URE2/YNL229C Literature Guide Help

Other names published for URE2: [URE3], YNL229C

URE2 - Protein-protein Interactions (58)

Results: 1 - 30 of 58 records
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ReferenceOther Genes Addressed
Sabate R, et al.  (2012) Temperature dependence of the aggregation kinetics of Sup35 and Ure2p yeast prions. Biomacromolecules 13(2):474-83
Kanneganti V, et al.  (2011) Btn3 is a negative regulator of Btn2-mediated endosomal protein trafficking and prion curing in yeast. Mol Biol Cell 22(10):1648-63
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
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
Yu Y, et al.  (2011) Flexibility of the Ure2 prion domain is important for amyloid fibril formation. Biochem J 434(1):143-151
Breitkreutz A, et al.  (2010) A global protein kinase and phosphatase interaction network in yeast. Science 328(5981):1043-6
Fei L and Perrett S  (2010) New insights into the molecular mechanism of amyloid formation from cysteine scanning. Prion 4(1):9-12
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
Ross ED and Toombs JA  (2010) The effects of amino acid composition on yeast prion formation and prion domain interactions. Prion 4(2):60-5
Alberti S, et al.  (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137(1):146-58
Choe YJ, et al.  (2009) Increased [PSI+] appearance by fusion of Rnq1 with the prion domain of Sup35 in Saccharomyces cerevisiae. Eukaryot Cell 8(7):968-76
Crapeau M, et al.  (2009) The cellular concentration of the yeast ure2p prion protein affects its propagation as a prion. Mol Biol Cell 20(8):2286-96
Fei L and Perrett S  (2009) Disulfide Bond Formation Significantly Accelerates the Assembly of Ure2p Fibrils because of the Proximity of a Potential Amyloid Stretch. J Biol Chem 284(17):11134-41
Knowles TP, et al.  (2009) An analytical solution to the kinetics of breakable filament assembly. Science 326(5959):1533-7
Loquet A, et al.  (2009) Prion fibrils of Ure2p assembled under physiological conditions contain highly ordered, natively folded modules. J Mol Biol 394(1):108-18
Pieri L, et al.  (2009) Synthetic lipid vesicles recruit native-like aggregates and affect the aggregation process of the prion Ure2p: insights on vesicle permeabilization and charge selectivity. Biophys J 96(8):3319-30
Ross CD, et al.  (2009) A Promiscuous Prion: Efficient Induction of [URE3] Prion Formation by Heterologous Prion Domains. Genetics 183(3):929-40
Sharma D, et al.  (2009) Curing of Yeast [URE3] Prion by the Hsp40 Cochaperone Ydj1p Is Mediated by Hsp70. Genetics 181(1):129-37
Shewmaker F, et al.  (2009) Two prion variants of Sup35p have in-register parallel beta-sheet structures, independent of hydration. Biochemistry 48(23):5074-82
Kryndushkin DS, et al.  (2008) Curing of the [URE3] prion by Btn2p, a Batten disease-related protein. EMBO J 27(20):2725-35
Savistchenko J, et al.  (2008) Molecular chaperones and the assembly of the prion ure2p in vitro. J Biol Chem 283(23):15732-9
Watzky MA, et al.  (2008) Fitting yeast and mammalian prion aggregation kinetic data with the Finke-Watzky two-step model of nucleation and autocatalytic growth. Biochemistry 47(40):10790-800
Baxa U, et al.  (2007) Characterization of beta-Sheet Structure in Ure2p(1)(-)(89) Yeast Prion Fibrils by Solid-State Nuclear Magnetic Resonance. Biochemistry 46(45):13149-13162
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
Lian HY, et al.  (2007) Hsp40 Interacts Directly with the Native State of the Yeast Prion Protein Ure2 and Inhibits Formation of Amyloid-like Fibrils. J Biol Chem 282(16):11931-40
Loovers HM, et al.  (2007) Importance of the hsp70 ATPase domain in yeast prion propagation. Genetics 175(2):621-30
Shewmaker F, et al.  (2007) Ure2p Function Is Enhanced by Its Prion Domain in Saccharomyces cerevisiae. Genetics 176(3):1557-65
Cecchini M, et al.  (2006) A molecular dynamics approach to the structural characterization of amyloid aggregation. J Mol Biol 357(4):1306-21
Results: 1 - 30 of 58 records
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