Kyushu University Academic Staff Educational and Research Activities Database
List of Papers
Matsuoka Ken Last modified date:2024.06.03

Professor / Division of Molecular Bioscience / Department of Bioscience and Biotechnology / Faculty of Agriculture

1. Arinze Boniface Nweke Daiki Nagasato Ken Matsuoka, Secreted Arabinogalactan Protein from Salt-Adapted Tobacco BY-2 Cells Appears to Be Glycosylphosphatidyl Inositol-Anchored and Associated with Lipophilic Moieties, Bioscience, Biotechnology, and Biochemistry,, 87, 11, 1274-1284, 2023.11.
2. Eguchi, Toshihiko, #Igarashi, Kenshin, #Sato, Haruna, Yoshida, Satoshi, Matsuoka, Ken , Drying Method Affects Sugar Content in the Corm of the Medicinal Plant Pinellia ternata Breit, Environmental Control in Biology,, 61, 55-57, 2023.08.
3. Daiki Nagasato Yuto Sugita Yuhei Tsuno RutsukoTanaka Maki Fukuda Ken Matsuoka, Glycosylphosphatidylinositol-anchoring is required for the proper transport and extensive glycosylation of a classical arabinogalactan protein precursor in tobacco BY-2 cells, Bioscience, Biotechnology, and Biochemistry,, 87, 9, 991-1008, 2023.07.
4. Eguchi, T. Tanaka, H. Sagawa, M. Yoshida, S. Matsuoka, K., Time-course Pattern of Growth of the Medicinal Plant Pinellia ternata Breit. Grown under Controlled Environments, Environmental Control in Biology, DOI: 10.2525/ecb.60.191, 60, 4, 191-194, 2022.10.
5. Eguchi, T. Tanaka, H. Yoshida, S. Matsuoka, K., Nutrient Solution Electrical Conductivity and pH on the Productivity of the Medicinal Plant Pinellia ternata Breit, Environmental Control in Biology, DOI: 10.2525/ecb.60.149, 60, 2, 149-151, 2022.04.
6. Masaki NAGAHAMA Satoru ASATSUMA Masami SHIMIZU Ken MATSUOKA, Nutrient limitation alters the levels of two distinct forms of cyclin-dependent kinase G2, a putative autophagy progression modulator in tobacco BY-2 cells, J. Fac. Agric., Kyushu Univ,, 66, 1-10, 2021.03.
7. Eguchi, T. Tanaka, H. #Moriuchi, D. Yoshida, S. Matsuoka, K., Temperature effects on the photosynthesis by the medicinal plant pinellia ternata breit, Environmental Control in Biology,, 58, 2, 49-50, 2020.05.
8. #Yamato Oda, Satoru Asatsuma, #Hiroaki Nakasone, Ken Matsuoka, Sucrose starvation induces the degradation of proteins in trans-Golgi network and secretory vesicle cluster in tobacco BY-2 cells, Bioscience, Biotechnology, and Biochemistry,, 2020.04, Endomembrane transport system begins at the endoplasmic reticulum (ER), continues to the Golgi apparatus and subsequent compartment called trans-Golgi network (TGN). We found that SUT2, a tobacco sucrose-transporter ortholog and was localized in the TGN, decreased significantly under a sucrose-starvation condition. The tobacco SNARE protein SYP41, localized in the TGN and secretory vesicle cluster (SVC), also decreased under the starvation. Similarly, the SCAMP2-RFP fusion protein, which is localized in TGN, SVC, and plasma membrane (PM), was distributed solely in the PM under the starvation. Under the same starvation condition, protein secretion was not arrested but pectin deposition to cell wall was suppressed. These data indicated that the protein composition in TGN and existence of the SVC are regulated by sugar availability. Furthermore, our findings as well as the involvement of SVC in pectin secretion suggested that synthesis and transport of pectin are regulated by the level of extracellular sugars..
9. Toshihiko EGUCHI, Hiroyuki TANAKA, Satoshi YOSHIDA, Ken MATSUOKA, Temperature Effects on the Yield and Quality of the Medicinal Plant Pinellia ternata Breit., Environmental Control in Biology, 57, 83-85, 2019.06.
10. Kentaro Kaneko, Takeshi Takamatsu, Takuya Inomata, Kazusato Oikawa, Kimiko Itoh, Kazuko Hirose, Maho Amano, Shin-Ichiro Nishimura, Kiminori Toyooka, Ken Matsuoka, Javier Pozueta-Romero, Toshiaki Mitsui, N-glycomic and microscopic subcellular localization analyses of NPP1, 2 and 6 strongly indicate that trans-Golgi compartments participate in the Golgi-to-plastid traffic of nucleotide pyrophosphatase/phosphodiesterases in rice., Plant Cell Physiology, 10.1093/pcp/pcw089, 57, 1610-1628, 2016.08.
11. Kiminori Toyooka, Mayumi Wakasugi, Mayuko Sato, Ken Matsuoka, Morphological and quantitative changes in mitochondria, plastids, and peroxisomes during the log-to-stationary transition of the growth phase in cultured tobacco BY-2 cells, Plant Signaling & Behavior, in press, 2016.01.
12. Jianping Liu, Kyoko Hayashi, Ken Matsuoka, Membrane Topology of Golgi-Localized Probable S-Adenosylmethionine-Dependent Methyltransferase in Tobacco (Nicotiana tabacum) BY-2 Cells, Bioscience, Biotechnology, and Biochemistry, DOI:10.1080/09168451.2015.1069700, 79, 12, 2007-2013, 2015.12.
13. Silvia M. Velasquez, et al., Ken Matsuoka (22人中16番目), Complex Regulation of Prolyl-4-Hydroxylases Impacts Root Hair Expansion, Molecular Plant,, 8, 5, 734-746, 2015.05, Root hairs are single cells that develop by tip growth, a process shared with pollen tubes, axons, and fungal hyphae. However, structural plant cell walls impose constraints to accomplish tip growth. In addition to polysaccharides, plant cell walls are composed of hydroxyproline-rich glycoproteins (HRGPs), which include several groups of O-glycoproteins, including extensins (EXTs). Proline hydroxylation, an early post-translational modification (PTM) of HRGPs catalyzed by prolyl 4-hydroxylases (P4Hs), defines their subsequent O-glycosylation sites. In this work, our genetic analyses prove that P4H5, and to a lesser extent P4H2 and P4H13, are pivotal for root hair tip growth. Second, we demonstrate that P4H5 has in vitro preferred specificity for EXT substrates rather than for other HRGPs. Third, by P4H promoter and protein swapping approaches, we show that P4H2 and P4H13 have interchangeable functions but cannot replace P4H5. These three P4Hs are shown to be targeted to the secretory pathway, where P4H5 forms dimers with P4H2 and P4H13. Finally, we explore the impact of deficient proline hydroxylation on the cell wall architec- ture. Taken together, our results support a model in which correct peptidyl-proline hydroxylation on EXTs, and possibly in other HRGPs, is required for proper cell wall self-assembly and hence root hair elongation in Arabidopsis thaliana..
14. Toshihiko Eguchi, Hiroyuki Tanaka, Satoshi Yoshida, Ken Matsuoka, Influence of Ground Water Level on the Growth of the Medicinal Plant Pinellia ternata Breit. in a Solid Substrate Culture System, The international conference on plant factory 2014, 2014.11.
15. Kiminori Toyooka, Mayuko Sato, Natsumaro Kutsuna, Takumi Higaki, Fumie Sawaki, Mayumi Wakazaki, Yumi Goto, Seiichiro Hasezawa, Noriko Nagata, Ken Matsuoka, Wide-range High-resolution Transmission Electron Microscopy Reveals Morphological and Distributional Changes of Endomembrane Compartments during Log-to-stationary Transition of Growth Phase in Tobacco BY-2 Cells, Plant Cell Physiol., 10.1093/pcp/pcu084, 55, 9, 1544-1555, 2014.09, Rapid growth of plant cells by cell division and expansion requires an endomembrane trafficking system. The endomembrane compartments, such as the Golgi stacks, endosome and vesicles, are important in the synthesis and trafficking of cell wall materials during cell elongation. However, changes in the morphology, distribution and number of these compartments during the different stages of cell proliferation and differentiation have not yet been clarified. In this study, we examined these changes at the ultrastructural level in tobacco Bright yellow 2 (BY-2) cells during the log and stationary phases of growth. We analyzed images of the BY-2 cells prepared by the high-pressure freezing/freeze substitution technique with the aid of an auto-acquisition transmission electron microscope system. We quantified the distribution of secretory and endosomal compartments in longitudinal sections of whole cells by using wide-range gigapixel-class images obtained by merging thousands of transmission electron micrographs. During the log phase, all Golgi stacks were composed of several thick cisternae. Approximately 20 vesicle clusters (VCs), including the trans-Golgi network and secretory vesicle cluster, were observed throughout the cell. In the stationary-phase cells, Golgi stacks were thin with small cisternae, and only a few VCs were observed. Nearly the same number of multivesicular body and small high-density vesicles were observed in both the stationary and log phases. Results from electron microscopy and live fluorescence imaging indicate that the morphology and distribution of secretory-related compartments dramatically change when cells transition from log to stationary phases of growth..
16. Fumie Saito, Akiko Suyama, Takuji Oka, Takehiko Yoko-o, Ken Matsuoka, Yoshifumi Jigami, Yoh-ichi Shimma, Identification of novel peptidyl serine α-galactosyltransferase gene family in plants, J. Biol. Chem., 10.1074/jbc.M114.553933, 289, 20405-20420, 2014.06, In plants, serine residues in extensin, a cell wall protein, are glycosylated with O-linked galactose. However, the enzyme that is involved in the galactosylation of serine had not yet been identified. To identify the peptidyl serine O-α-galactosyltransferase (SGT), we chose Chlamydomonas reinhardtii as a model. We established an assay system for SGT activity using C. reinhardtii and Arabidopsis thaliana cell extracts. SGT protein was partially purified from cell extracts of C. reinhardtii and analyzed by tandem mass spectrometry to determine its amino acid sequence. The sequence matched the open reading frame XP_001696927 in the C. reinhardtii proteome database, and a corresponding DNA fragment encoding 748 amino acids (BAL63043) was cloned from a C. reinhardtii cDNA library. The 748-amino acid protein (CrSGT1) was produced using a yeast expression system, and the SGT activity was examined. Hydroxylation of proline residues adjacent to a serine in acceptor peptides was required for SGT activity. Genes for proteins containing conserved domains were found in various plant genomes, including A. thaliana and Nicotiana tabacum. The AtSGT1 and NtSGT1 proteins also showed SGT activity when expressed in yeast. In addition, knock-out lines of AtSGT1 and knockdown lines of NtSGT1 showed no or reduced SGT activity. The SGT1 sequence, which contains a conserved DXD motif and a C-terminal membrane spanning region, is the first example of a glycosyltransferase with type I membrane protein topology, and it showed no homology with known glycosyltransferases, indicating that SGT1 belongs to a novel glycosyltransferase gene family existing only in the plant kingdom..
17. Maiko Tasaki, Satoru Asatsuma, Ken Matsuoka, Monitoring protein turnover during phosphate starvation-dependent autophagic degradation using a photoconvertible fluorescent protein aggregate in tobacco BY-2 cells., Front. Plant Sci., doi: 10.3389/fpls.2014.00172, 5, 2014.04, [URL], We have developed a system for quantitative monitoring of autophagic degradation in transformed tobacco BY-2 cells using an aggregate-prone protein comprised of cytochrome b5 (Cyt b5) and a tetrameric red fluorescent protein (RFP). Unfortunately, this system is of limited use for monitoring the kinetics of autophagic degradation because the proteins synthesized before and after induction of autophagy cannot be distinguished. To overcome this problem, we developed a system using kikume green-red (KikGR), a photoconvertible and tetrameric fluorescent protein that changes its fluorescence from green to red upon irradiation with purple light. Using the fusion protein of Cyt b5 and KikGR together with a method for the bulk conversion of KikGR, which we had previously used to convert the Golgi-localized monomeric KikGR fusion protein, we were able to monitor both the growth and de novo formation of aggregates. Using this system, we found that tobacco cells do not cease protein synthesis under conditions of phosphate (Pi)-starvation. Induction of autophagy under Pi-starvation, but not under sugar- or nitrogen-starvation, was specifically inhibited by phosphite, which is an analog of Pi with a different oxidation number. Therefore, the mechanism by which BY-2 cells can sense Pi-starvation and induce autophagy does not involve sensing a general decrease in energy supply and a specific Pi sensor might be involved in the induction of autophagy under Pi-starvation..
18. Noboru Yamauchi, Tadashi Gosho, Satoru Asatsuma, Kiminori Toyooka, Toru Fujiwara, Ken Matsuoka, Polarized localization and borate-dependent degradation of the Arabidopsis borate transporter BOR1 in tobacco BY-2 cells, F1000Research, 2, 185, [v1; ref status: indexed,], 2013.10, In Arabidopsis the borate transporter BOR1, which is located in the plasma membrane, is degraded in the presence of excess boron by an endocytosis-mediated mechanism. A similar mechanism was suggested in rice as excess boron decreased rice borate transporter levels, although in this case whether the decrease was dependent on an increase in degradation or a decrease in protein synthesis was not elucidated. To address whether the borate-dependent degradation mechanism is conserved among plant cells, we analyzed the fate of GFP-tagged BOR1 (BOR1-GFP) in transformed tobacco BY-2 cells. Cells expressing BOR1-GFP displayed GFP fluorescence at the plasma membrane, especially at the membrane between two attached cells. The plasma membrane signal was abolished when cells were incubated in medium with a high concentration of borate (3 to 5 mM). This decrease in BOR1-GFP signal was mediated by a specific degradation of the protein after internalization by endocytosis from the plasma membrane. Pharmacological analysis indicated that the decrease in BOR1-GFP largely depends on the increase in degradation rate and that the degradation was mediated by a tyrosine-motif and the actin cytoskeleton. Tyr mutants of BOR1-GFP, which has been shown to inhibit borate-dependent degradation in Arabidopsis root cells, did not show borate-dependent endocytosis in tobacco BY-2 cells. These findings indicate that the borate-dependent degradation machinery of the borate transporter is conserved among plant species. - See more at:
19. Moses O. Abiodun, Ken Matsuoka, Proliferation of the Golgi apparatus in tobacco BY-2 cells during cell proliferation after release from the stationary phase of growth, Plant Signaling and Behavior,  eLocation ID: e25027, 2013.05.
20. Moses O. Abiodun, Ken Matsuoka, Evidence that Proliferation of Golgi Apparatus Depends on both de novo Generation from the Endoplasmic Reticulum and Formation from Pre-existing Stacks during the Growth of Tobacco BY-2 Cells., Plant Cell Physiol., 10.1093/pcp/pct014, 54, 4, 541-554, 2013.04, [URL], In higher plants, the numbers of cytoplasmic-distributed Golgi stacks differ based on function, age and cell type. It has not been clarified how the numbers are controlled, whether all the Golgi apparatus in a cell function equally and whether the increase in Golgi number is a result of the de novo formation from the endoplasmic reticulum (ER) or fission of pre-existing stacks. A tobacco prolyl 4-hydroxylase (NtP4H1.1), which is a cis-Golgi-localizing type II membrane protein, was tagged with a photoconvertible fluorescent protein, mKikGR (monomeric Kikume green red), and expressed in tobacco bright yellow 2 (BY-2) cells. Transformed cells were exposed to purple light to convert the fluorescence from green to red. A time-course analysis after the conversion revealed a progressive increase in green puncta and a decrease in the red puncta. From 3 to 6 h, we observed red, yellow and green fluorescent puncta corresponding to pre-existing Golgi; Golgi containing both pre-existing and newly synthesized protein; and newly synthesized Golgi. Analysis of the number and fluorescence of Golgi at different phases of the cell cycle suggested that an increase in Golgi number with both division and de novo synthesis occurred concomitantly with DNA replication. Investigation with different inhibitors suggested that the formation of new Golgi and the generation of Golgi containing both pre-existing and newly synthesized protein are mediated by different machineries. These results and modeling based on quantified results indicate that the Golgi apparatuses in tobacco BY-2 cells are not uniform and suggest that both de novo synthesis from the ER and Golgi division contribute almost equally to the increase in proliferating cells..
21. Koshiba, T, Kobayashi, M., Matsuoka, K., Fujiwara, T, Matoh, T. , Boron Nutrition of Cultured Tobacco BY-2 Cells VII. Rapid Induction of Metabolic Dysfunction in Cells Deprived of Boron Revealed by Microarray Analysis. , Soil Sci. Plant Nutr, 59, 2, 189-194, 2013.01.
22. Naoko Munemasa, Akiko Suyama, Ken Matsuoka, Role of lumenal domain on intracellular localization of tobacco membrane-anchored prolyl 4-hydroxylase, Biosci. Biotechnol. Biochem, 76, 2159-2161, 2012.11.
23. H. Shikata, M. Nakashima, K. Matsuoka, T. Matsushita, Deletion of the RS domain of RRC1 impairs phytochrome B signaling in Arabidopsis, Plant Signaling & Behavior, 7, 8, 933 - 936, 2012.08.
24. H. Shikata, M. Shibata, T. Ushijima, M. Nakashima, S.-G. Kong, K. Matsuoka, C. Lin, T. Matsushita, The RS domain of Arabidopsis splicing factor RRC1 is required for phytochrome B signal transduction, Plant J. , doi: 10.1111/j.1365-313X.2012.04937.x., 70, 5, 727-738, 2012.06.
25. Kobayashi, Keiko., Kawabata, Masuyo., Hisano, Keizo., Kazama, Tomohiko., Matsuoka, Ken., Sugita, Mamoru., Nakamura, Takahiro, Identification and characterization of the RNA binding surface of the pentatricopeptide repeat protein, Nucleic Acids Research, 40, 6, 2712-2723, 2012.03.
26. Masaru Kobayashi, Nagisa Kouzu, Akina Inami, Yuki Konishi, Kiminori Toyooka, Ken Matsuoka, Toru Matoh, Characterization of Arabidopsis CTP:3-deoxy-D-manno-2-octulosonate cytidylyltransferase (CMP-KDO synthetase), the enzyme that activates KDO during rhamnogalacturonan II biosynthesis, Plant Cell Physiol., 52, 10, 1832-1843, 2011.10.
27. Masaro Akai, Kiyoshi Onai, Miyako Kusano, Mayuko Sato, Henning Redestig, Kiminori Toyooka, Megumi Morishita, Hiroshi Miyake, Akihiro Hazama, Vanessa Checchetto, Ildikò, Szabò, Ken Matsuoka Kazuki Saito, Masato Yasui, Masahiro Ishiura and Nobuyuki Uozumi, Plasma membrane aquaporin AqpZ is essential for glucose metabolism during photomixotrophic growth of Synechocystis sp. PCC 6803, J. Biol. Chem, 286, 25224-25235, 2011.07.
28. Ryo Moriguchi, Chiaya Matsuoka, Akiko Suyama, Ken Matsuoka, Reduction of Plant-specific Arabinogalactan-type O-Glycosylation by Treating Tobacco Plants with Ferrous Chelator 2,2'-Dipyridyl, Bioscience, Biotechnology, and Biochemistry, 75, 5, 994-996, 2011.05.
29. Banu, M. N. A., Hoque, M. A., Watanabe-Sugimoto, M., Islam, M. M., Uraji, M., Matsuoka, K., Nakamura, Y., and Murata, Y., Proline and glycinebetaine ameliorate NaCl stress via scavenging hydrogen peroxide and methylglyoxal but not superoxide and nitric oxide in Tobacco Cultured Cells., Biosci. Biotechnol. Biochem, 74, 2043-2049, 2010.10.
30. Onkokesung, N. , Galis , I., von Dahl, C.C. , Matsuoka, K. , Saluz, H-P , and Baldwin, I.T, Jasmonic acid and ethylene modulate local responses to wounding and simulated herbivory in Nicotiana attenuata leaves., Plant Physiol., 153, 785-798, 2010.04.
31. Sasaki , T., Mori, I., Furuichi, T., Munemasa, S., Toyooka, K., Matsuoka, K., Murata, Y. Yamamoto, Y. , Closing plant stomata requires a homolog of an aluminum-activated malate transporter., Plant Cell Physiol, 51, 354-365, 2010.02.
32. Takuji Oka, Fumie Saito, Yoh-ichi Shimma, Takehiko Yoko-o, Yoshiyuki Nomura, Ken Matsuoka, Yoshifumi Jigami, Characterization of ER localized UDP-D-galactose: hydroxyproline O-galactosyltransferase using synthetic peptide substrates in Arabidopsis thaliana, Plant Physiol , 152, 332-340, 2010.01.
33. Kiminori Toyooka, Ken Matsuoka, Exo- and Endocytotic trafficking of SCAMP2, Plant Signaling and Behavior, in press, 2009.09.
34. Kitajima, A., Asatsumaa, S., Okada, H., Hamada, Y., Kanekoa, K., Nanjoa,Y., Kawagoe, Y., Toyooka, K., , Matsuoka, K., Takeuchi, M., , Nakano, A. and Mitsui, T., Plastid targeting of α-amylase glycoprotein from the Golgi apparatus through the secretory pathway, Plant Cell, 21, 2844-2858, 2009.09.
35. Tsunekawa K, Shijuku T, Hayashimoto M, Kojima Y, Onai K, Morishita M, Ishiura M, Kuroda T, Nakamura T, Kobayashi H, Sato M, Toyooka K, Matsuoka K, Omata T, Uozumi N., Identification and characterization of the Na+/H+ antiporter NHAS3 from the thylakoid membrane of synechocystis SP. PCC 6803, J. Biol. Chem, Jun 12;284(24):16513-21, 2009.04.
36. Toyooka, K., Goto, Y., Asatsuma, S., Koizumi, M., Mitsui, T. and Matsuoka, K., A mobile secretory vesicle cluster involved in mass transport from the Golgi to plant cell exterior., Plant Cell, Apr;21(4):1212-29, 2009.04, Secretory proteins and extracellular glycans are transported to the extracellular space during cell growth. These materials are carried in secretory vesicles generated at the trans-Golgi network (TGN). Analysis of the mammalian post-Golgi secretory pathway demonstrated the movement of separated secretory vesicles in the cell. Using secretory carrier membrane protein 2 (SCAMP2) as a marker for secretory vesicles and tobacco (Nicotiana tabacum) BY-2 cell as a model cell, we characterized the transport machinery in plant cells. A combination of analyses, including electron microscopy of quick-frozen cells and four-dimensional analysis of cells expressing fluorescent-tagged SCAMP2, enabled the identification of a clustered structure of secretory vesicles generated from TGN that moves in the cell and eventually fuses with plasma membrane. This structure was termed the secretory vesicle cluster (SVC). The SVC was also found in Arabidopsis thaliana and rice (Oryza sativa) cells and moved to the cell plate in dividing tobacco cells. Thus, the SVC is a motile structure involved in mass transport from the Golgi to the plasma membrane and cell plate in plant cells..
37. Suzuki,S., Gális, I., Kato, K., Araki, S., Demura, T., Criqui, M-C., Potuschak, T., Genschik, P., Matsuoka, K., and Ito, M, Preferential up-regulation of G2/M phase-specific genes by overexpression of hyperactive form of NtmybA2 lacking its negative regulation domain in tobacco BY2 cells, Plant Physiol, Apr;149(4):1945-57, 2009.03.
38. Shoji T, Inai K, Yazaki Y, Sato Y, Takase H, Shitan N, Yazaki K, Goto Y, Toyooka K, Matsuoka K, Hashimoto T., Multidrug and toxic compound extrusion-type transporters implicated in vacuolar sequestration of nicotine in tobacco roots., Plant Physiol., 149(2):708-18, 2009.02.
39. Banu MN, Hoque MA, Watanabe-Sugimoto M, Matsuoka K, Nakamura Y, Shimoishi Y, Murata Y., Proline and glycinebetaine induce antioxidant defense gene expression and suppress cell death in cultured tobacco cells under salt stress., J Plant Physiol. , 166(2):146-56, 2009.02.
40. Hamamoto, S., Marui, J., Matsuoka, K., Higasihi, K., Igarashi,K., Nakagawa, T., Mori, Y., Murata, Y., Nakanishi, Y., Maeshima, M., Yabe, I., Uozumi, N., Characterization of a Tobacco TPK-type K+ Channel as a Novel Tonoplast K+ Channel Using Yeast Tonoplasts., J. Biol. Chem., 283:1911-192, 2008.01.
41. Ukitsu, H., Kuromori, T., Toyooka, K., Goto, Y., Matsuoka, K., Sakuradani, E., Shimizu, S., Kamiya, A., Imura, Y.,Yuguchi, M., Wada, T., Hirayama, T., Shinozaki, K. , Cytological and Biochemical Analysis of COF1, an Arabidopsis Mutant of an ABC Transporter Gene, Plant and Cell Physiology, 48:1524-1533, 2007.11.
42. Tomonori Shinya , Ivan Galis, Tomoko Narisawa, Mami Sasaki, Hiroo Fukuda, Hideaki Matsuoka, Mikako Saito, Ken Matsuoka , Comprehensive Analysis of Glucan Elicitor-Regulated Gene Expression in Tobacco BY-2 Cells Reveals a Novel MYB Transcription Factor Involved in the Regulation of Phenylpropanoid Metabolism, Plant and Cell Physiology, 48(10): 1404–1413, 2007.10.
43. Nakagawa, T., Kurose, T., Hino, T., Tanaka, K., Kawamukai, M., , Niwa, Y., Toyooka, K., Matsuoka, K., Jinbo, T., Kimura, T, Development of the series of gateway binary vectors, pGWB, realize efficient construction of fusion genes for plant transformation., J. Biosci. Bioeng, 104:34-41, 2007.07.
44. Matsuki, Y., Ohmura-Hoshino, M., , Goto, E., Aoki, M., Mito-Yoshida,M., Uematsu, M., Hasegawa, T., Koseki, H., Ohara, O., Nakayama, M., Toyooka, K., Matsuoka, K., Hotta, H., Yamamoto, A. and Ishido, S., Novel regulation of MHC class II function in B cells, EMBO J., 26:846-854, 2007.02.
45. Shinya, T., Hanai, K., Suzuki, K., Matsuoka, K., Matsuoka, H., Saito, M, Characterization of NtChitIV, a class IV chitinase induced by β -1,3-, 1,6-glucan elicitor from Alternaria alternata 102: Antagonistic effect of salicylic acid and methyl jasmonate on the induction of NtChitIV, Biochem. Biophys. Res. Commun, 353:311-317, 2007.02.
46. Kasukabe, N., Watanabe-Sugimoto, M., Matsuoka, K., Okuma, E., Obi, I., Nakamura, Y., Shimoishi, Y., Murata, Y., Kakutani, K., Expression and Ca2+ Dependency of Plasma Membrane K+ Channels of Tobacco Suspension Cells Adapted to Salt Stress, Plant Cell Physiol, 47: 1674-1677, 2006.12.