{"id":57,"date":"2023-07-14T16:13:57","date_gmt":"2023-07-14T07:13:57","guid":{"rendered":"https:\/\/bsw3.naist.jp\/LabsW\/microbial_interaction\/?page_id=57"},"modified":"2026-03-24T17:53:53","modified_gmt":"2026-03-24T08:53:53","slug":"publication","status":"publish","type":"page","link":"https:\/\/bsw3.naist.jp\/microbial_interaction\/publication\/","title":{"rendered":"Publication"},"content":{"rendered":"\n

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  1. K. Morinaka, Y. Isida, M. Watanabe, D. Watanabe<\/span>, T. Goshima, T. Akao, M. Yamada, and H. Shimoi*; Role of the CYR1G2066A<\/sup><\/em> mutation in ethanol tolerance of sake yeast Kyokai No. 11; J. Biosci. Bioeng. <\/em>(in press)<\/li>\n\n\n\n
  2. M. Yoshioka, N. Akasaka, Y. Masuda, M. Mariko, and D. Watanabe<\/span>*; Ethanolphilic lactic acid bacterium Fructilactobacillus fructivorans<\/em> as the key microorganism for fermentation of narazuke, a traditional Japanese preserved food; Appl. Environ. Microbiol.<\/em> 91(12):<\/strong> e0173025 (2025)<\/li>\n\n\n\n
  3. Y. Nakase, N. S. Lee, A. Shibatani, T. Yomogita, Y. Morozumi, D. Watanabe<\/span>, H. Takagi, and K. Shiozaki*; Multiple ammonium transporters in fission yeast are coordinated by transcriptional and localization regulation in response to nitrogen starvation; bioRxiv<\/em> (preprint) DOI: 10.1101\/2025.10.25.684503<\/li>\n\n\n\n
  4. Y. Miyamoto, N. Katsuhiro, K. Okumura, R. Takase, D. Watanabe<\/span>, K. Ogura, and W. Hashimoto*; A horizontally transferred alginate metabolism gene cluster in the human gut genus Bacteroides<\/em>; J. Appl. Glycosci.<\/em> 72(4)<\/strong>: 7204106 (2025)<\/li>\n\n\n\n
  5. N. Akasaka, Y. Sugimoto, T. Kajihara, H. Takagi, and D. Watanabe<\/span>*; Control of alcoholic fermentation through modulation of nitrogen metabolism in Saccharomyces cerevisiae<\/em>; J. Biotechnol.<\/em> 405:<\/strong> 159-168 (2025)<\/li>\n\n\n\n
  6. Y. Gong, N. Klinkaewboonwong, R. Hayashi, Y. Zhou, I. Nishida, R. Saito, T. Goshima, T. Nishi, D. Watanabe<\/span>, D. Hirata, T. Akao, and Y. Ohya*; Combinatory breeding of sake yeast strains with mutations that enhance Ginjo aroma production; Biosci. Biotechnol. Biochem.<\/em> 89(6):<\/strong> 910-917 (2025)<\/li>\n\n\n\n
  7. D. Watanabe<\/span>*, M. Kumano, Y. Sugimoto, and H. Takagi; Spontaneous attenuation of alcoholic fermentation via the dysfunction of Cyc8p in Saccharomyces cerevisiae<\/em>; Int. J. Mol. Sci.<\/em> 25(1):<\/strong> 304 (2024)<\/li>\n\n\n\n
  8. H. Iwase, Y. Yamamoto, A. Yamada, K. Kawai, S. Oiki, D. Watanabe<\/span>, B. Mikami, R. Takase, and W. Hashimoto*; Crystal structures of Lacticaseibacillus<\/em> 4-deoxy-L-threo<\/em>-5-hexosuloseuronate ketol-isomerase KduI in complex with substrate analogs; J. Appl. Glycosci.<\/em> 70(4):<\/strong> 99-107 (2023)<\/li>\n\n\n\n
  9. D. Watanabe<\/span>*, M. Kawashima, N. Yoshioka, Y. Sugimoto, and H. Takagi; Rational design of alcoholic fermentation targeting extracellular carbon; NPJ Sci. Food<\/em> 7(1):<\/strong> 37 (2023)<\/li>\n\n\n\n
  10. D. Watanabe<\/span> and W. Hashimoto*; Adaptation of yeast Saccharomyces cerevisiae<\/em> to grape-skin environment; Sci. Rep.<\/em> 13:<\/strong> 9279 (2023)<\/li>\n\n\n\n
  11. K. Anamizu, R. Takase, M. Hio, D. Watanabe<\/span>, B. Mikami, and W. Hashimoto*; Substrate size-dependent conformational changes of bacterial pectin-binding protein crucial for chemotaxis and assimilation; Sci. Rep.<\/em> 12:<\/strong> 12653 (2022)<\/li>\n\n\n\n
  12. S. Yabuuchi, S. Oiki, S. Minami, R. Takase, D. Watanabe<\/span>, and W. Hashimoto*; Enhanced propagation of Granulicatella adiacens<\/em> from human oral microbiota by hyaluronan; Sci. Rep.<\/em> 12:<\/strong> 10948 (2022)<\/li>\n\n\n\n
  13. S. Nakatsuji, K. Okumura, R. Takase, D. Watanabe<\/span>, B. Mikami, and W. Hashimoto*; Crystal structures of EfeB and EfeO in a bacterial siderophore-independent iron transport system; Biochem. Biophys. Res. Commun. <\/em>594:<\/strong> 124-130 (2022)<\/li>\n\n\n\n
  14. T. Chadani, S. Ohnuki, A. Isogai, T. Goshima, M. Kashima, F. Ghanegolmohammadi, T. Nishi, D. Hirata, D. Watanabe<\/span>, K. Kitamoto, T. Akao, and Y. Ohya*; Genome editing to generate sake yeast strains with eight mutations that confer excellent brewing characteristics; Cells<\/em> 10(6):<\/strong> 1299 (2021)<\/li>\n\n\n\n
  15. T. Murakami, M. Watanabe, M. Takaki, H. Suetsugu-Sasaki, D. Watanabe<\/span>, T. Goshima, H. Fukuda, H. Shimoi, and T. Akao*; Isolation of novel alcohol-tolerant spontaneous mutant strains from sake yeast Kyokai no. 6 and no. 7, and their brewing characteristics; J. Brew. Soc. Japan<\/em> 116(2):<\/strong> 131-141 (2021) [Japanese]<\/li>\n\n\n\n
  16. R. Tanahashi, T. S. N. Afiah, A. Nishimura, D. Watanabe<\/span>, and H. Takagi*; The C2 domain of the ubiquitin ligase Rsp5 is required for ubiquitination of the endocytic protein Rvs167 upon change of nitrogen source; FEMS Yeast Res.<\/em> 20(7):<\/strong> foaa058 (2020)<\/li>\n\n\n\n
  17. H. Sugiura, A. Nagase, S. Oiki, B. Mikami, D. Watanabe<\/span>, and W. Hashimoto*; Bacterial inducible expression of plant cell wall-binding protein YesO through conflict between Glycine max<\/em> and saprophytic Bacillus subtilis<\/em>; Sci. Rep.<\/em> 10(1):<\/strong> 18691 (2020)<\/li>\n\n\n\n
  18. M. Kanai*, T. Kawata, T. Morimoto, M. Mizunuma, D. Watanabe<\/span>, T. Akao, T. Fujii, and H. Iefuji; The sake yeast YHR032W\/ERC1<\/em> allele contributes to the regulation of the tetrahydrofolate content in the folate synthetic pathway in sake yeast strains; Biosci. Biotechnol. Biochem.<\/em> 84(5):<\/strong> 1073-1076 (2020)<\/li>\n\n\n\n
  19. S. Nakata, M. Hio, R. Takase, S. Kawai, D. Watanabe<\/span>, and W. Hashimoto*; Polyunsaturated fatty acids-enriched lipid from reduced sugar alcohol mannitol by marine yeast Rhodosporidiobolus fluvialis<\/em> Y2; Biochem. Biophys. Res. Commun. <\/em>526(4):<\/strong> 1138-1142 (2020)<\/li>\n\n\n\n
  20. N. S. B. Mat Nanyan, D. Watanabe<\/span>, Y. Sugimoto, and H. Takagi*; Effect of the deubiquitination enzyme gene UBP6<\/em> on the stress-responsive transcription factor Msn2-mediated control of the amino acid permease Gnp1 in yeast. J. Biosci. Bioeng. <\/em>129(4):<\/strong> 423-427 (2020)<\/li>\n\n\n\n
  21. Y. Mukai*, Y. Kamei, X. Liu, S. Jiang, Y. Sugimoto, N. S. B. Mat Nanyan, D. Watanabe<\/span>, and H. Takagi*; Proline metabolism regulates replicative lifespan in the yeast Saccharomyces cerevisiae<\/em>; Microb. Cell<\/em> 6(10):<\/strong> 482-490 (2019)<\/li>\n\n\n\n
  22. N. S. B. Mat Nanyan\u2020<\/sup>, D. Watanabe<\/span>\u2020<\/sup>, Y. Sugimoto, and H. Takagi*; Involvement of the stress-responsive transcription factor gene MSN2<\/em> in the control of amino acid uptake in Saccharomyces cerevisiae<\/em>; FEMS Yeast Res.<\/em>19(5):<\/strong> foz052 (2019) [\u2020<\/sup>equally contributed]<\/li>\n\n\n\n
  23. D. Watanabe<\/span>, S. Tashiro, D. Shintani, Y. Sugimoto, A. Iwami, Y. Kajiwara, H. Takashita, and H. Takagi*; Loss of Rim15p in shochu yeast alters carbon utilization during barley shochu fermentation; Biosci. Biotechnol. Biochem.<\/em> 83(8):<\/strong> 1594-1597 (2019)<\/li>\n\n\n\n
  24. M. Ohashi, R. Nasuno, D. Watanabe<\/span>, and H. Takagi*; Stable N<\/em>-acetyltransferase Mpr1 improves ethanol productivity in the sake yeast Saccharomyces cerevisiae<\/em>; J. Ind. Microbiol. Biotechnol.<\/em> 46(7):<\/strong> 1039-1045 (2019)<\/li>\n\n\n\n
  25. T. Abe, Y. Toyokawa, Y. Sugimoto, H. Azuma, K. Tsukahara, R. Nasuno, D. Watanabe<\/span>, M. Tsukahara*, and H. Takagi*; Characterization of a new Saccharomyces cerevisiae<\/em> isolated from hibiscus flower and its mutant with l-leucine accumulation for awamori brewing; Front. Genet.<\/em> 10:<\/strong> 490 (2019)<\/li>\n\n\n\n
  26. H. Shimoi*, Y. Hanazumi, N. Kawamura, M. Yamada, S. Shimizu, T. Suzuki, D. Watanabe<\/span>, and T. Akao; Meiotic chromosomal recombination defect in sake yeasts; J. Biosci. Bioeng.<\/em> 127(2):<\/strong> 190-196 (2019)<\/li>\n\n\n\n
  27. D. Watanabe<\/span>*, T. Kajihara, Y. Sugimoto, K. Takagi, M. Mizuno, Y. Zhou, J. Chen, K. Takeda, H. Tatebe, K. Shiozaki, N. Nakazawa, S. Izawa, T. Akao, H. Shimoi, T. Maeda, and H. Takagi; Nutrient signaling via the TORC1-Greatwall-PP2AB55\u03b4<\/sup> pathway is responsible for the high initial rates of alcoholic fermentation in sake yeast strains of Saccharomyces cerevisiae<\/em>; Appl. Environ. Microbiol.<\/em> 85(1):<\/strong> e02083-18 (2019)<\/li>\n\n\n\n
  28. M. Oomuro*, D. Watanabe<\/span>, Y. Sugimoto, T. Kato, Y. Motoyama, T. Watanabe, and H. Takagi; Accumulation of intracellular S<\/em>-adenosylmethionine increases the fermentation rate of bottom-fermenting brewer’s yeast during high-gravity brewing; J. Biosci. Bioeng.<\/em> 126(6):<\/strong> 736-741 (2018)<\/li>\n\n\n\n
  29. D. Watanabe<\/span>*, M. Kumano, Y. Sugimoto, M. Ito, M. Ohashi, K. Sunada, T. Takahashi, T. Yamada, and H. Takagi; Metabolic switching of sake yeast by kimoto lactic acid bacteria through the [GAR+<\/sup><\/em>] non-genetic element; J. Biosci. Bioeng.<\/em> 126(5):<\/strong> 624-629 (2018)<\/li>\n\n\n\n
  30. T. Akao*, Y. Zhou, D. Watanabe<\/span>, N. Okazaki, and H. Shimoi; Development of DNA markers to differentiate good Kyokai sake yeast and other yeast strains; J. Brew. Soc. Japan<\/em> 113(10):<\/strong> 631-641 (2018) [Japanese]<\/li>\n\n\n\n
  31. D. Watanabe<\/span>, H. Sekiguchi, Y. Sugimoto, A. Nagasawa, N. Kida, and H. Takagi*; Importance of proteasome gene expression during model dough fermentation after preservation of baker\u2019s yeast cells by freezing; Appl. Environ. Microbiol.<\/em> 84(12): <\/strong>e00406-18 (2018)<\/li>\n\n\n\n
  32. N. Takpho, D. Watanabe<\/span>, and H. Takagi*; Valine biosynthesis in Saccharomyces cerevisiae<\/em> is regulated by the mitochondrial branched-chain amino acid aminotransferase Bat1; Microb. Cell<\/em> 5(6):<\/strong> 293-299 (2018)<\/li>\n\n\n\n
  33. N. Takpho, D. Watanabe<\/span>, and H. Takagi*; High-level production of valine by expression of the feedback inhibition-insensitive acetohydroxyacid synthase in Saccharomyces cerevisiae<\/em>; Metab. Eng.<\/em> 46:<\/strong> 60-67 (2018)<\/li>\n\n\n\n
  34. A. Watcharawipas, D. Watanabe<\/span>, and H. Takagi*; Enhanced sodium acetate tolerance in Saccharomyces cerevisiae<\/em> by the Thr255Ala mutation of the ubiquitin ligase Rsp5; FEMS Yeast Res.<\/em> 17(8):<\/strong> fox083 (2017)<\/li>\n\n\n\n
  35. S. Ohnuki, H. Okada, A. Friedrich, Y. Kanno, T. Goshima, H. Hasuda, M. Inahashi, N. Okazaki, H. Tamura, R. Nakamura, D. Hirata, H. Fukuda, H. Shimoi, K. Kitamoto, D. Watanabe<\/span>, J. Schacherer, T. Akao*, and Y. Ohya*; Phenotypic diagnosis of lineage and differentiation during sake yeast breeding; G3: Genes Genom. Genet.<\/em> 7(8): <\/strong>2807-2820 (2017)<\/li>\n\n\n\n
  36. D. Watanabe<\/span>, A. Kaneko, Y. Sugimoto, S. Ohnuki, H. Takagi, and Y. Ohya*; Promoter engineering of the Saccharomyces cerevisiae RIM15<\/em> gene for improvement of alcoholic fermentation rates under stress conditions; J. Biosci. Bioeng.<\/em> 123(2):<\/strong> 183-189 (2017)<\/li>\n\n\n\n
  37. M. Kanai*, T. Kawata, Y. Yoshida, Y. Kita, T. Ogawa, M. Mizunuma, D. Watanabe<\/span>, H. Shimoi, A. Mizuno, O. Yamada, T. Fujii, and H. Iefuji; Sake yeast YHR032W\/ERC1 <\/em>haplotype contributes to high S<\/em>-adenosylmethionine accumulation in sake yeast strains; J. Biosci. Bioeng.<\/em> 123(1):<\/strong> 8-14 (2017)<\/li>\n\n\n\n
  38. A. Tsolmonbaatar, K. Hashida, Y. Sugimoto, D. Watanabe<\/span>, S. Furukawa, and H. Takagi*; Isolation of baker’s yeast mutants with proline accumulation that showed enhanced tolerance to baking-associated stresses; Int. J. Food Microbiol.<\/em> 238:<\/strong> 233-240 (2016)<\/li>\n\n\n\n
  39. M. Oomuro*, T. Kato, Y. Zhou, D. Watanabe<\/span>, Y. Motoyama, H. Yamagishi, T. Akao, and M. Aizawa; Defective quiescence entry promotes the fermentation performance of bottom-fermenting brewer’s yeast; J. Biosci. Bioeng.<\/em> 122(5):<\/strong> 577-582 (2016)<\/li>\n\n\n\n
  40. I. Nishida, D. Watanabe<\/span>, and H. Takagi*; Putative mitochondrial \u03b1-ketoglutarate- dependent dioxygenase Fmp12 controls utilization of proline as an energy source in Saccharomyces cerevisiae<\/em>; Microb. Cell<\/em> 3(10):<\/strong> 522-528 (2016)<\/li>\n\n\n\n
  41. Y. Tatehashi, D. Watanabe<\/span>, and H. Takagi*; \u03b3-Glutamyl kinase is involved in selective autophagy of ribosomes in Saccharomyces cerevisiae<\/em>; FEBS Lett.<\/em> 590(17):<\/strong> 2906-2914 (2016)<\/li>\n\n\n\n
  42. I. Nishida\u2020<\/sup>, D. Watanabe<\/span>\u2020<\/sup>, A. Tsolmonbaatar, T. Kaino, I. Ohtsu, and H. Takagi*; Vacuolar amino acid transporters upregulated by exogenous proline and involved in cellular localization of proline in Saccharomyces cerevisiae<\/em>. J. Gen. Appl. Microbiol. <\/em>62(3):<\/strong> 132-139 (2016) [\u2020<\/sup>equally contributed]<\/li>\n\n\n\n
  43. Y. Yoshikawa, R. Nasuno, N. Kawahara, A. Nishimura, D. Watanabe<\/span>, and H. Takagi*; Regulatory mechanism of the flavoprotein Tah18-dependent nitric oxide synthesis and cell death in yeast. Nitric Oxide<\/em> 57:<\/strong> 85-91 (2016)<\/li>\n\n\n\n
  44. R. Nasuno, S. Hirase, S. Norifune, D. Watanabe<\/span>, and H. Takagi*; Structure-based molecular design for thermostabilization of N<\/em>-acetyltransferase Mpr1 involved in a novel pathway of l-arginine synthesis in yeast; J. Biochem.<\/em> 159(2):<\/strong> 271-277 (2016)<\/li>\n\n\n\n
  45. R. I. Astuti\u2020<\/sup>, D. Watanabe<\/span>\u2020<\/sup>, and H. Takagi*; Nitric oxide signaling and its role in oxidative stress response in Schizosaccharomyces pombe<\/em>. Nitric Oxide<\/em>52:<\/strong> 29-40 (2016) [\u2020<\/sup>equally contributed]<\/li>\n\n\n\n
  46. D. Watanabe<\/span>, Y. Zhou, A. Hirata, Y. Sugimoto, K. Takagi, T. Akao, Y. Ohya, H. Takagi, and H. Shimoi*; Inhibitory role of Greatwall-like protein kinase Rim15p in alcoholic fermentation via upregulating the UDP-glucose synthesis pathway in Saccharomyces cerevisiae<\/em>; Appl. Environ. Microbiol.<\/em> 82(1):<\/strong> 340-351 (2016)<\/li>\n\n\n\n
  47. E. Funahashi, K. Saiki, K. Honda, Y. Sugiura, Y. Kawano, I. Ohtsu*, D. Watanabe<\/span>, Y. Wakabayashi, T. Abe, T. Nakanishi, M. Suematsu, and H. Takagi; Finding of thiosulfate pathway for synthesis of organic sulfur compounds in Saccharomyces cerevisiae<\/em> and improvement of ethanol production; J. Biosci. Bioeng.<\/em> 120(6): <\/strong>666-669 (2015)<\/li>\n\n\n\n
  48. D. Watanabe<\/span>, H. Murai, R. Tanahashi, K. Nakamura, T. Sasaki, and H. Takagi*; Cooperative and selective roles of the WW domains of the yeast Nedd4-like ubiquitin ligase Rsp5 in the recognition of the arrestin-like adaptors Bul1 and Bul2; Biochem. Biophys. Res. Commun.<\/em> 463(1-2):<\/strong> 76-81 (2015)<\/li>\n\n\n\n
  49. S. Hirayama, M. Shimizu, N. Tsuchiya, S. Furukawa, D. Watanabe<\/span>, H. Shimoi, H. Takagi, H. Ogihara, and Y. Morinaga*; Awa1p on the cell surface of sake yeast inhibits biofilm formation and the co-aggregation between sake yeasts and Lactobacillus plantarum<\/em> ML11-11; J. Biosci. Bioeng.<\/em> 119(5):<\/strong> 532-537 (2015)<\/li>\n\n\n\n
  50. I. Wijayanti\u2020<\/sup>, D. Watanabe<\/span>\u2020<\/sup>, S. Oshiro, and H. Takagi*; Isolation and functional analysis of yeast ubiquitin ligase Rsp5 variants that alleviate the toxicity of human \u03b1-synuclein; J. Biochem.<\/em>157(4):<\/strong> 251-260 (2015) [\u2020<\/sup>equally contributed]<\/li>\n\n\n\n
  51. H. Takagi*, K. Hashida, D. Watanabe<\/span>, R. Nasuno, M. Ohashi, T. Iha, M. Nezuo, and M. Tsukahara; Isolation and characterization of awamori yeast mutants with l-leucine accumulation that overproduce isoamyl alcohol; J. Biosci. Bioeng.<\/em> 119(2):<\/strong> 140-147 (2015)<\/li>\n\n\n\n
  52. K. Uehara*, J. Watanabe, T. Akao, D. Watanabe<\/span>, Y. Mogi, and H. Shimoi; Screening of high-level 4-hydroxy-2 (or 5)-ethyl-5 (or 2)-methyl-3(2H)-furanone-producing strains from a collection of gene deletion mutants of Saccharomyces cerevisiae<\/em>; Appl. Environ. Microbiol.<\/em> 81(1):<\/strong> 453-460 (2015)<\/li>\n\n\n\n
  53. T. Shiga, N. Yoshida, Y. Shimizu, E. Suzuki, T. Sasaki, D. Watanabe<\/span>, and H. Takagi*; Quality control of plasma membrane proteins by Saccharomyces cerevisiae<\/em> Nedd4-like ubiquitin ligase Rsp5p under environmental stress conditions; Eukaryot. Cell<\/em> 13(9): <\/strong>1191-1199 (2014)<\/li>\n\n\n\n
  54. D. Watanabe<\/span>, R. Kikushima, M. Aitoku, A. Nishimura, I. Ohtsu, R. Nasuno, and H. Takagi*; Exogenous addition of histidine reduces copper availability in the yeast Saccharomyces cerevisiae<\/em>; Microb. Cell<\/em> 1(7): <\/strong>241-246 (2014)<\/li>\n\n\n\n
  55. S. Uesugi, D. Watanabe<\/span>, M. Kitajima, R. Watanabe, Y. Kawamura, M. Ohnishi, H. Takagi, and K. Kimura*; Calcineurin inhibitors suppress the high-temperature stress sensitivity of the yeast ubiquitin ligase Rsp5 mutant: a new method of screening for calcineurin inhibitors; FEMS Yeast Res.<\/em> 14(4):<\/strong> 567-574 (2014)<\/li>\n\n\n\n
  56. T. Inaba, D. Watanabe<\/span>, Y. Yoshiyama, K. Tanaka, J. Ogawa, H. Takagi, H. Shimoi, and J. Shima*; An organic acid-tolerant HAA1<\/em>-overexpression mutant of an industrial bioethanol strain of Saccharomyces cerevisiae<\/em> and its application to the production of bioethanol from sugarcane molasses; AMB Express<\/em> 3(1):<\/strong> 74 (2013)<\/li>\n\n\n\n
  57. D. Watanabe<\/span>, N. Hashimoto, M. Mizuno, Y. Zhou, T. Akao, and H. Shimoi*; Accelerated alcoholic fermentation caused by defective gene expression related to glucose derepression in Saccharomyces cerevisiae<\/em>; Biosci. Biotechnol. Biochem.<\/em> 77(11): <\/strong>2255-2262 (2013)<\/li>\n\n\n\n
  58. T. Inai\u2020<\/sup>, D. Watanabe<\/span>\u2020<\/sup>, Y. Zhou, R. Fukada, T. Akao, J. Shima, H. Takagi, and H. Shimoi*; Rim15p-mediated regulation of sucrose utilization during molasses fermentation using Saccharomyces cerevisiae<\/em> strain PE-2; J. Biosci. Bioeng.<\/em>116(5): <\/strong>591-594 (2013) [\u2020equally contributed]<\/li>\n\n\n\n
  59. K. Wakabayashi, A. Isogai*, D. Watanabe<\/span>, A. Fujita, and S. Sudo; Involvement of methionine salvage pathway genes of Saccharomyces cerevisiae<\/em> in the production of precursor compounds of dimethyl trisulfide (DMTS); J. Biosci. Bioeng.<\/em> 116(4):<\/strong> 475-479 (2013)<\/li>\n\n\n\n
  60. D. Watanabe<\/span>, Y. Araki, Y. Zhou, N. Maeya, T. Akao, and H. Shimoi*; A loss-of-function mutation in the PAS kinase Rim15p is related to defective quiescence entry and high fermentation rates in Saccharomyces cerevisiae<\/em> sake yeast strains; Appl. Environ. Microbiol.<\/em> 78(11):<\/strong> 4008-4016 (2013)<\/li>\n\n\n\n
  61. Y. Sasano\u2020<\/sup>, D. Watanabe<\/span>\u2020<\/sup>, K. Ukibe, T. Inai, I. Ohtsu, H. Shimoi, and H. Takagi*; Overexpression of the yeast transcription activator Msn2 confers furfural resistance and increases the initial fermentation rate in ethanol production; J. Biosci. Bioeng. <\/em>113(4): <\/strong>451-455 (2012) [\u2020<\/sup>equally contributed]<\/li>\n\n\n\n
  62. C. Noguchi\u2020<\/sup>, D. Watanabe<\/span>\u2020<\/sup>, Y. Zhou, T. Akao, and H. Shimoi*; Association of constitutive hyperphosphorylation of Hsf1p with a defective ethanol stress response in Saccharomyces cerevisiae <\/em>sake yeast strains; Appl. Environ. Microbiol.<\/em>78(2):<\/strong> 385-392 (2012) [\u2020<\/sup>equally contributed]<\/li>\n\n\n\n
  63. D. Watanabe<\/span>, S. Nogami, Y. Ohya, Y. Kanno, Y. Zhou, T. Akao, and H. Shimoi*; Ethanol fermentation driven by elevated expression of the G1<\/sub> cyclin gene CLN3<\/em> in sake yeast; J. Biosci. Bioeng.<\/em> 112(6):<\/strong> 577-582 (2011)<\/li>\n\n\n\n
  64. T. Akao, I. Yashiro, A. Hosoyama, H. Kitagaki, H. Horikawa, D. Watanabe<\/span>, R. Akada, Y. Ando, S. Harashima, T. Inoue, Y. Inoue, S. Kajiwara, K. Kitamoto, N. Kitamoto, O. Kobayashi, S. Kuhara, T. Masubuchi, H. Mizoguchi, Y. Nakao, A. Nakazato, M. Namise, T. Oba, T. Ogata, A. Ohta, M. Sato, S. Shibasaki, Y. Takatsume, S. Tanimoto, H. Tsuboi, A. Nishimura, K. Yoda, T. Ishikawa, K. Iwashita, N. Fujita, and H. Shimoi*; Whole-genome sequencing of sake yeast Saccharomyces cerevisiae<\/em> Kyokai no. 7; DNA Res.<\/em> 18(6):<\/strong> 423-434 (2011)<\/li>\n\n\n\n
  65. D. Watanabe<\/span>, T. Ota, F. Nitta, T. Akao, and H. Shimoi*; Automatic measurement of sake fermentation kinetics using a multi-channel gas monitor system; J. Biosci. Bioeng. <\/em>112(1): <\/strong>54-57 (2011)<\/li>\n\n\n\n
  66. H. Urbanczyk, C. Noguchi, H. Wu, D. Watanabe<\/span>, T. Akao, H. Takagi, and H. Shimoi*; Sake yeast strains have difficulty in entering a quiescent state after cell growth cessation; J. Biosci. Bioeng.<\/em> 112(1):<\/strong> 44-48 (2011)<\/li>\n\n\n\n
  67. D. Watanabe<\/span>, H. Wu, C. Noguchi, Y. Zhou, T. Akao, and H. Shimoi*; Enhancement of the initial rate of ethanol fermentation due to dysfunction of yeast stress response components Msn2p and\/or Msn4p; Appl. Environ. Microbiol.<\/em> 77(3):<\/strong> 934-941 (2011)<\/li>\n\n\n\n
  68. M. Watanabe, D. Watanabe<\/span>, S. Nogami, S. Morishita, and Y. Ohya*; Comprehensive and quantitative analysis of yeast deletion mutants defective in apical and isotropic bud growth; Curr. Genet.<\/em> 55(4):<\/strong> 365-380 (2009)<\/li>\n\n\n\n
  69. M. Watanabe, D. Watanabe<\/span>, T. Akao, and H. Shimoi*; Overexpression of MSN2<\/em> in a sake yeast strain promotes ethanol tolerance and increases ethanol production in sake brewing; J. Biosci. Bioeng.<\/em> 107(5):<\/strong> 516-518 (2009)<\/li>\n\n\n\n
  70. M. Suzuki, Y. Asada, D. Watanabe<\/span>, and Y. Ohya*; Cell shape and growth of budding yeast cells in restrictive microenvironments; Yeast<\/em> 21(12):<\/strong> 983-989 (2004)<\/li>\n\n\n\n
  71. T. L. Saito*, M. Ohtani, H. Sawai, F. Sano, A. Saka, D. Watanabe<\/span>, M. Yukawa, Y. Ohya, and S. Morishita; SCMD: Saccharomyces<\/em> cerevisiae morphological database; Nucleic Acids Res.<\/em> 32(Database issue): <\/strong>D319-D322 (2004)<\/li>\n\n\n\n
  72. M. Sekiya-Kawasaki, M. Abe, A. Saka, D. Watanabe<\/span>, K. Kono, M. Minemura-Asakawa, S. Ishihara, T. Watanabe, and Y. Ohya*; Dissection of upstream regulatory components of the Rho1p effector, 1,3-\u03b2-glucan synthase, in Saccharomyces cerevisiae<\/em>; Genetics<\/em> 162(2):<\/strong> 663-676 (2002)<\/li>\n\n\n\n
  73. T. Utsugi, M. Minemura, A. Hirata, M. Abe, D. Watanabe<\/span>, and Y. Ohya*; Movement of yeast 1,3-\u03b2-glucan synthase is essential for uniform cell wall synthesis; Genes Cells <\/em>7(1):<\/strong> 1-9 (2002)<\/li>\n\n\n\n
  74. D. Watanabe<\/span>, M. Abe, and Y. Ohya*; Yeast Lrg1p acts as a specialized RhoGAP regulating 1,3-\u03b2-glucan synthesis; Yeast<\/em> 18(10): <\/strong>943-951 (2001)<\/li>\n<\/ol>\n\n\n\n

    \u3010\u8457\u66f8\u3011<\/h2>\n\n\n\n
      \n
    1. \u6e21\u8fba\u5927\u8f14<\/span>; \u6e05\u9152\u9175\u6bcd\u306e\u30b9\u30c8\u30ec\u30b9\u5fdc\u7b54\u6b20\u640d\u3068\u9ad8\u767a\u9175\u6027; \u300e\u6e05\u9152\u9175\u6bcd\u30fb\u9eb9\u306e\u7814\u7a76\uff0d2000\u5e74\u4ee3\u306e\u7814\u7a76\uff0d\u300f \u6e05\u9152\u9175\u6bcd\u30fb\u9eb9\u7814\u7a76\u4f1a \u7de8 p.28-33, \u72ec\u7acb\u884c\u653f\u6cd5\u4eba\u9152\u985e\u7dcf\u5408\u7814\u7a76\u6240 (2026)<\/li>\n\n\n\n
    2. \u6e21\u8fba\u5927\u8f14<\/span>, \u4e0b\u98ef\u4ec1; \u6e05\u9152\u9175\u6bcd\u306b\u304a\u3051\u308b\u907a\u4f1d\u5b50\u767a\u73fe\u30d7\u30ed\u30d5\u30a1\u30a4\u30eb\u306e\u89e3\u6790; \u300e\u6e05\u9152\u9175\u6bcd\u30fb\u9eb9\u306e\u7814\u7a76\uff0d2000\u5e74\u4ee3\u306e\u7814\u7a76\uff0d\u300f \u6e05\u9152\u9175\u6bcd\u30fb\u9eb9\u7814\u7a76\u4f1a \u7de8 p.6-10, \u72ec\u7acb\u884c\u653f\u6cd5\u4eba\u9152\u985e\u7dcf\u5408\u7814\u7a76\u6240 (2026)<\/li>\n\n\n\n
    3. D. Watanabe<\/span>; Towards the Establishment of Yeast Alcoholic Fermentation Design Technology; “Fermentation in Food Industry” R. Tang (ed.)<\/em> IntechOpen (2025)<\/li>\n\n\n\n
    4. \u6e21\u8fba\u5927\u8f14<\/span>: \u9175\u6bcd\u306e\u30a2\u30eb\u30b3\u30fc\u30eb\u767a\u9175\u30c7\u30b6\u30a4\u30f3\u6280\u8853\u306e\u78ba\u7acb\u306b\u5411\u3051\u3066; \u300e\u767a\u9175\u30fb\u91b8\u9020\u306e\u65b0\u5c55\u958b\u3000\u80b2\u7a2e\u3001\u30d7\u30ed\u30bb\u30b9DX\u304b\u3089\u7cbe\u5bc6\u767a\u9175\u3001\u30a2\u30c3\u30d7\u30b5\u30a4\u30af\u30eb\u307e\u3067\u300f\u91d1\u5185\u8aa0 \u76e3\u4fee p.63-71, \u682a\u5f0f\u4f1a\u793e\u30a8\u30cc\u30fb\u30c6\u30a3\u30fc\u30fb\u30a8\u30b9 (2025)<\/li>\n\n\n\n
    5. \u6e21\u8fba\u5927\u8f14<\/span>; \u751f\u7269\u5de5\u5b66\u306b\u304a\u3051\u308b\u91b8\u9020\u7814\u7a76\u306e\u3053\u308c\u304b\u3089\u306b\u3064\u3044\u3066;\u300e\u65e5\u672c\u751f\u7269\u5de5\u5b66\u4f1a100\u5e74\u53f2\u300f\u65e5\u672c\u751f\u7269\u5de5\u5b66\u4f1a100 \u5e74\u53f2\u7de8\u96c6\u59d4\u54e1\u4f1a \u7de8 p.63-64, (2022)<\/li>\n\n\n\n
    6. \u6e21\u8fba\u5927\u8f14<\/span>; \u6e05\u9152\u9175\u6bcd\u306e\u30a2\u30eb\u30b3\u30fc\u30eb\u767a\u9175\u3068\u7d30\u80de\u8cea\u907a\u4f1d\u56e0\u5b50;\u300e\u767a\u9175\u30fb\u91b8\u9020\u98df\u54c1\u306e\u6700\u524d\u7ddaII\u300f \u5317\u672c\u52dd\u3072\u3053 \u76e3\u4fee p.75-92, \u30b7\u30fc\u30a8\u30e0\u30b7\u30fc\u51fa\u7248 (2022)<\/li>\n\n\n\n
    7. \u6e21\u8fba\u5927\u8f14<\/span>; \u51fa\u82bd\u9175\u6bcd\u306b\u304a\u3051\u308b\u5b9f\u9a13\u5ba4\u682a\u3068\u5b9f\u7528\u682a\u306e\u9055\u3044;\u300e\u91b8\u9020\u306e\u4e8b\u5178\u300f \u5317\u672c\u52dd\u3072\u3053\u3089 \u7de8 p.158-159, \u671d\u5009\u66f8\u5e97 (2021)<\/li>\n\n\n\n
    8. \u6e21\u8fba\u5927\u8f14<\/span>; \u9175\u6bcd\u306e\u30ad\u30e9\u30fc\u56e0\u5b50\u3068\u30d7\u30ea\u30aa\u30f3;\u300e\u91b8\u9020\u306e\u4e8b\u5178\u300f \u5317\u672c\u52dd\u3072\u3053\u3089 \u7de8 p.84-85, \u671d\u5009\u66f8\u5e97 (2021)<\/li>\n\n\n\n
    9. \u6e21\u8fba\u5927\u8f14<\/span>; \u30a6\u30a3\u30b9\u30ad\u30fc\u3068\u9175\u6bcd;\u300e\u98df\u3068\u5fae\u751f\u7269\u306e\u4e8b\u5178\u300f \u5317\u672c\u52dd\u3072\u3053\u3089 \u7de8 p.78-79, \u671d\u5009\u66f8\u5e97 (2017)<\/li>\n\n\n\n
    10. \u6e21\u8fba\u5927\u8f14<\/span>; \u6e05\u9152\u9175\u6bcd;\u300e\u98df\u3068\u5fae\u751f\u7269\u306e\u4e8b\u5178\u300f \u5317\u672c\u52dd\u3072\u3053\u3089 \u7de8 p.6-7, \u671d\u5009\u66f8\u5e97 (2017)<\/li>\n\n\n\n
    11. D. Watanabe<\/span>, H. Takagi, and H. Shimoi; Mechanism of High Alcoholic Fermentation Ability of Sake Yeast; \u201dStress Biology of Yeasts and Fungi: Applications for Industrial Brewing and Fermentation\u201d H. Takagi and H. Kitagaki (eds.)<\/em> p.59-75, Springer (2015)<\/li>\n\n\n\n
    12. \u9ad8\u6728\u535a\u53f2, \u6e21\u8fba\u5927\u8f14<\/span>, \u585a\u539f\u6b63\u4fca; \u6709\u7528\u30a2\u30df\u30ce\u9178\u3092\u9ad8\u751f\u7523\u3059\u308b\u6ce1\u76db\u9175\u6bcd\u306e\u80b2\u7a2e\u3068\u6ce1\u76db\u306e\u9ad8\u4ed8\u52a0\u4fa1\u5024\u5316\u3078\u306e\u5fdc\u7528;\u300e\u767a\u9175\u30fb\u91b8\u9020\u98df\u54c1\u306e\u6700\u524d\u7dda\u300f \u5317\u672c\u52dd\u3072\u3053 \u76e3\u4fee p.257-269, \u30b7\u30fc\u30a8\u30e0\u30b7\u30fc\u51fa\u7248 (2015)<\/li>\n\n\n\n
    13. \u6e21\u8fba\u5927\u8f14<\/span>, \u9ad8\u6728\u535a\u53f2, \u4e0b\u98ef \u4ec1; \u6e05\u9152\u9175\u6bcd\u306e\u9ad8\u767a\u9175\u6027\u539f\u56e0\u5909\u7570\u3068\u305d\u306e\u5fdc\u7528;\u300e\u767a\u9175\u30fb\u91b8\u9020\u98df\u54c1\u306e\u6700\u524d\u7dda\u300f \u5317\u672c\u52dd\u3072\u3053 \u76e3\u4fee p.101-108, \u30b7\u30fc\u30a8\u30e0\u30b7\u30fc\u51fa\u7248 (2015)<\/li>\n\n\n\n
    14. \u5927\u77e2\u798e\u4e00, \u6e21\u8fba\u5927\u8f14<\/span>, \u5ca1\u7530\u5553\u5e0c; \u9175\u6bcd\u306e\u5f62\u614b\u60c5\u5831\u3092\u767a\u9175\u30fb\u91b8\u9020\u306b\u751f\u304b\u3059;\u300e\u767a\u9175\u30fb\u91b8\u9020\u98df\u54c1\u306e\u6700\u524d\u7dda\u300f \u5317\u672c\u52dd\u3072\u3053 \u76e3\u4fee p.1-11, \u30b7\u30fc\u30a8\u30e0\u30b7\u30fc\u51fa\u7248 (2015)<\/li>\n\n\n\n
    15. \u6e21\u8fba\u5927\u8f14<\/span>, \u4e0b\u98ef \u4ec1; \u6e05\u9152\u9175\u6bcd\u306e\u30b9\u30c8\u30ec\u30b9\u5fdc\u7b54\u6b20\u640d\u3068\u9ad8\u30a8\u30bf\u30ce\u30fc\u30eb\u767a\u9175\u6027;\u300e\u767a\u9175\u30fb\u91b8\u9020\u98df\u54c1\u306e\u6700\u65b0\u6280\u8853\u3068\u6a5f\u80fd\u6027II\u300f \u5317\u672c\u52dd\u3072\u3053 \u76e3\u4fee p.150-160, \u30b7\u30fc\u30a8\u30e0\u30b7\u30fc\u51fa\u7248 (2011)<\/li>\n\n\n\n
    16. \u6e21\u8fba\u5927\u8f14<\/span>; \u30ac\u30b9\u767a\u751f\u91cf\u8a08\u6e2c\u30b7\u30b9\u30c6\u30e0\u3092\u7528\u3044\u305f\u6e05\u9152\u767a\u9175\u30d7\u30ed\u30d5\u30a1\u30a4\u30eb\u306e\u5b9a\u91cf\u7684\u89e3\u6790;\u300e\u767a\u9175\u30fb\u91b8\u9020\u98df\u54c1\u306e\u6700\u65b0\u6280\u8853\u3068\u6a5f\u80fd\u6027II\u300f \u5317\u672c\u52dd\u3072\u3053 \u76e3\u4fee p.140-149, \u30b7\u30fc\u30a8\u30e0\u30b7\u30fc\u51fa\u7248 (2011)<\/li>\n\n\n\n
    17. \u963f\u90e8\u5145\u5b8f, \u6e21\u8fba\u5927\u8f14<\/span>, \u5927\u77e2\u798e\u4e00; 1990\u5e74\u4ee3\u306e\u9175\u6bcd\u7814\u7a76\u306e\u9032\u5c55\uff0f1-6 \u5f62\u614b\u5f62\u6210; \u300e\u6e05\u9152\u9175\u6bcd\u306e\u7814\u7a76\uff0d90\u5e74\u4ee3\u306e\u7814\u7a76\uff0d\u300f \u6e05\u9152\u9175\u6bcd\u30fb\u9eb9\u7814\u7a76\u4f1a \u7de8 p.30-39, \u8ca1\u56e3\u6cd5\u4eba\u65e5\u672c\u91b8\u9020\u5354\u4f1a (2003)<\/li>\n<\/ol>\n\n\n\n

      \u3010\u7dcf\u8aac\u3011<\/h2>\n\n\n\n
        \n
      1. N. Akasaka, D. Watanabe<\/span>, K. Yasukawa, and S. Fujiwara; Solid-state cultivation-specific agmatine production by Aspergillus oryzae<\/em>: current understanding and perspectives; Amino Acids<\/em> 58:<\/strong> 13 (2026)<\/li>\n\n\n\n
      2. \u8d64\u5742\u76f4\u7d00, \u6e21\u8fba\u5927\u8f14<\/span>; \u4f1d\u7d71\u7684\u767a\u9175\u98df\u54c1\u3092\u652f\u3048\u308b\u5fae\u751f\u7269\u305f\u3061\u3068\u305d\u306e\u6a5f\u80fd\u306e\u958b\u62d3; \u98df\u54c1\u3068\u958b\u767a<\/em> 61:<\/strong> 8-11 (2026)<\/li>\n\n\n\n
      3. \u6e21\u8fba\u5927\u8f14<\/span>; \u690d\u7269\u30af\u30c1\u30af\u30e9\u5c64\u306b\u5bbf\u308b\u5fae\u751f\u7269\u751f\u614b\u7cfb\u306e\u53ef\u80fd\u6027\u3092\u63a2\u308b; \u6708\u520a \u7d30\u80de<\/em> 57:<\/strong> 337-339 (2025)<\/li>\n\n\n\n
      4. \u5409\u5ca1\u6c42, \u6e21\u8fba\u5927\u8f14<\/span>; \u4f1d\u7d71\u7684\u767a\u9175\u98df\u54c1\u306e\u751f\u614b\u7cfb\u3092\u5f62\u3065\u304f\u308b\u5fae\u751f\u7269\u9593\u76f8\u4e92\u4f5c\u7528; \u65e5\u672c\u91b8\u9020\u5354\u4f1a\u8a8c<\/em> 119:<\/strong> 338-346 (2024)<\/li>\n\n\n\n
      5. \u6e21\u8fba\u5927\u8f14<\/span>; \u690d\u7269\u30af\u30c1\u30af\u30e9\u5c64\u306b\u5fae\u751f\u7269\u751f\u614b\u7cfb\u306f\u6210\u7acb\u3059\u308b\u306e\u304b; \u30a2\u30b0\u30ea\u30d0\u30a4\u30aa<\/em> 8:<\/strong> 40-42 (2024)<\/li>\n\n\n\n
      6. \u6e21\u8fba\u5927\u8f14<\/span>, \u6a4b\u672c\u6e09; \u91b8\u9020\u5fae\u751f\u7269\u306e\u771f\u306e\u3059\u307f\u304b\u3068\u306f \uff5e\u30ef\u30a4\u30f3\u9175\u6bcd\u7814\u7a76\u306b\u57fa\u3065\u304f\u4e00\u8003\u5bdf\uff5e; \u65e5\u672c\u91b8\u9020\u5354\u4f1a\u8a8c<\/em> 119:<\/strong> 142-148 (2024)<\/li>\n\n\n\n
      7. D. Watanabe<\/span>; Sake yeast symbiosis with lactic acid bacteria and alcoholic fermentation; Biosci. Biotechnol. Biochem.<\/em> 88:<\/strong> 237-241 (2024)<\/li>\n\n\n\n
      8. \u6e21\u8fba\u5927\u8f14<\/span>; \u9175\u6bcd\u306f\u7d30\u80de\u58c1\u306e\u539a\u3055\u3092\u8abf\u7bc0\u3057\u3066\u30a2\u30eb\u30b3\u30fc\u30eb\u767a\u9175\u529b\u3092\u5236\u5fa1\u3059\u308b; \u30d0\u30a4\u30aa\u30b5\u30a4\u30a8\u30f3\u30b9\u3068\u30a4\u30f3\u30c0\u30b9\u30c8\u30ea\u30fc<\/em> 82:<\/strong> 156-157 (2024)<\/li>\n\n\n\n
      9. <\/a>\u6e21\u8fba\u5927\u8f14<\/span>; \u4f1d\u7d71\u7684\u767a\u9175\u98df\u54c1\u306b\u304a\u3051\u308b\u9175\u6bcd\u306e\u3075\u308b\u307e\u3044\u3092\u8ffd\u7a76\u3059\u308b; \u751f\u7269\u5de5\u5b66\u4f1a\u8a8c<\/em> 101:<\/strong> 540-542 (2023)<\/li>\n\n\n\n
      10. \u6e21\u8fba\u5927\u8f14<\/span>; \u6e05\u9152\u9175\u6bcd\u306e\u5171\u751f\u3068\u30a2\u30eb\u30b3\u30fc\u30eb\u767a\u9175; \u6e29\u6545\u77e5\u65b0<\/em> <\/strong>60:<\/strong> 67-72 (2023)<\/li>\n\n\n\n
      11. \u6e21\u8fba\u5927\u8f14<\/span>, \u9ad8\u6728\u535a\u53f2; \u9175\u6bcd\u306f\u4f55\u3092\u611f\u77e5\u3057\u3066\u30a2\u30eb\u30b3\u30fc\u30eb\u767a\u9175\u3092\u8abf\u7bc0\u3057\u3066\u3044\u308b\u306e\u304b\uff1f; \u751f\u7269\u5de5\u5b66\u4f1a\u8a8c<\/em> 98:<\/strong> 170-173 (2020)<\/li>\n\n\n\n
      12. D. Watanabe<\/span> and H. Takagi; Yeast prion-based metabolic reprogramming induced by bacteria in fermented foods; FEMS Yeast Res. <\/em>19:<\/strong> foz061 (2019)<\/li>\n\n\n\n
      13. \u6e21\u8fba\u5927\u8f14<\/span>, \u9ad8\u6728\u535a\u53f2; \u9175\u6bcd\u30e6\u30d3\u30ad\u30c1\u30f3Rsp5\u306b\u3088\u308b\u9078\u629e\u7684\u306a\u57fa\u8cea\u8a8d\u8b58\u3068\u305d\u306e\u5fdc\u7528\u3078\u306e\u53ef\u80fd\u6027; \u5316\u5b66\u3068\u751f\u7269<\/em> 57: <\/strong>36-42 (2019)<\/li>\n\n\n\n
      14. A. Watcharawipas, D. Watanabe<\/span>, and H. Takagi; Sodium acetate tolerance in Saccharomyces cerevisiae<\/em> and the ubiquitin ligase Rsp5; Front. Microbiol.<\/em> 9: <\/strong>2495 (2018)<\/li>\n\n\n\n
      15. \u6e21\u8fba\u5927\u8f14<\/span>, \u9ad8\u6728\u535a\u53f2; \u5fae\u751f\u7269\u9593\u76f8\u4e92\u4f5c\u7528\u3068\u4ee3\u8b1d\uff0c\u305d\u3057\u3066\u30d7\u30ea\u30aa\u30f3; \u751f\u7269\u5de5\u5b66\u4f1a\u8a8c<\/em> 96:<\/strong> 463-466 (2018)<\/li>\n\n\n\n
      16. \u6e21\u8fba\u5927\u8f14<\/span>; \u30d1\u30f3\u9175\u6bcd\u306f\u306a\u305c\u30a2\u30eb\u30b3\u30fc\u30eb\u767a\u9175\u529b\u304c\u9ad8\u3044\u306e\u304b\uff1f; \u88fd\u30d1\u30f3\u5de5\u696d<\/em> 47:<\/strong> 12-21 (2017)<\/li>\n\n\n\n
      17. \u6e21\u8fba\u5927\u8f14<\/span>, \u9ad8\u6728\u535a\u53f2; \u304a\u9152\u3092\u3064\u304f\u308b\u9175\u6bcd\u2015\u30b2\u30ce\u30e0\u304b\u3089\u89e3\u304d\u660e\u304b\u3059\u91b8\u9020\u7279\u6027\u306e\u3072\u307f\u3064; \u751f\u7269\u306e\u79d1\u5b66 \u907a\u4f1d<\/em> 71:<\/strong> 206-212 (2017)<\/li>\n\n\n\n
      18. D. Watanabe<\/span> and H. Takagi; Pleiotropic functions of the yeast Greatwall-family protein kinase Rim15p: a novel target for the control of alcoholic fermentation; Biosci. Biotech. Biochem.<\/em> 81:<\/strong> 1061-1068 (2017)<\/li>\n\n\n\n
      19. \u6e21\u8fba\u5927\u8f14<\/span>, \u9ad8\u6728\u535a\u53f2; \u3053\u3053\u307e\u3067\u308f\u304b\u3063\u305f\uff01\u304d\u3087\u3046\u304b\u3044\u9175\u6bcd\uff08\u6e05\u9152\u7528\uff09\u306e\u9ad8\u767a\u9175\u529b\u3092\u751f\u307f\u51fa\u3059RIM15<\/em>\u5909\u7570\u907a\u4f1d\u5b50; \u65e5\u672c\u91b8\u9020\u5354\u4f1a\u8a8c<\/em> 111:<\/strong> 638-647 (2016)<\/li>\n\n\n\n
      20. \u6e21\u8fba\u5927\u8f14<\/span>, \u9ad8\u6728\u535a\u53f2; \u9175\u6bcd\u306e\u30a8\u30bf\u30ce\u30fc\u30eb\u8010\u6027\uff1a\u5185\u3068\u5916\u304b\u3089\u7d30\u80de\u3092\u8b77\u308b; \u751f\u7269\u5de5\u5b66\u4f1a\u8a8c<\/em> 93: <\/strong>460-463 (2015)<\/li>\n\n\n\n
      21. \u6e21\u8fba\u5927\u8f14<\/span>; \u6e05\u9152\u9175\u6bcd\u306e\u9ad8\u767a\u9175\u6027\u306b\u95a2\u3059\u308b\u907a\u4f1d\u5b66\u7684\u7814\u7a76; \u751f\u7269\u5de5\u5b66\u4f1a\u8a8c<\/em> 91:<\/strong> 2-9 (2013)<\/li>\n\n\n\n
      22. \u6e21\u8fba\u5927\u8f14<\/span>; \u306a\u305c\u6e05\u9152\u9175\u6bcd\u306f\u30a2\u30eb\u30b3\u30fc\u30eb\u767a\u9175\u529b\u304c\u9ad8\u3044\u306e\u304b\uff1f; \u5316\u5b66\u3068\u751f\u7269<\/em> 50:<\/strong> 723-729 (2012)<\/li>\n\n\n\n
      23. \u4e0b\u98ef \u4ec1, \u8d64\u5c3e \u5065, \u6e21\u8fba\u5927\u8f14<\/span>; \u30b2\u30ce\u30e0\u304b\u3089\u898b\u305f\u6e05\u9152\u9175\u6bcd\u306e\u9032\u5316\u3068\u91b8\u9020\u7279\u6027\u306e\u89e3\u6790; \u751f\u7269\u5de5\u5b66\u4f1a\u8a8c<\/em> 89:<\/strong> 532-535 (2011)<\/li>\n\n\n\n
      24. \u6e21\u8fba\u5927\u8f14<\/span>; \u6e05\u9152\u9175\u6bcd\u306b\u304a\u3051\u308b\u30b9\u30c8\u30ec\u30b9\u5fdc\u7b54\u6a5f\u69cb\u306e\u6a5f\u80fd\u4e0d\u5168; \u30d0\u30a4\u30aa\u30b5\u30a4\u30a8\u30f3\u30b9\u3068\u30a4\u30f3\u30c0\u30b9\u30c8\u30ea\u30fc<\/em> 69:<\/strong> 311-313 (2011)<\/li>\n\n\n\n
      25. \u6e21\u8fba\u5927\u8f14<\/span>, \u4e0b\u98ef \u4ec1; \u6e05\u9152\u9175\u6bcd\u306e\u30b9\u30c8\u30ec\u30b9\u5fdc\u7b54\u3068\u30a8\u30bf\u30ce\u30fc\u30eb\u767a\u9175; \u30d0\u30a4\u30aa\u30a4\u30f3\u30c0\u30b9\u30c8\u30ea\u30fc<\/em>28(6):<\/strong> 42-48 (2011)<\/li>\n\n\n\n
      26. \u6e21\u8fba\u5927\u8f14<\/span>, \u5927\u8c37\u672a\u7a1a, \u68ee\u4e0b\u771f\u4e00, \u5927\u77e2\u798e\u4e00; \u753b\u50cf\u89e3\u6790\u306b\u57fa\u3065\u304f\u7db2\u7f85\u7684\u306a\u8868\u73fe\u578b\u89e3\u6790; \u7d30\u80de\u5de5\u5b66<\/em> 23:<\/strong> 439-443 (2004)<\/li>\n\n\n\n
      27. \u6e21\u8fba\u5927\u8f14<\/span>, \u5927\u8c37\u672a\u7a1a, \u6589\u85e4\u592a\u90ce, \u68ee\u4e0b\u771f\u4e00, \u5927\u77e2\u798e\u4e00; \u51fa\u82bd\u9175\u6bcd\u306b\u304a\u3051\u308b\u7db2\u7f85\u7684\u5f62\u614b\u89e3\u6790; \u5316\u5b66\u3068\u751f\u7269<\/em> 42:<\/strong> 240-248 (2004)<\/li>\n\n\n\n
      28. \u6e21\u8fba\u5927\u8f14<\/span>, \u5927\u77e2\u798e\u4e00; \u751f\u547d\u79d1\u5b66\u306e\u5922\u3092\u3075\u304f\u3089\u307e\u3059\uff0d\u30d1\u30f3\u9175\u6bcd\uff0d; \u7d30\u80de\u5de5\u5b66<\/em> 21:<\/strong> 20-24<\/li>\n<\/ol>\n\n\n\n

        \u3010\u7279\u8a31\u3011<\/h2>\n\n\n\n
          \n
        1. \u4e2d\u702c\u7531\u8d77\u5b50, \u4e21\u89d2\u4f51\u4e00, \u6e21\u8fba\u5927\u8f14<\/span>, \u6749\u672c\u5e78\u5b50; \u30a2\u30eb\u30b3\u30fc\u30eb\u767a\u9175\u65b9\u6cd5\u304a\u3088\u3073\u30a2\u30eb\u30b3\u30fc\u30eb\u767a\u9175\u4fc3\u9032\u5264; \u7279\u98582023-132508<\/li>\n\n\n\n
        2. D. Watanabe<\/span>, K. Takagi, and H. Takagi; Method for promoting fermentation through loss of function of vacuolar transporter chaperone complex of yeast; PCT\/JP2017\/004212<\/li>\n\n\n\n
        3. \u6e21\u8fba\u5927\u8f14<\/span>, \u9ad8\u6728\u5065\u4e00, \u9ad8\u6728\u535a\u53f2; \u9175\u6bcd\u306e\u6db2\u80de\u30c8\u30e9\u30f3\u30b9\u30dd\u30fc\u30bf\u30fc\u30b7\u30e3\u30da\u30ed\u30f3\u8907\u5408\u4f53\u306e\u6a5f\u80fd\u6b20\u640d\u306b\u3088\u308b\u767a\u9175\u4fc3\u9032\u65b9\u6cd5; \u7279\u98582016-025324<\/li>\n\n\n\n
        4. \u5927\u6a4b\u6b63\u5b5d, \u9ad8\u6728\u535a\u53f2, \u6e21\u8fba\u5927\u8f14<\/span>; \u30aa\u30eb\u30cb\u30c1\u30f3\u9ad8\u84c4\u7a4d\u9175\u6bcd\u53ca\u3073\u305d\u306e\u53d6\u5f97\u65b9\u6cd5\u4e26\u3073\u306b\u5f53\u8a72\u9175\u6bcd\u3092\u7528\u3044\u305f\u9152\u985e\u305d\u306e\u4ed6\u98df\u54c1\u306e\u88fd\u9020\u65b9\u6cd5; \u7279\u98582015-020780 [\u7279\u8a31\u7b2c6268544\u53f7]<\/li>\n\n\n\n
        5. \u4e0a\u539f\u5065\u4e8c, \u6e21\u90e8 \u6f64, \u8302\u6728\u559c\u4fe1, \u4e0b\u98ef \u4ec1, \u8d64\u5c3e \u5065, \u6e21\u8fba\u5927\u8f14<\/span>; HEMF\u9ad8\u542b\u6709\u767a\u9175\u98df\u54c1\u306e\u88fd\u9020\u6cd5; \u7279\u98582013-015210 [\u7279\u8a31\u7b2c6049015\u53f7]<\/li>\n\n\n\n
        6. \u6e21\u8fba\u5927\u8f14<\/span>, \u8352\u6728\u60a0\u77e2, \u8d64\u5c3e \u5065, \u4e0b\u98ef \u4ec1; \u6e05\u9152\u9175\u6bcd\u53ca\u3073\u305d\u308c\u3092\u7528\u3044\u305f\u9152\u985e\u53c8\u306f\u98df\u54c1\u306e\u88fd\u9020\u65b9\u6cd5; \u7279\u98582012-036571<\/li>\n\n\n\n
        7. \u82e5\u6797 \u8208, \u78ef\u8c37\u6566\u5b50, \u6e21\u8fba\u5927\u8f14<\/span>, \u85e4\u7530\u6643\u5b50, \u9808\u85e4\u8302\u4fca; 1,2-\u30b8\u30d2\u30c9\u30ed\u30ad\u30b7-5-\u30e1\u30c1\u30eb\u30b9\u30eb\u30d5\u30a3\u30cb\u30eb\u30da\u30f3\u30bf\u30f3-3-\u30aa\u30f3\u751f\u6210\u80fd\u304c\u4f4e\u4e0b\u3057\u305f\u9175\u6bcd\u306e\u4f5c\u51fa\u65b9\u6cd5; \u7279\u98582012-035773<\/li>\n\n\n\n
        8. \u6e21\u8fba\u5927\u8f14<\/span>, \u8352\u6728\u60a0\u77e2, \u5468 \u5ef6; \u4e95\u5185\u667a\u7f8e, \u8d64\u5c3e \u5065, \u4e0b\u98ef \u4ec1; \u30a8\u30bf\u30ce\u30fc\u30eb\u306e\u88fd\u9020\u65b9\u6cd5; \u7279\u98582011-057852 [\u7279\u8a31\u7b2c5828447\u53f7]<\/li>\n\n\n\n
        9. \u4f50\u85e4\u667a\u7f8e, \u8d64\u5c3e \u5065, \u6e21\u8fba\u5927\u8f14<\/span>, \u4e0b\u98ef \u4ec1; \u91b8\u9020\u9152\u306b\u542b\u307e\u308c\u308b\u5fae\u751f\u7269\u7531\u6765\u306eDNA\u306e\u691c\u51fa\u65b9\u6cd5; \u7279\u98582010-036529 [\u7279\u8a31\u7b2c5574221\u53f7]<\/li>\n\n\n\n
        10. \u6e21\u8fba\u5927\u8f14<\/span>, \u8d64\u5c3e \u5065, \u4e0b\u98ef \u4ec1; \u30a8\u30bf\u30ce\u30fc\u30eb\u306e\u88fd\u9020\u65b9\u6cd5; \u7279\u98582009-278555 [\u7279\u8a31\u7b2c5585952\u53f7]<\/li>\n<\/ol>\n","protected":false},"excerpt":{"rendered":"

          \u3010\u8ad6\u6587\u3011 \u3010\u8457\u66f8\u3011 \u3010\u7dcf\u8aac\u3011 \u3010\u7279\u8a31\u3011<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-57","page","type-page","status-publish"],"_links":{"self":[{"href":"https:\/\/bsw3.naist.jp\/microbial_interaction\/wp-json\/wp\/v2\/pages\/57","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/bsw3.naist.jp\/microbial_interaction\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/bsw3.naist.jp\/microbial_interaction\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/bsw3.naist.jp\/microbial_interaction\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/bsw3.naist.jp\/microbial_interaction\/wp-json\/wp\/v2\/comments?post=57"}],"version-history":[{"count":0,"href":"https:\/\/bsw3.naist.jp\/microbial_interaction\/wp-json\/wp\/v2\/pages\/57\/revisions"}],"wp:attachment":[{"href":"https:\/\/bsw3.naist.jp\/microbial_interaction\/wp-json\/wp\/v2\/media?parent=57"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}