RNQ1/YCL028W Literature Guide Help

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

RNQ1 - Additional Literature (75)

ReferenceOther Genes Addressed
Reidy M, et al.  (2013) Schizosaccharomyces pombe Disaggregation Machinery Chaperones Support Saccharomyces cerevisiae Growth and Prion Propagation. Eukaryot Cell 12(5):739-45
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
Desantis ME, et al.  (2012) Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients. Cell 151(4):778-93
Duennwald ML, et al.  (2012) Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 10(6):e1001346
Halfmann R, et al.  (2012) Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature 482(7385):363-8
Harbi D, et al.  (2012) PrionHome: A Database of Prions and Other Sequences Relevant to Prion Phenomena. PLoS ONE 7(2):e31785
Kochneva-Pervukhova NV, et al.  (2012) Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast. PLoS One 7(1):e29832
Ma Z, et al.  (2012) Multiple roles for the Ess1 prolyl isomerase in the RNA polymerase II transcription cycle. Mol Cell Biol 32(17):3594-607
Reidy M, et al.  (2012) Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions. Genetics 192(1):185-93
Wickner RB, et al.  (2012) Study of amyloids using yeast. Methods Mol Biol 849():321-46
Bryan AW Jr, et al.  (2011) STITCHER: Dynamic assembly of likely amyloid and prion beta-structures from secondary structure predictions.LID - 10.1002/prot.23203 [doi] Proteins ()
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
Hines JK, et al.  (2011) Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements. Prion 5(4):238-44
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
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
Kryndushkin DS, et al.  (2011) Molecular chaperone Hsp104 can promote yeast prion generation. Genetics 188(2):339-48
Newnam GP, et al.  (2011) Destabilization and recovery of a yeast prion after mild heat shock. J Mol Biol 408(3):432-48
Specht S, et al.  (2011) Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae. J Cell Biol 195(4):617-29
Summers DW and Cyr DM  (2011) Use of yeast as a system to study amyloid toxicity. Methods 53(3):226-31
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
Walter GM, et al.  (2011) Ordered assembly of heat shock proteins, Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probes. J Biol Chem 286(47):40486-93
Garrity SJ, et al.  (2010) Conversion of a yeast prion protein to an infectious form in bacteria. Proc Natl Acad Sci U S A 107(23):10596-601
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
Noree C, et al.  (2010) Identification of novel filament-forming proteins in Saccharomyces cerevisiae and Drosophila melanogaster. J Cell Biol 190(4):541-51
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
Saifitdinova AF, et al.  (2010) [NSI (+)]: a novel non-Mendelian nonsense suppressor determinant in Saccharomyces cerevisiae. Curr Genet 56(5):467-78
Toombs JA, et al.  (2010) Compositional determinants of prion formation in yeast. Mol Cell Biol 30(1):319-32
Alberti S, et al.  (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137(1):146-58