Reduced proteinase K resistance and infectivity of prions after pressure treatment at 60 °C

References

1. Akasaka K., Tezuka T., Yamada H. 1997; Pressure induced changes in the folded structure of lysozyme. J Mol Biol 271:671–678
   [Google Scholar]
2. Brown P., Rau E. H., Johnson B. K., Bacote A. E., Gibbs C. J. Jr, Gajdusek C. 2000; New studies on the heat resistance of hamster adapted scrapie agent: threshold survival after ashing at 600 °C suggests an inorganic template of replication. Proc Natl Acad Sci U S A 97:3418–3421
   [Google Scholar]
3. Brown P., Meyer R., Cardone F., Pocchiari M. 2003; Ultra-high-pressure inactivation of prion infectivity in processed meat: a practical method to prevent human infection. Proc Natl Acad Sci U S A 100:6093–6097
   [Google Scholar]
4. Dubois J., Ismail A. A., Chan S. L., Ali-Khan Z. 1999; Fourier transform infrared spectroscopic investigation of temperature- and pressure-induced disaggregation of amyloid A. Scand J Immunol 49:376–380
   [Google Scholar]
5. Ferrao-Gonzales A. D., Souto S. O., Silva J. L., Foguel D. 2000; The pre-aggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state. Proc Natl Acad Sci U S A 97:6445–6450
   [Google Scholar]
6. Heremans K., Smeller L. 1998; Protein structure and dynamics at high pressure. Biochim Biophys Acta 1386:353–370
   [Google Scholar]
7. Kuwata K., Hua L., Yamada H., Legname G., Prusiner S., Akasaka A., James T. L. 2002; Locally disordered conformer of the hamster prion protein: a crucial intermediate to PrP^Sc?. Biochemistry 41:12277–12283
   [Google Scholar]
8. Mozhaev V. V., Heremans K., Frank J., Masson P., Balny C. 1996; High pressure effects on protein structure and function. Proteins 24:81–91
   [Google Scholar]
9. Prusiner S. B. 1991; Molecular biology of prion diseases. Science 252:1515–1522
   [Google Scholar]
10. Prusiner S. B., Cochran S. P., Groth D. F., Downey D. E., Bowman K. A., Martinez H. M. 1982; Measurement of the scrapie agent using an incubation time interval assay. Ann Neurol 11:353–358
    [Google Scholar]
11. Randolph T. W., Seefeldt M., Carpenter J. F. 2002; High hydrostatic pressure as a tool to study protein aggregation and amyloidosis. Biochim Biophys Acta 1495224–234
    [Google Scholar]
12. Riesner D., Kellings K., Post K., Wille H., Serban H., Groth D., Baldwin M. A., Prusiner S. B. 1996; Disruption of prion rods generates 10-nm spherical particles having high α -helical content and lacking scrapie infectivity. J Virol 19961714–1722
    [Google Scholar]
13. Telling G. C., Scott J., Mastrianni R., Gabizon R., Torchia M., Cohen F. E., DeArmond S. J., Prusiner S. B. 1995; Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83:79–90
    [Google Scholar]
14. Torrent J., Alvarez Martinez M. T., Heitz F., Liautard J.-P., Balny C., Lange R. 2003; Alternative prion structural changes revealed by high pressure. Biochemistry 42:1318–1325
    [Google Scholar]
15. Zhou J.-M., Zhu L., Balny C., Perrett S. 2001; Pressure denaturation of the yeast prion protein Ure2. Biochem Biophys Res Commun 287:147–152
    [Google Scholar]