The [Het-s] Prion, an Amyloid Fold as a Cell Death Activation Trigger

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Vyšlo v časopise: The [Het-s] Prion, an Amyloid Fold as a Cell Death Activation Trigger. PLoS Pathog 8(5): e32767. doi:10.1371/journal.ppat.1002687
Kategorie: Pearls
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1002687

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1. ToyamaBHWeissmanJS 2011 Amyloid structure: conformational diversity and consequences. Annu Rev Biochem 80 557 585

2. EichnerTRadfordSE 2011 A diversity of assembly mechanisms of a generic amyloid fold. Mol Cell 43 8 18

3. ColbyDWPrusinerSB 2011 Prions. Cold Spring Harb Perspect Biol 3 a006833

4. CrowETLiL 2011 Newly identified prions in budding yeast, and their possible functions. Semin Cell Dev Biol 22 452 459

5. Garcia-FruitosESabateRde GrootNSVillaverdeAVenturaS 2011 Biological role of bacterial inclusion bodies: a model for amyloid aggregation. Febs J 278 2419 2427

6. GreenwaldJRiekR 2010 Biology of amyloid: structure, function, and regulation. Structure 18 1244 1260

7. HalfmannRAlbertiSLindquistS 2010 Prions, protein homeostasis, and phenotypic diversity. Trends Cell Biol 20 125 133

8. HalfmannRJaroszDFJonesSKChangALancasterAK 2012 Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature 482 363 368

9. NakayashikiTKurtzmanCPEdskesHKWicknerRB 2005 Yeast prions [URE3] and [PSI+] are diseases. Proc Natl Acad Sci U S A 102 10575 10580

10. SaupeSJ 2011 The [Het-s] prion of Podospora anserina and its role in heterokaryon incompatibility. Semin Cell Dev Biol 22 460 468

11. PaolettiMSaupeSJ 2009 Fungal incompatibility: evolutionary origin in pathogen defense? Bioessays 31 1201 1210

12. BalguerieADos ReisSRitterCChaignepainSCoulary-SalinB 2003 Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina. Embo J 22 2071 2081

13. GreenwaldJBuhtzCRitterCKwiatkowskiWChoeS 2010 The mechanism of prion inhibition by HET-S. Mol Cell 38 889 899

14. WasmerCLangeAVan MelckebekeHSiemerABRiekR 2008 Amyloid fibrils of the HET-s(218–289) prion form a beta solenoid with a triangular hydrophobic core. Science 319 1523 1526

15. BenkemounLNessFSabateRCeschinJBretonA 2011 Two structurally similar fungal prions efficiently cross-seed in vivo but form distinct polymers when coexpressed. Molecular Microbiology 82 1392 1405

16. WasmerCZimmerASabateRSoragniASaupeSJ 2010 Structural similarity between the prion domain of HET-s and a homologue can explain amyloid cross-seeding in spite of limited sequence identity. J Mol Biol 402 311 325

17. MathurVSeuringCRiekRSaupeSJLiebmanSW 2012 Localization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity. Mol Cell Biol 32 139 153

18. DaskalovAPaolettiMNessFSaupeSJ 2012 Genomic clustering and homology between HET-S and the NWD2 STAND protein in various fungal genomes. PLoS ONE 7 e34854 doi:10.1371/journal.pone.0034854

19. SalehM 2011 The machinery of Nod-like receptors: refining the paths to immunity and cell death. Immunol Rev 243 235 246