SUP35/YDR172W Literature Guide Help

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

SUP35 - Techniques and Reagents (48)

Results: 1 - 30 of 48 records
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ReferenceOther Genes Addressed
Halfmann R, et al.  (2012) Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature 482(7385):363-8
Mitkevich OV, et al.  (2012) DNA aptamers detecting generic amyloid epitopes. Prion 6(4):400-6
Wickner RB, et al.  (2012) Study of amyloids using yeast. Methods Mol Biol 849():321-46
Zhong Z, et al.  (2012) [Quantification of the curing effects of phenanthridine on yeast prion [PSI+]]. Sheng Wu Gong Cheng Xue Bao 28(6):737-46
Castro CE, et al.  (2011) Physical properties of polymorphic yeast prion amyloid fibers. Biophys J 101(2):439-48
Hines JK, et al.  (2011) Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements. Prion 5(4):238-44
Hong JY, et al.  (2011) A new colour assay for [URE3] prion in a genetic background used to score for the [PSI?] prion. Yeast 28(7):555-60
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
Garrity SJ, et al.  (2010) Conversion of a yeast prion protein to an infectious form in bacteria. Proc Natl Acad Sci U S A 107(23):10596-601
Goehler H, et al.  (2010) Pathogenic polyglutamine tracts are potent inducers of spontaneous sup35 and rnq1 amyloidogenesis. PLoS One 5(3):e9642
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
Mathur V, et al.  (2010) Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast. Mol Biol Cell 21(9):1449-61
Men D, et al.  (2010) An auto-biotinylated bifunctional protein nanowire for ultra-sensitive molecular biosensing. Biosens Bioelectron 26(4):1137-41
Tanaka M  (2010) A protein transformation protocol for introducing yeast prion particles into yeast. Methods Enzymol 470():681-93
Yeh V, et al.  (2010) The Hofmeister effect on amyloid formation using yeast prion protein. Protein Sci 19(1):47-56
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
Greene LE, et al.  (2009) Application of GFP-labeling to study prions in yeast. Protein Pept Lett 16(6):635-41
Men D, et al.  (2009) Seeding-induced self-assembling protein nanowires dramatically increase the sensitivity of immunoassays. Nano Lett 9(6):2246-50
Voisset C, et al.  (2009) Procedure for identification and characterization of drugs efficient against Mammalian prion: from a yeast-based antiprion drug screening assay to in vivo mouse models. Infect Disord Drug Targets 9(1):31-9
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
Bolger TA, et al.  (2008) The mRNA export factor Gle1 and inositol hexakisphosphate regulate distinct stages of translation. Cell 134(4):624-33
Ono BI, et al.  (2008) Effects of mutations in yeast prion [PSI(+)] on amyloid toxicity manifested in Escherichia coli strain BL21. Prion 2(1):37-41
Puchalla J, et al.  (2008) Burst analysis spectroscopy: a versatile single-particle approach for studying distributions of protein aggregates and fluorescent assemblies. Proc Natl Acad Sci U S A 105(38):14400-5
[No authors listed]  (2008) [Estimating of changes in the amyloid and prion content of yeast cells] Tsitologiia 50(1):40-8
Tessier PM and Lindquist S  (2007) Prion recognition elements govern nucleation, strain specificity and species barriers. Nature 447(7144):556-61
Inoue Y and Yoshida M  (2006) In vitro assay for fragmentation of amyloid fibers of yeast prion protein. Methods 39(1):56-60
King CY, et al.  (2006) Transformation of yeast by infectious prion particles. Methods 39(1):68-71
Kushnirov VV, et al.  (2006) Purification and analysis of prion and amyloid aggregates. Methods 39(1):50-5
Tanaka M and Weissman JS  (2006) An efficient protein transformation protocol for introducing prions into yeast. Methods Enzymol 412:185-200
Results: 1 - 30 of 48 records
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