SUP35/YDR172W Literature Guide Help

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

SUP35 - Primary Literature (257)

Results: 1 - 30 of 257 records
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ReferenceOther Genes Addressed
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
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 2(3):415-30
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
Bateman DA and Wickner RB  (2012) [PSI+] Prion transmission barriers protect Saccharomyces cerevisiae from infection: intraspecies 'species barriers'. Genetics 190(2):569-79
DeSantis ME and Shorter J  (2012) Hsp104 drives "protein-only" positive selection of Sup35 prion strains encoding strong [PSI(+)]. Chem Biol 19(11):1400-10
Espargaro A, et al.  (2012) Yeast prions form infectious amyloid inclusion bodies in bacteria. Microb Cell Fact 11(1):89
Halfmann R, et al.  (2012) Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature 482(7385):363-8
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
Kelly AC, et al.  (2012) Sex, prions, and plasmids in yeast. Proc Natl Acad Sci U S A 109(40):E2683-90
Kervestin S, et al.  (2012) Testing the faux-UTR model for NMD: analysis of Upf1p and Pab1p competition for binding to eRF3/Sup35p. Biochimie 94(7):1560-71
Klucevsek KM, et al.  (2012) The Paf1 complex subunit Rtf1 buffers cells against the toxic effects of [PSI+] and defects in Rkr1-dependent protein quality control in Saccharomyces cerevisiae. Genetics 191(4):1107-18
Kochneva-Pervukhova NV, et al.  (2012) Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast. PLoS One 7(1):e29832
Krishnan R, et al.  (2012) Conserved features of intermediates in amyloid assembly determine their benign or toxic states. Proc Natl Acad Sci U S A 109(28):11172-7
Sharma J and Liebman SW  (2012) [PSI(+) ] prion variant establishment in yeast.LID - 10.1111/mmi.12024 [doi] Mol Microbiol ()
Torabi N and Kruglyak L  (2012) Genetic basis of hidden phenotypic variation revealed by increased translational readthrough in yeast. PLoS Genet 8(3):e1002546
Wang IF, et al.  (2012) The self-interaction of native TDP-43 C terminus inhibits its degradation and contributes to early proteinopathies. Nat Commun 3():766
Zhao X, et al.  (2012) Sequestration of Sup35 by aggregates of huntingtin fragments causes toxicity of [PSI+] yeast. J Biol Chem 287(28):23346-55
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
Baxa U, et al.  (2011) In Sup35p filaments (the [PSI+] prion), the globular C-terminal domains are widely offset from the amyloid fibril backbone. Mol Microbiol 79(2):523-32
Castro CE, et al.  (2011) Physical properties of polymorphic yeast prion amyloid fibers. Biophys J 101(2):439-48
Disalvo S, et al.  (2011) Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation. Nat Struct Mol Biol 18(4):486-92
Foo CK, et al.  (2011) Radically different amyloid conformations dictate the seeding specificity of a chimeric sup35 prion. J Mol Biol 408(1):1-8
Hines JK, et al.  (2011) Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements. Prion 5(4):238-44
Inoue Y, et al.  (2011) Yeast prion protein New1 can break Sup35 amyloid fibrils into fragments in an ATP-dependent manner. Genes Cells 16(5):545-56
Kabani M, et al.  (2011) A mutation within the C-terminal domain of Sup35p that affects [PSI+] prion propagation. Mol Microbiol 81(3):640-58
Results: 1 - 30 of 257 records
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