SUP35/YDR172W Literature Guide Help

Other names published for SUP35: GST1, PNM2, SAL3, SUF12, SUP2, SUP36, [PSI], [PSI(+)], eRF3, YDR172W

SUP35 - Reviews (155)

ReferenceOther Genes Addressed
Tomson BN and Arndt KM  (2013) The many roles of the conserved eukaryotic Paf1 complex in regulating transcription, histone modifications, and disease states. Biochim Biophys Acta 1829(1):116-26
Tycko R and Wickner RB  (2013) Molecular Structures of Amyloid and Prion Fibrils: Consensus versus Controversy. Acc Chem Res ()
Wickner RB, et al.  (2013) Amyloids and yeast prion biology. Biochemistry 52(9):1514-27
Wickner RB, et al.  (2013) Viruses and prions of Saccharomyces cerevisiae. Adv Virus Res 86():1-36
Helsen CW and Glover JR  (2012) A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI (+) ]. Prion 6(3):234-9
Hofmann J, et al.  (2012) Creutzfeldt-Jakob disease and mad cows: lessons learnt from yeast cells. Swiss Med Wkly 142():1-11
Josse L, et al.  (2012) Probing the role of structural features of mouse PrP in yeast by expression as Sup35-PrP fusions. Prion 6(3):201-10
Li L and Kowal AS  (2012) Environmental regulation of prions in yeast. PLoS Pathog 8(11):e1002973
Liebman SW and Chernoff YO  (2012) Prions in yeast. Genetics 191(4):1041-72
Parker R  (2012) RNA Degradation in Saccharomyces cerevisae. Genetics 191(3):671-702
Shoemaker CJ and Green R  (2012) Translation drives mRNA quality control. Nat Struct Mol Biol 19(6):594-601
Soto C  (2012) Transmissible proteins: expanding the prion heresy. Cell 149(5):968-77
Staniforth GL and Tuite MF  (2012) Fungal prions. Prog Mol Biol Transl Sci 107():417-56
Thirumalai D, et al.  (2012) Role of water in protein aggregation and amyloid polymorphism. Acc Chem Res 45(1):83-92
Tyedmers J  (2012) Patterns of [PSI (+) ] aggregation allow insights into cellular organization of yeast prion aggregates. Prion 6(3):191-200
Wickner RB  (2012) Discovering protein-based inheritance through yeast genetics. J Biol Chem 287(18):14432-42
Winkler J, et al.  (2012) Chaperone networks in protein disaggregation and prion propagation. J Struct Biol 179(2):152-60
Afanasieva EG, et al.  (2011) Interspecies transmission of prions. Biochemistry (Mosc) 76(13):1375-84
Baudin-Baillieu A, et al.  (2011) Are prions part of the dark matter of the cell? Prion 5(4):299-304
Bruce KL and Chernoff YO  (2011) Sequence specificity and fidelity of prion transmission in yeast. Semin Cell Dev Biol 22(5):444-51
Crow ET and Li L  (2011) Newly identified prions in budding yeast, and their possible functions. Semin Cell Dev Biol 22(5):452-9
DiSalvo S and Serio TR  (2011) Insights into prion biology: integrating a protein misfolding pathway with its cellular environment. Prion 5(2):76-83
Du Z  (2011) The complexity and implications of yeast prion domains. Prion 5(4):311-6
Duennwald ML  (2011) Polyglutamine misfolding in yeast: toxic and protective aggregation. Prion 5(4):285-90
Durand S and Lykke-Andersen J  (2011) SnapShot: Nonsense-mediated mRNA decay. Cell 145(2):324-324.e2
Goldsbury C, et al.  (2011) Amyloid structure and assembly: Insights from scanning transmission electron microscopy. J Struct Biol 173(1):1-13
Hines JK and Craig EA  (2011) The sensitive [SWI (+)] prion: new perspectives on yeast prion diversity. Prion 5(3):164-8
Inge-Vechtomov SG  (2011) [Yeast prions as a model of neurodegenerative infectious amyloidoses in humans]. Ontogenez 42(5):337-45
Kabani M and Melki R  (2011) Yeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies. Prion 5(4):277-84
Kurahashi H, et al.  (2011) A bipolar personality of yeast prion proteins. Prion 5(4):305-10