SUP35/YDR172W Literature Guide Help

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

SUP35 - Protein Sequence Features (119)

Results: 1 - 30 of 119 records
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ReferenceOther Genes Addressed
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
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
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
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
Du Z  (2011) The complexity and implications of yeast prion domains. Prion 5(4):311-6
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
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
Lewandowski JR, et al.  (2011) Structural complexity of a composite amyloid fibril. J Am Chem Soc 133(37):14686-98
Marcelino-Cruz AM, et al.  (2011) Site-specific structural analysis of a yeast prion strain with species-specific seeding activity. Prion 5(3):208-14
Nevzglyadova OV, et al.  (2011) The effect of red pigment on the amyloidization of yeast proteins. Yeast 28(7):505-26
Toombs JA, et al.  (2011) [PSI] Maintenance Is Dependent on the Composition, Not Primary Sequence, of the Oligopeptide Repeat Domain. PLoS One 6(7):e21953
Verges KJ, et al.  (2011) Strain conformation, primary structure and the propagation of the yeast prion [PSI(+)]. Nat Struct Mol Biol 18(4):493-9
Ader C, et al.  (2010) Amyloid-like interactions within nucleoporin FG hydrogels. Proc Natl Acad Sci U S A 107(14):6281-5
Andrey SB, et al.  (2010) HRMAS (1)H NMR Conformational Study of the Resin-Bound Amyloid-Forming Peptide GNNQQNY from the Yeast Prion Sup35. J Phys Chem A 114(10):3457-65
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
Chen B, et al.  (2010) Genetic and epigenetic control of the efficiency and fidelity of cross-species prion transmission. Mol Microbiol 76(6):1483-99
Dong J, et al.  (2010) Optical trapping with high forces reveals unexpected behaviors of prion fibrils. Nat Struct Mol Biol 17(12):1422-30
Ferreon AC, et al.  (2010) Single-molecule fluorescence studies of intrinsically disordered proteins. Methods Enzymol 472():179-204
Goehler H, et al.  (2010) Pathogenic polyglutamine tracts are potent inducers of spontaneous sup35 and rnq1 amyloidogenesis. PLoS One 5(3):e9642
Marshall KE, et al.  (2010) Characterizing the Assembly of the Sup35 Yeast Prion Fragment, GNNQQNY: Structural Changes Accompany a Fiber-to-Crystal Switch. Biophys J 98(2):330-338
Ohhashi Y, et al.  (2010) Differences in prion strain conformations result from non-native interactions in a nucleus. Nat Chem Biol 6(3):225-230
Ross ED and Toombs JA  (2010) The effects of amino acid composition on yeast prion formation and prion domain interactions. Prion 4(2):60-5
Results: 1 - 30 of 119 records
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