RPS24A/YER074W Literature Guide Help

Other names published for RPS24A: RPS24EA, S24A, S24e, ribosomal 40S subunit protein S24A, YER074W

RPS24A - 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
Kuroha K, et al.  (2010) Receptor for activated C kinase 1 stimulates nascent polypeptide-dependent translation arrest. EMBO Rep 11(12):956-61
Dieci G, et al.  (2009) Positive modulation of RNA polymerase III transcription by ribosomal proteins. Biochem Biophys Res Commun 379(2):489-93
Nanda JS, et al.  (2009) eIF1 controls multiple steps in start codon recognition during eukaryotic translation initiation. J Mol Biol 394(2):268-85
Oeffinger M, et al.  (2007) Comprehensive analysis of diverse ribonucleoprotein complexes. Nat Methods 4(11):951-6
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
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
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