| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Tsukasa Mashima, Fumiko Nishikawa, Yuji O Kamatari, Hiromichi Fujiwara, Masayuki Saimura, Takashi Nagata, Tsutomu Kodaki, Satoshi Nishikawa, Kazuo Kuwata, Masato Katahir. Anti-prion activity of an RNA aptamer and its structural basis. Nucleic acids research. vol 41. issue 2. 2013-04-04. PMID:23180780. |
the conversion of a normal cellular form (prp(c)) of prp into an abnormal form (prp(sc)) is thought to be associated with the pathogenesis. |
2013-04-04 |
2023-08-12 |
mouse |
| Tsukasa Mashima, Fumiko Nishikawa, Yuji O Kamatari, Hiromichi Fujiwara, Masayuki Saimura, Takashi Nagata, Tsutomu Kodaki, Satoshi Nishikawa, Kazuo Kuwata, Masato Katahir. Anti-prion activity of an RNA aptamer and its structural basis. Nucleic acids research. vol 41. issue 2. 2013-04-04. PMID:23180780. |
here, we show that an rna aptamer comprising only 12 residues, r(ggaggaggagga) (r12), reduces the prp(sc) level in mouse neuronal cells persistently infected with the transmissible spongiform encephalopathy agent. |
2013-04-04 |
2023-08-12 |
mouse |
| Ivana Biljan, Gregor Ilc, Gabriele Giachin, Janez Plavec, Giuseppe Legnam. Structural rearrangements at physiological pH: nuclear magnetic resonance insights from the V210I human prion protein mutant. Biochemistry. vol 51. issue 38. 2013-04-01. PMID:22947063. |
a major focus in prion structural biology studies is unraveling the molecular mechanism leading to the structural conversion of prp(c) to its pathological form, prp(sc). |
2013-04-01 |
2023-08-12 |
human |
| Ivana Biljan, Gregor Ilc, Gabriele Giachin, Janez Plavec, Giuseppe Legnam. Structural rearrangements at physiological pH: nuclear magnetic resonance insights from the V210I human prion protein mutant. Biochemistry. vol 51. issue 38. 2013-04-01. PMID:22947063. |
in our recent studies, we attempted to understand the early events of the conformational changes leading to prp(sc) using as investigative tools point mutations clustered in the open reading frame of the human prp gene and linked to genetic forms of human prion diseases. |
2013-04-01 |
2023-08-12 |
human |
| Tuane C R G Vieira, Daniel P Reynaldo, Mariana P B Gomes, Marcius S Almeida, Yraima Cordeiro, Jerson L Silv. Heparin binding by murine recombinant prion protein leads to transient aggregation and formation of RNA-resistant species. Journal of the American Chemical Society. vol 133. issue 2. 2013-04-01. PMID:21142149. |
the conversion of cellular prion protein (prp(c)) into the pathological conformer prp(sc) requires contact between both isoforms and probably also requires a cellular factor, such as a nucleic acid or a glycosaminoglycan (gag). |
2013-04-01 |
2023-08-12 |
Not clear |
| Larry H Stanker, Miles C Scotcher, Alice Lin, Jeffery McGarvey, Stanley B Prusiner, Robert Hnask. Novel epitopes identified by anti-PrP monoclonal antibodies produced following immunization of Prnp0/0 Balb/cJ mice with purified scrapie prions. Hybridoma (2005). vol 31. issue 5. 2013-03-29. PMID:23098297. |
prions are composed solely of an aberrantly folded isoform (prp(sc)) of a normal cellular protein (prp(c)). |
2013-03-29 |
2023-08-12 |
mouse |
| Larry H Stanker, Miles C Scotcher, Alice Lin, Jeffery McGarvey, Stanley B Prusiner, Robert Hnask. Novel epitopes identified by anti-PrP monoclonal antibodies produced following immunization of Prnp0/0 Balb/cJ mice with purified scrapie prions. Hybridoma (2005). vol 31. issue 5. 2013-03-29. PMID:23098297. |
shared sequence identity of prp(sc) with prp(c) has limited the detection sensitivity of immunochemical assays, as antibodies specific for the disease-causing prp(sc) isoform have not been developed. |
2013-03-29 |
2023-08-12 |
mouse |
| Larry H Stanker, Miles C Scotcher, Alice Lin, Jeffery McGarvey, Stanley B Prusiner, Robert Hnask. Novel epitopes identified by anti-PrP monoclonal antibodies produced following immunization of Prnp0/0 Balb/cJ mice with purified scrapie prions. Hybridoma (2005). vol 31. issue 5. 2013-03-29. PMID:23098297. |
here we report the generation of three new monoclonal antibodies (mabs) to prp, which were isolated following immunization of prnp(0/0) balb/cj mice with highly purified prp(sc) isolated from brain lipid rafts. |
2013-03-29 |
2023-08-12 |
mouse |
| Larry H Stanker, Miles C Scotcher, Alice Lin, Jeffery McGarvey, Stanley B Prusiner, Robert Hnask. Novel epitopes identified by anti-PrP monoclonal antibodies produced following immunization of Prnp0/0 Balb/cJ mice with purified scrapie prions. Hybridoma (2005). vol 31. issue 5. 2013-03-29. PMID:23098297. |
the drm1-60 mab binds a single linear epitope localized to the β2-α2 loop region of prp, whereas drm2-118 binds an epitope that includes sequences within the octarepeat region and near the site of n-terminal truncation of prp(sc) by proteinase k. our novel anti-prp mabs with defined prp epitopes may be useful in deciphering the conformational conversion of prp(c) into prp(sc). |
2013-03-29 |
2023-08-12 |
mouse |
| Pascal Baillod, Julian Garrec, Maria-Carola Colombo, Ivano Tavernelli, Ursula Rothlisberge. Enhanced sampling molecular dynamics identifies PrP(Sc) structures harboring a C-terminal β-core. Biochemistry. vol 51. issue 49. 2013-03-29. PMID:23163312. |
enhanced sampling molecular dynamics identifies prp(sc) structures harboring a c-terminal β-core. |
2013-03-29 |
2023-08-12 |
mouse |
| Pascal Baillod, Julian Garrec, Maria-Carola Colombo, Ivano Tavernelli, Ursula Rothlisberge. Enhanced sampling molecular dynamics identifies PrP(Sc) structures harboring a C-terminal β-core. Biochemistry. vol 51. issue 49. 2013-03-29. PMID:23163312. |
in contrast to the so-called spiral and β-helix models suggesting that the β-rich core of the scrapie isoform (prp(sc)) comprises the n-terminal tail and part of the c-terminal domain up to helix 1 (h1), we present putative structural models for monomeric precursors of prp(sc) and prp β-oligomers that are characterized by a c-terminal β-rich core, in agreement with the suggestions of a series of recent experiments. |
2013-03-29 |
2023-08-12 |
mouse |
| Marko Snajder, Tanja Vilfan, Maja Cernilec, Ruth Rupreht, Mara Popović, Polona Juntes, Vladka Čurin Serbec, Nataša Poklar Ulri. Enzymatic degradation of PrPSc by a protease secreted from Aeropyrum pernix K1. PloS one. vol 7. issue 6. 2013-03-21. PMID:22761822. |
an r30 fraction from the growth medium of aeropyrum pernix was analyzed for the protease that can digest the pathological prion protein isoform (prp(sc)) from different species (human, bovine, deer and mouse). |
2013-03-21 |
2023-08-12 |
mouse |
| Kay M Uppington, David R Brow. Modelling neurodegeneration in prion disease - applications for drug development. Expert opinion on drug discovery. vol 2. issue 6. 2013-03-18. PMID:23488996. |
they are believed to be caused by the conversion of the prion protein (prp), a host expressed protein, into a toxic form (prp(sc)). |
2013-03-18 |
2023-08-12 |
Not clear |
| Kay M Uppington, David R Brow. Modelling neurodegeneration in prion disease - applications for drug development. Expert opinion on drug discovery. vol 2. issue 6. 2013-03-18. PMID:23488996. |
prp(sc) accumulates in the brain, resulting in neuronal loss and the typical spongiform appearance of the brain. |
2013-03-18 |
2023-08-12 |
Not clear |
| Susanne Krasemann, Melanie Neumann, Beata Szalay, Carol Stocking, Markus Glatze. Protease-sensitive prion species in neoplastic spleens of prion-infected mice with uncoupling of PrP(Sc) and prion infectivity. The Journal of general virology. vol 94. issue Pt 2. 2013-03-14. PMID:23136363. |
protease-sensitive prion species in neoplastic spleens of prion-infected mice with uncoupling of prp(sc) and prion infectivity. |
2013-03-14 |
2023-08-12 |
mouse |
| Susanne Krasemann, Melanie Neumann, Beata Szalay, Carol Stocking, Markus Glatze. Protease-sensitive prion species in neoplastic spleens of prion-infected mice with uncoupling of PrP(Sc) and prion infectivity. The Journal of general virology. vol 94. issue Pt 2. 2013-03-14. PMID:23136363. |
an important step in disease pathophysiology is the conversion of cellular prion protein (prp(c)) to disease-associated misfolded conformers (prp(sc)). |
2013-03-14 |
2023-08-12 |
mouse |
| Susanne Krasemann, Melanie Neumann, Beata Szalay, Carol Stocking, Markus Glatze. Protease-sensitive prion species in neoplastic spleens of prion-infected mice with uncoupling of PrP(Sc) and prion infectivity. The Journal of general virology. vol 94. issue Pt 2. 2013-03-14. PMID:23136363. |
in the latter, prp(sc) is thought to replicate mainly in follicular dendritic cells within spleen follicles. |
2013-03-14 |
2023-08-12 |
mouse |
| Susanne Krasemann, Melanie Neumann, Beata Szalay, Carol Stocking, Markus Glatze. Protease-sensitive prion species in neoplastic spleens of prion-infected mice with uncoupling of PrP(Sc) and prion infectivity. The Journal of general virology. vol 94. issue Pt 2. 2013-03-14. PMID:23136363. |
although the presence of prp(sc) is a hallmark for prion disease and serves as a main diagnostic criterion, in certain instances the amount of prp(sc) does not correlate well with neurotoxicity or prion infectivity. |
2013-03-14 |
2023-08-12 |
mouse |
| Susanne Krasemann, Melanie Neumann, Beata Szalay, Carol Stocking, Markus Glatze. Protease-sensitive prion species in neoplastic spleens of prion-infected mice with uncoupling of PrP(Sc) and prion infectivity. The Journal of general virology. vol 94. issue Pt 2. 2013-03-14. PMID:23136363. |
although follicular integrity was completely disturbed, titres of prion infectivity in neoplastic spleens were not significantly altered, yet no protease-resistant prp(sc) was detectable. |
2013-03-14 |
2023-08-12 |
mouse |
| Susanne Krasemann, Melanie Neumann, Beata Szalay, Carol Stocking, Markus Glatze. Protease-sensitive prion species in neoplastic spleens of prion-infected mice with uncoupling of PrP(Sc) and prion infectivity. The Journal of general virology. vol 94. issue Pt 2. 2013-03-14. PMID:23136363. |
these results indicate the dissociation of prp(sc) and prion infectivity and showed the presence of non-prp(sc) prp species in spleen with divergent biochemical properties that become apparent after tissue architecture disruption. |
2013-03-14 |
2023-08-12 |
mouse |