Hiroji Aiba
Affiliations: | Suzuka University of Medical Sciences |
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Morita T, Aiba H. (2019) Mechanism and physiological significance of autoregulation of the gene. Rna (New York, N.Y.). 25: 264-276 |
Morita T, Nishino R, Aiba H. (2017) Role of the terminator hairpin in the biogenesis of functional Hfq-binding sRNAs. Rna (New York, N.Y.). 23: 1419-1431 |
Morita T, Ueda M, Kubo K, et al. (2015) Insights into transcription termination of Hfq-binding sRNAs of Escherichia coli and characterization of readthrough products. Rna (New York, N.Y.). 21: 1490-501 |
Ishikawa H, Otaka H, Maki K, et al. (2012) The functional Hfq-binding module of bacterial sRNAs consists of a double or single hairpin preceded by a U-rich sequence and followed by a 3' poly(U) tail. Rna (New York, N.Y.). 18: 1062-74 |
Otaka H, Ishikawa H, Morita T, et al. (2011) PolyU tail of rho-independent terminator of bacterial small RNAs is essential for Hfq action. Proceedings of the National Academy of Sciences of the United States of America. 108: 13059-64 |
Ikeda Y, Yagi M, Morita T, et al. (2011) Hfq binding at RhlB-recognition region of RNase E is crucial for the rapid degradation of target mRNAs mediated by sRNAs in Escherichia coli. Molecular Microbiology. 79: 419-32 |
Maki K, Morita T, Otaka H, et al. (2010) A minimal base-pairing region of a bacterial small RNA SgrS required for translational repression of ptsG mRNA. Molecular Microbiology. 76: 782-92 |
Maki K, Uno K, Morita T, et al. (2008) RNA, but not protein partners, is directly responsible for translational silencing by a bacterial Hfq-binding small RNA. Proceedings of the National Academy of Sciences of the United States of America. 105: 10332-7 |
Sunohara T, Jojima K, Yamamoto Y, et al. (2004) Nascent-peptide-mediated ribosome stalling at a stop codon induces mRNA cleavage resulting in nonstop mRNA that is recognized by tmRNA. Rna (New York, N.Y.). 10: 378-86 |
Sunohara T, Jojima K, Tagami H, et al. (2004) Ribosome stalling during translation elongation induces cleavage of mRNA being translated in Escherichia coli. The Journal of Biological Chemistry. 279: 15368-75 |