| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Ilaria Poggiolini, Daniela Saverioni, Piero Parch. Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions. International journal of cell biology. vol 2013. 2014-06-24. PMID:24454379. |
prion strains are tse isolates that, after inoculation into syngenic hosts, cause disease with distinct characteristics, such as incubation period, pattern of prp(sc) distribution, and regional severity of histopathological changes in the brain. |
2014-06-24 |
2023-08-12 |
Not clear |
| Ilaria Poggiolini, Daniela Saverioni, Piero Parch. Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions. International journal of cell biology. vol 2013. 2014-06-24. PMID:24454379. |
in analogy with other amyloid forming proteins, prp(sc) toxicity is thought to derive from the existence of various intermediate structures prior to the amyloid fiber formation and/or their specific interaction with membranes. |
2014-06-24 |
2023-08-12 |
Not clear |
| Ilaria Poggiolini, Daniela Saverioni, Piero Parch. Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions. International journal of cell biology. vol 2013. 2014-06-24. PMID:24454379. |
the latter appears particularly relevant for the pathogenesis of tses associated with gpi-anchored prp(sc), which involves major cellular membrane distortions in neurons. |
2014-06-24 |
2023-08-12 |
Not clear |
| Ilaria Poggiolini, Daniela Saverioni, Piero Parch. Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions. International journal of cell biology. vol 2013. 2014-06-24. PMID:24454379. |
in this review, we update the current knowledge on the molecular mechanisms underlying three fundamental aspects of the basic biology of prions such as the putative mechanism of prion protein conversion to the pathogenic form prp(sc) and its propagation, the molecular basis of prion strains, and the mechanism of induced neurotoxicity by prp(sc) aggregates. |
2014-06-24 |
2023-08-12 |
Not clear |
| Wu-Ling Xie, Qi Shi, Jin Zhang, Bao-Yun Zhang, Han-Shi Gong, Yan Guo, Shao-Bin Wang, Yin Xu, Ke Wang, Cao Chen, Yong Liu, Xiao-Ping Don. Abnormal activation of microglia accompanied with disrupted CX3CR1/CX3CL1 pathway in the brains of the hamsters infected with scrapie agent 263K. Journal of molecular neuroscience : MN. vol 51. issue 3. 2014-06-23. PMID:23526370. |
however, the detailed regional distribution between microglia and prp(sc) deposition has not been presented, and investigation of fractalkine signaling which is involved in the regulation of activation of microglia in prion disease is not well documented. |
2014-06-23 |
2023-08-12 |
rat |
| Wu-Ling Xie, Qi Shi, Jin Zhang, Bao-Yun Zhang, Han-Shi Gong, Yan Guo, Shao-Bin Wang, Yin Xu, Ke Wang, Cao Chen, Yong Liu, Xiao-Ping Don. Abnormal activation of microglia accompanied with disrupted CX3CR1/CX3CL1 pathway in the brains of the hamsters infected with scrapie agent 263K. Journal of molecular neuroscience : MN. vol 51. issue 3. 2014-06-23. PMID:23526370. |
under the dynamic analysis on hallmarks of activation of microglia, a time-dependent increase of iba1 and cd68 was detected, accompanied by accumulation of prp(sc) and progression of neurodegenerative symptoms. |
2014-06-23 |
2023-08-12 |
rat |
| Wu-Ling Xie, Qi Shi, Jin Zhang, Bao-Yun Zhang, Han-Shi Gong, Yan Guo, Shao-Bin Wang, Yin Xu, Ke Wang, Cao Chen, Yong Liu, Xiao-Ping Don. Abnormal activation of microglia accompanied with disrupted CX3CR1/CX3CL1 pathway in the brains of the hamsters infected with scrapie agent 263K. Journal of molecular neuroscience : MN. vol 51. issue 3. 2014-06-23. PMID:23526370. |
with serial brain sections and double staining of iba1 and prp(sc), we observed that the microglia distributed around prp(sc) deposits in 263k-infected hamsters' brains, proposing prp(sc) phagocytosis. |
2014-06-23 |
2023-08-12 |
rat |
| XiuJin Yang, LiFeng Yang, XiangMei Zhou, Sher Hayat Khan, HuiNuan Wang, XiaoMin Yin, Zhen Yuan, ZhiQi Song, WenYu Wu, DeMing Zha. Using protein misfolding cyclic amplification generates a highly neurotoxic PrP dimer causing neurodegeneration. Journal of molecular neuroscience : MN. vol 51. issue 3. 2014-06-23. PMID:23771785. |
under the "protein-only" hypothesis, prion-based diseases are proposed to result from an infectious agent that is an abnormal isoform of the prion protein in the scrapie form, prp(sc). |
2014-06-23 |
2023-08-12 |
Not clear |
| XiuJin Yang, LiFeng Yang, XiangMei Zhou, Sher Hayat Khan, HuiNuan Wang, XiaoMin Yin, Zhen Yuan, ZhiQi Song, WenYu Wu, DeMing Zha. Using protein misfolding cyclic amplification generates a highly neurotoxic PrP dimer causing neurodegeneration. Journal of molecular neuroscience : MN. vol 51. issue 3. 2014-06-23. PMID:23771785. |
however, since prp(sc) is highly insoluble and easily aggregates in vivo, this view appears to be overly simplistic, implying that the presence of prp(sc) may indirectly cause neurodegeneration through its intermediate soluble form. |
2014-06-23 |
2023-08-12 |
Not clear |
| XiuJin Yang, LiFeng Yang, XiangMei Zhou, Sher Hayat Khan, HuiNuan Wang, XiaoMin Yin, Zhen Yuan, ZhiQi Song, WenYu Wu, DeMing Zha. Using protein misfolding cyclic amplification generates a highly neurotoxic PrP dimer causing neurodegeneration. Journal of molecular neuroscience : MN. vol 51. issue 3. 2014-06-23. PMID:23771785. |
we generated a neurotoxic prp dimer with partial pathogenic characteristics of prp(sc) by protein misfolding cyclic amplification in the presence of 1-palmitoyl-2-oleoylphosphatidylglycerol consisting of recombinant hamster prp (23-231). |
2014-06-23 |
2023-08-12 |
Not clear |
| Ke Wang, Jin Zhang, Yin Xu, Ke Ren, Wu-Ling Xie, Yu-E Yan, Bao-Yun Zhang, Qi Shi, Yong Liu, Xiao-Ping Don. Abnormally upregulated αB-crystallin was highly coincidental with the astrogliosis in the brains of scrapie-infected hamsters and human patients with prion diseases. Journal of molecular neuroscience : MN. vol 51. issue 3. 2014-06-23. PMID:23832485. |
ihc and ifa of the serial brain sections of infected hamsters showed no colocalization and correlation between prp(sc) deposits and αb-crystallin increase. |
2014-06-23 |
2023-08-12 |
human |
| Allen Herbst, Pamela Banser, Camilo Duque Velasquez, Charles E Mays, Valerie L Sim, David Westaway, Judd M Aiken, Debbie McKenzi. Infectious prions accumulate to high levels in non proliferative C2C12 myotubes. PLoS pathogens. vol 9. issue 11. 2014-06-23. PMID:24244171. |
prion diseases are driven by the strain-specific, template-dependent transconformation of the normal cellular prion protein (prp(c)) into a disease specific isoform prp(sc). |
2014-06-23 |
2023-08-12 |
Not clear |
| Allen Herbst, Pamela Banser, Camilo Duque Velasquez, Charles E Mays, Valerie L Sim, David Westaway, Judd M Aiken, Debbie McKenzi. Infectious prions accumulate to high levels in non proliferative C2C12 myotubes. PLoS pathogens. vol 9. issue 11. 2014-06-23. PMID:24244171. |
using non-replicating cells allows the accumulation of higher levels of prp(sc) and, thus, greater amounts of infectivity. |
2014-06-23 |
2023-08-12 |
Not clear |
| Allen Herbst, Pamela Banser, Camilo Duque Velasquez, Charles E Mays, Valerie L Sim, David Westaway, Judd M Aiken, Debbie McKenzi. Infectious prions accumulate to high levels in non proliferative C2C12 myotubes. PLoS pathogens. vol 9. issue 11. 2014-06-23. PMID:24244171. |
we demonstrate that prion-infected myotubes generate substantial amounts of prp(sc) and that the level of infectivity produced in these post-mitotic cells, 10(5.5) l.d.50/mg of total protein, approaches that observed in vivo. |
2014-06-23 |
2023-08-12 |
Not clear |
| Jifeng Bian, Hae-Eun Kang, Glenn C Tellin. Quinacrine promotes replication and conformational mutation of chronic wasting disease prions. Proceedings of the National Academy of Sciences of the United States of America. vol 111. issue 16. 2014-06-17. PMID:24711410. |
quinacrine's ability to reduce levels of pathogenic prion protein (prp(sc)) in mouse cells infected with experimentally adapted prions led to several unsuccessful clinical studies in patients with prion diseases, a 10-y investment to understand its mechanism of action, and the production of related compounds with expectations of greater efficacy. |
2014-06-17 |
2023-08-13 |
mouse |
| Jifeng Bian, Hae-Eun Kang, Glenn C Tellin. Quinacrine promotes replication and conformational mutation of chronic wasting disease prions. Proceedings of the National Academy of Sciences of the United States of America. vol 111. issue 16. 2014-06-17. PMID:24711410. |
we show here, in stark contrast to this reported inhibitory effect, that quinacrine enhances deer and elk prp(sc) accumulation and promotes propagation of prions causing chronic wasting disease (cwd), a fatal, transmissible, neurodegenerative disorder of cervids of uncertain zoonotic potential. |
2014-06-17 |
2023-08-13 |
mouse |
| Jifeng Bian, Hae-Eun Kang, Glenn C Tellin. Quinacrine promotes replication and conformational mutation of chronic wasting disease prions. Proceedings of the National Academy of Sciences of the United States of America. vol 111. issue 16. 2014-06-17. PMID:24711410. |
surprisingly, despite increased prion titers in quinacrine-treated cells, transmission of the resulting prions produced prolonged incubation times and altered prp(sc) deposition patterns in the brains of diseased transgenic mice. |
2014-06-17 |
2023-08-13 |
mouse |
| Jifeng Bian, Hae-Eun Kang, Glenn C Tellin. Quinacrine promotes replication and conformational mutation of chronic wasting disease prions. Proceedings of the National Academy of Sciences of the United States of America. vol 111. issue 16. 2014-06-17. PMID:24711410. |
accordingly, quinacrine-treated cwd prions were comprised of an altered prp(sc) conformation. |
2014-06-17 |
2023-08-13 |
mouse |
| Rob Goold, Chris McKinnon, Samira Rabbanian, John Collinge, Giampietro Schiavo, Sarah J Tabriz. Alternative fates of newly formed PrPSc upon prion conversion on the plasma membrane. Journal of cell science. vol 126. issue Pt 16. 2014-06-15. PMID:23813960. |
prion diseases are fatal neurodegenerative diseases characterised by the accumulation of misfolded prion protein (prp(sc)) in the brain. |
2014-06-15 |
2023-08-12 |
human |
| Rob Goold, Chris McKinnon, Samira Rabbanian, John Collinge, Giampietro Schiavo, Sarah J Tabriz. Alternative fates of newly formed PrPSc upon prion conversion on the plasma membrane. Journal of cell science. vol 126. issue Pt 16. 2014-06-15. PMID:23813960. |
they are caused by the templated misfolding of normal cellular protein, prp(c), by prp(sc). |
2014-06-15 |
2023-08-12 |
human |