1. ColbyDW, PrusinerSB (2011) Prions. Cold Spring Harb Perspect Biol 3: a006833.
2. CollingeJ, ClarkeAR (2007) A general model of prion strains and their pathogenicity. Science 318: 930–936.
3. BessenRA, MarshRF (1994) Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J Virol 68: 7859–7868.
4. RequenaJR, WilleH (2014) The structure of the infectious prion protein: Experimental data and molecular models. Prion 8: 60–66.
5. ToyamaBH, WeissmanJS (2011) Amyloid Structure: Conformational Diversity and Consequences. Annu Rev Biochem 80: 557–585.
6. EisenbergD, JuckerM (2012) The Amyloid State of Proteins in Human Diseases. Cell 148: 1188–1203.
7. SurewiczWK, ApostolMI (2011) Prion Protein and Its Conformational Conversion: A Structural Perspective. Top Curr Chem 305: 135–167.
8. SmirnovasV, BaronGS, OfferdahlDK, RaymondGJ, CaugheyB, et al. (2011) Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange. Nat Struct Mol Biol 18: 504–506.
9. KimC, HaldimanT, CohenY, ChenW, BlevinsJ, et al. (2011) Protease-Sensitive Conformers in Broad Spectrum of Distinct PrPSc Structures in Sporadic Creutzfeldt-Jakob Disease Are Indicator of Progression Rate. PLoS Pathog 7: e1002242.
10. LiebmanSW, ChernoffYO (2012) Prions in yeast. Genetics 191: 1041–1072.
11. DerkatchIL, ChernoffYO, KushnirovVV, Inge-VechtomovSG, LiebmanSW (1996) Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. Genetics 144: 1375–1386.
12. TanakaM, CollinsSR, ToyamaBH, WeissmanJS (2006) The physical basis of how prion conformations determine strain phenotypes. Nature 442: 585–589.
13. ToyamaBH, KellyMJS, GrossJD, WeissmanJS (2007) The structural basis of yeast prion strain variants. Nature 449: 233–237.
14. 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.
15. CobbNJ, ApostolMI, ChenS, SmirnovasV, SurewiczWK (2014) Conformational stability of mammalian prion protein amyloid fibrils is dictated by a packing polymorphism within the core region. J Biol Chem 289: 2643–2650.
16. AyersJI, SchuttCR, ShikiyaRA, AguzziA, KincaidAE, et al. (2011) The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease. PLoS Pathog 7: e1001317.
17. AngersRC, KangH-E, NapierD, BrowningS, SewardT, et al. (2010) Prion strain mutation determined by prion protein conformational compatibility and primary structure. Science 328: 1154–1158.
18. BradleyME, EdskesHK, HongJY, WicknerRB, LiebmanSW (2002) Interactions among prions and prion “strains” in yeast. Proc Natl Acad Sci USA 99 Suppl 4: 16392–16399.
19. HuangVJ, SteinKC, TrueHL (2013) Spontaneous Variants of the [RNQ+] Prion in Yeast Demonstrate the Extensive Conformational Diversity Possible with Prion Proteins. PLoS ONE 8: e79582.
20. KalastavadiT, TrueHL (2010) Analysis of the [RNQ+] prion reveals stability of amyloid fibers as the key determinant of yeast prion variant propagation. J Biol Chem 285: 20748–20755.
21. SteinKC, TrueHL (2014) Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions. PLoS Genet 10: e1004337.
22. WestergardL, TrueHL (2014) Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilities. Mol Microbiol 92: 183–193.
23. BelliM, RamazzottiM, ChitiF (2011) Prediction of amyloid aggregation in vivo. EMBO Rep 12: 657–663.
24. SteinKC, TrueHL (2011) The [RNQ+] prion: a model of both functional and pathological amyloid. Prion 5: 291–298.
25. DouglasPM, TreuschS, RenH-Y, HalfmannR, DuennwaldML, et al. (2008) Chaperone-dependent amyloid assembly protects cells from prion toxicity. Proc Natl Acad Sci U S A 105: 7206–7211.
26. FrederickKK, DebelouchinaGT, KayatekinC, DorminyT, JacavoneAC, et al. (2014) Distinct Prion Strains Are Defined by Amyloid Core Structure and Chaperone Binding Site Dynamics. Chem Biol 21: 295–305.
27. SupattaponeS (2013) Elucidating the role of cofactors in mammalian prion propagation. Prion 8: 100–104.
28. LiL, KowalAS (2012) Environmental Regulation of Prions in Yeast. PLoS Pathog 8: e1002973.
29. WestergardL, TrueHL (2014) Extracellular environment modulates the formation and propagation of particular amyloid structures. Mol Microbiol 92: 698–715.
30. PetkovaAT, IshiiY, BalbachJJ, AntzutkinON, LeapmanRD, et al. (2002) A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR. Proc Natl Acad Sci U S A 99: 16742–16747.
31. SawayaMR, SambashivanS, NelsonR, IvanovaMI, SieversSA, et al. (2007) Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 447: 453–457.
32. WiltziusJJW, LandauM, NelsonR, SawayaMR, ApostolMI, et al. (2009) Molecular mechanisms for protein-encoded inheritance. Nat Struct Mol Biol 16: 973–978.