SUP35/YDR172W Literature Guide Help

Other names published for SUP35: GST1, PNM2, SAL3, SUF12, SUP2, SUP36, [PSI], [PSI(+)], YDR172W

SUP35 - Function/Process (104)

Results: 1 - 30 of 104 records
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ReferenceOther Genes Addressed
Pezza JA, et al.  (2009) The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype. Mol Biol Cell 20(3):1068-80
Saini P, et al.  (2009) Hypusine-containing protein eIF5A promotes translation elongation. Nature 459(7243):118-21
Strawn LA, et al.  (2009) Mutants of the Paf1 complex alter phenotypic expression of the yeast prion [PSI+]. Mol Biol Cell 20(8):2229-41
Warkocki Z, et al.  (2009) Reconstitution of both steps of Saccharomyces cerevisiae splicing with purified spliceosomal components. Nat Struct Mol Biol 16(12):1237-43
Fan-Minogue H, et al.  (2008) Distinct eRF3 requirements suggest alternate eRF1 conformations mediate peptide release during eukaryotic translation termination. Mol Cell 30(5):599-609
[No authors listed]  (2008) [Overexpression of gene PPZ1 in the yeast Saccharomyces cerevisiae affects the efficiency of nonsense suppression] Genetika 44(2):177-84
von der Haar T  (2008) A quantitative estimation of the global translational activity in logarithmically growing yeast cells. BMC Syst Biol 287
Li LB, et al.  (2007) Suppression of polyglutamine toxicity by the yeast sup35 prion domain in Drosophila. J Biol Chem 282(52):37694-701
Volkov K, et al.  (2007) N-terminal extension of Saccharomyces cerevisiae translation termination factor eRF3 influences the suppression efficiency of sup35 mutations. FEMS Yeast Res 7(3):357-365
Liebman SW, et al.  (2006) Biochemical and genetic methods for characterization of [PIN+] prions in yeast. Methods 39(1):23-34
Ono B, et al.  (2006) Production of a Polymer-Forming Fusion Protein in Escerichia coli Strain BL21. Biosci Biotechnol Biochem 70(12):2813-23
Urakov VN, et al.  (2006) N-terminal region of Saccharomyces cerevisiae eRF3 is essential for the functioning of the eRF1/eRF3 complex beyond translation termination. BMC Mol Biol 7:34
Wei HY, et al.  (2006) [Dynamics of in vitro amyloid fiber formation of yeast prion protein Sup35NM] Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi 20(1):39-42
Allen KD, et al.  (2005) Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]. Genetics 169(3):1227-42
Borchsenius AS, et al.  (2005) [Association between defects of karyogamy and translation termination in yeast Saccharomyces cerevisiae] Genetika 41(2):178-86
He Y, et al.  (2005) Fibrillogenesis of apomyoglobin facilitated by aggregation sequence of yeast Sup35 in various regions. FEBS Lett 579(6):1503-8
Ross ED, et al.  (2005) Primary sequence independence for prion formation. Proc Natl Acad Sci U S A 102(36):12825-30
Salnikova AB, et al.  (2005) Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids. J Biol Chem 280(10):8808-12
Tanaka M  (2005) [Final proof of "prion hypothesis" in the yeast prion [PSI+] system] Tanpakushitsu Kakusan Koso 50(3):207-14
Wilson MA, et al.  (2005) Genetic interactions between [PSI+] and nonstop mRNA decay affect phenotypic variation. Proc Natl Acad Sci U S A 102(29):10244-9
Aguzzi A  (2004) Understanding the diversity of prions. Nat Cell Biol 6(4):290-2
Amrani N, et al.  (2004) A faux 3'-UTR promotes aberrant termination and triggers nonsense-mediated mRNA decay. Nature 432(7013):112-8
Bradley ME and Liebman SW  (2004) The Sup35 domains required for maintenance of weak, strong or undifferentiated yeast [PSI+] prions. Mol Microbiol 51(6):1649-59
Chabelskaya S, et al.  (2004) Nonsense mutations in the essential gene SUP35 of Saccharomyces cerevisiae are non-lethal. Mol Genet Genomics 272(3):297-307
Jones G, et al.  (2004) Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding. Mol Cell Biol 24(9):3928-37
Kimura Y, et al.  (2004) The role of pre-existing aggregates in Hsp104-dependent polyglutamine aggregate formation and epigenetic change of yeast prions. Genes Cells 9(8):685-96
King CY and Diaz-Avalos R  (2004) Protein-only transmission of three yeast prion strains. Nature 428(6980):319-23
Kishimoto A, et al.  (2004) beta-Helix is a likely core structure of yeast prion Sup35 amyloid fibers. Biochem Biophys Res Commun 315(3):739-45
Kobayashi T, et al.  (2004) The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay. J Biol Chem 279(44):45693-700
Masison DC  (2004) Cell biology: designer prions. Nature 429(6987):37-8
Results: 1 - 30 of 104 records
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