RPS5/YJR123W Literature Guide Help

Other names published for RPS5: S2, S5, YS8, rp14, S7, ribosomal 40S subunit protein S5, YJR123W

RPS5 - Protein-protein Interactions (16)

ReferenceOther 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
Kuroha K, et al.  (2010) Receptor for activated C kinase 1 stimulates nascent polypeptide-dependent translation arrest. EMBO Rep 11(12):956-61
Neueder A, et al.  (2010) A local role for the small ribosomal subunit primary binder rpS5 in final 18S rRNA processing in yeast. PLoS One 5(4):e10194
Dieci G, et al.  (2009) Positive modulation of RNA polymerase III transcription by ribosomal proteins. Biochem Biophys Res Commun 379(2):489-93
Harreman M, et al.  (2009) Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation. Proc Natl Acad Sci U S A 106(49):20705-10
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
Rempola B, et al.  (2006) Fcf1p and Fcf2p are novel nucleolar Saccharomyces cerevisiae proteins involved in pre-rRNA processing. Biochem Biophys Res Commun 346(2):546-54
Tagwerker C, et al.  (2006) A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking. Mol Cell Proteomics 5(4):737-48
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
Grandi P, et al.  (2002) 90S pre-ribosomes include the 35S pre-rRNA, the U3 snoRNP, and 40S subunit processing factors but predominantly lack 60S synthesis factors. Mol Cell 10(1):105-15
Stevens SW, et al.  (2002) Composition and functional characterization of the yeast spliceosomal penta-snRNP. Mol Cell 9(1):31-44
Menetret JF, et al.  (2000) The structure of ribosome-channel complexes engaged in protein translocation. Mol Cell 6(5):1219-32
Xiang RH and Lee JC  (1989) Identification of proteins crosslinked to RNA in 40S ribosomal subunits of Saccharomyces cerevisiae. Biochimie 71(11-12):1201-4