| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| 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. |
accumulation of prp(sc) and coincident activation of retinal glia were first detected at 90 dpi. |
2017-05-16 |
2023-08-13 |
mouse |
| Rie Hasebe, Misaki Tanaka, Akio Suzuki, Takeshi Yamasaki, Motohiro Horiuch. Complement factors alter the amount of PrP(Sc) in primary-cultured mouse cortical neurons associated with increased membrane permeability. Virology. vol 496. 2017-05-04. PMID:27236741. |
complement factors alter the amount of prp(sc) in primary-cultured mouse cortical neurons associated with increased membrane permeability. |
2017-05-04 |
2023-08-13 |
mouse |
| Rie Hasebe, Misaki Tanaka, Akio Suzuki, Takeshi Yamasaki, Motohiro Horiuch. Complement factors alter the amount of PrP(Sc) in primary-cultured mouse cortical neurons associated with increased membrane permeability. Virology. vol 496. 2017-05-04. PMID:27236741. |
the amount of protease k (pk)-resistant abnormal form of prion protein (prp(sc)) reached a maximum level at 12 and 16 days post exposure (dpe) in 22l- and chandler-infected neurons, respectively. |
2017-05-04 |
2023-08-13 |
mouse |
| Rie Hasebe, Misaki Tanaka, Akio Suzuki, Takeshi Yamasaki, Motohiro Horiuch. Complement factors alter the amount of PrP(Sc) in primary-cultured mouse cortical neurons associated with increased membrane permeability. Virology. vol 496. 2017-05-04. PMID:27236741. |
this was followed by a decrease of pk-resistant prp(sc) at 16 and 20dpe. |
2017-05-04 |
2023-08-13 |
mouse |
| Rie Hasebe, Misaki Tanaka, Akio Suzuki, Takeshi Yamasaki, Motohiro Horiuch. Complement factors alter the amount of PrP(Sc) in primary-cultured mouse cortical neurons associated with increased membrane permeability. Virology. vol 496. 2017-05-04. PMID:27236741. |
membrane permeability also increased in 22l-infected neurons by reaction of complement factor c3, but interestingly, the amount of pk-resistant prp(sc) initially decreased, and then increased. |
2017-05-04 |
2023-08-13 |
mouse |
| Rie Hasebe, Misaki Tanaka, Akio Suzuki, Takeshi Yamasaki, Motohiro Horiuch. Complement factors alter the amount of PrP(Sc) in primary-cultured mouse cortical neurons associated with increased membrane permeability. Virology. vol 496. 2017-05-04. PMID:27236741. |
these results suggest that the reactivity of complement factors in prion-infected neurons depends on the amount of prp(sc) and the prion strain. |
2017-05-04 |
2023-08-13 |
mouse |
| Elizaveta Katorcha, Saurabh Srivastava, Nina Klimova, Ilia V Baskako. Sialylation of Glycosylphosphatidylinositol (GPI) Anchors of Mammalian Prions Is Regulated in a Host-, Tissue-, and Cell-specific Manner. The Journal of biological chemistry. vol 291. issue 33. 2017-05-04. PMID:27317661. |
prions or prp(sc) are proteinaceous infectious agents that consist of misfolded, self-replicating states of the prion protein or prp(c) prp(c) is posttranslationally modified with n-linked glycans and a sialylated glycosylphosphatidylinositol (gpi) anchor. |
2017-05-04 |
2023-08-13 |
Not clear |
| Elizaveta Katorcha, Saurabh Srivastava, Nina Klimova, Ilia V Baskako. Sialylation of Glycosylphosphatidylinositol (GPI) Anchors of Mammalian Prions Is Regulated in a Host-, Tissue-, and Cell-specific Manner. The Journal of biological chemistry. vol 291. issue 33. 2017-05-04. PMID:27317661. |
conformational conversion of prp(c) gives rise to glycosylated and gpi-anchored prp(sc) the question of the sialylation status of gpis within prp(sc) has been controversial. |
2017-05-04 |
2023-08-13 |
Not clear |
| Elizaveta Katorcha, Saurabh Srivastava, Nina Klimova, Ilia V Baskako. Sialylation of Glycosylphosphatidylinositol (GPI) Anchors of Mammalian Prions Is Regulated in a Host-, Tissue-, and Cell-specific Manner. The Journal of biological chemistry. vol 291. issue 33. 2017-05-04. PMID:27317661. |
previous studies that examined scrapie brains reported that both sialo- and asialo-gpis were present in prp(sc), with the majority being asialo-gpis. |
2017-05-04 |
2023-08-13 |
Not clear |
| Elizaveta Katorcha, Saurabh Srivastava, Nina Klimova, Ilia V Baskako. Sialylation of Glycosylphosphatidylinositol (GPI) Anchors of Mammalian Prions Is Regulated in a Host-, Tissue-, and Cell-specific Manner. The Journal of biological chemistry. vol 291. issue 33. 2017-05-04. PMID:27317661. |
in contrast, recent work that employed cultured cells claimed that only prp(c) with sialylo-gpis could be recruited into prp(sc), whereas prp(c) with asialo-gpis inhibited conversion. |
2017-05-04 |
2023-08-13 |
Not clear |
| Elizaveta Katorcha, Saurabh Srivastava, Nina Klimova, Ilia V Baskako. Sialylation of Glycosylphosphatidylinositol (GPI) Anchors of Mammalian Prions Is Regulated in a Host-, Tissue-, and Cell-specific Manner. The Journal of biological chemistry. vol 291. issue 33. 2017-05-04. PMID:27317661. |
to resolve this controversy, we analyzed the sialylation status of gpis within prp(sc) generated in the brain, spleen, or cultured n2a or c2c12 myotube cells. |
2017-05-04 |
2023-08-13 |
Not clear |
| Elizaveta Katorcha, Saurabh Srivastava, Nina Klimova, Ilia V Baskako. Sialylation of Glycosylphosphatidylinositol (GPI) Anchors of Mammalian Prions Is Regulated in a Host-, Tissue-, and Cell-specific Manner. The Journal of biological chemistry. vol 291. issue 33. 2017-05-04. PMID:27317661. |
we found that recruiting prp(c) with both sialo- and asialo-gpis is a common feature of prp(sc) the mixtures of sialo- and asialo-gpis were observed in prp(sc) universally regardless of prion strain as well as host, tissue, or type of cells that produced prp(sc) remarkably, the proportion of sialo- versus asialo-gpis was found to be controlled by host, tissue, and cell type but not prion strain. |
2017-05-04 |
2023-08-13 |
Not clear |
| Elizaveta Katorcha, Saurabh Srivastava, Nina Klimova, Ilia V Baskako. Sialylation of Glycosylphosphatidylinositol (GPI) Anchors of Mammalian Prions Is Regulated in a Host-, Tissue-, and Cell-specific Manner. The Journal of biological chemistry. vol 291. issue 33. 2017-05-04. PMID:27317661. |
instead, this work suggests that the sialylation status of gpis within prp(sc) is regulated in a cell-, tissue-, or host-specific manner and is likely to be determined by the specifics of gpi biosynthesis. |
2017-05-04 |
2023-08-13 |
Not clear |
| Katie A Langenfeld, Ronald A Shikiya, Anthony E Kincaid, Jason C Bart. Incongruity between Prion Conversion and Incubation Period following Coinfection. Journal of virology. vol 90. issue 12. 2017-05-03. PMID:27053546. |
first, we found that 139h is transported along the same neuroanatomical tracks as hy tme, adding to the growing body of evidence indicating that prp(sc) favors retrograde transneuronal transport. |
2017-05-03 |
2023-08-13 |
Not clear |
| Katie A Langenfeld, Ronald A Shikiya, Anthony E Kincaid, Jason C Bart. Incongruity between Prion Conversion and Incubation Period following Coinfection. Journal of virology. vol 90. issue 12. 2017-05-03. PMID:27053546. |
under conditions where 139h blocked hy tme from causing disease, the strain-specific properties of prp(sc) corresponded with the strain that caused disease, consistent with our previous findings. |
2017-05-03 |
2023-08-13 |
Not clear |
| Katie A Langenfeld, Ronald A Shikiya, Anthony E Kincaid, Jason C Bart. Incongruity between Prion Conversion and Incubation Period following Coinfection. Journal of virology. vol 90. issue 12. 2017-05-03. PMID:27053546. |
in the groups of animals where incubation periods were not altered, we found that the animals contained a mixture of 139h and hy tme prp(sc) this finding expands the definition of strain interference to include conditions where prp(sc) formation is altered yet disease outcome is unaltered. |
2017-05-03 |
2023-08-13 |
Not clear |
| Eri Saijo, Andrew G Hughson, Gregory J Raymond, Akio Suzuki, Motohiro Horiuchi, Byron Caughe. PrPSc-Specific Antibody Reveals C-Terminal Conformational Differences between Prion Strains. Journal of virology. vol 90. issue 10. 2017-04-26. PMID:26937029. |
understanding the structure of prp(sc) and its strain variation has been one of the major challenges in prion disease biology. |
2017-04-26 |
2023-08-13 |
mouse |
| Eri Saijo, Andrew G Hughson, Gregory J Raymond, Akio Suzuki, Motohiro Horiuchi, Byron Caughe. PrPSc-Specific Antibody Reveals C-Terminal Conformational Differences between Prion Strains. Journal of virology. vol 90. issue 10. 2017-04-26. PMID:26937029. |
to study the strain-dependent conformations of prp(sc), we purified proteinase-resistant prp(sc) (prp(res)) from mouse brains with three different murine-adapted scrapie strains (chandler, 22l, and me7) and systematically tested the accessibility of epitopes of a wide range of anti-prp and anti-prp(sc) specific antibodies by indirect enzyme-linked immunosorbent assay (elisa). |
2017-04-26 |
2023-08-13 |
mouse |
| Eri Saijo, Andrew G Hughson, Gregory J Raymond, Akio Suzuki, Motohiro Horiuchi, Byron Caughe. PrPSc-Specific Antibody Reveals C-Terminal Conformational Differences between Prion Strains. Journal of virology. vol 90. issue 10. 2017-04-26. PMID:26937029. |
however, reactivities to a prp(sc)-specific conformational c-terminal antibody showed significant differences among the three different prion strains. |
2017-04-26 |
2023-08-13 |
mouse |
| Eri Saijo, Andrew G Hughson, Gregory J Raymond, Akio Suzuki, Motohiro Horiuchi, Byron Caughe. PrPSc-Specific Antibody Reveals C-Terminal Conformational Differences between Prion Strains. Journal of virology. vol 90. issue 10. 2017-04-26. PMID:26937029. |
our results provide evidence for strain-dependent conformational variation near the c termini of molecules within prp(sc) multimers. |
2017-04-26 |
2023-08-13 |
mouse |