URE2/YNL229C Literature Guide Help

Other names published for URE2: [URE3], YNL229C

URE2 - Primary Literature (138)

Results: 61 - 90 of 138 records
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ReferenceOther Genes Addressed
Brachmann A, et al.  (2005) Prion generation in vitro: amyloid of Ure2p is infectious. EMBO J 24(17):3082-92
Fay N, et al.  (2005) Structure of the prion Ure2p in protein fibrils assembled in vitro. J Biol Chem 280(44):37149-58
Kaeberlein M, et al.  (2005) Regulation of yeast replicative life span by TOR and Sch9 in response to nutrients. Science 310(5751):1193-6
Komar AA, et al.  (2005) Novel characteristics of the biological properties of the yeast Saccharomyces cerevisiae eukaryotic initiation factor 2A. J Biol Chem 280(16):15601-11
McGoldrick S, et al.  (2005) Glutathione transferase-like proteins encoded in genomes of yeasts and fungi: insights into evolution of a multifunctional protein superfamily. FEMS Microbiol Lett 242(1):1-12
Pierce MM, et al.  (2005) Is the Prion Domain of Soluble Ure2p Unstructured? Biochemistry 44(1):321-328
Ross ED, et al.  (2005) Primary sequence independence for prion formation. Proc Natl Acad Sci U S A 102(36):12825-30
Ross ED, et al.  (2005) Prion domains: sequences, structures and interactions. Nat Cell Biol 7(11):1039-44
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
Basu U, et al.  (2004) Reverse genetic analysis of the glutathione metabolic pathway suggests a novel role of PHGPX and URE2 genes in aluminum resistance in Saccharomyces cerevisiae. Mol Genet Genomics 271(5):627-37
Bousset L, et al.  (2004) Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p. Biochemistry 43(17):5022-32
Jiang Y, et al.  (2004) Amyloid nucleation and hierarchical assembly of Ure2p fibrils. Role of asparagine/glutamine repeat and nonrepeat regions of the prion domains. J Biol Chem 279(5):3361-9
Maloney B, et al.  (2004) Presence of a "CAGA box" in the APP gene unique to amyloid plaque-forming species and absent in all APLP-1/2 genes: implications in Alzheimer's disease. FASEB J 18(11):1288-90
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
Roberts BT, et al.  (2004) [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast. Yeast 21(2):107-17
Ross ED, et al.  (2004) Scrambled prion domains form prions and amyloid. Mol Cell Biol 24(16):7206-13
Baudin-Baillieu A, et al.  (2003) Conservation of the prion properties of Ure2p through evolution. Mol Biol Cell 14(8):3449-58
Bousset L, et al.  (2003) The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils. J Struct Biol 141(2):132-42
Chen EJ and Kaiser CA  (2003) LST8 negatively regulates amino acid biosynthesis as a component of the TOR pathway. J Cell Biol 161(2):333-47
Fay N, et al.  (2003) Assembly of the yeast prion Ure2p into protein fibrils. Thermodynamic and kinetic characterization. J Biol Chem 278(32):30199-205
Goehring AS, et al.  (2003) Urmylation: a ubiquitin-like pathway that functions during invasive growth and budding in yeast. Mol Biol Cell 14(11):4329-41
Komar AA, et al.  (2003) Internal initiation drives the synthesis of Ure2 protein lacking the prion domain and affects [URE3] propagation in yeast cells. EMBO J 22(5):1199-209
Martin O, et al.  (2003) Improved anaerobic use of arginine by Saccharomyces cerevisiae. Appl Environ Microbiol 69(3):1623-8
Oliveira EM, et al.  (2003) The role of the GATA factors Gln3p, Nil1p, Dal80p and the Ure2p on ASP3 regulation in Saccharomyces cerevisiae. Yeast 20(1):31-7
Rai R, et al.  (2003) Ure2, a prion precursor with homology to glutathione S-transferase, protects Saccharomyces cerevisiae cells from heavy metal ion and oxidant toxicity. J Biol Chem 278(15):12826-33
Resende CG, et al.  (2003) Prion protein gene polymorphisms in Saccharomyces cerevisiae. Mol Microbiol 49(4):1005-17
Ripaud L, et al.  (2003) The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products. EMBO J 22(19):5251-9
Zhu L, et al.  (2003) Relationship between stability of folding intermediates and amyloid formation for the yeast prion Ure2p: a quantitative analysis of the effects of pH and buffer system. J Mol Biol 328(1):235-54
Zhu L, et al.  (2003) Small angle X-ray scattering study of the yeast prion Ure2p. Biochem Biophys Res Commun 311(2):525-32
Baxa U, et al.  (2002) Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein. Proc Natl Acad Sci U S A 99(8):5253-60
Results: 61 - 90 of 138 records
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