RNQ1/YCL028W Literature Guide Help

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

RNQ1 - Protein-protein Interactions (44)

Results: 1 - 30 of 44 records
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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
Duennwald ML, et al.  (2012) Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 10(6):e1001346
Kochneva-Pervukhova NV, et al.  (2012) Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast. PLoS One 7(1):e29832
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
Winkler J, et al.  (2012) Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol 198(3):387-404
Sideri TC, et al.  (2011) Methionine oxidation of Sup35 protein induces formation of the [PSI+] prion in a yeast peroxiredoxin mutant. J Biol Chem 286(45):38924-31
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
Goehler H, et al.  (2010) Pathogenic polyglutamine tracts are potent inducers of spontaneous sup35 and rnq1 amyloidogenesis. PLoS One 5(3):e9642
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
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
Alberti S, et al.  (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137(1):146-58
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
Douglas PM, et al.  (2009) Reciprocal efficiency of RNQ1 and polyglutamine detoxification in the cytosol and nucleus. Mol Biol Cell 20(19):4162-73
Kota P, et al.  (2009) Identification of a consensus motif in substrates bound by a Type I Hsp40. Proc Natl Acad Sci U S A 106(27):11073-8
Kurahashi H, et al.  (2009) Selfish prion of Rnq1 mutant in yeast. Genes Cells 14(5):659-68
Nevzglyadova OV, et al.  (2009) Prion-associated proteins in yeast: comparative analysis of isogenic [PSI(+)] and [psi(-)] strains. Yeast 26(11):611-31
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
Summers DW, et al.  (2009) The Type I Hsp40 Ydj1 Utilizes a Farnesyl Moiety and Zinc Finger-like Region to Suppress Prion Toxicity. J Biol Chem 284(6):3628-39
Vishveshwara N and Liebman SW  (2009) Heterologous cross-seeding mimics cross-species prion conversion in a yeast model. BMC Biol 7:26
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
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
Tipton KA, et al.  (2008) In Vivo Monitoring of the Prion Replication Cycle Reveals a Critical Role for Sis1 in Delivering Substrates to Hsp104. Mol Cell 32(4):584-591
Watzky MA, et al.  (2008) Fitting yeast and mammalian prion aggregation kinetic data with the Finke-Watzky two-step model of nucleation and autocatalytic growth. Biochemistry 47(40):10790-800
Wickner RB, et al.  (2008) Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register {beta}-sheet structure. Proc Natl Acad Sci U S A 105(7):2403-8
Aron R, et al.  (2007) J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation. EMBO J 26(16):3794-803
Patel BK and Liebman SW  (2007) "Prion-proof" for [PIN+]: infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) induces [PIN+]. J Mol Biol 365(3):773-82
Results: 1 - 30 of 44 records
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