| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Emeka A Okoroma, Diane Purchase, Hemda Garelick, Roger Morris, Michael H Neale, Otto Windl, Oduola O Abiol. Enzymatic formulation capable of degrading scrapie prion under mild digestion conditions. PloS one. vol 8. issue 7. 2014-02-19. PMID:23874511. |
a feather-degrading bacillus licheniformis n22 keratinase has been isolated which degraded scrapie prion to undetectable level of prp(sc) signals as determined by western blot analysis. |
2014-02-19 |
2023-08-12 |
Not clear |
| Emeka A Okoroma, Diane Purchase, Hemda Garelick, Roger Morris, Michael H Neale, Otto Windl, Oduola O Abiol. Enzymatic formulation capable of degrading scrapie prion under mild digestion conditions. PloS one. vol 8. issue 7. 2014-02-19. PMID:23874511. |
an enzymatic formulation combining n22 keratinase and biosurfactant derived from pseudomonas aeruginosa degraded prp(sc) at 65 °c in 10 min to undetectable level -. |
2014-02-19 |
2023-08-12 |
Not clear |
| Emeka A Okoroma, Diane Purchase, Hemda Garelick, Roger Morris, Michael H Neale, Otto Windl, Oduola O Abiol. Enzymatic formulation capable of degrading scrapie prion under mild digestion conditions. PloS one. vol 8. issue 7. 2014-02-19. PMID:23874511. |
a time-course degradation analysis carried out at 50 °c over 2 h revealed the progressive attenuation of prp(sc) intensity. |
2014-02-19 |
2023-08-12 |
Not clear |
| Emeka A Okoroma, Diane Purchase, Hemda Garelick, Roger Morris, Michael H Neale, Otto Windl, Oduola O Abiol. Enzymatic formulation capable of degrading scrapie prion under mild digestion conditions. PloS one. vol 8. issue 7. 2014-02-19. PMID:23874511. |
test of residual infectivity by standard cell culture assay confirmed that the enzymatic formulation reduced prp(sc) infectivity to undetectable levels as compared to cells challenged with untreated standard scrapie sheep prion (ssbp/1) (p-value = 0.008 at 95% confidence interval). |
2014-02-19 |
2023-08-12 |
Not clear |
| Guo-Ping Zhou, Ri-Bo Huan. The pH-triggered conversion of the PrP(c) to PrP(sc.). Current topics in medicinal chemistry. vol 13. issue 10. 2014-02-07. PMID:23647538. |
the ph-triggered conversion of the prp(c) to prp(sc.). |
2014-02-07 |
2023-08-12 |
Not clear |
| Guo-Ping Zhou, Ri-Bo Huan. The pH-triggered conversion of the PrP(c) to PrP(sc.). Current topics in medicinal chemistry. vol 13. issue 10. 2014-02-07. PMID:23647538. |
transmissible spongiform encephalopathies (tses) are prion protein misfolding diseases that involve the accumulation of an abnormal β-sheet-rich prion protein aggregated form (prp(sc)) of the normal α- helix-rich prion protein (prp(c)) within the central nervous system (cns) and other organs. |
2014-02-07 |
2023-08-12 |
Not clear |
| Guo-Ping Zhou, Ri-Bo Huan. The pH-triggered conversion of the PrP(c) to PrP(sc.). Current topics in medicinal chemistry. vol 13. issue 10. 2014-02-07. PMID:23647538. |
a soluble intermediate, called prp(β) or β(o), exhibiting many of the same features as prp(sc), can be generated using a combination of low ph and/or mild denaturing conditions. |
2014-02-07 |
2023-08-12 |
Not clear |
| Guo-Ping Zhou, Ri-Bo Huan. The pH-triggered conversion of the PrP(c) to PrP(sc.). Current topics in medicinal chemistry. vol 13. issue 10. 2014-02-07. PMID:23647538. |
here, we review the current knowledge on the following five issues relevant to the conversion mechanisms of prp(c) to prp(sc) : (1) how is the stability of the helical structures in the native prp(c) related to the primary structure of the prp(c) (2) why the low ph solution system is a ideal trigger of prp(c) to prp(sc) conversion (3) how are the structural and dynamical characteristics of the α-helixrich intermediates determined using nmr data (4) how are the premolten (prp(α4) and prp(αβ)) and β-oligomer (prp(β)) intermediates detected and assayed, and (5) can the disordered n-terminal domain be folded into the structural segment? |
2014-02-07 |
2023-08-12 |
Not clear |
| Leah M Kyle, Theodore R John, Hermann M Schätzl, Randolph V Lewi. Introducing a rigid loop structure from deer into mouse prion protein increases its propensity for misfolding in vitro. PloS one. vol 8. issue 6. 2014-02-07. PMID:23825561. |
prion diseases are fatal neurodegenerative disorders characterized by misfolding of the cellular prion protein (prp(c)) into the disease-associated isoform (prp(sc)) that has increased β-sheet content and partial resistance to proteolytic digestion. |
2014-02-07 |
2023-08-12 |
mouse |
| Richard Rubenstein, Binggong Chan. Re-assessment of PrP(Sc) distribution in sporadic and variant CJD. PloS one. vol 8. issue 7. 2014-02-07. PMID:23843953. |
re-assessment of prp(sc) distribution in sporadic and variant cjd. |
2014-02-07 |
2023-08-12 |
mouse |
| Richard Rubenstein, Binggong Chan. Re-assessment of PrP(Sc) distribution in sporadic and variant CJD. PloS one. vol 8. issue 7. 2014-02-07. PMID:23843953. |
human prion diseases are fatal neurodegenerative disorders associated with an accumulation of prp(sc) in the central nervous system (cns). |
2014-02-07 |
2023-08-12 |
mouse |
| Richard Rubenstein, Binggong Chan. Re-assessment of PrP(Sc) distribution in sporadic and variant CJD. PloS one. vol 8. issue 7. 2014-02-07. PMID:23843953. |
peripheral tissue involvement in prion disease, as judged by prp(sc) accumulation in the tonsil, spleen, and lymph node has been reported in vcjd as well as several animal models of prion diseases. |
2014-02-07 |
2023-08-12 |
mouse |
| Richard Rubenstein, Binggong Chan. Re-assessment of PrP(Sc) distribution in sporadic and variant CJD. PloS one. vol 8. issue 7. 2014-02-07. PMID:23843953. |
however, this distribution of prp(sc) has not been consistently reported for scjd. |
2014-02-07 |
2023-08-12 |
mouse |
| Richard Rubenstein, Binggong Chan. Re-assessment of PrP(Sc) distribution in sporadic and variant CJD. PloS one. vol 8. issue 7. 2014-02-07. PMID:23843953. |
we reexamined cns and non-cns tissue distribution and levels of prp(sc) in both scjd and vcjd. |
2014-02-07 |
2023-08-12 |
mouse |
| Richard Rubenstein, Binggong Chan. Re-assessment of PrP(Sc) distribution in sporadic and variant CJD. PloS one. vol 8. issue 7. 2014-02-07. PMID:23843953. |
using a sensitive immunoassay, termed sofia, we also assessed prp(sc) levels in human body fluids from scjd as well as in vcjd-infected humanized transgenic mice (tg666). |
2014-02-07 |
2023-08-12 |
mouse |
| Richard Rubenstein, Binggong Chan. Re-assessment of PrP(Sc) distribution in sporadic and variant CJD. PloS one. vol 8. issue 7. 2014-02-07. PMID:23843953. |
unexpectedly, the levels of prp(sc) in non-cns human tissues (spleens, lymph nodes, tonsils) from both scjd and vcjd did not differ significantly and, as expected, were several logs lower than in the brain. |
2014-02-07 |
2023-08-12 |
mouse |
| Richard Rubenstein, Binggong Chan. Re-assessment of PrP(Sc) distribution in sporadic and variant CJD. PloS one. vol 8. issue 7. 2014-02-07. PMID:23843953. |
using protein misfolding cyclic amplification (pmca) followed by sofia, prp(sc) was detected in cerebrospinal fluid (csf), but not in urine or blood, in scjd patients. |
2014-02-07 |
2023-08-12 |
mouse |
| Richard Rubenstein, Binggong Chan. Re-assessment of PrP(Sc) distribution in sporadic and variant CJD. PloS one. vol 8. issue 7. 2014-02-07. PMID:23843953. |
these studies provide a comparison of prp(sc) in scjd vs. vcjd as well as analysis of body fluids. |
2014-02-07 |
2023-08-12 |
mouse |
| Richard Rubenstein, Binggong Chan. Re-assessment of PrP(Sc) distribution in sporadic and variant CJD. PloS one. vol 8. issue 7. 2014-02-07. PMID:23843953. |
further, these studies also provide circumstantial evidence that in human prion diseases, as in the animal prion diseases, a direct comparison and intraspecies correlation cannot be made between the levels of prp(sc) and infectivity. |
2014-02-07 |
2023-08-12 |
mouse |
| Biswanath Chatterjee, Chung-Yu Lee, Chen Lin, Eric H-L Chen, Chao-Li Huang, Chien-Chih Yang, Rita P-Y Che. Amyloid core formed of full-length recombinant mouse prion protein involves sequence 127-143 but not sequence 107-126. PloS one. vol 8. issue 7. 2014-02-07. PMID:23844138. |
the principal event underlying the development of prion disease is the conversion of soluble cellular prion protein (prp(c)) into its disease-causing isoform, prp(sc). |
2014-02-07 |
2023-08-12 |
mouse |