Other names published for RPS20: URP2, S10, ribosomal 40S subunit protein S20, YHL015W
RPS20 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
RPS20 - Protein-protein Interactions (11)
| Reference | Other Genes Addressed |
|---|---|
| Karaskova M, et al. (2012) Functional characterization of the role of the N-terminal domain of the c/Nip1 subunit of eukaryotic initiation factor 3 (eIF3) in AUG recognition. J Biol Chem 287(34):28420-34 | |
| Cuchalova L, et al. (2010) The RNA Recognition Motif of Eukaryotic Translation Initiation Factor 3g (eIF3g) Is Required for Resumption of Scanning of Posttermination Ribosomes for Reinitiation on GCN4 and Together with eIF3i Stimulates Linear Scanning. Mol Cell Biol 30(19):4671-86 | |
| Granneman S, et al. (2010) Cracking pre-40S ribosomal subunit structure by systematic analyses of RNA-protein cross-linking. EMBO J 29(12):2026-36 | |
| Kuroha K, et al. (2010) Receptor for activated C kinase 1 stimulates nascent polypeptide-dependent translation arrest. EMBO Rep 11(12):956-61 | |
| Nanda JS, et al. (2009) eIF1 controls multiple steps in start codon recognition during eukaryotic translation initiation. J Mol Biol 394(2):268-85 | |
| Passmore LA, et al. (2007) The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome. Mol Cell 26(1):41-50 | |
| Swatkoski S, et al. (2007) Integration of Residue-Specific Acid Cleavage into Proteomic Workflows. J Proteome Res 6(11):4525-4527 | |
| Roberts TM, et al. (2006) Slx4 regulates DNA damage checkpoint-dependent phosphorylation of the BRCT domain protein Rtt107/Esc4. Mol Biol Cell 17(1):539-48 | |
| Fekete CA, et al. (2005) The eIF1A C-terminal domain promotes initiation complex assembly, scanning and AUG selection in vivo. EMBO J 24(20):3588-601 | |
| George R, et al. (2002) The nascent polypeptide-associated complex (NAC) promotes interaction of ribosomes with the mitochondrial surface in vivo. FEBS Lett 516(1-3):213-6 | |
| Yeh YC, et al. (1986) Protein topography of the 40 S ribosomal subunit from Saccharomyces cerevisiae as shown by chemical cross-linking. J Biol Chem 261(30):14148-53 |



