SUP35/YDR172W Literature Guide Help

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

SUP35 - Strains/Constructs (151)

ReferenceOther Genes Addressed
Khoshnevis S, et al.  (2010) The iron-sulphur protein RNase L inhibitor functions in translation termination. EMBO Rep ()
Ohhashi Y, et al.  (2010) Differences in prion strain conformations result from non-native interactions in a nucleus. Nat Chem Biol ()
Speare JO, et al.  (2010) GPI anchoring facilitates propagation and spread of misfolded Sup35 aggregates in mammalian cells. EMBO J ()
Toombs JA, et al.  (2010) Compositional determinants of prion formation in yeast. Mol Cell Biol 30(1):319-32
Alberti S, et al.  (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137(1):146-58
Bardill JP and True HL  (2009) Heterologous prion interactions are altered by mutations in the prion protein rnq1p. J Mol Biol 388(3):583-96
Byrne LJ, et al.  (2009) The number and transmission of [PSI] prion seeds (Propagons) in the yeast Saccharomyces cerevisiae. PLoS ONE 4(3):e4670
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
Greene LE, et al.  (2009) Application of GFP-labeling to study prions in yeast. Protein Pept Lett 16(6):635-41
Kawai-Noma S, et al.  (2009) Single mother-daughter pair analysis to clarify the diffusion properties of yeast prion Sup35 in guanidine-HCl-treated [PSI] cells. Genes Cells 14(9):1045-54
Krammer C, et al.  (2009) The yeast Sup35NM domain propagates as a prion in mammalian cells. Proc Natl Acad Sci U S A 106(2):462-7
Mathur V, et al.  (2009) Ssa1 overexpression and [PIN(+)] variants cure [PSI(+)] by dilution of aggregates. J Mol Biol 390(2):155-67
Men D, et al.  (2009) Seeding-induced self-assembling protein nanowires dramatically increase the sensitivity of immunoassays. Nano Lett 9(6):2246-50
Nemecek J, et al.  (2009) A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen. Proc Natl Acad Sci U S A 106(6):1892-6
Nevzglyadova OV, et al.  (2009) Prion-associated proteins in yeast: comparative analysis of isogenic [PSI(+)] and [psi(-)] strains. Yeast 26(11):611-31
Reddy G, et al.  (2009) Dynamics of locking of peptides onto growing amyloid fibrils. Proc Natl Acad Sci U S A 106(29):11948-53
Roberts BE, et al.  (2009) A synergistic small-molecule combination directly eradicates diverse prion strain structures. Nat Chem Biol 5(12):936-46
Ross CD, et al.  (2009) A Promiscuous Prion: Efficient Induction of [URE3] Prion Formation by Heterologous Prion Domains. Genetics 183(3):929-40
Senechal P, et al.  (2009) The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion. PLoS One 4(9):e6939
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
Tank EM and True HL  (2009) Disease-associated mutant ubiquitin causes proteasomal impairment and enhances the toxicity of protein aggregates. PLoS Genet 5(2):e1000382
Valouev IA, et al.  (2009) Elongation factor eEF1B modulates functions of the release factors eRF1 and eRF3 and the efficiency of translation termination in yeast. BMC Mol Biol 10:60
Vishveshwara N and Liebman SW  (2009) Heterologous cross-seeding mimics cross-species prion conversion in a yeast model. BMC Biol 7:26
Vishveshwara N, et al.  (2009) Sequestration of essential proteins causes prion associated toxicity in yeast. Mol Microbiol 73(6):1101-14
Zhang H, et al.  (2009) Alcohol oxidase (AOX1) from Pichia pastoris is a novel inhibitor of prion propagation and a potential ATPase. Mol Microbiol 71(3):702-716
Akhmaloka, et al.  (2008) Mutation at tyrosine in AMLRY (GILRY like) motif of yeast eRF1 on nonsense codons suppression and binding affinity to eRF3. Int J Biol Sci 4(2):87-95
Alexandrov IM, et al.  (2008) Appearance and Propagation of Polyglutamine-based Amyloids in Yeast: TYROSINE RESIDUES ENABLE POLYMER FRAGMENTATION. J Biol Chem 283(22):15185-92
Amrani N, et al.  (2008) Translation factors promote the formation of two states of the closed-loop mRNP. Nature 453(7199):1276-80
Bolger TA, et al.  (2008) The mRNA export factor Gle1 and inositol hexakisphosphate regulate distinct stages of translation. Cell 134(4):624-33
Breslow DK, et al.  (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8