SUP35/YDR172W Literature Guide Help

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

SUP35 - Other Features (107)

Results: 1 - 30 of 107 records
   1  2  3  4 
ReferenceOther Genes Addressed
Lancaster DL, et al.  (2013) Chaperone proteins select and maintain [PIN+] prion conformations in Saccharomyces cerevisiae. J Biol Chem 288(2):1266-76
Halfmann R, et al.  (2012) Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature 482(7385):363-8
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
Verma M, et al.  (2012) Curcumin Prevents Formation of Polyglutamine Aggregates by Inhibiting Vps36, a Component of the ESCRT-II Complex. PLoS One 7(8):e42923
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
Hines JK, et al.  (2011) [SWI], the Prion Formed by the Chromatin Remodeling Factor Swi1, Is Highly Sensitive to Alterations in Hsp70 Chaperone System Activity. PLoS Genet 7(2):e1001309
Lin JY, et al.  (2011) Inter-Allelic Prion Propagation Reveals Conformational Relationships among a Multitude of [PSI] Strains. PLoS Genet 7(9):e1002297
Nemecek J, et al.  (2011) Retraction for Nemecek et al.: A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen. Proc Natl Acad Sci U S A 108(24):10022
Redeker V, et al.  (2011) Qualitative and quantitative multiplexed proteomic analysis of complex yeast protein fractions that modulate the assembly of the yeast prion sup35p. PLoS One 6(9):e23659
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
Yin W, et al.  (2011) [Mechanism and application of molecular self-assembly in Sup35 prion domain of Saccharomyces cerevisiae]. Sheng Wu Gong Cheng Xue Bao 27(10):1401-7
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
Pogoda AA, et al.  (2010) [PIN (+)]-dependent induction of protease-resistant amyloids by Ade2p protein fused with prionizing NM domain of Sup35 protein of the yeast Saccharomyces cerevisiae. Dokl Biochem Biophys 433():183-6
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
Urakov VN, et al.  (2010) Interdependence of amyloid formation in yeast: implications for polyglutamine disorders and biological functions. Prion 4(1):45-52
Ishiwata M, et al.  (2009) A G-protein gamma subunit mimic is a general antagonist of prion propagation in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 106(3):791-6
Krammer C, et al.  (2009) The yeast Sup35NM domain propagates as a prion in mammalian cells. Proc Natl Acad Sci U S A 106(2):462-7
Masel J and Griswold CK  (2009) The Strength of Selection Against the Yeast Prion [PSI+]. Genetics 181(3):1057-63
Park HJ, et al.  (2009) Increased -1 ribosomal frameshifting efficiency by yeast prion-like phenotype [PSI+]. FEBS Lett 583(4):665-9
Sikora J, et al.  (2009) Yeast prion [PSI(+)] lowers the levels of mitochondrial prohibitins. Biochim Biophys Acta 1793(11):1703-9
Tang H, et al.  (2009) Fibrinogen has chaperone-like activity. Biochem Biophys Res Commun 378(3):662-7
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
Feng BY, et al.  (2008) Small-molecule aggregates inhibit amyloid polymerization. Nat Chem Biol 4(3):197-9
Joseph SB and Kirkpatrick M  (2008) Effects of the [PSI+] prion on rates of adaptation in yeast. J Evol Biol 21(3):773-80
Kurahashi H, et al.  (2008) A regulatory role of the Rnq1 nonprion domain for prion propagation and polyglutamine aggregates. Mol Cell Biol 28(10):3313-23
Namy O, et al.  (2008) Epigenetic control of polyamines by the prion [PSI+]. Nat Cell Biol 10(9):1069-75
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
Sadlish H, et al.  (2008) Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS ONE 3(3):e1763
Sharma D and Masison DC  (2008) Functionally redundant isoforms of a yeast hsp70 chaperone subfamily have different antiprion effects. Genetics 179(3):1301-11
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 107 records
   1  2  3  4