URE2/YNL229C Literature Guide Help

Other names published for URE2: [URE3], YNL229C

URE2 - Protein/Nucleic Acid Structure (55)

Results: 1 - 30 of 55 records
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ReferenceOther Genes Addressed
Espargaro A, et al.  (2012) Yeast prions form infectious amyloid inclusion bodies in bacteria. Microb Cell Fact 11(1):89
Habenstein B, et al.  (2012) A native-like conformation for the C-terminal domain of the prion Ure2p within its fibrillar form. Angew Chem Int Ed Engl 51(32):7963-6
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
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
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
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
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)
Berryman JT, et al.  (2009) Thermodynamic description of polymorphism in Q- and N-rich peptide aggregates revealed by atomistic simulation. Biophys J 97(1):1-11
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
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
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
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
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
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
Edskes HK, et al.  (2006) Nitrogen source and the retrograde signalling pathway affect detection, not generation, of the [URE3] prion. Yeast 23(11):833-40
Fayard B, et al.  (2006) Packing of the prion Ure2p in protein fibrils probed by fluorescence X-ray near-edge structure spectroscopy at sulfur K-edge. J Mol Biol 356(4):843-9
Ranson N, et al.  (2006) Insights into the architecture of the Ure2p yeast protein assemblies from helical twisted fibrils. Protein Sci 15(11):2481-7
Baxa U, et al.  (2005) Filaments of the Ure2p prion protein have a cross-beta core structure. J Struct Biol 150(2):170-9
Brachmann A, et al.  (2005) Prion generation in vitro: amyloid of Ure2p is infectious. EMBO J 24(17):3082-92
Catharino S, et al.  (2005) Characterization of oligomeric species in the fibrillization pathway of the yeast prion Ure2p. Biol Chem 386(7):633-41
Chan JC, et al.  (2005) Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p. Biochemistry 44(31):10669-80
Fay N, et al.  (2005) Structure of the prion Ure2p in protein fibrils assembled in vitro. J Biol Chem 280(44):37149-58
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
Results: 1 - 30 of 55 records
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