URE2/YNL229C Literature Guide Help

Other names published for URE2: [URE3], YNL229C

URE2 - Protein Physical Properties (28)

ReferenceOther Genes Addressed
Espargaro A, et al.  (2012) Yeast prions form infectious amyloid inclusion bodies in bacteria. Microb Cell Fact 11(1):89
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
Sabate R, et al.  (2012) Temperature dependence of the aggregation kinetics of Sup35 and Ure2p yeast prions. Biomacromolecules 13(2):474-83
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
Sharma D and Masison DC  (2011) Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p. Proc Natl Acad Sci U S A 108(33):13665-70
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
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
Savistchenko J, et al.  (2008) Molecular chaperones and the assembly of the prion ure2p in vitro. J Biol Chem 283(23):15732-9
Shewmaker F, et al.  (2008) Amyloids of Shuffled Prion Domains That Form Prions Have a Parallel In-Register beta-Sheet Structure. Biochemistry 47(13):4000-4007
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
Redeker V, et al.  (2007) Hydrogen/Deuterium exchange mass spectrometric analysis of conformational changes accompanying the assembly of the yeast prion ure2p into protein fibrils. J Mol Biol 369(4):1113-25
Brachmann A, et al.  (2005) Prion generation in vitro: amyloid of Ure2p is infectious. EMBO J 24(17):3082-92
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
Baxa U, et al.  (2004) The N-terminal prion domain of Ure2p converts from an unfolded to a thermally resistant conformation upon filament formation. J Mol Biol 339(2):259-64
Ross ED, et al.  (2004) Scrambled prion domains form prions and amyloid. Mol Cell Biol 24(16):7206-13
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
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
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
Bousset L, et al.  (2002) Structure and assembly properties of the yeast prion Ure2p. C R Biol 325(1):3-8
Edskes HK and Wickner RB  (2002) Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein. Proc Natl Acad Sci U S A 99 Suppl 4:16384-91
Masison DC, et al.  (1997) The prion model for [URE3] of yeast: spontaneous generation and requirements for propagation. Proc Natl Acad Sci U S A 94(23):12503-8
Masison DC and Wickner RB  (1995) Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science 270(5233):93-5
Coschigano PW and Magasanik B  (1991) The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione s-transferases. Mol Cell Biol 11(2):822-32