Eukaryotic translation initiation factor 1 (eIF1) is a protein that in humans is encoded by the EIF1gene.[5][6][7]
eIF1 interacts with the eukaryotic small (40S) ribosomal subunit and eIF3, and is a component of the 43S preinitiation complex (PIC).[8] eIF1 and eIF1A bind cooperatively to the 40S to stabilize an "open" conformation of the preinitiation complex (PIC) during eukaryotic translation initiation.[8] eIF1 binds to a region near the ribosomal A-site in the 40S subunit and functions in a manner similar to the structurally related bacterial counterpart IF1.[9]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Fields C, Adams MD (Jan 1994). "Expressed sequence tags identify a human isolog of the suil translation initiation factor". Biochemical and Biophysical Research Communications. 198 (1): 288–91. doi:10.1006/bbrc.1994.1040. PMID7904817.
^Sheikh MS, Fernandez-Salas E, Yu M, Hussain A, Dinman JD, Peltz SW, Huang Y, Fornace AJ (Jun 1999). "Cloning and characterization of a human genotoxic and endoplasmic reticulum stress-inducible cDNA that encodes translation initiation factor 1(eIF1(A121/SUI1))". The Journal of Biological Chemistry. 274 (23): 16487–93. doi:10.1074/jbc.274.23.16487. PMID10347211.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Lian Z, Pan J, Liu J, Zhang S, Zhu M, Arbuthnot P, Kew M, Feitelson MA (Mar 1999). "The translation initiation factor, hu-Sui1 may be a target of hepatitis B X antigen in hepatocarcinogenesis". Oncogene. 18 (9): 1677–87. doi:10.1038/sj.onc.1202470. PMID10208429.
Chin LS, Singh SK, Wang Q, Murray SF (2000). "Identification of okadaic-acid-induced genes by mRNA differential display in glioma cells". Journal of Biomedical Science. 7 (2): 152–9. doi:10.1007/BF02256622. PMID10754390.
Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (Jan 2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nature Biotechnology. 23 (1): 94–101. doi:10.1038/nbt1046. PMID15592455.