RNQ1/YCL028W Literature Guide Help

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

RNQ1 - Mutants/Phenotypes (51)

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
Alexandrov AI, et al.  (2012) The effects of amino Acid composition of glutamine-rich domains on amyloid formation and fragmentation. PLoS One 7(10):e46458
Kelly AC, et al.  (2012) Sex, prions, and plasmids in yeast. Proc Natl Acad Sci U S A 109(40):E2683-90
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
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
Chernova TA, et al.  (2011) Prion induction by the short-lived, stress-induced protein lsb2 is regulated by ubiquitination and association with the actin cytoskeleton. Mol Cell 43(2):242-52
Halfmann R, et al.  (2011) Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins. Mol Cell 43(1):72-84
Kabani M, et al.  (2011) A mutation within the C-terminal domain of Sup35p that affects [PSI+] prion propagation. Mol Microbiol 81(3):640-58
Konopka CA, et al.  (2011) A yeast model for polyalanine-expansion aggregation and toxicity. Mol Biol Cell 22(12):1971-84
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
Manogaran AL, et al.  (2011) Prion formation and polyglutamine aggregation are controlled by two classes of genes. PLoS Genet 7(5):e1001386
Kadnar ML, et al.  (2010) Distinct type of transmission barrier revealed by study of multiple prion determinants of rnq1. PLoS Genet 6(1):e1000824
Kalastavadi T and True HL  (2010) Analysis of the [RNQ+] prion reveals stability of amyloid fibers as the key determinant of yeast prion variant propagation. J Biol Chem 285(27):20748-55
Manogaran AL, et al.  (2010) Most, but not all, yeast strains in the deletion library contain the [PIN(+)] prion. Yeast 27(3):159-66
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
Noree C, et al.  (2010) Identification of novel filament-forming proteins in Saccharomyces cerevisiae and Drosophila melanogaster. J Cell Biol 190(4):541-51
Saifitdinova AF, et al.  (2010) [NSI (+)]: a novel non-Mendelian nonsense suppressor determinant in Saccharomyces cerevisiae. Curr Genet 56(5):467-78
Urakov VN, et al.  (2010) Interdependence of amyloid formation in yeast: implications for polyglutamine disorders and biological functions. Prion 4(1):45-52
Bardill JP and True HL  (2009) Heterologous prion interactions are altered by mutations in the prion protein rnq1p. J Mol Biol 388(3):583-96
Bardill JP, et al.  (2009) Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prion. Prion 3(3):151-60
Choe YJ, et al.  (2009) Increased [PSI+] appearance by fusion of Rnq1 with the prion domain of Sup35 in Saccharomyces cerevisiae. Eukaryot Cell 8(7):968-76
Couthouis J, et al.  (2009) Screening for toxic amyloid in yeast exemplifies the role of alternative pathway responsible for cytotoxicity. PLoS ONE 4(3):e4539
Douglas PM, et al.  (2009) Reciprocal efficiency of RNQ1 and polyglutamine detoxification in the cytosol and nucleus. Mol Biol Cell 20(19):4162-73
Kurahashi H, et al.  (2009) Selfish prion of Rnq1 mutant in yeast. Genes Cells 14(5):659-68
Shibata S, et al.  (2009) Localization of prion-destabilizing mutations in the N-terminal non-prion domain of Rnq1 in Saccharomyces cerevisiae. Prion 3(4):250-8
Vishveshwara N and Liebman SW  (2009) Heterologous cross-seeding mimics cross-species prion conversion in a yeast model. BMC Biol 7:26
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
Douglas PM, et al.  (2008) Chaperone-dependent amyloid assembly protects cells from prion toxicity. Proc Natl Acad Sci U S A 105(20):7206-11
Kaganovich D, et al.  (2008) Misfolded proteins partition between two distinct quality control compartments. Nature 454(7208):1088-95