SUP35/YDR172W Literature Guide Help

Other names published for SUP35: GST1, PNM2, SAL3, SUF12, SUP2, SUP36, [PSI], [PSI(+)], eRF3, YDR172W

SUP35 - Function/Process (114)

ReferenceOther Genes Addressed
Bateman DA and Wickner RB  (2012) [PSI+] Prion transmission barriers protect Saccharomyces cerevisiae from infection: intraspecies 'species barriers'. Genetics 190(2):569-79
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
Nizhnikov AA, et al.  (2012) [NSI+] determinant has a pleiotropic phenotypic manifestation that is modulated by SUP35, SUP45, and VTS1 genes. Curr Genet 58(1):35-47
Afanasieva EG, et al.  (2011) Molecular Basis for Transmission Barrier and Interference between Closely Related Prion Proteins in Yeast. J Biol Chem 286(18):15773-80
McGlinchey RP, et al.  (2011) Suicidal [PSI+] is a lethal yeast prion. Proc Natl Acad Sci U S A 108(13):5337-41
Derdowski A, et al.  (2010) A size threshold limits prion transmission and establishes phenotypic diversity. Science 330(6004):680-3
Shoemaker CJ, et al.  (2010) Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay. Science 330(6002):369-72
Sideri TC, et al.  (2010) Ribosome-associated peroxiredoxins suppress oxidative stress-induced de novo formation of the [PSI+] prion in yeast. Proc Natl Acad Sci U S A 107(14):6394-9
Tyedmers J, et al.  (2010) Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation. Proc Natl Acad Sci U S A 107(19):8633-8
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
Doronina VA, et al.  (2008) Site-specific release of nascent chains from ribosomes at a sense codon. Mol Cell Biol 28(13):4227-39
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