URE2/YNL229C Literature Guide Help

Other names published for URE2: [URE3], YNL229C

URE2 - Reviews (112)

ReferenceOther Genes Addressed
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
Bruckner S and Mosch HU  (2012) Choosing the right lifestyle: adhesion and development in Saccharomyces cerevisiae. FEMS Microbiol Rev 36(1):25-58
Cordente AG, et al.  (2012) Flavour-active wine yeasts. Appl Microbiol Biotechnol 96(3):601-18
Kupiec M and Weisman R  (2012) TOR links starvation responses to telomere length maintenance. Cell Cycle 11(12):2268-71
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
Ljungdahl PO and Daignan-Fornier B  (2012) Regulation of Amino Acid, Nucleotide, and Phosphate Metabolism in Saccharomyces cerevisiae. Genetics 190(3):885-929
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
Sutphin GL, et al.  (2012) Genome-wide analysis of yeast aging. Subcell Biochem 57():251-89
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
de Virgilio C  (2012) The essence of yeast quiescence. FEMS Microbiol Rev 36(2):306-39
Afanasieva EG, et al.  (2011) Interspecies transmission of prions. Biochemistry (Mosc) 76(13):1375-84
Bruce KL and Chernoff YO  (2011) Sequence specificity and fidelity of prion transmission in yeast. Semin Cell Dev Biol 22(5):444-51
Chen LJ, et al.  (2011) The yeast prion protein Ure2: insights into the mechanism of amyloid formation. Biochem Soc Trans 39(5):1359-64
Crow ET and Li L  (2011) Newly identified prions in budding yeast, and their possible functions. Semin Cell Dev Biol 22(5):452-9
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
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
Maclea KS and Ross ED  (2011) Strategies for identifying new prions in yeast. Prion 5(4):263-8
Nelson AC and Ross ED  (2011) Interactions between non-identical prion proteins. Semin Cell Dev Biol 22(5):437-43
Reidy M and Masison DC  (2011) Modulation and elimination of yeast prions by protein chaperones and co-chaperones. Prion 5(4):245-9
Song Y, et al.  (2011) The yeast prion case: could there be a uniform concept underlying complex protein folding? J Biomol Struct Dyn 28(4):663-5; discussion 669-674