The Evolution of Transmissible Prions: The Role of Deformed Templating

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Vyšlo v časopise: The Evolution of Transmissible Prions: The Role of Deformed Templating. PLoS Pathog 9(12): e32767. doi:10.1371/journal.ppat.1003759
Kategorie: Pearls
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1003759

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1. CollingeJ (2010) Prion strain mutation and selection. Science 328: 1111–1112.

2. LiJ, BrowningS, MahalSP, OelschlegelAM, WeissmannC (2010) Darwinian evolution of prions in cell culture. Science 327: 869–872.

3. GhaemmaghamiS, AhnM, LessardP, GilesK, LegnameG, et al. (2009) Continuous quinacrine treatment results in the formation of drug-resistant prions. PLoS Pathog 5: e1000673 doi:10.1371/journal.ppat.1000673

4. MakaravaN, BaskakovIV (2012) Genesis of transmissible protein states vie deformed templating. Prion 6: 252–255.

5. MakaravaN, OstapchenkoVG, SavtchenkoR, BaskakovIV (2009) Conformational switching within individual amyloid fibrils. J Biol Chem 284: 14386–14395.

6. MahalSP, JablonskiJ, Suponitsky-KroyterI, OrlschlegelAM, HervaME, et al. (2012) Propagating of RML prions in mice expressing PrP devoid of GPI anchor leads to formation of a novel, stable prion strain. PLoS Pathog 8: e1002746 doi:10.1371/journal.ppat.1002746

7. CancellottiE, MahalSP, SomervilleR, DiackA, BrownD, et al. (2013) Post-translational changes to PrP alter transmissible spongiform encephalopathy strain properties. EMBO J 32: 756–769.

8. Gonzalez-MontalbanN, LeeYJ, MakaravaN, SavtchenkoR, BaskakovIV (2013) Changes in prion replication environemnt cause prion strain mutation. FASEB J 27: 3702–3710.

9. LegnameG, BaskakovIV, NguyenHOB, RiesnerD, CohenFE, et al. (2004) Synthetic mammalian prions. Science 305: 673–676.

10. ColbyDW, GilesK, LegnameG, WilleH, BaskakovIV, et al. (2009) Design and construction of diverse mammalian prion strains. Proc Natl Acad Sci U S A 106: 20417–20422.

11. ColbyDW, WainR, BaskakovIV, LegnameG, PalmerCG, et al. (2010) Protease-sensitive synthetic prions. PLoS Pathogen 6: e1000736 doi:10.1371/journal.ppat.1000736

12. MakaravaN, KovacsGG, BocharovaOV, SavtchenkoR, AlexeevaI, et al. (2010) Recombinant prion protein induces a new transmissible prion disease in wild type animals. Acta Neuropathol 119: 177–187.

13. WilleH, BianW, McDonaldM, KendallA, ColbyDW, et al. (2009) Natural and synthetic prion structure from X-ray fiber diffraction. Proc Natl Acad Sci U S A 106: 16990–16995.

14. MakaravaN, KovacsGG, SavtchenkoR, AlexeevaI, BudkaH, et al. (2011) Genesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion disease. PLoS Pathogen 7: e1002419 doi:10.1371/journal.ppat.1002419

15. MakaravaN, KovacsGG, SavtchenkoR, AlexeevaI, OstapchenkoVG, et al. (2012) A new mechanism for transmissible prion diseases. J Neurosci 32: 7345–7355.

16. MakaravaN, KovacsGG, SavtchenkoR, AlexeevaI, BudkaH, et al. (2012) Stabilization of a prion strain of synthetic origin requires multiple serial passages. J Biol Chem 287: 30205–30214.

17. GhaemmaghamiS, ColbyDW, NquyenHO, HayashiS, OehlerA, et al. (2013) Convergent replication of mouse synthetic prion strains. Am J Pathol 182: 866–874.

18. MakaravaN, SavtchenkoR, BaskakovIV (2013) Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification. J Biol Chem 288: 33–41.

19. Gonzalez-MontalbanN, BaskakovIV (2012) Assessment of strain-specific PrPSc elongation rates revealed a transformation of PrPSc properties during Protein Misfolding Cyclic Amplification. PLoS ONE 7: e41210 doi:10.1371/journal.pone.0041210

20. LiJ, MahalSP, DemczykCA, WeissmannC (2011) Mutability of prions. EMBO Rep 12: 1243–1250.