Other names published for URE2: [URE3], YNL229C
URE2 LITERATURE TOPICS
- Curated Literature
- Additional Literature
- All Curated References
- Primary Literature
- Reviews
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
URE2 - Primary Literature (138)
| Reference | Other 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 () | |
| 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) | |
| Zhao J, et al. (2010) The protein kinase Hal5p is the high-copy suppressor of lithium-sensitive mutations of genes involved in the sporulation and meiosis as well as the ergosterol biosynthesis in Saccharomyces cerevisiae. Genomics 95(5):290-8 |



