| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Li-Li Qing, Hui Zhao, Lin-Lin Li. Progress on low susceptibility mechanisms of transmissible spongiform encephalopathies. Dong wu xue yan jiu = Zoological research. vol 35. issue 5. 2015-03-09. PMID:25297084. |
the "protein-only" hypothesis of tse suggests that prions are transmissible particles devoid of nucleic acid and the primary pathogenic event is thought to be the conversion of cellular prion protein (prp(c)) into the disease-associated isoform (prp(sc)). |
2015-03-09 |
2023-08-13 |
Not clear |
| Kyriakos Tsangaras, Sergios-Orestis Kolokotronis, Rainer G Ulrich, Serge Morand, Johan Michaux, Alex D Greenwoo. Negative purifying selection drives prion and doppel protein evolution. Journal of molecular evolution. vol 79. issue 1-2. 2015-03-05. PMID:25038839. |
the prion protein (prp) when misfolded into the pathogenic conformer prp(sc) is the major causative agent of several lethal transmissible spongiform encephalopathies in mammals. |
2015-03-05 |
2023-08-13 |
Not clear |
| Gabriella Marcon, Antonio Indaco, Giuseppe Di Fede, Silvia Suardi, Nicoletta Finato, Valentino Moretti, Sandro Micoli, Paolo Fociani, Pietro Zerbi, Alessandro Pincherle, Veronica Redaelli, Fabrizio Tagliavini, Giorgio Giaccon. Panencephalopathic Creutzfeldt-Jakob disease with distinct pattern of prion protein deposition in a patient with D178N mutation and homozygosity for valine at codon 129 of the prion protein Gene. Brain pathology (Zurich, Switzerland). vol 24. issue 2. 2015-02-21. PMID:24118545. |
western blot analysis showed the presence of type 1 prp(sc) (parchi classification). |
2015-02-21 |
2023-08-12 |
human |
| M Enamul Kabir, Jiri G Safa. Implications of prion adaptation and evolution paradigm for human neurodegenerative diseases. Prion. vol 8. issue 1. 2015-02-21. PMID:24401672. |
prions cause lethal neurodegenerative diseases in humans, the most prevalent being sporadic creutzfeldt-jakob disease (scjd); they self-replicate and spread by converting the cellular form of prion protein (prp(c)) to a misfolded pathogenic conformer (prp(sc)). |
2015-02-21 |
2023-08-12 |
human |
| M Enamul Kabir, Jiri G Safa. Implications of prion adaptation and evolution paradigm for human neurodegenerative diseases. Prion. vol 8. issue 1. 2015-02-21. PMID:24401672. |
the extensive phenotypic heterogeneity of human prion diseases is determined by polymorphisms in the prion protein gene, and by prion strain-specific conformation of prp(sc). |
2015-02-21 |
2023-08-12 |
human |
| M Enamul Kabir, Jiri G Safa. Implications of prion adaptation and evolution paradigm for human neurodegenerative diseases. Prion. vol 8. issue 1. 2015-02-21. PMID:24401672. |
in the course of our investigation of this process, we isolated distinct populations of prp(sc) particles that frequently co-exist in scjd. |
2015-02-21 |
2023-08-12 |
human |
| M Enamul Kabir, Jiri G Safa. Implications of prion adaptation and evolution paradigm for human neurodegenerative diseases. Prion. vol 8. issue 1. 2015-02-21. PMID:24401672. |
exposed to mutant substrate, the winning prp(sc) conformers are subject to further evolution by natural selection of the subpopulation with the highest replication rate due to the lowest stability. |
2015-02-21 |
2023-08-12 |
human |
| M Enamul Kabir, Jiri G Safa. Implications of prion adaptation and evolution paradigm for human neurodegenerative diseases. Prion. vol 8. issue 1. 2015-02-21. PMID:24401672. |
thus, the evolution and adaptation of human prions is enabled by a dynamic collection of distinct populations of particles, whose evolution is governed by the selection of progressively less stable, faster replicating prp(sc) conformers. |
2015-02-21 |
2023-08-12 |
human |
| M Enamul Kabir, Jiri G Safa. Implications of prion adaptation and evolution paradigm for human neurodegenerative diseases. Prion. vol 8. issue 1. 2015-02-21. PMID:24401672. |
this fundamental biological mechanism may explain the drug resistance that some prions gained after exposure to compounds targeting prp(sc). |
2015-02-21 |
2023-08-12 |
human |
| Ryan Taschuk, Kristen Marciniuk, Pekka Määttänen, Claudia Madampage, Peter Hedlin, Andrew Potter, Jeremy Lee, Neil R Cashman, Philip J Griebel, Scott Nappe. Safety, specificity and immunogenicity of a PrP(Sc)-specific prion vaccine based on the YYR disease specific epitope. Prion. vol 8. issue 1. 2015-02-21. PMID:24509522. |
safety, specificity and immunogenicity of a prp(sc)-specific prion vaccine based on the yyr disease specific epitope. |
2015-02-21 |
2023-08-12 |
Not clear |
| Ryan Taschuk, Kristen Marciniuk, Pekka Määttänen, Claudia Madampage, Peter Hedlin, Andrew Potter, Jeremy Lee, Neil R Cashman, Philip J Griebel, Scott Nappe. Safety, specificity and immunogenicity of a PrP(Sc)-specific prion vaccine based on the YYR disease specific epitope. Prion. vol 8. issue 1. 2015-02-21. PMID:24509522. |
prions are a novel form of infectivity based on the misfolding of a self-protein (prp(c)) into a pathological, infectious isomer (prp(sc)). |
2015-02-21 |
2023-08-12 |
Not clear |
| Ryan Taschuk, Kristen Marciniuk, Pekka Määttänen, Claudia Madampage, Peter Hedlin, Andrew Potter, Jeremy Lee, Neil R Cashman, Philip J Griebel, Scott Nappe. Safety, specificity and immunogenicity of a PrP(Sc)-specific prion vaccine based on the YYR disease specific epitope. Prion. vol 8. issue 1. 2015-02-21. PMID:24509522. |
our priority is to develop a prp(sc)-specific prion vaccine based on epitopes that are uniquely exposed upon misfolding. |
2015-02-21 |
2023-08-12 |
Not clear |
| Ryan Taschuk, Kristen Marciniuk, Pekka Määttänen, Claudia Madampage, Peter Hedlin, Andrew Potter, Jeremy Lee, Neil R Cashman, Philip J Griebel, Scott Nappe. Safety, specificity and immunogenicity of a PrP(Sc)-specific prion vaccine based on the YYR disease specific epitope. Prion. vol 8. issue 1. 2015-02-21. PMID:24509522. |
here we review outcomes of the translation of a prion dse into a prp(sc)-specific vaccine based on the criteria of immunogenicity, safety and specificity. |
2015-02-21 |
2023-08-12 |
Not clear |
| Christopher J Silv. Applying the tools of chemistry (mass spectrometry and covalent modification by small molecule reagents) to the detection of prions and the study of their structure. Prion. vol 8. issue 1. 2015-02-21. PMID:24509645. |
prions are molecular pathogens, able to convert a normal cellular prion protein (prp(c)) into a prion (prp(sc)). |
2015-02-21 |
2023-08-12 |
Not clear |
| Christopher J Silv. Applying the tools of chemistry (mass spectrometry and covalent modification by small molecule reagents) to the detection of prions and the study of their structure. Prion. vol 8. issue 1. 2015-02-21. PMID:24509645. |
the information necessary for this conversion is contained in the conformation of prp(sc). |
2015-02-21 |
2023-08-12 |
Not clear |
| Christopher J Silv. Applying the tools of chemistry (mass spectrometry and covalent modification by small molecule reagents) to the detection of prions and the study of their structure. Prion. vol 8. issue 1. 2015-02-21. PMID:24509645. |
mass spectrometry has been used to define elements of the secondary and tertiary structure of wild-type prp(sc) and gpi-anchorless prp(sc). |
2015-02-21 |
2023-08-12 |
Not clear |
| Christopher J Silv. Applying the tools of chemistry (mass spectrometry and covalent modification by small molecule reagents) to the detection of prions and the study of their structure. Prion. vol 8. issue 1. 2015-02-21. PMID:24509645. |
it has also been used to study the quaternary structure of the prp(sc) multimer. |
2015-02-21 |
2023-08-12 |
Not clear |
| Christopher J Silv. Applying the tools of chemistry (mass spectrometry and covalent modification by small molecule reagents) to the detection of prions and the study of their structure. Prion. vol 8. issue 1. 2015-02-21. PMID:24509645. |
small molecule reagents react differently with the same lysine in the prp(c) conformation than in the prp(sc) conformation. |
2015-02-21 |
2023-08-12 |
Not clear |
| Christopher J Silv. Applying the tools of chemistry (mass spectrometry and covalent modification by small molecule reagents) to the detection of prions and the study of their structure. Prion. vol 8. issue 1. 2015-02-21. PMID:24509645. |
this permits the detection of prp(sc) without the need for proteinase k pretreatment and can be used to distinguish among prion strains. |
2015-02-21 |
2023-08-12 |
Not clear |
| Berta Puig, Hermann Altmeppen, Markus Glatze. The GPI-anchoring of PrP: implications in sorting and pathogenesis. Prion. vol 8. issue 1. 2015-02-21. PMID:24509692. |
when it changes its conformation to a pathological isoform (then referred to as prp(sc)), it is an essential part of the prion, the agent causing fatal and transmissible neurodegenerative prion diseases. |
2015-02-21 |
2023-08-12 |
Not clear |