SUP35/YDR172W Literature Guide Help

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

SUP35 - Protein Physical Properties (62)

Results: 1 - 30 of 62 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
Bucciantini M, et al.  (2012) Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1. FASEB J 26(2):818-31
Espargaro A, et al.  (2012) Yeast prions form infectious amyloid inclusion bodies in bacteria. Microb Cell Fact 11(1):89
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
Sabate R, et al.  (2012) Temperature dependence of the aggregation kinetics of Sup35 and Ure2p yeast prions. Biomacromolecules 13(2):474-83
Sharma J and Liebman SW  (2012) [PSI(+) ] prion variant establishment in yeast.LID - 10.1111/mmi.12024 [doi] Mol Microbiol ()
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
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
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
Liu Y, et al.  (2011) Prefibrillar aggregates of yeast prion Sup35NM and its variant are toxic to mammalian cells. Neurol Sci 32(6):1147-52
Measey TJ and Schweitzer-Stenner R  (2011) Vibrational Circular Dichroism as a Probe of Fibrillogenesis: The Origin of the Anomalous Intensity Enhancement of Amyloid-like Fibrils. J Am Chem Soc 133(4):1066-76
Nevzglyadova OV, et al.  (2011) The effect of red pigment on the amyloidization of yeast proteins. Yeast 28(7):505-26
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
Dong J, et al.  (2010) Optical trapping with high forces reveals unexpected behaviors of prion fibrils. Nat Struct Mol Biol 17(12):1422-30
Kawai-Noma S, et al.  (2010) In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells. J Cell Biol 190(2):223-31
Lancaster AK, et al.  (2010) The spontaneous appearance rate of the yeast prion [PSI+] and its implications for the evolution of the evolvability properties of the [PSI+] system. Genetics 184(2):393-400
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
Song Y, et al.  (2010) Quantitative Effects of Magnesium Chloride Stress on Aggregation of Sup35p in [psi(-)] Yeast Cells. Protein Pept Lett 17(12):1489-94
Tyedmers J, et al.  (2010) Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation. Proc Natl Acad Sci U S A 107(19):8633-8
Yeh V, et al.  (2010) The Hofmeister effect on amyloid formation using yeast prion protein. Protein Sci 19(1):47-56
van der Wel PC, et al.  (2010) Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR. Biochemistry 49(44):9457-69
Chen B, et al.  (2009) Measurement of amyloid fibril mass-per-length by tilted-beam transmission electron microscopy. Proc Natl Acad Sci U S A 106(34):14339-44
Kawai-Noma S, et al.  (2009) Single mother-daughter pair analysis to clarify the diffusion properties of yeast prion Sup35 in guanidine-HCl-treated [PSI] cells. Genes Cells 14(9):1045-54
Knowles TP, et al.  (2009) An analytical solution to the kinetics of breakable filament assembly. Science 326(5959):1533-7
Mathur V, et al.  (2009) Ssa1 overexpression and [PIN(+)] variants cure [PSI(+)] by dilution of aggregates. J Mol Biol 390(2):155-67
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
Warkocki Z, et al.  (2009) Reconstitution of both steps of Saccharomyces cerevisiae splicing with purified spliceosomal components. Nat Struct Mol Biol 16(12):1237-43
Fabret C, et al.  (2008) A novel mutant of the Sup35 protein of Saccharomyces cerevisiae defective in translation termination and in GTPase activity still supports cell viability. BMC Mol Biol 9:22
Results: 1 - 30 of 62 records
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