| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Elizaveta Katorcha, Natallia Makarava, Regina Savtchenko, Ilia V Baskako. Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio. Scientific reports. vol 5. 2016-09-15. PMID:26576925. |
however, when partially desialylated prp(c) was used as a substrate, recruitment of three glycoforms into prp(sc) was found to be proportional to their respective populations in the substrate. |
2016-09-15 |
2023-08-13 |
Not clear |
| Natallia Makarava, Regina Savtchenko, Irina Alexeeva, Robert G Rohwer, Ilia V Baskako. New Molecular Insight into Mechanism of Evolution of Mammalian Synthetic Prions. The American journal of pathology. vol 186. issue 4. 2016-09-06. PMID:26873446. |
previous studies established that transmissible prion diseases could be induced by in vitro-produced recombinant prion protein (prp) fibrils with structures that are fundamentally different from that of authentic prp scrapie isoform (prp(sc)). |
2016-09-06 |
2023-08-13 |
mouse |
| Natallia Makarava, Regina Savtchenko, Irina Alexeeva, Robert G Rohwer, Ilia V Baskako. New Molecular Insight into Mechanism of Evolution of Mammalian Synthetic Prions. The American journal of pathology. vol 186. issue 4. 2016-09-06. PMID:26873446. |
however, overexpression of prp(c) did not facilitate the second step of synthetic strain evolution-transition from atypical prpres to prp(sc), which is attributed to the stochastic nature of rare deformed templating events. |
2016-09-06 |
2023-08-13 |
mouse |
| Daniela Valensin, Emilia Maria Padula, Aleksandra Hecel, Marek Luczkowski, Henryk Kozlowsk. Specific binding modes of Cu(I) and Ag(I) with neurotoxic domain of the human prion protein. Journal of inorganic biochemistry. vol 155. 2016-08-26. PMID:26606290. |
prion diseases are neurodegenerative disorders associated with a conformational change of the normal cellular isoform of the prion protein (prp(c)) to an abnormal scrapie isoform (prp(sc)). |
2016-08-26 |
2023-08-13 |
human |
| Ilia V Baskakov, Elizaveta Katorch. Multifaceted Role of Sialylation in Prion Diseases. Frontiers in neuroscience. vol 10. 2016-08-23. PMID:27551257. |
mammalian prion or prp(sc) is a proteinaceous infectious agent that consists of a misfolded, self-replicating state of a sialoglycoprotein called the prion protein, or prp(c). |
2016-08-23 |
2023-08-13 |
Not clear |
| Ilia V Baskakov, Elizaveta Katorch. Multifaceted Role of Sialylation in Prion Diseases. Frontiers in neuroscience. vol 10. 2016-08-23. PMID:27551257. |
first, we discuss the correlation between sialylation of prp(sc) glycans and prion infectivity and describe the factors that control sialylation of prp(sc). |
2016-08-23 |
2023-08-13 |
Not clear |
| Ilia V Baskakov, Elizaveta Katorch. Multifaceted Role of Sialylation in Prion Diseases. Frontiers in neuroscience. vol 10. 2016-08-23. PMID:27551257. |
second, we explain how glycan sialylation contributes to the prion replication barrier, defines strain-specific glycoform ratios, and imposes constraints for prp(sc) structure. |
2016-08-23 |
2023-08-13 |
Not clear |
| Jae Wook Hyeon, Jiwon Choi, Su Yeon Kim, Rajiv Gandhi Govindaraj, Kyu Jam Hwang, Yeong Seon Lee, Seong Soo A An, Myung Koo Lee, Jong Young Joung, Kyoung Tai No, Jeongmin Le. Discovery of Novel Anti-prion Compounds Using In Silico and In Vitro Approaches. Scientific reports. vol 5. 2016-08-17. PMID:26449325. |
prion diseases are associated with the conformational conversion of the physiological form of cellular prion protein (prp(c)) to the pathogenic form, prp(sc). |
2016-08-17 |
2023-08-13 |
Not clear |
| Jae Wook Hyeon, Jiwon Choi, Su Yeon Kim, Rajiv Gandhi Govindaraj, Kyu Jam Hwang, Yeong Seon Lee, Seong Soo A An, Myung Koo Lee, Jong Young Joung, Kyoung Tai No, Jeongmin Le. Discovery of Novel Anti-prion Compounds Using In Silico and In Vitro Approaches. Scientific reports. vol 5. 2016-08-17. PMID:26449325. |
compounds that inhibit this process by blocking conversion to the prp(sc) could provide useful anti-prion therapies. |
2016-08-17 |
2023-08-13 |
Not clear |
| Jae Wook Hyeon, Jiwon Choi, Su Yeon Kim, Rajiv Gandhi Govindaraj, Kyu Jam Hwang, Yeong Seon Lee, Seong Soo A An, Myung Koo Lee, Jong Young Joung, Kyoung Tai No, Jeongmin Le. Discovery of Novel Anti-prion Compounds Using In Silico and In Vitro Approaches. Scientific reports. vol 5. 2016-08-17. PMID:26449325. |
some compounds effectively reduced prp(sc) levels and one of these compounds also showed a high binding affinity for prp(c). |
2016-08-17 |
2023-08-13 |
Not clear |
| Timm Konold, Laura J Phelan, Saira Cawthraw, Marion M Simmons, Melanie J Chaplin, Lorenzo Gonzále. Abnormalities in Brainstem Auditory Evoked Potentials in Sheep with Transmissible Spongiform Encephalopathies and Lack of a Clear Pathological Relationship. Frontiers in veterinary science. vol 3. 2016-08-17. PMID:27532040. |
scrapie is transmissible spongiform encephalopathy (tse), which causes neurological signs in sheep, but confirmatory diagnosis is usually made postmortem on examination of the brain for tse-associated markers like vacuolar changes and disease-associated prion protein (prp(sc)). |
2016-08-17 |
2023-08-13 |
cattle |
| Timm Konold, Laura J Phelan, Saira Cawthraw, Marion M Simmons, Melanie J Chaplin, Lorenzo Gonzále. Abnormalities in Brainstem Auditory Evoked Potentials in Sheep with Transmissible Spongiform Encephalopathies and Lack of a Clear Pathological Relationship. Frontiers in veterinary science. vol 3. 2016-08-17. PMID:27532040. |
the proportion of sheep with abnormalities did not appear to be influenced by tse strain or prp(sc) gene polymorphisms. |
2016-08-17 |
2023-08-13 |
cattle |
| Timm Konold, Laura J Phelan, Saira Cawthraw, Marion M Simmons, Melanie J Chaplin, Lorenzo Gonzále. Abnormalities in Brainstem Auditory Evoked Potentials in Sheep with Transmissible Spongiform Encephalopathies and Lack of a Clear Pathological Relationship. Frontiers in veterinary science. vol 3. 2016-08-17. PMID:27532040. |
when the magnitude of tse-associated markers in the auditory pathways was compared between a subset of 12 sheep with and 12 sheep without baep abnormalities in group 2, no significant differences in the total prp(sc) or vacuolation scores in the auditory pathways could be found. |
2016-08-17 |
2023-08-13 |
cattle |
| Timm Konold, Laura J Phelan, Saira Cawthraw, Marion M Simmons, Melanie J Chaplin, Lorenzo Gonzále. Abnormalities in Brainstem Auditory Evoked Potentials in Sheep with Transmissible Spongiform Encephalopathies and Lack of a Clear Pathological Relationship. Frontiers in veterinary science. vol 3. 2016-08-17. PMID:27532040. |
however, the data suggested that there was a difference in the prp(sc) scores depending on the tse strain because prp(sc) scores were significantly higher in sheep with baep abnormalities infected with classical and l-type bse, but not with cs. |
2016-08-17 |
2023-08-13 |
cattle |
| Timm Konold, Laura J Phelan, Saira Cawthraw, Marion M Simmons, Melanie J Chaplin, Lorenzo Gonzále. Abnormalities in Brainstem Auditory Evoked Potentials in Sheep with Transmissible Spongiform Encephalopathies and Lack of a Clear Pathological Relationship. Frontiers in veterinary science. vol 3. 2016-08-17. PMID:27532040. |
the results indicated that baeps may be abnormal in sheep infected with tses but the test is not specific for tses and that neither vacuolation nor prp(sc) accumulation appears to be responsible for the clinical abnormalities. |
2016-08-17 |
2023-08-13 |
cattle |
| Jennifer T Burchell, Peter K Panegyre. Prion diseases: immunotargets and therapy. ImmunoTargets and therapy. vol 5. 2016-08-16. PMID:27529062. |
the causative agent is a misfolded version of the physiological prion protein called prp(sc) in the brain. |
2016-08-16 |
2023-08-13 |
human |
| Jennifer T Burchell, Peter K Panegyre. Prion diseases: immunotargets and therapy. ImmunoTargets and therapy. vol 5. 2016-08-16. PMID:27529062. |
vaccines utilizing antibodies generally target disease-specific epitopes that are only exposed in the misfolded prp(sc) conformation. |
2016-08-16 |
2023-08-13 |
human |
| Belinda B Guo, Shayne A Bellingham, Andrew F Hil. Stimulating the Release of Exosomes Increases the Intercellular Transfer of Prions. The Journal of biological chemistry. vol 291. issue 10. 2016-08-09. PMID:26769968. |
prion disease arises upon misfolding of the normal cellular prion protein, prp(c), into the disease-associated isoform, prp(sc). |
2016-08-09 |
2023-08-13 |
Not clear |
| Bruno Macedo, Ricardo Sant'Anna, Susanna Navarro, Yraima Cordeiro, Salvador Ventur. Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria. Microbial cell factories. vol 14. 2016-07-26. PMID:26536866. |
the structural conversion of the cellular prion protein (prp(c)), into its misfolded pathogenic form (prp(sc)) is the central event of prion-driven pathologies. |
2016-07-26 |
2023-08-13 |
Not clear |
| Rachel Pass, Karen Frudd, James P Barnett, Claudia A Blindauer, David R Brow. Prion infection in cells is abolished by a mutated manganese transporter but shows no relation to zinc. Molecular and cellular neurosciences. vol 68. 2016-07-11. PMID:26253862. |
in contrast we found that a gain of function mutant of a manganese transporter caused reduction of manganese levels in prion infected cells, loss of observable prp(sc) in cells and resistance to prion infection. |
2016-07-11 |
2023-08-13 |
Not clear |