Other names published for SUP35: GST1, PNM2, SAL3, SUF12, SUP2, SUP36, [PSI], [PSI(+)], eRF3, YDR172W
SUP35 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
SUP35 - Cellular Location (15)
| Reference | Other Genes Addressed |
|---|---|
| Bucciantini M, et al. (2012) Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1. FASEB J 26(2):818-31 | |
| Espargaro A, et al. (2012) Yeast prions form infectious amyloid inclusion bodies in bacteria. Microb Cell Fact 11(1):89 | |
| Park YN, et al. (2012) Differences in the Curing of [PSI(+)] Prion by Various Methods of Hsp104 Inactivation. PLoS One 7(6):e37692 | |
| Sharma J and Liebman SW (2012) [PSI(+) ] prion variant establishment in yeast.LID - 10.1111/mmi.12024 [doi] Mol Microbiol () | |
| 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 | |
| Tsuji T, et al. (2011) Single-particle tracking of quantum dot-conjugated prion proteins inside yeast cells. Biochem Biophys Res Commun 405(4):638-43 | |
| 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 | |
| Kawai-Noma S, et al. (2009) Single mother-daughter pair analysis to clarify the diffusion properties of yeast prion Sup35 in guanidine-HCl-treated [PSI] cells. Genes Cells 14(9):1045-54 | |
| Bolger TA, et al. (2008) The mRNA export factor Gle1 and inositol hexakisphosphate regulate distinct stages of translation. Cell 134(4):624-33 | |
| Buchan JR, et al. (2008) P bodies promote stress granule assembly in Saccharomyces cerevisiae. J Cell Biol 183(3):441-55 | |
| 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 | |
| Ganusova EE, et al. (2006) Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast. Mol Cell Biol 26(2):617-29 | |
| Kawai-Noma S, et al. (2006) Dynamics of yeast prion aggregates in single living cells. Genes Cells 11(9):1085-96 | |
| Kimura Y, et al. (2003) Analysis of yeast prion aggregates with amyloid-staining compound in vivo. Cell Struct Funct 28(3):187-93 | |
| Singh A, et al. (1979) Mutation of the non-Mendelian suppressor, Psi, in yeast by hypertonic media. Proc Natl Acad Sci U S A 76(4):1952-1956 | |




