SUP35/YDR172W Literature Guide Help

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

SUP35 - Protein/Nucleic Acid Structure (106)

Results: 1 - 30 of 106 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
Espargaro A, et al.  (2012) Yeast prions form infectious amyloid inclusion bodies in bacteria. Microb Cell Fact 11(1):89
Kochneva-Pervukhova NV, et al.  (2012) Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast. PLoS One 7(1):e29832
Portillo AM, et al.  (2012) Effect of electrostatics on aggregation of prion protein Sup35 peptide. J Phys Condens Matter 24(16):164205
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
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 ()
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
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
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
McGlinchey RP, et al.  (2011) Suicidal [PSI+] is a lethal yeast prion. Proc Natl Acad Sci U S A 108(13):5337-41
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
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
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
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
Sideri TC, et al.  (2010) Ribosome-associated peroxiredoxins suppress oxidative stress-induced de novo formation of the [PSI+] prion in yeast. Proc Natl Acad Sci U S A 107(14):6394-9
van der Wel PC, et al.  (2010) Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR. Biochemistry 49(44):9457-69
Berryman JT, et al.  (2009) Thermodynamic description of polymorphism in Q- and N-rich peptide aggregates revealed by atomistic simulation. Biophys J 97(1):1-11
Palhano FL, et al.  (2009) A fluorescent mutant of the NM domain of the yeast prion Sup35 provides insight into fibril formation and stability. Biochemistry 48(29):6811-23
Periole X, et al.  (2009) Factors That Affect the Degree of Twist in beta-Sheet Structures: A Molecular Dynamics Simulation Study of a Cross-beta Filament of the GNNQQNY Peptide. J Phys Chem B 113(6):1728-1737
Reddy G, et al.  (2009) Dynamics of locking of peptides onto growing amyloid fibrils. Proc Natl Acad Sci U S A 106(29):11948-53
Shewmaker F, et al.  (2009) Two prion variants of Sup35p have in-register parallel beta-sheet structures, independent of hydration. Biochemistry 48(23):5074-82
Shibata S, et al.  (2009) Localization of prion-destabilizing mutations in the N-terminal non-prion domain of Rnq1 in Saccharomyces cerevisiae. Prion 3(4):250-8
Suhre MH, et al.  (2009) Influence of divalent copper, manganese and zinc ions on fibril nucleation and elongation of the amyloid-like yeast prion determinant Sup35p-NM. J Inorg Biochem 103(12):1711-20
Bagriantsev SN, et al.  (2008) Variant-specific [PSI+] Infection Is Transmitted by Sup35 Polymers within [PSI+] Aggregates with Heterogeneous Protein Composition. Mol Biol Cell 19(6):2433-43
Krammer C, et al.  (2008) Prion protein/protein interactions: fusion with yeast Sup35p-NM modulates cytosolic PrP aggregation in mammalian cells. FASEB J 22(3):762-73
Shewmaker F, et al.  (2008) Amyloids of Shuffled Prion Domains That Form Prions Have a Parallel In-Register beta-Sheet Structure. Biochemistry 47(13):4000-4007
Results: 1 - 30 of 106 records
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