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The Evolution of Transmissible Prions: The Role of Deformed Templating
article has not abstract
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.1003759Souhrn
article has not abstract
Zdroje
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.
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