Other names published for RNQ1: [PIN(+)], YCL028W
RNQ1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
RNQ1 - Protein/Nucleic Acid Structure (18)
| Reference | Other Genes Addressed |
|---|---|
| Kochneva-Pervukhova NV, et al. (2012) Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast. PLoS One 7(1):e29832 | |
| 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 () | |
| 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 | |
| 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 | |
| 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 | |
| Allen KD, et al. (2007) Effects of ubiquitin system alterations on the formation and loss of a yeast prion. J Biol Chem 282(5):3004-13 | |
| 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 | |
| Vitrenko YA, et al. (2007) Visualization of aggregation of the Rnq1 prion domain and cross-seeding interactions with Sup35NM. J Biol Chem 282(3):1779-87 | |
| Salnikova AB, et al. (2005) Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids. J Biol Chem 280(10):8808-12 | |
| Bagriantsev S and Liebman SW (2004) Specificity of prion assembly in vivo. [PSI+] and [PIN+] form separate structures in yeast. J Biol Chem 279(49):51042-8 | |
| Derkatch IL, et al. (2004) Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro. Proc Natl Acad Sci U S A 101(35):12934-9 | |
| Kimura Y, et al. (2004) The role of pre-existing aggregates in Hsp104-dependent polyglutamine aggregate formation and epigenetic change of yeast prions. Genes Cells 9(8):685-96 | |
| Bradley ME and Liebman SW (2003) Destabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants. Genetics 165(4):1675-85 | |
| Meriin AB, et al. (2003) Aggregation of expanded polyglutamine domain in yeast leads to defects in endocytosis. Mol Cell Biol 23(21):7554-65 | |
| Barrette I, et al. (2001) Pseudoknots in prion protein mRNAs confirmed by comparative sequence analysis and pattern searching. Nucleic Acids Res 29(3):753-8 | |
| Sondheimer N and Lindquist S (2000) Rnq1: an epigenetic modifier of protein function in yeast. Mol Cell 5(1):163-72 |



