| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Rohana P Dassanayake, Thomas C Truscott, M Özgür Özyiğit, Dongyue Zhuang, David A Schneider, Katherine I O'Rourk. Accumulation profiles of PrP(Sc) in hemal nodes of naturally and experimentally scrapie-infected sheep. BMC veterinary research. vol 9. 2013-12-10. PMID:23601183. |
although prp(sc) accumulation profiles are well-characterized in ovine lymphoid tissues, there is limited information on such profiles in hemal nodes. |
2013-12-10 |
2023-08-12 |
Not clear |
| Rohana P Dassanayake, Thomas C Truscott, M Özgür Özyiğit, Dongyue Zhuang, David A Schneider, Katherine I O'Rourk. Accumulation profiles of PrP(Sc) in hemal nodes of naturally and experimentally scrapie-infected sheep. BMC veterinary research. vol 9. 2013-12-10. PMID:23601183. |
therefore, the objective of this study was to compare the follicular accumulation of prp(sc) within hemal nodes and lymph nodes by prion epitope mapping and western blot studies. |
2013-12-10 |
2023-08-12 |
Not clear |
| Jodi D Smith, Eric M Nicholson, Justin J Greenle. Evaluation of a combinatorial approach to prion inactivation using an oxidizing agent, SDS, and proteinase K. BMC veterinary research. vol 9. 2013-12-10. PMID:23886483. |
we recently demonstrated that exposure of the rml scrapie agent to a commercial product containing sodium percarbonate (spc-p) with or without sodium dodecyl sulfate (sds) rendered prp(sc) sensitive to proteinase k (pk), but did not eliminate infectivity. |
2013-12-10 |
2023-08-12 |
mouse |
| Jodi D Smith, Eric M Nicholson, Justin J Greenle. Evaluation of a combinatorial approach to prion inactivation using an oxidizing agent, SDS, and proteinase K. BMC veterinary research. vol 9. 2013-12-10. PMID:23886483. |
treated samples were evaluated for prp(sc)-immunoreactivity by western blot, and residual infectivity by mouse bioassay. |
2013-12-10 |
2023-08-12 |
mouse |
| Catherine E Vrentas, Justin J Greenlee, Thierry Baron, Maria Caramelli, Stefanie Czub, Eric M Nicholso. Stability properties of PrP(Sc) from cattle with experimental transmissible spongiform encephalopathies: use of a rapid whole homogenate, protease-free assay. BMC veterinary research. vol 9. 2013-12-10. PMID:23945217. |
stability properties of prp(sc) from cattle with experimental transmissible spongiform encephalopathies: use of a rapid whole homogenate, protease-free assay. |
2013-12-10 |
2023-08-12 |
cattle |
| Catherine E Vrentas, Justin J Greenlee, Thierry Baron, Maria Caramelli, Stefanie Czub, Eric M Nicholso. Stability properties of PrP(Sc) from cattle with experimental transmissible spongiform encephalopathies: use of a rapid whole homogenate, protease-free assay. BMC veterinary research. vol 9. 2013-12-10. PMID:23945217. |
transmissible spongiform encephalopathies (tses), including scrapie in sheep, chronic wasting disease (cwd) in cervids, transmissible mink encephalopathy (tme), and bovine spongiform encephalopathy (bse), are fatal diseases of the nervous system associated with accumulation of misfolded prion protein (prp(sc)). |
2013-12-10 |
2023-08-12 |
cattle |
| Catherine E Vrentas, Justin J Greenlee, Thierry Baron, Maria Caramelli, Stefanie Czub, Eric M Nicholso. Stability properties of PrP(Sc) from cattle with experimental transmissible spongiform encephalopathies: use of a rapid whole homogenate, protease-free assay. BMC veterinary research. vol 9. 2013-12-10. PMID:23945217. |
different strains of tses exist, associated with different prp(sc) conformations that can be probed by the stability assay, in which prp(sc) is treated with increasing concentrations of the denaturant guanidine hydrochloride (gdnhcl). |
2013-12-10 |
2023-08-12 |
cattle |
| Qi Shi, Yuan-Yuan Jing, Shao-Bin Wang, Cao Chen, Han Sun, Yin Xu, Chen Gao, Jin Zhang, Chan Tian, Yan Guo, Ke Ren, Xiao-Ping Don. PrP octarepeats region determined the interaction with caveolin-1 and phosphorylation of caveolin-1 and Fyn. Medical microbiology and immunology. vol 202. issue 3. 2013-12-09. PMID:23283514. |
with co-immunoprecipitation tests, prp(c)-cav-1 and prp(sc)-cav-1 complexes were identified in the brain homogenates of normal and scrapie agent 263k-infected hamsters, respectively. |
2013-12-09 |
2023-08-12 |
human |
| Qi Shi, Yuan-Yuan Jing, Shao-Bin Wang, Cao Chen, Han Sun, Yin Xu, Chen Gao, Jin Zhang, Chan Tian, Yan Guo, Ke Ren, Xiao-Ping Don. PrP octarepeats region determined the interaction with caveolin-1 and phosphorylation of caveolin-1 and Fyn. Medical microbiology and immunology. vol 202. issue 3. 2013-12-09. PMID:23283514. |
significant alterations in the cultured cells, either the distributions of prp and cav-1 morphologically or the up-regulations of p-cav-1 and p-fyn, induced by antibody-mediated cross-linking or fibrous forms of prp may suggest a possible internalization process of prp(sc). |
2013-12-09 |
2023-08-12 |
human |
| Zhu Lin, Deming Zhao, Lifeng Yan. Interaction between misfolded PrP and the ubiquitin-proteasome system in prion-mediated neurodegeneration. Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23449072. |
prion diseases are associated with the conformational conversion of cellular prion protein (prp(c)) to pathological β-sheet isoforms (prp(sc)), which is the infectious agent beyond comprehension. |
2013-12-09 |
2023-08-12 |
mouse |
| Zhu Lin, Deming Zhao, Lifeng Yan. Interaction between misfolded PrP and the ubiquitin-proteasome system in prion-mediated neurodegeneration. Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23449072. |
increasing evidence indicated that an unknown toxic gain of function of prp(sc) underlies neuronal death. |
2013-12-09 |
2023-08-12 |
mouse |
| Zhu Lin, Deming Zhao, Lifeng Yan. Interaction between misfolded PrP and the ubiquitin-proteasome system in prion-mediated neurodegeneration. Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23449072. |
furthermore, the common properties of β-sheet-rich isoform such as prp(sc) and β amyloid protein become the lynchpin that interprets the general pathological mechanism of protein misfolding diseases. |
2013-12-09 |
2023-08-12 |
mouse |
| Zhu Lin, Deming Zhao, Lifeng Yan. Interaction between misfolded PrP and the ubiquitin-proteasome system in prion-mediated neurodegeneration. Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23449072. |
both prp(c) and prp(sc) accumulate in cells after proteasome inhibition, which leads to increased cell death. |
2013-12-09 |
2023-08-12 |
mouse |
| Chan Tian, Xiaoping Don. The structure of prion: is it enough for interpreting the diverse phenotypes of prion diseases? Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23459557. |
the most accepted etiology for prion disease is 'prion', which arises from the conversion from cellular prp(c) to the pathological prp(sc). |
2013-12-09 |
2023-08-12 |
human |
| Chan Tian, Xiaoping Don. The structure of prion: is it enough for interpreting the diverse phenotypes of prion diseases? Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23459557. |
this review discussed the characteristic structure of prp, including prnp gene, prp(c), prp(sc), prp amyloid, and prion strains. |
2013-12-09 |
2023-08-12 |
human |
| Hao Yao, Deming Zhao, Sher Hayat Khan, Lifeng Yan. Role of autophagy in prion protein-induced neurodegenerative diseases. Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23459558. |
prion diseases, characterized by spongiform degeneration and the accumulation of misfolded and aggregated prp(sc) in the central nervous system, are one of fatal neurodegenerative and infectious disorders of humans and animals. |
2013-12-09 |
2023-08-12 |
Not clear |
| Hao Yao, Deming Zhao, Sher Hayat Khan, Lifeng Yan. Role of autophagy in prion protein-induced neurodegenerative diseases. Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23459558. |
in case of prion infection, increasing evidence indicates that autophagy has a crucial ability of eliminating pathological prp(sc) accumulated within neurons. |
2013-12-09 |
2023-08-12 |
Not clear |
| Pei Huang, Fulin Lian, Yi Wen, Chenyun Guo, Donghai Li. Prion protein oligomer and its neurotoxicity. Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23557632. |
according to the 'protein only' hypothesis, the key molecular event in the pathogenesis of prion disease is the conformational conversion of the host-derived cellular prion protein (prp(c)) into a misfolded form (scrapie prp, prp(sc)). |
2013-12-09 |
2023-08-12 |
Not clear |
| Pei Huang, Fulin Lian, Yi Wen, Chenyun Guo, Donghai Li. Prion protein oligomer and its neurotoxicity. Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23557632. |
both the prion oligomer and prp(sc) are rich in β-sheet structure and resistant to the proteolysis of proteinase k. the prion oligomer is soluble in physiologic environments whereas prp(sc) is insoluble. |
2013-12-09 |
2023-08-12 |
Not clear |
| Pei Huang, Fulin Lian, Yi Wen, Chenyun Guo, Donghai Li. Prion protein oligomer and its neurotoxicity. Acta biochimica et biophysica Sinica. vol 45. issue 6. 2013-12-09. PMID:23557632. |
prion oligomers exhibited more neurotoxicity both in vitro and in vivo than the fibrillar forms of prp(sc), implying that prion oligomers could be potential drug targets for attacking prion diseases. |
2013-12-09 |
2023-08-12 |
Not clear |