Publication listi2001`2019j

 

2019”N

M. Takei, S. Kogure, C. Yokoyama, Y. Kouzuma, Y. Suzuki, Identification of an aldehyde oxidase involved in indole-3-acetic acid synthesis in Bombyx mori silk gland.: Biosci. Biotechnol. Biochem., 83, 129-136 (2019). [PubMed], [PDF]

 

2017”N

C. Yokoyama, M. Takei, Y. Kouzuma, S. Nagata, and Y.Suzuki, Novel tryptophan metabolic pathways in auxin biosynthesis in silkworm: J. Insect Physiol, 101, 91-96 (2017). [PubMed], [PDF]

 

2015”N

C. F. Moro, Y. Fukao, J. Shibato, R. Rakwal, G. K. Agrawal, Y. Shioda, Y. Kouzuma, and M. Yonekura, Seed Endosperm and Embryo Proteomics of the Lotus (Nelumbo Nucifera Gaertn.) by One-Dimensional Gel-Based Tandem Mass Spectrometry and a Comparison with the Mature Endosperm Proteome: Proteomes, 3, 184-235 (2015). [PubMed], [Website], [PDF]

 

C. F. Moro, Y. Fukao, J. Shibato, R. Rakwal, A. M. Timperio, L. Zolla, G. K. Agrawal, Y. Shioda, Y. Kouzuma, and M. Yonekura, Unraveling the seed endosperm proteome of the lotus (Nelumbo nucifera Gaertn.) utilizing 1DE and 2DE separation in conjunction with tandem mass spectrometry: Proteomics, 15, 1717-1735 (2015). [PubMed], [PDF]

 

2014”N

Y. Kouzuma, S. Irie, R. Yamazaki, and M. Yonekura, Purification and cDNA cloning of a lectin and a lectin-like protein from Apios americana Medikus tubers: Biosci. Biotechnol. Biochem., 78, 574-581 (2014). [PubMed], [PDF]

 

2013”N

C.F. Moro, M. Yonekura, Y. Kouzuma, G. K. Agrawal,and R. Rakwal, Lotus A Source of Food and Medicine: Current Status and Future Perspectives in Context of the Seed Proteomics: Int. J. Life Sci., 7, 1-5 (2013).  [Website], [PDF]

 

2012”N

Y. Shimizu, H. Yamazaki, S. Yoshida, M. Yonekura, and Y. Kouzuma, Molecular cloning, recombinant expression, and characterization of isolectin genes of hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata: Biosci. Biotechnol. Biochem., 76, 276-282 (2012). [PubMed], [PDF]

 

2011”N

Y. Zhang, C. Zhou, S. Tang, X. Yu, Y. Kouzuma, and M. Yonekura, Effect of AATI, a Bowman-Birk type inhibitor from Apios americana, on proliferation of cancer cell lines: Food Chem., 128, 909-915 (2011). [PubMed], [Website], [PDF]

 

2010”N

T. Miyaji,S. Murayama, Y. Kouzuma, N. Kimura, M. R. Kanost, K. J. Kramer,and M. Yonekura, Molecular cloning of a multidomain cysteine protease and protease inhibitor precursor gene from the tobacco hornworm (Manduca sexta) and functional expression of the cathepsin F-like cysteine protease domain: Insect Biochem. Mol. Biol., 40, 835-846 (2010). [PubMed], [PDF]

 

Y. Kimura, H. Nagai, M. Miyamoto, M. Kimura, and M. Yonekura, Identification of a royal jelly glycoprotein that carries unique complex-type N-glycans harboring the T-antigen (Galƒΐ1-3GalNAc) unit: Biosci Biotechnol Biochem., 74, 2148-2150 (2010). [PubMed], [PDF]

 

2009”N

K. Doi-Kawano, E. Nishimoto, Y. Kouzuma, D. Takahashi, S. Yamashita, and M. Kimura, Steady-State and Time-Resolved Fluorescence Spectroscopic Studies on Interaction of the N-terminal Region with the Hairpin Loop of the Phytocystain Scb: J. Fluoresc., 19, 631-639 (2009). [PubMed], [PDF]

 

H. Guo, Y. Kouzuma, and M. Yonekura, Structures and properties of antioxidative peptides derived from royal jelly protein: Food Chem., 113,@238-245 (2009). [PubMed], [PDF]

 

2008”N

S. Sirisattha, E. Kitagawa, M. Yonekura, and H. Iwahashi, Functional Genomics Analysis of n-Alkyl Sulfates Toxicity in the Yeast Saccharomyces cerevisiae: Chem-Bio Info. J., 8, 69-84 (2008). [PubMed], [PDF]

 

H. Guo, A. Ekusa, K. Iwai, M. Yonekura, Y. Takahata, and F. Morimatsu, Royal Jelly Peptides Inhibit Lipid Peroxidation in Vitro and In Vivo: J. Nutr. Sci. Vitaminol., 54, 191-195 (2008). [PubMed], [PDF]

 

T. Furusawa, R. Rakwal, H. W. Nam, J. Shibato, G. K. Agrawal, Y. S. Kim, Y. Ogawa, Y. Yoshida, Y. Kouzuma, Y. Masuo, and M. Yonekura, Comprehensive royal jelly (RJ) proteomics using one- and two-dimensional proteomics platforms reveals novel RJ proteins and potential phospho/glycoproteins: J. Proteome Res.,7, 3194-3229 (2008). [PubMed]

 

K. Horie, R. Rakwal, M. Hirano, J. Shibato, H. W. Nam, Y. S. Kim, Y. Kouzuma, G. K. Agrawal, Y. Masuo, and M. Yonekura, Proteomics of two cultivated mushrooms Sparassis crispa and Hericium erinaceum provides insight into their numerous functional protein components and diversity: J. Proteome Res., 7, 1819-1835 (2008). [PubMed]

 

T. Furusawa, R. Rakwal, H. W. Nam, M. Hirano, J. Shibato, Y. S. Kim, Y. Ogawa, Y. Yoshida, K. J. Kramer, Y. Kouzuma, G. K. Agrawal, and M. Yonekura, Systematic investigation of the hemolymph proteome of Manduca sexta at the fifth instar larvae stage using one- and two-dimensional proteomics platforms: J. Proteome Res., 7, 938-959 (2008). [PubMed]

 

Y. Zhang, Y. Kouzuma, T. Miyaji and M. Yonekura, Purification, characterization, and cDNA cloning of a Bowman-Birk type trypsin inhibitor from Apios americana Medikus tubers: Biosci. Biotechnol. Biochem., 72, 171-178 (2008). [PubMed], [PDF]

 

2007”N

S. Yoshida, Y. Shimada, D. Kondoh, Y. Kouzuma, A. K. Ghosh, M. Jacobs-Lorena, R. E. Sinden, Hemolytic C-type lectin CEL-III from sea cucumber expressed in transgenic mosquitoes impairs malaria parasite development: PLoS Pathog., 3, 1962-1970 (2007). [PubMed], [Full text], [PDF]

 

T. Hatakeyama, H. Unno, Y. Kouzuma, T. Uchida, S. Eto, H. Hidemura, N. Kato, M. Yonekura, and M. Kusunoki, C-type lectin-like carbohydrate-recognition of the hemolytic lectin CEL-III containing ricin-type beta-trefoil folds: J. Biol. Chem., 282, 37826-37835 (2007). [PubMed], [PDF]

 

T. Miyaji, Y. Kouzuma, J. Yaguchi, R. Matsumoto, M. R. Kanost, K. J. Kramer, and M. Yonekura, Purification of a cysteine protease inhibitor from larval hemolymph of the tobacco hornworm (Manduca sexta) and functional expression of the recombinant protein: Insect Biochem. Mol. Biol., 37, 960-968 (2007). [PubMed], [PDFiCampus only)]

 

2006”N

Y. H. Jung, R. Rakwal, G. K. Agrawal, J. Shibato, J. A. Kim, M. O. Lee, P. K. Choi, S. H. Jung, S. H. Kim, H. J. Koh, M. Yonekura, H. Iwahashi, and N. S. Jwa, Differential expression of defense/stress-related marker proteins in leaves of a unique rice blast lesion mimic mutant (blm): J. Proteome Res., 5, 2586-2598 (2006). [PubMed]

 

G. K. Agrawal, N. S. Jwa, Y. Iwahashi, M. Yonekura, H. Iwahashi, and R. Rakwal, Rejuvenating rice proteomics: facts, challenges, and visions: Proteomics, 6,5549-5576 (2006). [PubMed]

 

N. S. Jwa, G. K. Agrawal, S. Tamogami, M. Yonekura, O. Han, H. Iwahashi, and R. Rakwal, Role of defense/stress-related marker genes, proteins and secondary metabolites in defining rice self-defense mechanisms: Plant Physiol. Biochem., 44, 261-273 (2006). [PubMed], [PDF]

 

R. Matsumoto, R. Rakwal, G. K. Agrawal, Y. H. Jung, N. S. Jwa, M. Yonekura, H. Iwahashi, and K. Akama, Search for novel stress-responsive protein components using a yeast mutant lacking two cytosolic Hsp70 genes, SSA1 and SSA2: Mol. Cells, 21, 381-388 (2006). [PubMed], [PDF (download)]

 

2005”N

H. Guo, Y. Kouzuma, and M. Yonekura, Isolation and properites of antioxidative peptides from water-soluble royal jelly protein hydrolyzate: Food Sci. Technol. Res., 11, 222-230 (2005). [Abstract], [PDF]

 

G. K. Agrawal, M. Yonekura, Y. Iwahashi, H. Iwahashi, and R. Rakwal, System, trends and perspectives of proteomics in dicot plants, Part III: Unraveling the proteomes influenced by the environment, and at the levels of function and genetic relationships: J. Chromatogr. B Analyt. Technol. Biomed. Life Sci, 815, 137-145 (2005). [PubMed]

 

G. K. Agrawal, M. Yonekura, Y. Iwahashi, H. Iwahashi, and R. Rakwal, System, trends and perspectives of proteomics in dicot plants Part II: Proteomes of the complex developmental stages: J. Chromatogr. B Analyt. Technol. Biomed. Life Sci, 815, 125-136 (2005). [PubMed]

 

G. K. Agrawal, M. Yonekura, Y. Iwahashi, H. Iwahashi, and R. Rakwal, System, trends and perspectives of proteomics in dicot plants Part I: Technologies in proteome establishment: J. Chromatogr. B Analyt. Technol. Biomed. Life Sci, 815, 109-123 (2005). [PubMed]

 

Differential activation of phytoalexin production and induction of proteins by amino acid conjugates of jasmonic acid in rice (Oryza sativa L.) seedlings leaves: Nepal J. Sci. Technol., 6, 15-21 (2005).

 

Y. Kouzuma, Y. Tsutsumi, M. Abe, T. Hayashi, K. Hada, K. Uehashi, Y. Shimada, K. Tashiro, S. Kuhara, M. Kimura, Comprehensive analysis of wound-inducible genes from the Nicotiana glutinosa leaves using a full-length cDNA microarray: J. Fac. Agr., Kyushu Univ., 50, 635-648 (2005). [Summary], [PDF]

 

S. Iwanaga, N. Yamasaki, M. Kimura, Y. Kouzuma, Contribution of conserved Asn residues to the inhibitory activities of kunitz-type protease inhibitors from plants: Biosci. Biotechnol. Biochem., 69, 220-223 (2005). [PubMed], [PDF]

 

 

2004”N

Y. Arao, A. Kikuchi, M. Kishida, M. Yonekura, A. Inoue, S. Yasuda, S. Wada, K. Ikeda, and F. Kayama, Stability of A+U-rich element binding factor 1(AUF-1)-binding messenger ribonucleic acid correlates with the subcelluar relocalization of AUF1 in the rat uterus upon estrogen treatment: Mol. Endocrinol., 18, 2255-2267 (2004). [PubMed], [PDF]

 

 

2003”N

M. Kimura, Y. Kimura, K. Tsumura, K. Okihara, H. Sugimoto, H. Yamada, and M. Yonekura, 350-kDa royal jelly glycoprotein (Apisin), which stimulates proliferation of human monocytes, bears the beta 1-3galactosylated N-glycan: Analysis of the N-glycosylation site: Biosci. Biotechnol. Biochem., 67, 2055-2058 (2003). [PubMed], [PDF]

 

Novel insight into kinetin-inducible stress responses in rice seedlings: Plant Physiol. Biochem., 41, 453-457 (2003).

 

Defense/stress responses elicited in rice seedlings exposed to the gaseous air pollutant sulfur dioxide: Environ.and Exp.Bot., 49, 223-235 (2003).

 

T. Hayashi, D. Kobayashi, T. Kariu, M. Tahara, K. Hada, Y. Kouzuma, M. Kimura, Genomic cloning of ribonucleases in Nicotiana glutinosa leaves, as induced in response to wounding or to TMV-infection, and characterization of their promoters: Biosci. Biotechnol. Biochem., 67, 2574-2583 (2003). [PubMed], [PDF]

 

Y. Kouzuma, Y. Suzuki, M. Nakano, K. Matsuyama, S. Tojo, M. Kimura, T. Yamasaki, H. Aoyagi, T. Hatakeyama, Characterization of functional domains of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata: J. Biochem., 134, 395-402 (2003). [PubMed], [PDFiCampus only)]

 

Y. Kouzuma, M. Mizoguchi, H. Takagi, H. Fukuhara, M. Tsukamoto, T. Numata, and M. Kimura, Reconstitution of archaeal ribonuclease P from RNA and four protein components: Biochem. Biophys. Res. Commun., 306, 666-673 (2003). [PubMed], [PDF (Campus only)]

 

 

2002”N

Chitosan activates defense/stress response(s) in the leaves of Oryza sativa seedlings: Plant Physiol. Biochem., 40, 1061-1069 (2002).

 

Rapid induction of defense/stress-related proteins in leaves of rice (Oryza sativa) seedlings exposed to ozone is preceded by newly phosphorylated proteins and changes in a 66-kDa ERK-type MAPK: J. Plant Physiol., 159, 361-369 (2002).

 

G. K. Agrawal, R. Rakwal, M. Yonekura, A. Kubo, H. Saji, Proteome analysis of differentially displayed proteins as a tool for investigating ozone stress in rice (Oryza sativa L.) seedlings: Proteiomics, 2, 947-959 (2002). [PubMed]

 

K. Iwasaki, S. Kikukawa, S. Kawamura, Y.Kouzuma, I. Tanaka, and M. Kimura, On the interaction of ribosomal protein L5 with 5S rRNA: Biosci. Biotechnol. Biochem., 66, 103-109 (2002). [PubMed], [PDF]

 

T. Hayashi, M. Tahara, K. Iwasaki, Y. Kouzuma,and M. Kimura, Requirement for C-terminal extension to the RNA binding domain for efficient RNA binding by ribosomal protein L2: Biosci. Biotechnol. Biochem., 66, 682-684 (2002). [PubMed], [PDF]

 

 

2001”N

M. Hajduch, R. Rakwal, G. K. Agrawal, M. Yonekura, and A. Pretova, High-resolution two-dimensional electrophoresis separation of proteins from metal-stressed rice (Oryza sativa L.) leaves: Drastic reductions/fragmentation of ribulose-1,5-bisphosphate carboxylase/oxygenase and induction of stress-related proteins: Electrophoresis., 22, 2824-2831 (2001). [PubMed]

 

Light-dependent induction of OsPR10 in rice (Oryza sativa L.) seedlings by the global stress signaling molecule jasmonic acid and protein phosphatase 2A inhibitors: Plant Sci., 161, 469-479 (2001).

 

Protein phosphatase inhibitors activate defense responses in rice (Oryza sativa) leaves: Physiol. Plantarum., 111, 151-157 (2001).

 

M. Kamakura, T. Fukuda T, M. Fukushima, and M. Yonekura, Storage-dependent degradation of 57-kDa protein in royal jelly: a possible marker for freshness: Biosci. Biotechnol. Biochem., 65,277-284 (2001). [PubMed], [PDF]

]

Y. Kouzuma, K. Tsukigata, H. Inanaga, K. Doi-Kawano, N. Yamasaki, and M. Kimura, Molecular cloning, functional expression of cDNA encoding the cysteine proteinase inhibitor Sca from sunflower seeds: Biosci. Biotechnol. Biochem., 65, 969-972 (2001). [PubMed], [PDF]

 

H. Inanaga, D. Kobayashi, Y. Kouzuma, C. Aoki-Yasunaga, K. Iiyama, and M. Kimura, Protein engineering of novel proteinase inhibitors and their effect on the growth of Spodoptera exigua larvae: Biosci. Biotechnol. Biochem., 65, 2259-2264 (2001). [PubMed], [PDF]

 

I. Sallay, S. Tojo, K. Nomiyama, Y. Kouzuma, M. Kimura, and N. Yamasaki, Calcium ions stabilize a protein structure of hemolytic lectin CEL-III from marine invertebrate Cucumaria echinata: Biosci. Biotechnol. Biochem., 65, 1347-1352 (2001). [PubMed], [PDF]