| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Natalia C Ferreira, Icaro A Marques, Wesley A Conceição, Bruno Macedo, Clarice S Machado, Alessandra Mascarello, Louise Domeneghini Chiaradia-Delatorre, Rosendo Augusto Yunes, Ricardo José Nunes, Andrew G Hughson, Lynne D Raymond, Pedro G Pascutti, Byron Caughey, Yraima Cordeir. Anti-prion activity of a panel of aromatic chemical compounds: in vitro and in silico approaches. PloS one. vol 9. issue 1. 2014-09-10. PMID:24400098. |
once formed, prp(sc) aggregates and catalyzes prp(c) misfolding into new prp(sc) molecules. |
2014-09-10 |
2023-08-12 |
Not clear |
| Natalia C Ferreira, Icaro A Marques, Wesley A Conceição, Bruno Macedo, Clarice S Machado, Alessandra Mascarello, Louise Domeneghini Chiaradia-Delatorre, Rosendo Augusto Yunes, Ricardo José Nunes, Andrew G Hughson, Lynne D Raymond, Pedro G Pascutti, Byron Caughey, Yraima Cordeir. Anti-prion activity of a panel of aromatic chemical compounds: in vitro and in silico approaches. PloS one. vol 9. issue 1. 2014-09-10. PMID:24400098. |
a diverse panel of aromatic compounds was screened in neuroblastoma cells persistently infected with prp(sc) (scn2a) for their ability to inhibit pk-resistant prp (prp(res)) accumulation. |
2014-09-10 |
2023-08-12 |
Not clear |
| Christine Pampeno, Irina L Derkatch, Daniel Meruel. Interaction of human laminin receptor with Sup35, the [PSI⁺] prion-forming protein from S. cerevisiae: a yeast model for studies of LamR interactions with amyloidogenic proteins. PloS one. vol 9. issue 1. 2014-09-08. PMID:24416454. |
furthermore, lamr interacts with both cellular and infectious forms of the prion protein, prp(c) and prp(sc). |
2014-09-08 |
2023-08-12 |
human |
| Christine Pampeno, Irina L Derkatch, Daniel Meruel. Interaction of human laminin receptor with Sup35, the [PSI⁺] prion-forming protein from S. cerevisiae: a yeast model for studies of LamR interactions with amyloidogenic proteins. PloS one. vol 9. issue 1. 2014-09-08. PMID:24416454. |
whether lamr interacts with prp(sc) exclusively in a capacity of the prp receptor, or lamr specifically recognizes prion determinants of prp(sc), is unclear. |
2014-09-08 |
2023-08-12 |
human |
| Adriana Gielbert, Linda A Davis, A Robin Sayers, Yue Tang, James Hope, Maurice J Saue. Quantitative profiling of PrP(Sc) peptides by high-performance liquid chromatography mass spectrometry to investigate the diversity of prions. Analytical biochemistry. vol 436. issue 1. 2014-09-05. PMID:23357236. |
quantitative profiling of prp(sc) peptides by high-performance liquid chromatography mass spectrometry to investigate the diversity of prions. |
2014-09-05 |
2023-08-12 |
Not clear |
| Adriana Gielbert, Linda A Davis, A Robin Sayers, Yue Tang, James Hope, Maurice J Saue. Quantitative profiling of PrP(Sc) peptides by high-performance liquid chromatography mass spectrometry to investigate the diversity of prions. Analytical biochemistry. vol 436. issue 1. 2014-09-05. PMID:23357236. |
the conversion of prp(c), the mammalian prion glycoprotein, to its prion form, prp(sc), in the brain is a precursor to progressive neurological degeneration, and the various folded forms of prp(sc) (defined by the size and glycosylation of protease-resistant core peptides of the prp aggregates, prp(res)) are characteristic of a particular neurodegenerative phenotype or prion disease. |
2014-09-05 |
2023-08-12 |
Not clear |
| Romany N N Abskharon, Gabriele Giachin, Alexandre Wohlkonig, Sameh H Soror, Els Pardon, Giuseppe Legname, Jan Steyaer. Probing the N-terminal β-sheet conversion in the crystal structure of the human prion protein bound to a nanobody. Journal of the American Chemical Society. vol 136. issue 3. 2014-09-04. PMID:24400836. |
prion diseases are caused by the structural conversion of the cellular prion protein, prp(c), into its misfolded oligomeric form, known as prion or prp(sc). |
2014-09-04 |
2023-08-12 |
human |
| Romany N N Abskharon, Gabriele Giachin, Alexandre Wohlkonig, Sameh H Soror, Els Pardon, Giuseppe Legname, Jan Steyaer. Probing the N-terminal β-sheet conversion in the crystal structure of the human prion protein bound to a nanobody. Journal of the American Chemical Society. vol 136. issue 3. 2014-09-04. PMID:24400836. |
compelling evidence indicates that an evolutionary n-terminal conserved motif agaaaaga (residues 113-120) plays an important role in the conversion to prp(sc). |
2014-09-04 |
2023-08-12 |
human |
| Romany N N Abskharon, Gabriele Giachin, Alexandre Wohlkonig, Sameh H Soror, Els Pardon, Giuseppe Legname, Jan Steyaer. Probing the N-terminal β-sheet conversion in the crystal structure of the human prion protein bound to a nanobody. Journal of the American Chemical Society. vol 136. issue 3. 2014-09-04. PMID:24400836. |
from this structure, it appears that the palindromic motif mediates β-enrichment in the prp(c) monomer as one of the early events in the conversion of prp(c) into prp(sc). |
2014-09-04 |
2023-08-12 |
human |
| Anja M Oelschlegel, Charles Weissman. Acquisition of drug resistance and dependence by prions. PLoS pathogens. vol 9. issue 2. 2014-09-02. PMID:23408888. |
the misfolded prion protein (prp(sc)) associated with a swainsonine-dependent variant was less rapidly cleared in pk1 cells than that associated with its drug-sensitive counterpart, indicating that likely structural differences of the misfolded prp underlie the properties of the prions. |
2014-09-02 |
2023-08-12 |
Not clear |
| Franc Llorens, Belén Ansoleaga, Paula Garcia-Esparcia, Saima Zafar, Oriol Grau-Rivera, Irene López-González, Rosi Blanco, Margarita Carmona, Jordi Yagüe, Carlos Nos, José Antonio Del Río, Ellen Gelpí, Inga Zerr, Isidre Ferre. PrP mRNA and protein expression in brain and PrP(c) in CSF in Creutzfeldt-Jakob disease MM1 and VV2. Prion. vol 7. issue 5. 2014-08-29. PMID:24047819. |
cjd displays distinctive clinical and pathological features which correlate with the genotype at the codon 129 (methionine or valine: m or v respectively) in the prion protein gene and with size of the protease-resistant core of the abnormal prion protein prp(sc) (type 1: 20/21 kda and type 2: 19 kda). |
2014-08-29 |
2023-08-12 |
Not clear |
| Franc Llorens, Belén Ansoleaga, Paula Garcia-Esparcia, Saima Zafar, Oriol Grau-Rivera, Irene López-González, Rosi Blanco, Margarita Carmona, Jordi Yagüe, Carlos Nos, José Antonio Del Río, Ellen Gelpí, Inga Zerr, Isidre Ferre. PrP mRNA and protein expression in brain and PrP(c) in CSF in Creutzfeldt-Jakob disease MM1 and VV2. Prion. vol 7. issue 5. 2014-08-29. PMID:24047819. |
total prp protein levels and prp(sc) levels in the frontal cortex and cerebellum accumulate differentially in scjd mm1 and scjd vv2 with no relation between prp(sc) deposition and spongiform degeneration and neuron loss, but with microgliosis, and il6 and tnf-α response. |
2014-08-29 |
2023-08-12 |
Not clear |
| Pavlina Sobrova, Iva Blazkova, Jana Chomoucka, Jana Drbohlavova, Marketa Vaculovicova, Pavel Kopel, Jaromir Hubalek, Rene Kizek, Vojtech Ada. Quantum dots and prion proteins: is this a new challenge for neurodegenerative diseases imaging? Prion. vol 7. issue 5. 2014-08-29. PMID:24055838. |
however, in transmissible spongiform encephalopathies, the infectious agent, prion protein (prp(sc)), has the same sequence of nucleic acids as a naturally occurring protein. |
2014-08-29 |
2023-08-12 |
Not clear |
| Pavlina Sobrova, Iva Blazkova, Jana Chomoucka, Jana Drbohlavova, Marketa Vaculovicova, Pavel Kopel, Jaromir Hubalek, Rene Kizek, Vojtech Ada. Quantum dots and prion proteins: is this a new challenge for neurodegenerative diseases imaging? Prion. vol 7. issue 5. 2014-08-29. PMID:24055838. |
the other issue with the diagnosing based on the prp(sc) detection is that the pathological form of prion protein is abundant only at late stages of the disease in a brain. |
2014-08-29 |
2023-08-12 |
Not clear |
| Pekka Määttänen, Ryan Taschuk, Li Ross, Kristen Marciniuk, Lisa Bertram, Andrew Potter, Neil R Cashman, Scott Nappe. PrP(Sc)-specific antibodies do not induce prion disease or misfolding of PrP(C) in highly susceptible Tga20 mice. Prion. vol 7. issue 5. 2014-08-29. PMID:24105298. |
prp(sc)-specific antibodies do not induce prion disease or misfolding of prp(c) in highly susceptible tga20 mice. |
2014-08-29 |
2023-08-12 |
mouse |
| Pekka Määttänen, Ryan Taschuk, Li Ross, Kristen Marciniuk, Lisa Bertram, Andrew Potter, Neil R Cashman, Scott Nappe. PrP(Sc)-specific antibodies do not induce prion disease or misfolding of PrP(C) in highly susceptible Tga20 mice. Prion. vol 7. issue 5. 2014-08-29. PMID:24105298. |
transmissible spongiform encephalopathies (tses) are fatal neurodegenerative disorders caused by misfolding of a cellular protein prp(c) into an infectious conformation prp(sc). |
2014-08-29 |
2023-08-12 |
mouse |
| Pekka Määttänen, Ryan Taschuk, Li Ross, Kristen Marciniuk, Lisa Bertram, Andrew Potter, Neil R Cashman, Scott Nappe. PrP(Sc)-specific antibodies do not induce prion disease or misfolding of PrP(C) in highly susceptible Tga20 mice. Prion. vol 7. issue 5. 2014-08-29. PMID:24105298. |
previously our group demonstrated induction of prp(sc)-specific antibodies with a sn6b vaccine that targets regions of the protein that are exposed upon misfolding. |
2014-08-29 |
2023-08-12 |
mouse |
| Pekka Määttänen, Ryan Taschuk, Li Ross, Kristen Marciniuk, Lisa Bertram, Andrew Potter, Neil R Cashman, Scott Nappe. PrP(Sc)-specific antibodies do not induce prion disease or misfolding of PrP(C) in highly susceptible Tga20 mice. Prion. vol 7. issue 5. 2014-08-29. PMID:24105298. |
to evaluate the consequences of prolonged exposure to prp(sc)-specific antibodies in a prion sensitized animal, tga20 mice were vaccinated with the sn6b vaccine. |
2014-08-29 |
2023-08-12 |
mouse |
| Mohammed I Y Elmallah, Uwe Borgmeyer, Christian Betzel, Lars Redeck. Impact of methionine oxidation as an initial event on the pathway of human prion protein conversion. Prion. vol 7. issue 5. 2014-08-29. PMID:24121542. |
prion diseases comprise a group of fatal neurodegenerative disorders characterized by the autocatalytic conversion of the cellular prion protein prp(c) into the infectious misfolded isoform prp(sc). |
2014-08-29 |
2023-08-12 |
human |
| Mohammed I Y Elmallah, Uwe Borgmeyer, Christian Betzel, Lars Redeck. Impact of methionine oxidation as an initial event on the pathway of human prion protein conversion. Prion. vol 7. issue 5. 2014-08-29. PMID:24121542. |
although the associated molecular mechanisms remain to be elucidated in detail, several studies currently suggest that methionine oxidation already detected in misfolded prp(sc) destabilizes the native prp fold as an early event in the conversion pathway. |
2014-08-29 |
2023-08-12 |
human |