RPS22B/YLR367W Literature Guide Help

Other names published for RPS22B: S22B, S24B, YS22, rp50, S8, ribosomal 40S subunit protein S22B, YLR367W

RPS22B - Protein-protein Interactions (12)

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
Strunk BS, et al.  (2012) A translation-like cycle is a quality control checkpoint for maturing 40S ribosome subunits. Cell 150(1):111-21
Visweswaraiah J, et al.  (2011) Evidence that eukaryotic translation elongation factor 1A (eEF1A) binds the Gcn2 protein C terminus and inhibits Gcn2 activity. J Biol Chem 286(42):36568-79
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
Nielsen KH, et al.  (2006) Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of eukaryotic initiation factor 3 in yeast. Mol Cell Biol 26(8):2984-98
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
Menetret JF, et al.  (2000) The structure of ribosome-channel complexes engaged in protein translocation. Mol Cell 6(5):1219-32