All Relations between sc and nucleus prepositus

Publication Sentence Publish Date Extraction Date Species
Jenna Crowell, Andrew Hughson, Byron Caughey, Richard A Besse. Host Determinants of Prion Strain Diversity Independent of Prion Protein Genotype. Journal of virology. vol 89. issue 20. 2015-12-15. PMID:26246570. phenotypic diversity in prion diseases can be specified by prion strains in which biological traits are propagated through an epigenetic mechanism mediated by distinct prp(sc) conformations. 2015-12-15 2023-08-13 mouse
Jenna Crowell, Andrew Hughson, Byron Caughey, Richard A Besse. Host Determinants of Prion Strain Diversity Independent of Prion Protein Genotype. Journal of virology. vol 89. issue 20. 2015-12-15. PMID:26246570. limited proteinase k digestion revealed strain-specific prp(sc) polypeptide patterns that were maintained in both hosts, but the solubility and conformational stability of prp(sc) differed for the cwd strains in a host-dependent manner. 2015-12-15 2023-08-13 mouse
Jenna Crowell, Andrew Hughson, Byron Caughey, Richard A Besse. Host Determinants of Prion Strain Diversity Independent of Prion Protein Genotype. Journal of virology. vol 89. issue 20. 2015-12-15. PMID:26246570. wst cwd produced prp(sc) amyloid plaques in the brain of the sgh that were partially insoluble and stable at a high concentration of protein denaturant. 2015-12-15 2023-08-13 mouse
Jenna Crowell, Andrew Hughson, Byron Caughey, Richard A Besse. Host Determinants of Prion Strain Diversity Independent of Prion Protein Genotype. Journal of virology. vol 89. issue 20. 2015-12-15. PMID:26246570. however, in transgenic mice, prp(sc) from wst cwd did not assemble into plaques, was highly soluble, and had low conformational stability. 2015-12-15 2023-08-13 mouse
Jenna Crowell, Andrew Hughson, Byron Caughey, Richard A Besse. Host Determinants of Prion Strain Diversity Independent of Prion Protein Genotype. Journal of virology. vol 89. issue 20. 2015-12-15. PMID:26246570. similar studies using the hy and dy strains of transmissible mink encephalopathy resulted in minor differences in prion biological and prp(sc) properties between transgenic mice and sgh. 2015-12-15 2023-08-13 mouse
Jenna Crowell, Andrew Hughson, Byron Caughey, Richard A Besse. Host Determinants of Prion Strain Diversity Independent of Prion Protein Genotype. Journal of virology. vol 89. issue 20. 2015-12-15. PMID:26246570. these findings indicate that host-specific pathways that are independent of prnp can alter the prp(sc) conformation of certain prion strains, leading to changes in the biophysical properties of prp(sc), neuropathology, and clinical prion disease. 2015-12-15 2023-08-13 mouse
Elizaveta Katorcha, Natallia Makarava, Regina Savtchenko, Alessandra D'Azzo, Ilia V Baskako. Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity. PLoS pathogens. vol 10. issue 9. 2015-12-08. PMID:25211026. the central event underlying prion diseases involves conformational change of the cellular form of the prion protein (prp(c)) into the disease-associated, transmissible form (prp(sc)). 2015-12-08 2023-08-13 Not clear
Elizaveta Katorcha, Natallia Makarava, Regina Savtchenko, Alessandra D'Azzo, Ilia V Baskako. Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity. PLoS pathogens. vol 10. issue 9. 2015-12-08. PMID:25211026. the current work highlights the previously unappreciated role of sialylation of prp(c) glycans in prion pathogenesis, including its role in controlling prion replication rate, infectivity, cross-species barrier and prp(sc) glycoform ratio. 2015-12-08 2023-08-13 Not clear
Elizaveta Katorcha, Natallia Makarava, Regina Savtchenko, Alessandra D'Azzo, Ilia V Baskako. Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity. PLoS pathogens. vol 10. issue 9. 2015-12-08. PMID:25211026. as a result, pmcab-derived prp(sc) was less sialylated than brain-derived prp(sc). 2015-12-08 2023-08-13 Not clear
Elizaveta Katorcha, Natallia Makarava, Regina Savtchenko, Alessandra D'Azzo, Ilia V Baskako. Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity. PLoS pathogens. vol 10. issue 9. 2015-12-08. PMID:25211026. nevertheless, enzymatic de-sialylation of prp(c) using sialidase was found to increase the rate of prp(sc) amplification in pmcab from 10- to 10,000-fold in a strain-dependent manner. 2015-12-08 2023-08-13 Not clear
Elizaveta Katorcha, Natallia Makarava, Regina Savtchenko, Alessandra D'Azzo, Ilia V Baskako. Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity. PLoS pathogens. vol 10. issue 9. 2015-12-08. PMID:25211026. surprisingly, the sialylation status of prp(c) was also found to control prp(sc) glycoform ratio. 2015-12-08 2023-08-13 Not clear
Elizaveta Katorcha, Natallia Makarava, Regina Savtchenko, Alessandra D'Azzo, Ilia V Baskako. Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity. PLoS pathogens. vol 10. issue 9. 2015-12-08. PMID:25211026. a decrease in pr(pc) sialylation levels resulted in a higher percentage of the diglycosylated glycoform in prp(sc). 2015-12-08 2023-08-13 Not clear
Hanna Wolf, Andrea Graßmann, Romina Bester, André Hossinger, Christoph Möhl, Lydia Paulsen, Martin H Groschup, Hermann Schätzl, Ina Vorber. Modulation of Glycosaminoglycans Affects PrPSc Metabolism but Does Not Block PrPSc Uptake. Journal of virology. vol 89. issue 19. 2015-12-07. PMID:26202247. mammalian prions are unconventional infectious agents composed primarily of the misfolded aggregated host prion protein prp, termed prp(sc). 2015-12-07 2023-08-13 Not clear
Hanna Wolf, Andrea Graßmann, Romina Bester, André Hossinger, Christoph Möhl, Lydia Paulsen, Martin H Groschup, Hermann Schätzl, Ina Vorber. Modulation of Glycosaminoglycans Affects PrPSc Metabolism but Does Not Block PrPSc Uptake. Journal of virology. vol 89. issue 19. 2015-12-07. PMID:26202247. chemical or genetic manipulation of glycosaminoglycans did not prevent prp(sc) uptake, arguing against their roles as essential prion attachment sites. 2015-12-07 2023-08-13 Not clear
Hanna Wolf, Andrea Graßmann, Romina Bester, André Hossinger, Christoph Möhl, Lydia Paulsen, Martin H Groschup, Hermann Schätzl, Ina Vorber. Modulation of Glycosaminoglycans Affects PrPSc Metabolism but Does Not Block PrPSc Uptake. Journal of virology. vol 89. issue 19. 2015-12-07. PMID:26202247. however, both treatments effectively antagonized de novo prion infection independently of the prion strain and reduced prp(sc) formation in chronically infected cells. 2015-12-07 2023-08-13 Not clear
Hanna Wolf, Andrea Graßmann, Romina Bester, André Hossinger, Christoph Möhl, Lydia Paulsen, Martin H Groschup, Hermann Schätzl, Ina Vorber. Modulation of Glycosaminoglycans Affects PrPSc Metabolism but Does Not Block PrPSc Uptake. Journal of virology. vol 89. issue 19. 2015-12-07. PMID:26202247. our results demonstrate that sulfated glycosaminoglycans are dispensable for prion internalization but play a pivotal role in persistently maintained prp(sc) formation independent of the prion strain. 2015-12-07 2023-08-13 Not clear
Hermann C Altmeppen, Johannes Prox, Susanne Krasemann, Berta Puig, Katharina Kruszewski, Frank Dohler, Christian Bernreuther, Ana Hoxha, Luise Linsenmeier, Beata Sikorska, Pawel P Liberski, Udo Bartsch, Paul Saftig, Markus Glatze. The sheddase ADAM10 is a potent modulator of prion disease. eLife. vol 4. 2015-12-03. PMID:25654651. the prion protein (prp(c)) is highly expressed in the nervous system and critically involved in prion diseases where it misfolds into pathogenic prp(sc). 2015-12-03 2023-08-13 mouse
Hermann C Altmeppen, Johannes Prox, Susanne Krasemann, Berta Puig, Katharina Kruszewski, Frank Dohler, Christian Bernreuther, Ana Hoxha, Luise Linsenmeier, Beata Sikorska, Pawel P Liberski, Udo Bartsch, Paul Saftig, Markus Glatze. The sheddase ADAM10 is a potent modulator of prion disease. eLife. vol 4. 2015-12-03. PMID:25654651. upon prion infection of these mice, clinical, biochemical, and morphological data reveal that lack of adam10 significantly reduces incubation times and increases prp(sc) formation. 2015-12-03 2023-08-13 mouse
Qi Shi, Kang Xiao, Bao-Yun Zhang, Xiao-Mei Zhang, Li-Na Chen, Cao Chen, Chen Gao, Xiao-Ping Don. Successive passaging of the scrapie strains, ME7-ha and 139A-ha, generated by the interspecies transmission of mouse-adapted strains into hamsters markedly shortens the incubation times, but maintains their molecular and pathological properties. International journal of molecular medicine. vol 35. issue 4. 2015-12-01. PMID:25683243. the glycosylation patterns of brain prp(sc) in the animals infected with the 2nd passage of those 2 strains maintained similar features as those in the animals infected with the 1st passage of those strains, with predominantly diglycosylated prp(sc). 2015-12-01 2023-08-13 mouse
Qi Shi, Kang Xiao, Bao-Yun Zhang, Xiao-Mei Zhang, Li-Na Chen, Cao Chen, Chen Gao, Xiao-Ping Don. Successive passaging of the scrapie strains, ME7-ha and 139A-ha, generated by the interspecies transmission of mouse-adapted strains into hamsters markedly shortens the incubation times, but maintains their molecular and pathological properties. International journal of molecular medicine. vol 35. issue 4. 2015-12-01. PMID:25683243. neuropathological assays revealed comparable spongiform degeneration and microglia proliferation in the brain tissues from the infected mice and hamsters, but markedly more plaque-like deposits of prp(sc) and more severe astrogliosis in the brains of the hamster. 2015-12-01 2023-08-13 mouse