RNQ1/YCL028W Literature Guide Help

Other names published for RNQ1: [PIN(+)], YCL028W

RNQ1 - Other Features (23)

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
Sharma J and Liebman SW  (2012) [PSI(+) ] prion variant establishment in yeast.LID - 10.1111/mmi.12024 [doi] Mol Microbiol ()
Treusch S and Lindquist S  (2012) An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component. J Cell Biol 197(3):369-79
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
Kurahashi H, et al.  (2011) [PSI(+) ] aggregate enlargement in rnq1 nonprion domain mutants, leading to a loss of prion in yeast. Genes Cells 16(5):576-89
Tauber E, et al.  (2011) Functional gene expression profiling in yeast implicates translational dysfunction in mutant huntingtin toxicity. J Biol Chem 286(1):410-9
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
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
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
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
Sadlish H, et al.  (2008) Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS ONE 3(3):e1763
Aron R, et al.  (2005) In vivo bipartite interaction between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae. Genetics 169(4):1873-82
Borkhsenius AS, et al.  (2002) [Chimeric yeast prions with unstable inheritance] Genetika 38(3):300-5
Meriin AB, et al.  (2002) Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. J Cell Biol 157(6):997-1004
Wegrzyn RD, et al.  (2001) Mechanism of prion loss after Hsp104 inactivation in yeast. Mol Cell Biol 21(14):4656-69
Wickner RB, et al.  (2001) Prions beget prions: the [PIN+] mystery! Trends Biochem Sci 26(12):697-9
Zhou P, et al.  (2001) The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion-like elements [PSI(+)] and [PIN(+)]. Mol Microbiol 39(1):37-46
Boguta M  (2000) [Prions in yeast and filamentous fungi]. Postepy Biochem 46(2):108-14
Derkatch IL, et al.  (2000) Dependence and independence of [PSI(+)] and [PIN(+)]: a two-prion system in yeast? EMBO J 19(9):1942-52
Derkatch IL, et al.  (1998) Overexpression of the SUP45 gene encoding a Sup35p-binding protein inhibits the induction of the de novo appearance of the [PSI+] prion. Proc Natl Acad Sci U S A 95(5):2400-5
Derkatch IL, et al.  (1997) Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae. Genetics 147(2):507-19