SUP35/YDR172W Literature Guide Help

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

SUP35 - All Curated References (738)

ReferenceOther Genes Addressed
Arai C, et al.  (2013) Clearance of yeast prions by misfolded multi-transmembrane proteins. Biochimie 95(6):1223-32
Bateman DA and Wickner RB  (2013) The [PSI(+)] Prion Exists as a Dynamic Cloud of Variants. PLoS Genet 9(1):e1003257
Firczuk H, et al.  (2013) An in vivo control map for the eukaryotic mRNA translation machinery. Mol Syst Biol 9():635
Grousl T, et al.  (2013) Heat Shock-Induced Accumulation of Translation Elongation and Termination Factors Precedes Assembly of Stress Granules in S. cerevisiae. PLoS One 8(2):e57083
Hofmann JP, et al.  (2013) Cell-to-cell propagation of infectious cytosolic protein aggregates. Proc Natl Acad Sci U S A 110(15):5951-6
Kurata S, et al.  (2013) Possible steps of complete disassembly of post-termination complex by yeast eEF3 deduced from inhibition by translocation inhibitors. Nucleic Acids Res 41(1):264-76
Lancaster DL, et al.  (2013) Chaperone proteins select and maintain [PIN+] prion conformations in Saccharomyces cerevisiae. J Biol Chem 288(2):1266-76
Oishi K, et al.  (2013) A bipolar functionality of Q/N-rich proteins: Lsm4 amyloid causes clearance of yeast prions. Microbiologyopen ()
Osborne KL, et al.  (2013) Thermodynamic analysis of structural transitions during GNNQQNY aggregation. Proteins ()
Reidy M, et al.  (2013) Schizosaccharomyces pombe Disaggregation Machinery Chaperones Support Saccharomyces cerevisiae Growth and Prion Propagation. Eukaryot Cell 12(5):739-45
Tartakoff AM, et al.  (2013) Septin-containing barriers control the differential inheritance of cytoplasmic elements. Cell Rep 3(1):223-36
Tomson BN and Arndt KM  (2013) The many roles of the conserved eukaryotic Paf1 complex in regulating transcription, histone modifications, and disease states. Biochim Biophys Acta 1829(1):116-26
Tycko R and Wickner RB  (2013) Molecular Structures of Amyloid and Prion Fibrils: Consensus versus Controversy. Acc Chem Res ()
Wickner RB, et al.  (2013) Amyloids and yeast prion biology. Biochemistry 52(9):1514-27
Wickner RB, et al.  (2013) Viruses and Prions of Saccharomyces cerevisiae. Adv Virus Res 86():1-36
Yang Z, et al.  (2013) Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability. PLoS Genet 9(1):e1003236
Zhao JH, et al.  (2013) Molecular modeling to investigate the binding of Congo red toward GNNQQNY protofibril and in silico virtual screening for the identification of new aggregation inhibitors. J Mol Model 19(1):151-62
Alexandrov AI, et al.  (2012) The effects of amino Acid composition of glutamine-rich domains on amyloid formation and fragmentation. PLoS One 7(10):e46458
Bateman DA and Wickner RB  (2012) [PSI+] Prion transmission barriers protect Saccharomyces cerevisiae from infection: intraspecies 'species barriers'. Genetics 190(2):569-79
Bucciantini M, et al.  (2012) Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1. FASEB J 26(2):818-31
Cheng PN, et al.  (2012) Amyloid beta-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity. Nat Chem 4(11):927-33
Desantis ME, et al.  (2012) Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients. Cell 151(4):778-93
Duennwald ML, et al.  (2012) Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 10(6):e1001346
Espargaro A, et al.  (2012) Yeast prions form infectious amyloid inclusion bodies in bacteria. Microb Cell Fact 11(1):89
Gong H, et al.  (2012) Polyglutamine toxicity is controlled by prion composition and gene dosage in yeast. PLoS Genet 8(4):e1002634
Halfmann R, et al.  (2012) Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature 482(7385):363-8
Harbi D, et al.  (2012) PrionHome: A Database of Prions and Other Sequences Relevant to Prion Phenomena. PLoS ONE 7(2):e31785
Helsen CW and Glover JR  (2012) A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI (+) ]. Prion 6(3):234-9
Helsen CW and Glover JR  (2012) Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104). J Biol Chem 287(1):542-56
Hofmann J, et al.  (2012) Creutzfeldt-Jakob disease and mad cows: lessons learnt from yeast cells. Swiss Med Wkly 142():1-11