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研究業績

松尾 芳隆 准教授
鈴木 亨 助教

稲田 利文 教授

主な業績

Narita, M.#, Denk, T.#, Matsuo, Y., Sugiyama, T., Kikuguchi, C., Ito, S., Sato, N., Suzuki, T., Hashimoto, S., Machová, I., Tesina, P., Beckmann, R., Inada, T.(#Equal contribution)
A distinct mammalian disome collision interface harbors K63-linked polyubiquitination of uS10 to trigger hRQT-mediated subunit dissociation
Nat Commun.
doi:10.1038/s41467-022-34097-9
(2022)

Li, S.#, Ikeuchi, K.#, Kato, M., Buschauer, R., Sugiyama, T., Adachi, S., Kusano, H., Natsume, T., Berninghausen, O., Matsuo, Y., Becker, T., Beckmann, R., Inada, T.*(#Equal contribution)
Sensing of individual stalled 80S ribosomes by Fap1 for nonfunctional rRNA turnover
Mol. Cell 
doi:10.1016/j.molcel.2022.08.018
(2022) (Press release)

Udagawa,T., Seki, M. and Inada, T.*
Optimized protocol for tRNA identification in the ribosomal complexes from human cell lines

STAR Protocols
doi:10.1016/j.xpro.2021.100615
(2021)

Matsuo, Y* and Inada, T.*
Ribosome collision sensor Hel2 functions as preventive quality control in the secretory pathway
Cell Rep.
doi:10.1016/j.celrep.2021.108877
(2021) (Press release)

Mizuno, M.#, Ebine, S.#, Shounai, O., Nakajima, S., Tomomatsu, S., Ikeuchi, K., Matsuo, Y., and Inada, T.*(#Equal contribution)
The nascent polypeptide in the 60S subunit determines the Rqc2-dependency of ribosomal quality control.
Nucleic Acid Res.
doi:10.1093/nar/gkab005
(2021) (Press release)

Udagawa, T.#*, Seki, M.#, Okuyama, T.#, Adachi, S., Natsume, T., Noguchi, T., Matsuzawa, A., Inada, T.*(#Equal contribution)
Failure to degrade CAT-tailed proteins disrupts neuronal morphogenesis and cell survival.
Cell Rep.
doi:10.1016/j.celrep.2020.108599
(2021) (Press release)

Watada, E., Li S., Hori, Y., Fujiki, K., Shirahige, K., Inada, T.*, Kobayashi, T.*
Age-Dependent Ribosomal DNA Variations in Mice
Mol. Cell. Biol.

doi:10.1128/MBC.00268-20
(2020)

Matsuki, Y.#, Matsuo, Y.#, Nakano, Y., Iwasaki, S., Yoko, H., Udagawa, T., Li, S., Saeki, Y., Yoshihisa, T., Tanaka, K., Ingolia, NT., Inada, T.*(#Equal contribution)
Ribosomal protein S7 ubiquitination during ER stress in yeast is associated with selective mRNA translation and stress outcome.
Sci. Rep.
doi:10.1038/s41598-020-76239-3
(2020)

Nobuta, R., Machida, K., Sato, M., Hashimoto, S., Toriumi, Y., Nakajima, S., Suto, D., Imataka, H.*, Inada, T.*
eIF4G-driven translation initiation of downstream ORFs in mammalian cells
Nucleic Acid Res.
doi:10.1093/nar/gkaa728
(2020)

Matsuki, Y., Saito, T., Nakano, Y., Hashimoto, S., Matsuo, Y., Inada, T.*
Crucial role of leaky initiation of uORF3 in the downregulation of HNT1 by ER stress
Biochem Biophys Res Commun.
doi:10.1016/j.bbrc.2020.04.104
(2020)

Han, P., Shichino, Y., Schneider-Poetsch, T., Mito, M., Hashimoto, S., Udagawa, T., Kohno, K., Yoshida, M., Mishima, Y., Inada, T., Iwasaki, S.*
Genome-wide Survey of Ribosome Collision
Cell Rep.
doi:org/10.1016/j.celrep.2020.107610
(2020)

Buschauer, R.#, Matsuo, Y.#, Sugiyama, T., Chen, Y., Alhusaini, N., Sweet, T., Ikeuchi, K., Cheng, J., Matsuki, Y., Nobuta, R., Gilmozzi, A., Berninghausen, O., Tesina, P., Becker, T., Coller, J.*, Inada, T.*, Beckmann, R.*(#Equal contribution)
The Ccr4-Not complex monitors the translating ribosome for codon optimality
Science
doi:org/10.1126/science.aay6912
(2020)

Matsuo, Y.#, Tesina, P.#, Nakajima, S., Mizuno, M., Endo, A., Buschauer, R., Cheng, J., Shounai, O., Ikeuchi, K., Saeki, Y., Becker, T., Beckmann, R.*, Inada, T.*(#Equal contribution)
RQT complex dissociates ribosomes collided on endogenous RQC substrate SDD1
Nat. Struc. Mol. Biol.
doi:10.1038/s41594-020-0393-9
(2020) (Press release)

Hashimoto, S.#, Sugiyama, T.#, Yamazaki, R., Nobuta, R., Inada, T.* (#Equal contribution)
Identification of a novel trigger complex that facilitates ribosome-associated quality control in mammalian cells
Sci. Rep.
doi:10.1038/s41598-20-60241-w/
(2020)

Yasuda, S.#, Tsuchiya, H.#, Kaiho, A.#, Guo, Q., Ikeuchi, K., Endo, A., Arai, N., Ohtake, F., Murata, S., Inada, T., Baumeister, Wolfgang., Fernández-Busnadiego, R., Tanaka, K.* Saeki, Y.*(#Equal contribution)
Stress- and ubiquitylation-dependent phase separation of the proteasome
Nature
doi:10.1038/s41586-020-1982-9
(2020) (Press release)

Su, T.#, Izawa, T.#, Thoms, M., Yamashita, Y., Cheng, J., Berninghausen, O., Hartl,U., Inada, T., Neupert, W.* Beckmann, R.*(#Equal contribution)
Structure and function of Vms1 and Arb1 in RQC and mitochondrial proteome homeostasis
Nature
doi:10.1038/s41586-019-1307-z
(2019) (Press release)

Hashimoto, S., Nobuta, R., Izawa, T., Inada, T.*
Translation arrest as a protein quality control system for aberrant translation of the 3′-UTR in mammalian cells
FEBS Letters
doi:10.1002/1873-3468.13362
(2019)

Sugiyama, T.#, Li, S.#, Kato, M.#, Ikeuchi, K., Ichimura, A., Matsuo, Y., Inada, T.* (#Equal contribution)
Sequential ubiquitination of ribosomal protein uS3 triggers the degradation of non-functional 18S rRNA
Cell Rep.
doi:org/10.1016/j.celrep.2019.02.067
(2019) (Press release)

Ikeuchi, K., Tesina, P., Matsuo, Y., Sugiyama, T., Cheng, J., Saeki, Y., Tanaka, K., Becker, T., Beckmann, R.*, Inada, T.*
Collided ribosomes form a unique structural interface to induce Hel2‐driven quality control pathways
EMBO J.
doi:10.15252/embj.2018100276
(2019) (Press release)

Matsuo, Y., Ikeuchi, K., Saeki, Y., Iwasaki, S., Schmidt, C., Udagawa, T., Sato, F., Tsuchiya, H., Becker, T., Tanaka, K., Ingolia, NT., Beckmann, R., Inada, T.*
Ubiquitination of Stalled Ribosome Triggers Ribosome-associated Quality Control.
Nat. Commun.
doi:10.1038/s41467-017-00188-1
(2017) (Press release)

Sugiyama T, Nobuta R, Ando K, Matsuki Y, Inada, T.*
Crucial role of ATP-bound Sse1 in Upf1-dependent degradation of the truncated product.
Biochem Biophys Res Commun.
doi:10.1016/j.bbrc.2017.05.0
(2017)

Ikeuchi, K., Yazaki, E., Kudo, K., Inada, T.*
Conserved functions of human Pelota in mRNA quality controls for nonstop mRNA.
FEBS Let.
doi:10.1002/1873-3468.12366
(2016)

Ikeuchi, K. and Inada, T.*
Ribosome-associated Asc1/RACK1 is required for endonucleolytic cleavage induced by stalled ribosome at the 3′ end of nonstop mRNA.
Sci. Rep.
doi:10.1038/srep28234
(2016)

Tsuboi, T.#, Yamazaki, R.#, Nobuta, R., Ikecuhi, K., Makino, S., Ohtaki, Y., Suzuki, Y., Yoshihisa, T., Trotta, C., Inada, T.* (#Equal contribution)
The tRNA Splicing Endonuclease Complex Cleaves the Mitochondria-localized CBP1 mRNA.
J Biol. Chem.
doi:10.1074/jbc.M114.634592
(2015)

Makino, S., Mishima, Y., Inoue, K., Inada, T.*
Roles of mRNA-fate modulators Dhh1 and Pat1 in TNRC6-dependent gene silencing recapitulated in yeast.
J Biol. Chem.
doi:10.1074/jbc.M114.615088
(2015)

Matsuda, R., Ikecuhi, K., Nomura, S., Inada, T.*
Protein quality control systems associated with No-Go and Nonstop mRNA surveillance in yeast.
Genes Cells
doi:10.1111/gtc.12106
(2014)

Kuroha, K., Ando, K., Nakagawa, R., Inada, T.*
The Upf complex interacts with aberrant products derived from mRNAs containing a premature termination codon and facilitates their proteasomal degradation.
J Biol. Chem.
doi:10.1074/jbc.M113.460691
(2013)

Brandman, O., Ornstein, JS., Wong, D., Larson, A., Williams, C.C., Li, G.W., Zhou, S., King, D., Shen, P.S., Weibezahn, J., Dunn, J.G., Rouskin, S., Inada, T., Frost, A.*, Weissman, JS.*
A ribosome-bound quality control complex triggers nascent peptides and signals translation stress
Cell
doi:10.1016/j.cell.2012.10.044
(2012)

Tsuboi, T., Kuroha, K., Kudo, K., Makino, S., Inoue, E., Kashima, I., Inada, T.*
Dom34:Hbs1 Plays a General Role in Quality Control Systems by Dissociation of Stalled Ribosome at 3′ End of Aberrant mRNA.
Mol. Cell
doi:10.1016/j.molcel.2012.03.013
(2012) (Press release)

Izawa, T., Tsuboi, T., Kuroha, K., Inada, T., Nishikawa, SI.*, Endo T.*
Roles of Dom34:Hbs1 in Nonstop Protein Clearance from Translocators for Normal Organelle Protein Influx.
Cell Rep.
doi:10.1016/j.celrep.2012.08.010
(2012)

Kuroha, K., Akamatsu, M., Dimitrova, L., Ito, T., Kato, Y., Shirahige K., Inada, T.*
RACK1 stimulates nascent polypeptide-dependent translation arrest.
EMBO Rep.
doi:10.1038/embor.2010.169
(2010)

Tsuboi, T. and Inada, T.*
Tethering of poly(A) binding protein interferes with non-translated mRNA decay from 5′ end in yeast.
J. Biol. Chem.
doi:10.10074/jbc.M110.117150
(2010)

Kuroha, K., Tatematsu, T., Inada, T.*
Upf1p stimulates proteasome-mediated degradation of the product derived from the specific nonsense-containing mRNA.
EMBO Rep.
doi:10.1038/embor.2009.200
(2009)

Kuroha, K., Dimitrova, L., Tatematsu, T., Inada, T.*
Nascent peptide-dependent translation arrest leads to not4p-mediated protein degradation by the proteasome.
J. Biol. Chem.
doi:10.1074/jbc.808840200
(2009)

Ito-Harashima, S., Kuroha, K., Tatematsu, T., Inada, T.*
Translation of poly(A) tail plays crucial roles in nonstop mRNA surveillance via translation repression and protein destabilization by proteasome in yeast.
Genes Dev.
doi:10.1101/gad.1490207
(2007)

Inada, T.* and Aiba, H.
Translation of aberrant mRNAs lacking a termination codon or with a shortened 3′-UTR is repressed after initiation in yeast.
EMBO J.
doi:10.1038/sj.emboj.7600636(2005)

 

その他の業績

Alam, M., Shima, H., Matsuo, Y., Nguyen, CL., Matsumoto, M., Ishii, Y., Sato, N., Sugiyama, T., Nobuta, R., Hashimoto, S., Liu, L., Kaneko, MK., Kato, Y., Inada, T.*, Igarashi, K.*
mTORC1-independent translation control in mammalian cells by methionine adenosyltransferase 2A and S-adenosylmethionine
J Biol. Chem.
doi:10.1016/j.jbc.2022.102084(2022)

Mita Y., Uchida R., Yasuhara S., Kishi K., Hoshi T., Matsuo Y., Yokooji T., Shirakawa Y., Toyama T., Urano Y., Inada T., Noguchi N., Saito Y.*
Identification of a novel endogenous long non-coding RNA that inhibits selenoprotein P translation
Nucleic Acids Res.
doi:10.1093/nar/gkab498
(2021)

Takehara, Y., Yashiroda H., Matsuo Y., Zhao X., Kamigaki A., Matsuzaki T., Kosako H., Inada T., Murata S.*
The ubiquitination-deubiquitination cycle on the ribosomal protein eS7A is crucial for efficient translation
iScience
doi:10.1016/j.isci.2021.102145
(2021)

Nakagawa, T., Hattori S., Nobuta R., Kimura R., Nakagawa M., Matsumoto M., Nagasawa Y., Funayama R., Miyakawa T., Inada T., Osumi N., Nakayama KI., Nakayama K.*
The Autism-Related Protein SETD5 Controls Neural Cell Proliferation through Epigenetic Regulation of rDNA Expression
iScience
doi:10.1016/j.isci.2020.101030(2020)

Miki, A., Galipon, J., Sawai, S., Inada, T., Ohta, K.*
RNA decay systems enhance reciprocal switching of sense and antisense transcripts in response to glucose starvation.
Genes Cells
doi:10.1111/gtc.12443(2016)

Tanaka, Y., Tsuda, S., Kunikata, H., Sato, J., Kokubun, T., Yasuda, M., Nishiguchi, KM.,Inada, T., Nakazawa T.*
Profiles of extracellular miRNAs in the aqueous humor of glaucoma patients assessed with a microarray system.
Sci Rep.
doi:10.1038/srep05089(2014)

Galipon, J., Miki, A., Oda, A., Inada, T., Ohta, K.*
Stress-induced lncRNAs evade nuclear degradation and enter the translational machinery.
Genes Cells
doi:10.11111/gtc.12042(2013)

Iwasaki, YW.#, Kiga, K.#, Kayo, H., Fukuda-Yuzawa, Y., Weise, J., Inada, T., Tomita, M., Ishihama, Y., Fukao, T.* (#Equal contribution)
Global microRNA elevation by inducible Exportin 5 regulates cell cycle entry.
RNA
doi:10.1261/rna.036608.112(2013)

Mori, T., Ogasawara, C., Inada T., Englert, M., Beier, H., Takezawa, M., Endo, T., Yoshihisa, T.*
Dual functions of yeast tRNA ligase in the unfolded protein response: unconventional cytoplasmic splicing of HAC1 pre-mRNA is not sufficient to release translational attenuation.
Mol. Biol. Cell 
doi:10.1091/mbc.E10-08-0693(2010)

Kobayashi, K. Kikuno, I. Kuroha, K. Saito, K. Ito, K. Ishitani, R*. Inada, T. and Nureki, O.*
Structural Basis for mRNA Surveillance by Archaeal Pelota and GTP-bound EF1α Complex.
Proc. Natl. Acad. Sci. USA
doi:10.1073/pnas.1009598107(2010)

Endo, A., Matsumoto, M., Inada, T., Yamamoto, A., Nakayama, K.I., Kitamura, N. and Komada, M.*
Nucleolar structure and function regulated by a deubiquitinating enzyme USP36
J. Cell Sci.
doi:10.1242/jcs.044461(2009)

Kuroha , K., Horiguchi, N., Aiba, H. and Inada, T.*
Analysis of nonstop mRNA translation in the absence of tmRNA in E.coli.
Genes to Cells
doi:10.1111/j.1365-2443.2009.01204.x(2009)

Nukazuka, A., Fujisawa, H., Inada, T., Oda, Y., Takagi, S.*
Semaphorin controls epidermal morphogenesis by stimulating mRNA translation via eIF2a in Caenorhabditis elegans.
Genes Dev.
doi:10.1101/gad.1644008(2008)

Kawamoto, H., Morita, T., Shimizu, A., Inada, T., Aiba, H.*
Implication of membrane localization of target mRNA in the action of a small RNA: mechanism of post-transcriptional regulation of glucose transporter in Escherichia coli.
Genes Dev.
doi:10.1101/gad.1270605(2005)

Tadauchi, T.#, Inada, T.#, Matsumoto, K.* and Irie, K. * (#Equal contribution)
Post-transcriptional regulation of HO expression by the Mkt1-Pbp1 complex.
Mol. Cell Biol.
doi:10.1128/MBC.24.9.3681.2004(2004)

Sunohara, T., Jojima, K., Tagami, H., Inada, T. and Aiba, H.*
Ribosome stalling during translation elongation induces cleavage of mRNA being translated in Escherichia coli.
J. Biol. Chem.
doi:10.1074/jbc.M312805200(2004)

Sunohara, T., Jojima, K., Yamamoto, Y., Inada, T. and Aiba, H.*
Nascent peptide-mediated ribosome stalling at stop codons induces mRNA cleavages resulting in nonstop mRNAs that are recognized by tmRNA.
RNA
doi:10.1261/rna.5169404(2004)

El-Kazzaz, W.#, Morita, T.#, Tagami, H., Inada, T. and Aiba, H.* (#Equal contribution)
Metabolic block at early stages of glycolytic pathway leads to the activation RcsC/B system via perturbation in dTDP-glucose synthesis in Escherichia coli.
Mol. Microbiol.
doi:10.1046/j.1365-2958.2003.03888.x(2004)

Morita, T., El-Kazzaz, W., Tanaka, Y., Inada, T. and Aiba, H.*
Accumulation of glucose 6-phosphate or fructose 6-phosphate is responsible for destabilization of glucose transporter mRNA in Escherichia coli.
J. Biol. Chem.
doi:10.1074/jbc.M300177200(2003)

Yamamoto, Y., Sunohara, T., Jojima, K., Inada, T. and Aiba, H.*
SsrA-mediated trans-translation plays a role in mRNA quality control by facilitating degradation of truncated mRNAs.
RNA
doi:10.1261/rna.2174803(2003)

Baron-Benhamou, J., Fortes, P., Inada, T., Preiss, T.*, Hentze, MW. *
The interaction of the cap-binding complex (CBC) with eIF4G is dispensable for translation in yeast.
RNA
doi:10.1261/rna.5100903(2003)

Sunohara, T., Abo, T., Inada, T. and Aiba, H.*
The C-terminal amino acid sequence of nascent peptide is a major determinant of SsrA tagging at all three stop codons.
RNA
doi:10.1017/s1355838202020198(2002)

Inada, T., Winstall, E., Tarun, S. Z., Jr., Yates, J. R., 3rd, Schieltz, D. and Sachs, A. B.*
One-step affinity purification of the yeast ribosome and its associated proteins and mRNAs.
RNA
doi:10.1017/s1355838202026018(2002)

Kimata, K., Tanaka, Y., Inada, T. and Aiba, H.*
Expression of the glucose transporter gene, ptsG, is regulated at the mRNA degradation step in response to glycolytic flux in Escherichia coli.
EMBO J.
doi:10.1093/emboj/20.13.3587(2001)

Fortes, P., Inada, T., Preiss, T., Hentze, M. W., Mattaj, I. W. and Sachs, A. B.*
The yeast nuclear cap binding complex can interact with translation factor eIF4G and mediate translation initiation.
Mol. Cell
doi:org/10.1016/S1097-2765(05)00003-1(2000)

Inada, T., Abo, T., Ogawa, K. and Aiba, H.*
SsrA-mediated tagging and proteolysis of LacI and its role in the regulation of lac operon.
EMBO J.
doi:10.1093/emboj/19.14.3762(2000)

Tanaka, Y., Kimata, K., Inada, T., Tagami, H. and Aiba, H.*
Negative regulation of the pts operon by Mlc: mechanism underlying glucose induction in Escherichia coli.
Genes Cells
doi:10.1046/j.1365-2443.1999.00368(1999)

Dasgupta, S., Fernandez, L., Kameyama, L., Inada, T., Nakamura, Y., Pappas, A. and Court, D. L.*
Genetic uncoupling of the dsRNA-binding and RNA cleavage activities of the Escherichia coli endoribonuclease RNase III–the effect of dsRNA binding on gene expression.
Mol. Microbiol.
doi:10.1046/j.1365-2958.1998.00828.x(1998)

Hogema, B. M., Arents, J. C., Bader, R., Eijkemans, K., Inada, T., Aiba, H. and Postma, P. W.*
Inducer exclusion by glucose 6-phosphate in Escherichia coli.
Mol. Microbiol.
doi:10.1046/j.1365-2958.1998.00833.x(1998)

Kimata, K., Inada, T., Tagami, H. and Aiba, H.*
A global repressor (Mlc) is involved in glucose induction of the ptsG gene encoding major glucose transporter in Escherichia coli.
Mol. Microbiol.
doi:10.1046/j.1365-2958.1998.01035.x.(1998)

Takahashi, H., Inada, T., Postma, P. and Aiba, H.*
CRP down-regulates adenylate cyclase activity by reducing the level of phosphorylated IIA(Glc), the glucose-specific phosphotransferase protein, in Escherichia coli.
Mol. Gen. Genet.
doi:10.1007/s004380050818(1998)

Hogema, B. M., Arents, J. C., Inada, T., Aiba, H., van Dam, K. and Postma, P. W.*
Catabolite repression by glucose 6-phosphate, gluconate and lactose in Escherichia coli.
Mol. Microbiol.
doi:10.1046/j.1365-2958.1997.3991761.x(1997)

Kimata, K., Takahashi, H., Inada, T., Postma, P. and Aiba, H.*
cAMP receptor protein-cAMP plays a crucial role in glucose-lactose diauxie by activating the major glucose transporter gene in Escherichia coli.
Proc. Natl. Acad. Sci. USA
doi:10.1073/pnas.94.24.12914(1997)

Inada, T., Kimata, K. and Aiba, H.*
Mechanism responsible for glucose-lactose diauxie in Escherichia coli: challenge to the cAMP model.
Genes Cells
doi:10.1046/j.1365-2443.1996.24025.x(1996)

Inada, T., Takahashi, H., Mizuno, T. and Aiba, H.*
Down regulation of cAMP production by cAMP receptor protein in Escherichia coli: an assessment of the contributions of transcriptional and posttranscriptional control of adenylate cyclase.
Mol. Gen. Genet.iScience
doi:10.1007/s004380050313(1996)

Inada, T. and Nakamura, Y.*
Autogenous control of the suhB gene expression of Escherichia coli.
Biochimie
doi:10.1016/0300-9084(96)89508-3(1996)

Tagami, H.,Inada, T., Kunimura, T. and Aiba, H.*
Glucose lowers CRP* levels resulting in repression of the lac operon in cells lacking cAMP.
Mol. Microbiol
doi:10.1111/j.1365-2958.1995.mmi_17020251.x(1995)

Inada, T. and Nakamura, Y.*
Lethal double-stranded RNA processing activity of ribonuclease III in the absence of SuhB protein of Escherichia coli.
Biochimie
doi:10.1016/0300-9084(96)88139-9(1995)

Powell, B. S., Court, D. L.*, Inada, T., Nakamura, Y., Michotey, V., Cui, X., Reizer, A., Saier, M. H., Jr. and Reizer, J. *
Novel proteins of the phosphotransferase system encoded within the rpoN operon of Escherichia coli. Enzyme IIANtr affects growth on organic nitrogen and the conditional lethality of an erats mutant.
J. Biol. Chem. 
doi:10.1074/jbc.270.9.4822(1995)

Ishizuka, H., Hanamura, A.,Inada, T. and Aiba, H.*
Mechanism of the down-regulation of cAMP receptor protein by glucose in Escherichia coli: role of autoregulation of the crp gene.
EMBO J.
doi:10.1002/j.1460-2075.1994.tb06606.x(1994)

Akiyama, Y., Inada, T., Nakamura, Y. and Ito, K.*
SecY, a multispanning integral membrane protein, contains a potential leader peptidase cleavage site.
J. Bacteriol.
doi:10.1128/jb.172.6.2888-2893.1990(1990)

Inada, T., Court, D. L., Ito, K. and Nakamura, Y.*
Conditionally lethal amber mutations in the leader peptidase gene of Escherichia coli.
J. Bacteriol.
doi:10.1128/jb.171.1.585-587.1989(1989)

Inada, T., Kawakami, K., Chen, S. M., Takiff, H. E., Court, D. L. and Nakamura, Y.*
Temperature-sensitive lethal mutant of era, a G protein in Escherichia coli.
J. Bacteriol.
doi:10.1128/jb.171.9.5017-5024.1989(1989)

Kawakami, K., Inada, T., and Nakamura, Y.*
Conditionally lethal and recessive UGA-suppressor mutations in the prfB gene encoding peptide chain release factor 2 of Escherichia coli.
J. Bacteriol.
doi:10.1128/jb.170.11.5378-5381.1988(1988)

総説

Inada T.
The proteasome’s balancing act.
Nat. Plants  
doi:10.1038/s41477-019-0551-4
(2019)

Inada T.
tRNA recycling on stalled ribosomesThe proteasome’s balancing act.
Nat. Struct. Mol. Biol.  
doi:10.1038/s41594-019-0222-1
(2019)

Ikeuchi, K., Izawa T., Inada T.
Recent Progress on the Molecular Mechanism of Quality Controls by Ribosome Stalling.
Front. Genet. 
doi:10.3389/fgene.2018.00743
(2019)

Inada T., Makino, S.
Novel rolesof the multi-functional CCR4-NOT complex in post-transcriptional regulation.
Front. Genet. 
doi:10.3389/fgene.2014.00145
(2014)

Inada T.
Ribosome as a hub for protein and mRNA quality control and gene regulation.
Seikagaku 
(2013)

Inada T.
Quality control systems  for aberrant mRNAs induced by aberrant translation elongation and termination.
BioChim Biophys Acta.
doi:10.1016/j.bbagrm.2013.02.004
(2013)

 

東京大学医科学研究所基礎医科学部門

RNA制御学分野

〒108-8639 東京都港区白金台4丁目6−1

Division of RNA and Gene Regulation

The Institute of Medical Science, The University of Tokyo

4-6-1, Shirokanedai, Minato-ku, Tokyo 108-8639, Japan

Copyright © Division of RNA and Gene Regulation
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