Rich. In vitro amplification of scrapie and chronic wasting disease PrP(res) using baculovirus-expressed recombinant PrP as substrate. Prion. vol 8. issue 6. 2015-09-28. PMID:25495764. |
addition of species-specific in vitro transcribed prp mrna molecules stimulated the conversion efficiency resulting in increased prp(sc) or prp(cwd) production. |
2015-09-28 |
2023-08-13 |
Not clear |
| Ting Zhu, Sher Hayat Khan, Deming Zhao, Lifeng Yan. Regulation of proteasomes in prion disease. Acta biochimica et biophysica Sinica. vol 46. issue 7. 2015-09-14. PMID:24829398. |
the hallmark of prion disease is the accumulation of misfolded protein prp(sc), which is toxic to neuronal cells. |
2015-09-14 |
2023-08-13 |
human |
| Ting Zhu, Sher Hayat Khan, Deming Zhao, Lifeng Yan. Regulation of proteasomes in prion disease. Acta biochimica et biophysica Sinica. vol 46. issue 7. 2015-09-14. PMID:24829398. |
accumulated prp(sc) can directly or indirectly affect proteasome activity. |
2015-09-14 |
2023-08-13 |
human |
| Chan Tian, Di Liu, Wei Xiang, Hans A Kretzschmar, Qing-Lan Sun, Chen Gao, Yin Xu, Hui Wang, Xue-Yu Fan, Ge Meng, Wei Li, Xiao-Ping Don. Analyses of the similarity and difference of global gene expression profiles in cortex regions of three neurodegenerative diseases: sporadic Creutzfeldt-Jakob disease (sCJD), fatal familial insomnia (FFI), and Alzheimer's disease (AD). Molecular neurobiology. vol 50. issue 2. 2015-09-11. PMID:24902808. |
review of the clinical materials of 11 scjd patients identified the difference in brain prp(sc) deposits between two subgroups. |
2015-09-11 |
2023-08-13 |
Not clear |