SUP35/YDR172W Literature Guide Help

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

SUP35 - Strains/Constructs (215)

Results: 1 - 30 of 215 records
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ReferenceOther Genes Addressed
Lancaster DL, et al.  (2013) Chaperone proteins select and maintain [PIN+] prion conformations in Saccharomyces cerevisiae. J Biol Chem 288(2):1266-76
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
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
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
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
Saibil HR, et al.  (2012) Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures. Proc Natl Acad Sci U S A 109(37):14906-11
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
Verma M, et al.  (2012) Curcumin Prevents Formation of Polyglutamine Aggregates by Inhibiting Vps36, a Component of the ESCRT-II Complex. PLoS One 7(8):e42923
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
Winkler J, et al.  (2012) Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol 198(3):387-404
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
Chernova TA, et al.  (2011) Prion induction by the short-lived, stress-induced protein lsb2 is regulated by ubiquitination and association with the actin cytoskeleton. Mol Cell 43(2):242-52
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
Hines JK, et al.  (2011) Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements. Prion 5(4):238-44
Hines JK, et al.  (2011) [SWI], the Prion Formed by the Chromatin Remodeling Factor Swi1, Is Highly Sensitive to Alterations in Hsp70 Chaperone System Activity. PLoS Genet 7(2):e1001309
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
Lin JY, et al.  (2011) Inter-Allelic Prion Propagation Reveals Conformational Relationships among a Multitude of [PSI] Strains. PLoS Genet 7(9):e1002297
Manogaran AL, et al.  (2011) Prion formation and polyglutamine aggregation are controlled by two classes of genes. PLoS Genet 7(5):e1001386
Results: 1 - 30 of 215 records
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