URE2/YNL229C Literature Guide Help

Other names published for URE2: [URE3], YNL229C

URE2 - Techniques and Reagents (19)

ReferenceOther Genes Addressed
Han Z, et al.  (2012) Self-assembled amyloid-like oligomeric-cohesin Scaffoldin for augmented protein display on the saccharomyces cerevisiae cell surface. Appl Environ Microbiol 78(9):3249-55
Ngo S, et al.  (2012) Prion Domain of Yeast Ure2 Protein Adopts a Completely Disordered Structure: A Solid-Support EPR Study. PLoS One 7(10):e47248
Ngo S, et al.  (2012) Quantitative analysis of spin exchange interactions to identify ? strand and turn regions in Ure2 prion domain fibrils with site-directed spin labeling. J Struct Biol 180(2):374-81
Wickner RB, et al.  (2012) Study of amyloids using yeast. Methods Mol Biol 849():321-46
Edskes HK, et al.  (2011) Prion-forming ability of ure2 of yeasts is not evolutionarily conserved. Genetics 188(1):81-90
Hong JY, et al.  (2011) A new colour assay for [URE3] prion in a genetic background used to score for the [PSI?] prion. Yeast 28(7):555-60
Zhang C, et al.  (2010) Amyloid-like aggregates of the yeast prion protein ure2 enter vertebrate cells by specific endocytotic pathways and induce apoptosis.LID - e12529 [pii] PLoS One 5(9)
Voisset C, et al.  (2009) Procedure for identification and characterization of drugs efficient against Mammalian prion: from a yeast-based antiprion drug screening assay to in vivo mouse models. Infect Disord Drug Targets 9(1):31-9
Immel F, et al.  (2007) In Vitro Analysis of SpUre2p, a Prion-related Protein, Exemplifies the Relationship between Amyloid and Prion. J Biol Chem 282(11):7912-20
Brachmann A, et al.  (2006) Reporter assay systems for [URE3] detection and analysis. Methods 39(1):35-42
Freimoser FM, et al.  (2006) Systematic screening of polyphosphate (poly P) levels in yeast mutant cells reveals strong interdependence with primary metabolism. Genome Biol 7(11):R109
Tribouillard D, et al.  (2006) Using budding yeast to screen for anti-prion drugs. Biotechnol J 1(1):58-67
Pierce MM, et al.  (2005) Is the Prion Domain of Soluble Ure2p Unstructured? Biochemistry 44(1):321-328
Bai M, et al.  (2004) The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms. J Biol Chem 279(48):50025-30
Ripaud L, et al.  (2004) The [URE3] yeast prion results from protein aggregates that differ from amyloid filaments formed in vitro. J Biol Chem 279(49):50962-8
Bousset L, et al.  (2002) The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro. EMBO J 21(12):2903-11
Kuruvilla FG, et al.  (2002) Dissecting glucose signalling with diversity-oriented synthesis and small-molecule microarrays. Nature 416(6881):653-7
Thual C, et al.  (1999) Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2. J Biol Chem 274(19):13666-74
Komar AA, et al.  (1998) Enhanced expression of the yeast Ure2 protein in Escherichia coli: the effect of synonymous codon substitutions at a selected place in the gene. Biol Chem 379(10):1295-300