SUP35/YDR172W Literature Guide Help

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

SUP35 - Disease Gene Related (38)

Results: 1 - 30 of 38 records
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ReferenceOther Genes Addressed
Hofmann J, et al.  (2012) Creutzfeldt-Jakob disease and mad cows: lessons learnt from yeast cells. Swiss Med Wkly 142():1-11
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
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
Cushman M, et al.  (2010) Prion-like disorders: blurring the divide between transmissibility and infectivity. J Cell Sci 123(Pt 8):1191-201
Duennwald ML and Shorter J  (2010) Countering amyloid polymorphism and drug resistance with minimal drug cocktails. Prion 4(4):244-51
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
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
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
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
Alexandrov IM, et al.  (2008) Appearance and Propagation of Polyglutamine-based Amyloids in Yeast: TYROSINE RESIDUES ENABLE POLYMER FRAGMENTATION. J Biol Chem 283(22):15185-92
Kalastavadi T and True HL  (2008) Prion protein insertional mutations increase aggregation propensity but not fiber stability. BMC Biochem 9:7
Chen B, et al.  (2007) Prion species barrier between the closely related yeast proteins is detected despite coaggregation. Proc Natl Acad Sci U S A 104(8):2791-6
Kushnirov VV, et al.  (2007) Prion and nonprion amyloids: a comparison inspired by the yeast Sup35 protein. Prion 1(3):179-84
Shkundina IS and Ter-Avanesyan MD  (2007) Prions. Biochemistry (Mosc) 72(13):1519-36
Tessier PM and Lindquist S  (2007) Prion recognition elements govern nucleation, strain specificity and species barriers. Nature 447(7144):556-61
von der Haar T, et al.  (2007) Development of a Novel Yeast Cell-Based System for Studying the Aggregation of Alzheimer's Disease-Associated Abeta Peptides in vivo. Neurodegener Dis 4(2-3):136-47
Tanaka M, et al.  (2006) The physical basis of how prion conformations determine strain phenotypes. Nature 442(7102):585-9
Tribouillard D, et al.  (2006) Using budding yeast to screen for anti-prion drugs. Biotechnol J 1(1):58-67
Zheng J, et al.  (2006) Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure. Phys Biol 3(3):P1-4
Konno T, et al.  (2005) Covalent blocking of fibril formation and aggregation of intracellular amyloidgenic proteins by transglutaminase-catalyzed intramolecular cross-linking. Biochemistry 44(6):2072-9
Sigurdson C, et al.  (2005) Reconstructing prions: fibril assembly from simple yeast to complex mammals. Neurodegener Dis 2(1):1-5
Maloney B, et al.  (2004) Presence of a "CAGA box" in the APP gene unique to amyloid plaque-forming species and absent in all APLP-1/2 genes: implications in Alzheimer's disease. FASEB J 18(11):1288-90
Bradley ME and Liebman SW  (2003) Destabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants. Genetics 165(4):1675-85
Gsponer J, et al.  (2003) The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35. Proc Natl Acad Sci U S A 100(9):5154-9
Couzin J  (2002) Molecular biology. In yeast, prions' killer image doesn't apply. Science 297(5582):758-61
Perutz MF, et al.  (2002) Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques. Proc Natl Acad Sci U S A 99(8):5596-600
Perutz MF, et al.  (2002) Amyloid fibers are water-filled nanotubes. Proc Natl Acad Sci U S A 99(8):5591-5
Barrette I, et al.  (2001) Pseudoknots in prion protein mRNAs confirmed by comparative sequence analysis and pattern searching. Nucleic Acids Res 29(3):753-8
Lindquist S, et al.  (2001) Investigating protein conformation-based inheritance and disease in yeast. Philos Trans R Soc Lond B Biol Sci 356(1406):169-76
Xu S, et al.  (2001) The assembly of amyloidogenic yeast sup35 as assessed by scanning (atomic) force microscopy: an analogy to linear colloidal aggregation? Biophys J 81(1):446-54
Results: 1 - 30 of 38 records
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