| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Ambadi Thody Sabareesan, Jogender Singh, Samrat Roy, Jayant B Udgaonkar, M K Mathe. The Pathogenic A116V Mutation Enhances Ion-Selective Channel Formation by Prion Protein in Membranes. Biophysical journal. vol 110. issue 8. 2017-06-14. PMID:27119637. |
misfolded and aggregated forms of the prion protein (prp(sc)) have been associated with many prion diseases. |
2017-06-14 |
2023-08-13 |
mouse |
| Ambadi Thody Sabareesan, Jogender Singh, Samrat Roy, Jayant B Udgaonkar, M K Mathe. The Pathogenic A116V Mutation Enhances Ion-Selective Channel Formation by Prion Protein in Membranes. Biophysical journal. vol 110. issue 8. 2017-06-14. PMID:27119637. |
a transmembrane form of prp favored by the pathogenic mutation a116v is associated with gerstmann-sträussler-scheinker syndrome, but no accumulation of prp(sc) is detected. |
2017-06-14 |
2023-08-13 |
mouse |
| Atsuko Takeuchi, Atsushi Kobayashi, Piero Parchi, Masahito Yamada, Masanori Morita, Shusei Uno, Tetsuyuki Kitamot. Distinctive properties of plaque-type dura mater graft-associated Creutzfeldt-Jakob disease in cell-protein misfolding cyclic amplification. Laboratory investigation; a journal of technical methods and pathology. vol 96. issue 5. 2017-06-12. PMID:26878132. |
p-dcjd shows distinctive phenotypic features, namely numerous kuru plaques and an abnormal isoform of prion protein (prp(sc)) intermediate in size between types 1 and 2. |
2017-06-12 |
2023-08-13 |
human |
| Atsuko Takeuchi, Atsushi Kobayashi, Piero Parchi, Masahito Yamada, Masanori Morita, Shusei Uno, Tetsuyuki Kitamot. Distinctive properties of plaque-type dura mater graft-associated Creutzfeldt-Jakob disease in cell-protein misfolding cyclic amplification. Laboratory investigation; a journal of technical methods and pathology. vol 96. issue 5. 2017-06-12. PMID:26878132. |
moreover, by using a type 2 prp(sc)-specific antibody not recognizing prp(sc) in p-dcjd, we found that type 2 products are generated de novo from p-dcjd prions during pmca with the 129 v substrates. |
2017-06-12 |
2023-08-13 |
human |
| Tania Massignan, Sara Cimini, Claudia Stincardini, Milica Cerovic, Ilaria Vanni, Saioa R Elezgarai, Jorge Moreno, Matteo Stravalaci, Alessandro Negro, Valeria Sangiovanni, Elena Restelli, Geraldina Riccardi, Marco Gobbi, Joaquín Castilla, Tiziana Borsello, Romolo Nonno, Emiliano Biasin. A cationic tetrapyrrole inhibits toxic activities of the cellular prion protein. Scientific reports. vol 6. 2017-06-02. PMID:26976106. |
prion diseases are rare neurodegenerative conditions associated with the conformational conversion of the cellular prion protein (prp(c)) into prp(sc), a self-replicating isoform (prion) that accumulates in the central nervous system of affected individuals. |
2017-06-02 |
2023-08-13 |
mouse |
| Tania Massignan, Sara Cimini, Claudia Stincardini, Milica Cerovic, Ilaria Vanni, Saioa R Elezgarai, Jorge Moreno, Matteo Stravalaci, Alessandro Negro, Valeria Sangiovanni, Elena Restelli, Geraldina Riccardi, Marco Gobbi, Joaquín Castilla, Tiziana Borsello, Romolo Nonno, Emiliano Biasin. A cationic tetrapyrrole inhibits toxic activities of the cellular prion protein. Scientific reports. vol 6. 2017-06-02. PMID:26976106. |
the structure of prp(sc) is poorly defined, and likely to be heterogeneous, as suggested by the existence of different prion strains. |
2017-06-02 |
2023-08-13 |
mouse |
| Hiroyuki Okada, Kohtaro Miyazawa, Kentaro Masujin, Takashi Yokoyam. Coexistence of two forms of disease-associated prion protein in extracerebral tissues of cattle infected with H-type bovine spongiform encephalopathy. The Journal of veterinary medical science. vol 78. issue 7. 2017-05-25. PMID:27010466. |
h-bse is characterized by the presence of two proteinase k-resistant forms of disease-associated prion protein (prp(sc)), identified as prp(sc) #1 and prp(sc) #2, in the brain. |
2017-05-25 |
2023-08-13 |
cattle |
| Hiroyuki Okada, Kohtaro Miyazawa, Kentaro Masujin, Takashi Yokoyam. Coexistence of two forms of disease-associated prion protein in extracerebral tissues of cattle infected with H-type bovine spongiform encephalopathy. The Journal of veterinary medical science. vol 78. issue 7. 2017-05-25. PMID:27010466. |
to investigate the coexistence of different prp(sc) forms in the extracerebral tissues of cattle experimentally infected with h-bse, immunohistochemical and molecular analyses were performed by using n-terminal-, core-region- and c-terminal-specific anti-prion protein antibodies. |
2017-05-25 |
2023-08-13 |
cattle |
| Hiroyuki Okada, Kohtaro Miyazawa, Kentaro Masujin, Takashi Yokoyam. Coexistence of two forms of disease-associated prion protein in extracerebral tissues of cattle infected with H-type bovine spongiform encephalopathy. The Journal of veterinary medical science. vol 78. issue 7. 2017-05-25. PMID:27010466. |
our results demonstrated that two distinct forms of prp(sc) coexisted in the various extracerebral tissues. |
2017-05-25 |
2023-08-13 |
cattle |
| William B Titlow, Muhammad Waqas, Jihyun Lee, Jae Youl Cho, Sang Yeol Lee, Dae-Hwan Kim, Chongsuk Ryo. Effect of Polylysine on Scrapie Prion Protein Propagation in Spleen during Asymptomatic Stage of Experimental Prion Disease in Mice. Journal of microbiology and biotechnology. vol 26. issue 9. 2017-05-23. PMID:27221113. |
our previous study demonstrated that polylysine was effective in prolonging the incubation period in a rodent model and in alleviating the scrapie prion protein (prp(sc)) burden in the brain at the terminal stage of the disease. |
2017-05-23 |
2023-08-13 |
mouse |
| William B Titlow, Muhammad Waqas, Jihyun Lee, Jae Youl Cho, Sang Yeol Lee, Dae-Hwan Kim, Chongsuk Ryo. Effect of Polylysine on Scrapie Prion Protein Propagation in Spleen during Asymptomatic Stage of Experimental Prion Disease in Mice. Journal of microbiology and biotechnology. vol 26. issue 9. 2017-05-23. PMID:27221113. |
this study supports the congruence of prp(sc) inhibition by polylysine in both the spleen and brain. |
2017-05-23 |
2023-08-13 |
mouse |
| Maura Cescatti, Daniela Saverioni, Sabina Capellari, Fabrizio Tagliavini, Tetsuyuki Kitamoto, James Ironside, Armin Giese, Piero Parch. Analysis of Conformational Stability of Abnormal Prion Protein Aggregates across the Spectrum of Creutzfeldt-Jakob Disease Prions. Journal of virology. vol 90. issue 14. 2017-05-18. PMID:27122583. |
the wide phenotypic variability of prion diseases is thought to depend on the interaction of a host genotype with prion strains that have self-perpetuating biological properties enciphered in distinct conformations of the misfolded prion protein prp(sc) this concept is largely based on indirect approaches studying the effect of proteases or denaturing agents on the physicochemical properties of prp(sc) aggregates. |
2017-05-18 |
2023-08-13 |
Not clear |
| Maura Cescatti, Daniela Saverioni, Sabina Capellari, Fabrizio Tagliavini, Tetsuyuki Kitamoto, James Ironside, Armin Giese, Piero Parch. Analysis of Conformational Stability of Abnormal Prion Protein Aggregates across the Spectrum of Creutzfeldt-Jakob Disease Prions. Journal of virology. vol 90. issue 14. 2017-05-18. PMID:27122583. |
to fill this gap, we studied the effects of guanidine hydrochloride (gdnhcl) and heating on prp(sc) aggregates extracted from 60 sporadic creutzfeldt-jakob disease (cjd) and 6 variant cjd brains. |
2017-05-18 |
2023-08-13 |
Not clear |
| Maura Cescatti, Daniela Saverioni, Sabina Capellari, Fabrizio Tagliavini, Tetsuyuki Kitamoto, James Ironside, Armin Giese, Piero Parch. Analysis of Conformational Stability of Abnormal Prion Protein Aggregates across the Spectrum of Creutzfeldt-Jakob Disease Prions. Journal of virology. vol 90. issue 14. 2017-05-18. PMID:27122583. |
while denaturation curves obtained after exposure of prp(sc) to increasing gdnhcl concentrations showed similar profiles among the 7 cjd types analyzed, prp(sc) exposure to increasing temperature revealed significantly different and type-specific responses. |
2017-05-18 |
2023-08-13 |
Not clear |
| Maura Cescatti, Daniela Saverioni, Sabina Capellari, Fabrizio Tagliavini, Tetsuyuki Kitamoto, James Ironside, Armin Giese, Piero Parch. Analysis of Conformational Stability of Abnormal Prion Protein Aggregates across the Spectrum of Creutzfeldt-Jakob Disease Prions. Journal of virology. vol 90. issue 14. 2017-05-18. PMID:27122583. |
in particular, mm1 and vv2, the most prevalent and fast-replicating cjd types, showed stable and highly resistant prp(sc) aggregates, whereas vv1, a rare and slowly propagating type, revealed unstable aggregates that easily dissolved at low temperature. |
2017-05-18 |
2023-08-13 |
Not clear |
| Maura Cescatti, Daniela Saverioni, Sabina Capellari, Fabrizio Tagliavini, Tetsuyuki Kitamoto, James Ironside, Armin Giese, Piero Parch. Analysis of Conformational Stability of Abnormal Prion Protein Aggregates across the Spectrum of Creutzfeldt-Jakob Disease Prions. Journal of virology. vol 90. issue 14. 2017-05-18. PMID:27122583. |
taken together, our results indicate that the molecular interactions mediating the aggregation state of prp(sc), possibly enciphering strain diversity, are differently targeted by gdnhcl, temperature, and proteases. |
2017-05-18 |
2023-08-13 |
Not clear |
| Maura Cescatti, Daniela Saverioni, Sabina Capellari, Fabrizio Tagliavini, Tetsuyuki Kitamoto, James Ironside, Armin Giese, Piero Parch. Analysis of Conformational Stability of Abnormal Prion Protein Aggregates across the Spectrum of Creutzfeldt-Jakob Disease Prions. Journal of virology. vol 90. issue 14. 2017-05-18. PMID:27122583. |
furthermore, the detected positive correlation between the thermostability of prp(sc) aggregates and disease transmission efficiency makes inconsistent the proposed hypothesis that a decrease in conformational stability of prions results in an increase in their replication efficiency. |
2017-05-18 |
2023-08-13 |
Not clear |
| M Heather West Greenlee, Melissa Lind, Robyn Kokemuller, Najiba Mammadova, Naveen Kondru, Sireesha Manne, Jodi Smith, Anumantha Kanthasamy, Justin Greenle. Temporal Resolution of Misfolded Prion Protein Transport, Accumulation, Glial Activation, and Neuronal Death in the Retinas of Mice Inoculated with Scrapie. The American journal of pathology. vol 186. issue 9. 2017-05-16. PMID:27521336. |
our goal was to use an experimental model to determine the temporal relationship between the transport of misfolded prion protein (prp(sc)) from the brain to the retina, the accumulation of prp(sc) in the retina, the response of the surrounding retinal tissue, and loss of neurons. |
2017-05-16 |
2023-08-13 |
mouse |
| M Heather West Greenlee, Melissa Lind, Robyn Kokemuller, Najiba Mammadova, Naveen Kondru, Sireesha Manne, Jodi Smith, Anumantha Kanthasamy, Justin Greenle. Temporal Resolution of Misfolded Prion Protein Transport, Accumulation, Glial Activation, and Neuronal Death in the Retinas of Mice Inoculated with Scrapie. The American journal of pathology. vol 186. issue 9. 2017-05-16. PMID:27521336. |
antibody staining was used to assess accumulation of prp(sc) and the resulting response of retinal tissue. |
2017-05-16 |
2023-08-13 |
mouse |
| M Heather West Greenlee, Melissa Lind, Robyn Kokemuller, Najiba Mammadova, Naveen Kondru, Sireesha Manne, Jodi Smith, Anumantha Kanthasamy, Justin Greenle. Temporal Resolution of Misfolded Prion Protein Transport, Accumulation, Glial Activation, and Neuronal Death in the Retinas of Mice Inoculated with Scrapie. The American journal of pathology. vol 186. issue 9. 2017-05-16. PMID:27521336. |
prp(sc) seeding activity was first detected in all samples at 60 dpi. |
2017-05-16 |
2023-08-13 |
mouse |