| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| John G Gray, Sandor Dudas, Catherine Graham, Stefanie Czu. Performance analysis of rapid diagnostic tests on atypical bovine spongiform encephalopathy. Journal of veterinary diagnostic investigation : official publication of the American Association of Veterinary Laboratory Diagnosticians, Inc. vol 24. issue 5. 2013-01-14. PMID:22855378. |
although bse prp(sc) type had some effects on rapid-test performance, analytical sensitivity for atypical bse prp(sc) on all 3 platforms was not significantly compromised. |
2013-01-14 |
2023-08-12 |
cattle |
| John G Gray, Sandor Dudas, Catherine Graham, Stefanie Czu. Performance analysis of rapid diagnostic tests on atypical bovine spongiform encephalopathy. Journal of veterinary diagnostic investigation : official publication of the American Association of Veterinary Laboratory Diagnosticians, Inc. vol 24. issue 5. 2013-01-14. PMID:22855378. |
when testing for atypical bse prp(sc), the 3 tests were able to meet the same requirements that the european food safety authority set when evaluating the tests for c-type bse prp(sc). |
2013-01-14 |
2023-08-12 |
cattle |
| Hae-Eun Kang, Chu Chun Weng, Eri Saijo, Vicki Saylor, Jifeng Bian, Sehun Kim, Laylaa Ramos, Rachel Angers, Katie Langenfeld, Vadim Khaychuk, Carla Calvi, Jason Bartz, Nora Hunter, Glenn C Tellin. Characterization of conformation-dependent prion protein epitopes. The Journal of biological chemistry. vol 287. issue 44. 2013-01-07. PMID:22948149. |
whereas prion replication involves structural rearrangement of cellular prion protein (prp(c)), the existence of conformational epitopes remains speculative and controversial, and prp transformation is monitored by immunoblot detection of prp(27-30), a protease-resistant counterpart of the pathogenic scrapie form (prp(sc)) of prp. |
2013-01-07 |
2023-08-12 |
mouse |
| Christopher J Silv. Using small molecule reagents to selectively modify epitopes based on their conformation. Prion. vol 6. issue 2. 2013-01-03. PMID:22436143. |
prp(sc) is an infectious protein. |
2013-01-03 |
2023-08-12 |
mouse |
| Christopher J Silv. Using small molecule reagents to selectively modify epitopes based on their conformation. Prion. vol 6. issue 2. 2013-01-03. PMID:22436143. |
the only experimentally verified difference between prp(sc) and its normal cellular isoform (prp(c)) is conformational. |
2013-01-03 |
2023-08-12 |
mouse |
| Christopher J Silv. Using small molecule reagents to selectively modify epitopes based on their conformation. Prion. vol 6. issue 2. 2013-01-03. PMID:22436143. |
this work describes an approach to determining the presence of surface exposed or sequestered amino acids present in the prp(sc) isoform. |
2013-01-03 |
2023-08-12 |
mouse |
| Christopher J Silv. Using small molecule reagents to selectively modify epitopes based on their conformation. Prion. vol 6. issue 2. 2013-01-03. PMID:22436143. |
the 3f4, 6d11, ah6, and ge8 antibodies recognize an epitope that is encrypted in the prp(sc) isoform, but exposed in the prp(c) isoform. |
2013-01-03 |
2023-08-12 |
mouse |
| Christopher J Silv. Using small molecule reagents to selectively modify epitopes based on their conformation. Prion. vol 6. issue 2. 2013-01-03. PMID:22436143. |
in addition they can be used, with an appropriate antibody, to determine which amino acids of prp(sc) are exposed on the surface and which are encrypted, thus providing useful structural information. |
2013-01-03 |
2023-08-12 |
mouse |
| Eliezer Masliah, Edward Rockenstein, Chandra Inglis, Anthony Adame, Cyrus Bett, Melanie Lucero, Christina J Sigurdso. Prion infection promotes extensive accumulation of α-synuclein in aged human α-synuclein transgenic mice. Prion. vol 6. issue 2. 2013-01-03. PMID:22460692. |
in neurodegenerative disorders of the aging population, misfolded proteins, such as prp(sc), α-synuclein, amyloid β protein and tau, can interact resulting in enhanced aggregation, cross seeding and accelerated disease progression. |
2013-01-03 |
2023-08-12 |
mouse |
| Eliezer Masliah, Edward Rockenstein, Chandra Inglis, Anthony Adame, Cyrus Bett, Melanie Lucero, Christina J Sigurdso. Prion infection promotes extensive accumulation of α-synuclein in aged human α-synuclein transgenic mice. Prion. vol 6. issue 2. 2013-01-03. PMID:22460692. |
previous reports have shown that in creutzfeldt-jakob disease and scrapie, α-synuclein accumulates near prp(sc) deposits. |
2013-01-03 |
2023-08-12 |
mouse |
| Eliezer Masliah, Edward Rockenstein, Chandra Inglis, Anthony Adame, Cyrus Bett, Melanie Lucero, Christina J Sigurdso. Prion infection promotes extensive accumulation of α-synuclein in aged human α-synuclein transgenic mice. Prion. vol 6. issue 2. 2013-01-03. PMID:22460692. |
however, it is unclear if pre-existing human α-synuclein aggregates modified prion disease pathogenesis, or if prp(sc) exacerbates the α-synuclein pathology. |
2013-01-03 |
2023-08-12 |
mouse |
| Eliezer Masliah, Edward Rockenstein, Chandra Inglis, Anthony Adame, Cyrus Bett, Melanie Lucero, Christina J Sigurdso. Prion infection promotes extensive accumulation of α-synuclein in aged human α-synuclein transgenic mice. Prion. vol 6. issue 2. 2013-01-03. PMID:22460692. |
taken together, these studies support the notion that prp(sc) directly or indirectly promotes α-synuclein pathology. |
2013-01-03 |
2023-08-12 |
mouse |
| Lyne Jossé, Ricardo Marchante, Jo Zenthon, Tobias von der Haar, Mick F Tuit. Probing the role of structural features of mouse PrP in yeast by expression as Sup35-PrP fusions. Prion. vol 6. issue 3. 2013-01-02. PMID:22449853. |
one major target is the mammalian prion protein prp because we know little about what specific sequence and/or structural feature(s) of prp are important for its conversion to the infectious prion form, prp (sc) . |
2013-01-02 |
2023-08-12 |
mouse |
| Natallia Makarava, Ilia V Baskako. Genesis of tramsmissible protein states via deformed templating. Prion. vol 6. issue 3. 2013-01-02. PMID:22561163. |
recent studies demonstrated that authentic prp (sc) and transmissible prion disease could be generated in wild type animals by inoculation of recombinant prion protein amyloid fibrils, which are structurally different from prp (sc) and lack any detectable prp (sc) particles. |
2013-01-02 |
2023-08-12 |
Not clear |
| Xiangzhu Xiao, Jue Yuan, Wen-Quan Zo. Isolation of soluble and insoluble PrP oligomers in the normal human brain. Journal of visualized experiments : JoVE. issue 68. 2012-12-27. PMID:23070047. |
the central event in the pathogenesis of prion diseases involves a conversion of the host-encoded cellular prion protein prp(c) into its pathogenic isoform prp(sc 1). |
2012-12-27 |
2023-08-12 |
human |
| Xiangzhu Xiao, Jue Yuan, Wen-Quan Zo. Isolation of soluble and insoluble PrP oligomers in the normal human brain. Journal of visualized experiments : JoVE. issue 68. 2012-12-27. PMID:23070047. |
prp(c) is detergent-soluble and sensitive to proteinase k (pk)-digestion, whereas prp(sc) forms detergent-insoluble aggregates and is partially resistant to pk(2-6). |
2012-12-27 |
2023-08-12 |
human |
| Xiangzhu Xiao, Jue Yuan, Wen-Quan Zo. Isolation of soluble and insoluble PrP oligomers in the normal human brain. Journal of visualized experiments : JoVE. issue 68. 2012-12-27. PMID:23070047. |
the conversion of prp(c) to prp(sc) is known to involve a conformational transition of α-helical to β-sheet structures of the protein. |
2012-12-27 |
2023-08-12 |
human |
| Xiangzhu Xiao, Jue Yuan, Wen-Quan Zo. Isolation of soluble and insoluble PrP oligomers in the normal human brain. Journal of visualized experiments : JoVE. issue 68. 2012-12-27. PMID:23070047. |
a tentative endogenous prp(sc), intermediate prp* or "silent prion", has yet to be identified in the uninfected brain(7). |
2012-12-27 |
2023-08-12 |
human |
| Xiangzhu Xiao, Jue Yuan, Wen-Quan Zo. Isolation of soluble and insoluble PrP oligomers in the normal human brain. Journal of visualized experiments : JoVE. issue 68. 2012-12-27. PMID:23070047. |
the combination of these approaches isolates not only insoluble prp(sc) and prp(c) aggregates but also soluble prp(c) oligomers from the normal human brain. |
2012-12-27 |
2023-08-12 |
human |
| Xiangzhu Xiao, Jue Yuan, Wen-Quan Zo. Isolation of soluble and insoluble PrP oligomers in the normal human brain. Journal of visualized experiments : JoVE. issue 68. 2012-12-27. PMID:23070047. |
since the protocols described here have been used to isolate both prp(sc) from infected brains and iprp(c) from uninfected brains, they provide us with an opportunity to compare differences in physicochemical features, neurotoxicity, and infectivity between the two isoforms. |
2012-12-27 |
2023-08-12 |
human |