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Wiley Interdisciplinary Reviews. RNA|August 9, 2011
tRNA mimicry in translation termination and beyondYoshikazu Nakamura, Koichi ItoFEBS Letters|March 21, 2002
A tripeptide discriminator for stop codon recognitionYoshikazu Nakamura, Koichi ItoTrends in Biochemical Sciences|February 11, 2003
Making sense of mimic in translation terminationYoshikazu Nakamura, Koichi ItoProceedings of the National Academy of Sciences of the United States of America|February 21, 2002
Polypeptide release at sense and noncognate stop codons by localized charge-exchange alterations in translational release factorsMakiko Uno, Koichi Ito, Yoshikazu NakamuraFEBS Letters|January 2, 2010
A novel class of bacterial translation factor RF3 mutations suggests specific structural domains for premature peptidyl-tRNA drop-offYuya Watanabe, Yoshikazu Nakamura, Koichi ItoMolecular Microbiology|March 25, 2006
Ribosomal protein L11 mutations in two functional domains equally affect release factors 1 and 2 activityHanae Sato, Koichi Ito, Yoshikazu NakamuraGenes to Cells : Devoted to Molecular & Cellular Mechanisms|May 31, 2007
The role of N-terminal domain of translational release factor eRF3 for the control of functionality and stability in S. cerevisiaeHiroyuki Kodama, Koichi Ito, Yoshikazu NakamuraMolecular Microbiology|July 2, 2004
Ribosome recycling factor disassembles the post-termination ribosomal complex independent of the ribosomal translocase activity of elongation factor GToshinobu Fujiwara, Koichi Ito, Tohru Yamami, et al.Molecular Microbiology|December 23, 2004
Heterologous expression of Aquifex aeolicus ribosome recycling factor in Escherichia coli is dominant lethal by forming a complex that lacks functional co-ordination for ribosome disassemblyTohru Yamami, Koichi Ito, Toshinobu Fujiwara, et al.Molecular Cell|June 28, 2002
Elongation factor G participates in ribosome disassembly by interacting with ribosome recycling factor at their tRNA-mimicry domainsKoichi Ito, Toshinobu Fujiwara, Tomohiko Toyoda, et al.Pageof 78