SUP35/YDR172W Literature Guide Help

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

SUP35 - Omics (33)

ReferenceOther Genes Addressed
Harbi D, et al.  (2012) PrionHome: A Database of Prions and Other Sequences Relevant to Prion Phenomena. PLoS ONE 7(2):e31785
Kiktev DA, et al.  (2012) Regulation of chaperone effects on a yeast prion by cochaperone Sgt2. Mol Cell Biol 32(24):4960-70
Qi X, et al.  (2012) A Variational Model for Oligomer-Formation Process of GNNQQNY Peptide from Yeast Prion Protein Sup35. Biophys J 102(3):597-605
Ambroset C, et al.  (2011) Deciphering the molecular basis of wine yeast fermentation traits using a combined genetic and genomic approach. G3 (Bethesda) 1(4):263-81
Bryan AW Jr, et al.  (2011) STITCHER: Dynamic assembly of likely amyloid and prion beta-structures from secondary structure predictions.LID - 10.1002/prot.23203 [doi] Proteins ()
Kiktev DA, et al.  (2011) Identification of genes influencing synthetic lethality of genetic and epigenetic alterations in translation termination factors in yeast. Dokl Biochem Biophys 438():117-9
Manogaran AL, et al.  (2011) Prion formation and polyglutamine aggregation are controlled by two classes of genes. PLoS Genet 7(5):e1001386
Nasica-Labouze J, et al.  (2011) A Multiscale Approach to Characterize the Early Aggregation Steps of the Amyloid-Forming Peptide GNNQQNY from the Yeast Prion Sup-35. PLoS Comput Biol 7(5):e1002051
Nevzglyadova OV, et al.  (2011) The effect of red pigment on the amyloidization of yeast proteins. Yeast 28(7):505-26
Palmer KJ, et al.  (2011) Kinetic models of guanidine hydrochloride-induced curing of the yeast [PSI(+)] prion. J Theor Biol 274(1):1-11
Redeker V, et al.  (2011) Qualitative and quantitative multiplexed proteomic analysis of complex yeast protein fractions that modulate the assembly of the yeast prion sup35p. PLoS One 6(9):e23659
Skelly DA, et al.  (2011) A powerful and flexible statistical framework for testing hypotheses of allele-specific gene expression from RNA-seq data. Genome Res 21(10):1728-37
Berhanu WM and Masunov AE  (2010) Natural polyphenols as inhibitors of amyloid aggregation. Molecular dynamics study of GNNQQNY heptapeptide decamer. Biophys Chem 149(1-2):12-21
Reddy G, et al.  (2010) Dry amyloid fibril assembly in a yeast prion peptide is mediated by long-lived structures containing water wires. Proc Natl Acad Sci U S A 107(50):21459-64
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
Byrne LJ, et al.  (2009) The number and transmission of [PSI] prion seeds (Propagons) in the yeast Saccharomyces cerevisiae. PLoS ONE 4(3):e4670
Friedel CC, et al.  (2009) Bootstrapping the interactome: unsupervised identification of protein complexes in yeast. J Comput Biol 16(8):971-87
Griswold CK and Masel J  (2009) Complex Adaptations Can Drive the Evolution of the Capacitor [PSI], Even with Realistic Rates of Yeast Sex. PLoS Genet 5(6):e1000517
Knowles TP, et al.  (2009) An analytical solution to the kinetics of breakable filament assembly. Science 326(5959):1533-7
Masel J and Griswold CK  (2009) The Strength of Selection Against the Yeast Prion [PSI+]. Genetics 181(3):1057-63
Sikora J, et al.  (2009) Yeast prion [PSI(+)] lowers the levels of mitochondrial prohibitins. Biochim Biophys Acta 1793(11):1703-9
Breslow DK, et al.  (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8
Del Vescovo V, et al.  (2008) Role of Hog1 and Yaf9 in the transcriptional response of Saccharomyces cerevisiae to cesium chloride. Physiol Genomics 33(1):110-20
Tyedmers J, et al.  (2008) Prion switching in response to environmental stress. PLoS Biol 6(11):e294
von der Haar T  (2008) A quantitative estimation of the global translational activity in logarithmically growing yeast cells. BMC Syst Biol 287
Zhang Z, et al.  (2007) Identification of amyloid fibril-forming segments based on structure and residue-based statistical potential. Bioinformatics 23(17):2218-25
Zhang Z, et al.  (2007) Molecular Dynamics Simulations on the Oligomer-Formation Process of the GNNQQNY Peptide from Yeast Prion Protein Sup35. Biophys J 93(5):1484-92
Fay JC, et al.  (2004) Population genetic variation in gene expression is associated with phenotypic variation in Saccharomyces cerevisiae. Genome Biol 5(4):R26
Williams I, et al.  (2004) Genome-wide prediction of stop codon readthrough during translation in the yeast Saccharomyces cerevisiae. Nucleic Acids Res 32(22):6605-16