URE2/YNL229C Literature Guide Help

Other names published for URE2: [URE3], YNL229C

URE2 - Primary Literature (139)

ReferenceOther Genes Addressed
Delaney JR, et al.  (2013) Stress profiling of longevity mutants identifies Afg3 as a mitochondrial determinant of cytoplasmic mRNA translation and aging. Aging Cell 12(1):156-66
Feller A, et al.  (2013) Alterations in the Ure2 alphaCap domain elicit different GATA factor responses to rapamycin treatment and nitrogen limitation. J Biol Chem 288(3):1841-55
Gaytan BD, et al.  (2013) Functional profiling discovers the dieldrin organochlorinated pesticide affects leucine availability in yeast. Toxicol Sci 132(2):347-58
Harsch MJ and Gardner RC  (2013) Yeast genes involved in sulfur and nitrogen metabolism affect the production of volatile thiols from Sauvignon Blanc musts. Appl Microbiol Biotechnol 97(1):223-35
Oishi K, et al.  (2013) A bipolar functionality of Q/N-rich proteins: Lsm4 amyloid causes clearance of yeast prions. Microbiologyopen 2(3):415-30
Watanabe T, et al.  (2013) Genome-Wide Screening to Study Breeding Methods to Improve the Nitrogen Accumulation Ability of Yeast without Gene Recombinant Techniques. Biosci Biotechnol Biochem 77(5):917-22
Alex D, et al.  (2012) Amino acid-derived 1,2-benzisothiazolinone derivatives as novel small-molecule antifungal inhibitors: identification of potential genetic targets. Antimicrob Agents Chemother 56(9):4630-9
Espargaro A, et al.  (2012) Yeast prions form infectious amyloid inclusion bodies in bacteria. Microb Cell Fact 11(1):89
Kelly AC, et al.  (2012) Sex, prions, and plasmids in yeast. Proc Natl Acad Sci U S A 109(40):E2683-90
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
Chen L, et al.  (2011) Deletion of a Ure2 C-terminal prion-inhibiting region promotes the rate of fibril seed formation and alters interaction with Hsp40. Protein Eng Des Sel 24(1-2):69-78
Delaney JR, et al.  (2011) Sir2 deletion prevents lifespan extension in 32 long-lived mutants. Aging Cell 10(6):1089-91
Edskes HK, et al.  (2011) Prion-forming ability of ure2 of yeasts is not evolutionarily conserved. Genetics 188(1):81-90
Kryndushkin DS, et al.  (2011) The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-? structure: evidence from solid-state NMR. J Mol Biol 409(2):263-77
Kwan EX, et al.  (2011) Natural Polymorphism in BUL2 Links Cellular Amino Acid Availability with Chronological Aging and Telomere Maintenance in Yeast. PLoS Genet 7(8):e1002250
McGlinchey RP, et al.  (2011) Suicidal [PSI+] is a lethal yeast prion. Proc Natl Acad Sci U S A 108(13):5337-41
Ngo S, et al.  (2011) Hierarchical organization in the amyloid core of yeast prion protein Ure2. J Biol Chem 286(34):29691-9
Sideri TC, et al.  (2011) Methionine oxidation of Sup35 protein induces formation of the [PSI+] prion in a yeast peroxiredoxin mutant. J Biol Chem 286(45):38924-31
Ungar L, et al.  (2011) Tor complex 1 controls telomere length by affecting the level of Ku. Curr Biol 21(24):2115-20
Wang YQ, et al.  (2011) Relationship between Prion Propensity and the Rates of Individual Molecular Steps of Fibril Assembly. J Biol Chem 286(14):12101-7
Wang YQ, et al.  (2011) The fibrils of Ure2p homologs from Saccharomyces cerevisiae and Saccharoymyces paradoxus have similar cross-? structure in both dried and hydrated forms. J Struct Biol 174(3):505-11
Yu Y, et al.  (2011) Flexibility of the Ure2 prion domain is important for amyloid fibril formation. Biochem J 434(1):143-151
Bousset L, et al.  (2010) Structure and assembly properties of the N-terminal domain of the prion ure2p in isolation and in its natural context. PLoS One 5(3):e9760
Fei L and Perrett S  (2010) New insights into the molecular mechanism of amyloid formation from cysteine scanning. Prion 4(1):9-12
Fiumara F, et al.  (2010) Essential role of coiled coils for aggregation and activity of Q/N-rich prions and PolyQ proteins. Cell 143(7):1121-35
Ottosson LG, et al.  (2010) Sulfate Assimilation Mediates Tellurite Reduction and Toxicity in Saccharomyces cerevisiae. Eukaryot Cell 9(10):1635-1647
Redeker V, et al.  (2010) A region within the C-terminal domain of Ure2p is shown to interact with the molecular chaperone Ssa1p by the use of cross-linkers and mass spectrometry. FEBS J 277(24):5112-23
Todorova TT, et al.  (2010) Non-enzymatic roles for the URE2 glutathione S-transferase in the response of Saccharomyces cerevisiae to arsenic. Arch Microbiol 192(11):909-18
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)