徳島大学 / 教育研究者総覧 --- 松尾義則

個人のホームページ

https://researchmap.jp/read0184072 (researchmap)

専門分野

○	遺伝学 (Genetics)

研究テーマ

○	適応進化の遺伝学的研究 (キイロショウジョウバエ, 適応進化のメカニズム, 重複遺伝子群, 協調進化, GC含量) (ショウジョウバエを材料に用いて生物の適応進化のメカニズムをDNAなどの分子のレベルで解明する研究をおこなっている．重複遺伝子としてはヒストン遺伝子群，シトクロムP-450遺伝子群を解析し，特に遺伝子ファミリーの協調進化のメカニズムが生物の適応進化にどのように係わっているかに注目して研究している．塩基置換のパターン，コドンの偏った利用，GC含量の変化などを調べてそのメカニズムを明らかにし，生物の適応進化の分子レベルでの解明をめざしている．)

著書・論文

(著書・論文等の業績についてはhttps://researchmap.jp/read0184072 (researchmap)でも御覧頂けます．)

著書:

1.	松尾義則, 三宅端, 西郷薫, 柴忠義, 上田龍 : 13章，In vitro パッケージング/遺伝子ライブラリー/プラークハイブリダイゼーション, 講談社サイエンティフィク, 東京, 1984年9月.

学術論文(審査論文):

1.	N Nagoda, A Fukuda, Y Nakashima and Yoshinori Matsuo : Molecular characterization and evolution of the repeating units of histone genes in Drosophila americana: coexistence of quartet and quintet units in a genome, Insect Molecular Biology, 14, 6, 713-717, 2005. (要約) Quintet and quartet repeating units of the histone genes in Drosophila americana were cloned and characterized. Nucleotide sequence analysis of the units showed that a 3175 bp unit contained the core histone genes but lacked the H1 gene ('quartet unit') while a 5025 bp unit contained all five histone genes ('quintet unit'). Comparative analysis suggested that these repeating units diverged before the separation of D. americana and D. virilis. Multiple forms of H1 genes, differing by 5.8% of amino acids, were found in D. americana. The genomic organization of the histone gene family in D. americana was found to be very similar to that of D. virilis. (キーワード) Amino Acid Sequence / Animals / Base Sequence / Drosophila / Evolution, Molecular / Genes, Insect / Genome, Insect / Histones / Molecular Sequence Data / Multigene Family / Phylogeny / Sequence Homology, Amino Acid / Sequence Homology, Nucleic Acid / Species Specificity (出版サイトへのリンク) ● Publication site (DOI): 10.1111/j.1365-2583.2005.00603.x (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16313572 ● Search Scopus @ Elsevier (PMID): 16313572 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1365-2583.2005.00603.x (DOI: 10.1111/j.1365-2583.2005.00603.x, PubMed: 16313572)
2.	Yoshinori Matsuo, Mitsuru Kakita, Tsunenori Shimizu, Masami Emoto, Mariya Nagai, Miyo Takeguchi, Yuuki Hosono, Nahoko Kume, Toshikatsu Ozawa, Mayuko Ueda and Bhuiyan Islam Md.Shaidul : Divergence and heterogeneity of the histone gene repeating units in the Drosophila melanogaster species subgroup., Genes & Genetic Systems, 78, 5, 383-389, 2003. (要約) The repeating units of the histone gene cluster containing the H1, H2A, H2B and H4 genes were amplified by PCR from the Drosophila melanogaster species subgroup, i.e., D. yakuba, D. erecta, D. sechellia, D. mauritiana, D. teissieri and D. orena. The PCR products were cloned and their nucleotide sequences of about 4.6-4.8kbp were determined to elucidate the mechanism of molecular evolution of the histone gene family. The heterogeneity among the histone gene repeating units was 0.6% and 0.7% for D. yakuba and D. sechellia, respectively, indicating the same level of heterogeneity as in the H3 gene region of D. melanogaster. Divergence of the genes among species even in the most closely related ones was much greater than the heterogeneity among family members, indicating a concerted mode of evolution for the histone gene repeating units. Among the species in the D. melanogaster species subgroup, the histone gene regions as well as 3rd codon position of the coding region showed nearly the same GC contents. These results suggested that the previous conclusion on analysis of the H3 gene regions, the gene family evolution in a concerted fashion, holds true for the whole histone gene repeating unit. (キーワード) codon bias / concerted evolution / Drosophila melanogaster species subgroup / GC contents / histone gene (出版サイトへのリンク) ● Publication site (DOI): 10.1266/ggs.78.383 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 14676429 ● CiNii @ 国立情報学研究所 (CRID): 1390001205472893696 ● Search Scopus @ Elsevier (PMID): 14676429 ● Search Scopus @ Elsevier (DOI): 10.1266/ggs.78.383 (DOI: 10.1266/ggs.78.383, PubMed: 14676429, CiNii: 1390001205472893696)
3.	Mitsuru Kakita, Tsunenori Shimizu, Masami Emoto, Mariya Nagai, Miyo Takeguchi, Yuuki Hosono, Nahoko Kume, Toshikatsu Ozawa, Mayuko Ueda, Islam Md. Shaidul Bhuiyan and Yoshinori Matsuo : Divergence and heterogeneity of the histone gene repeating units in the Drosophila melanogaster species subgroup., Genes & Genetic Systems, 78, 5, 383-389, 2003. (要約) The repeating units of the histone gene cluster containing the H1, H2A, H2B and H4 genes were amplified by PCR from the Drosophila melanogaster species subgroup, i.e., D. yakuba, D. erecta, D. sechellia, D. mauritiana, D. teissieri and D. orena. The PCR products were cloned and their nucleotide sequences of about 4.6-4.8kbp were determined to elucidate the mechanism of molecular evolution of the histone gene family. The heterogeneity among the histone gene repeating units was 0.6% and 0.7% for D. yakuba and D. sechellia, respectively, indicating the same level of heterogeneity as in the H3 gene region of D. melanogaster. Divergence of the genes among species even in the most closely related ones was much greater than the heterogeneity among family members, indicating a concerted mode of evolution for the histone gene repeating units. Among the species in the D. melanogaster species subgroup, the histone gene regions as well as 3rd codon position of the coding region showed nearly the same GC contents. These results suggested that the previous conclusion on analysis of the H3 gene regions, the gene family evolution in a concerted fashion, holds true for the whole histone gene repeating unit. (キーワード) Amino Acid Sequence / Amino Acid Substitution / Animals / Base Composition / Drosophila Proteins / Drosophila melanogaster / Evolution, Molecular / Genetic Variation / Histones / Molecular Sequence Data / Multigene Family / Open Reading Frames / Phylogeny / Sequence Alignment (出版サイトへのリンク) ● Publication site (DOI): 10.1266/ggs.78.383 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 14676429 ● Summary page in Scopus @ Elsevier: 2-s2.0-0346102553 (DOI: 10.1266/ggs.78.383, PubMed: 14676429, Elsevier: Scopus)
4.	Yoshinori Matsuo : Evolution of the GC content of the histone 3 gene in seven Drosophila species., Genes & Genetic Systems, 78, 4, 309-318, 2003. (要約) The molecular evolution of the histone multigene family was studied by cloning and determining the nucleotide sequences of the histone 3 genes in seven Drosophila species, D. takahashii, D. lutescens, D. ficusphila, D. persimilis, D.pseudoobscura, D. americana and D. immigrans. CT repeats, a TATA box and an AGTG motif in the 5' region, and a hairpin loop and purine-rich motifs (CAA(T/G)GAGA) in the 3' region were conserved even in distantly related species. In D. hydei and D.americana, the GC content at the third codon position in the protein coding region was relatively low (49% and 45%), while in D. takahashii and D. lutescens it was relatively high (64% and 65%). The non- significant correlation between the GC contents in the 3' region and at the third codon position as well as the evidence of less constraint in the 3' region suggested that mutational bias may not be the major mechanism responsible for the biased nucleotide change at the third codon position or for codon usage bias. (キーワード) Animals / Base Composition / Cloning, Organism / Codon / DNA / Drosophila / Evolution, Molecular / Histones / Multigene Family / Phylogeny / Species Specificity (出版サイトへのリンク) ● Publication site (DOI): 10.1266/ggs.78.309 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 14532710 ● Search Scopus @ Elsevier (PMID): 14532710 ● Search Scopus @ Elsevier (DOI): 10.1266/ggs.78.309 (DOI: 10.1266/ggs.78.309, PubMed: 14532710)
5.	Kazunobu Tsunemoto and Yoshinori Matsuo : Molecular evolutionary analysis of a histone gene repeating unit from Drosophila simulans., Genes & Genetic Systems, 76, 6, 355-361, 2001. (要約) A repeating unit of the histone gene cluster from Drosophila simulans containing the H1, H2A, H2B and H4 genes (the H3 gene region has already been analyzed) was cloned and analyzed. A nucleotide sequence of about 4.6 kbp was determined to study the nucleotide divergence and molecular evolution of the histone gene cluster. Comparison of the structure and nucleotide sequence with those of Drosophila melanogaster showed that the four histone genes were located at identical positions and in the same directions. The proportion of different nucleotide sites was 6.3% in total. The amino acid sequence of H1 was divergent, with a 5.1% difference. However, no amino acid change has been observed for the other three histone proteins. Analysis of the GC contents and the base substitution patterns in the two lineages, D. melanogaster and D. simulans, with a common ancestor showed the following. 1) A strong negative correlation was found between the GC content and the nucleotide divergence in the whole repeating unit. 2) The mode of molecular evolution previously found for the H3 gene was also observed for the whole repeating unit of histone genes; the nucleotide substitutions were stationary in the 3' and spacer regions, and there was a directional change of the codon usage to the AT-rich codons. 3) No distinct difference in the mode or pattern of molecular evolution was detected for the histone gene repeating unit in the D. melanogaster and D. simulans lineages. These results suggest that selectional pressure for the coding regions of histones, which eliminate A and T, is less effective in the D. melanogaster and D. simulans lineages than in the other GC-rich species. (キーワード) Amino Acid Sequence / Animals / Base Sequence / Cloning, Molecular / Drosophila / Drosophila melanogaster / Evolution, Molecular / Histones / Molecular Sequence Data / Repetitive Sequences, Nucleic Acid / Sequence Analysis, DNA / Tandem Repeat Sequences (出版サイトへのリンク) ● Publication site (DOI): 10.1266/ggs.76.355 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11922104 ● Search Scopus @ Elsevier (PMID): 11922104 ● Search Scopus @ Elsevier (DOI): 10.1266/ggs.76.355 (DOI: 10.1266/ggs.76.355, PubMed: 11922104)
6.	Yoshinori Matsuo : Molecular evolution of the histone 3 multigene family in the Drosophila melanogaster species subgroup, Molecular Phylogenetics and Evolution, 16, 3, 339-343, 2000. (要約) Molecular evolution of the histone multigene family was studied by cloning and sequencing regions of the histone 3 gene in the Drosophila melanogaster species subgroup. Analysis of the nucleotide substitution pattern showed that in the coding region synonymous changes occurred more frequently to A or T in contrast to the GC-rich base composition, while in the 3' region the nucleotide substitutions were most likely in equilibrium. These results suggested that the base composition at the third codon position of the H3 gene, i.e., codon usage, has been changing to A or T in the Drosophila melanogaster species subgroup. (キーワード) Animals / DNA (DNA) / Drosophila / Drosophila melanogaster / 分子進化 (molecular evolution) / Histones / Molecular Sequence Data / Multigene Family / Phylogeny / Point Mutation / Sequence Analysis, DNA (出版サイトへのリンク) ● Publication site (DOI): 10.1006/mpev.2000.0810 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10991787 ● Search Scopus @ Elsevier (PMID): 10991787 ● Search Scopus @ Elsevier (DOI): 10.1006/mpev.2000.0810 (DOI: 10.1006/mpev.2000.0810, PubMed: 10991787)
7.	Yoshinori Matsuo : Evolutionary change of codon usage for the histone gene family in Drosophila melanogaster and Drosophila hydei., Molecular Phylogenetics and Evolution, 15, 2, 283-291, 2000. (要約) The nucleotide divergence in the protein-coding region for replication-dependent and replication-independent histone 3 and 4 genes of Drosophila melanogaster and Drosophila hydei occurred mostly at the synonymous site. Therefore, the pattern of codon usage was analyzed in the two species, considering the genomic codon bias, which is proposed for estimating the genomic composition pressure in the protein-coding regions. The results indicated that the codon usage in the histone gene family could be explained mostly by the genomic codon bias. However, biases for Ala and Arg were commonly observed for the histone 3 and histone 4 gene families, and biases for Ser, Leu, and Glu were observed in a gene-specific manner. This suggests that both genomic codon bias and gene- or codon-specific bias are responsible for the nucleotide differentiation in the protein-coding region of the histone genes. (キーワード) Animals / Codon / Drosophila / 分子進化 (molecular evolution) / Histones / Multigene Family / Species Specificity (出版サイトへのリンク) ● Publication site (DOI): 10.1006/mpev.1999.0749 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10837157 ● Search Scopus @ Elsevier (PMID): 10837157 ● Search Scopus @ Elsevier (DOI): 10.1006/mpev.1999.0749 (DOI: 10.1006/mpev.1999.0749, PubMed: 10837157)
8.	Yoshinori Matsuo, Nobuyuki Inomata and Tsuneyuki Yamazaki : Evolution of the amylase isozymes in the Drosophila melanogaster species subgroup., Biochemical Genetics, 37, 9-10, 289-300, 1999. (要約) The relationship between the net charge of molecules and their mobility on electrophoresis was analyzed for Drosophila alpha-amylases. Most of the differences in electrophoretic mobility, 98.2%, can be explained by the charge state. Therefore five reference amino acid sites, which are informative residues for charge differences among amylase isozymes, were considered for the evolution of the isozymes in Drosophila melanogaster. The amylase isozymes in D. melanogaster can be classified into three groups, I (AMY1, AMY2, and AMY3-A), II (AMY3-B and AMY4), and III (AMY5, AMY6-A, and AMY6-B), based on the differences in the reference sites. The most primitive amylase in D. melanogaster was found to belong to Group I, most likely the AMY2 isozyme. Groups II and III could have been derived from Group I. These results were confirmed by the analysis of 38 amino acid sites with charge differences in Drosophila. (キーワード) Amino Acid Sequence / Amylases / Animals / Drosophila melanogaster / Electrophoresis / Evolution, Molecular / Insect Proteins / Isoenzymes / Molecular Sequence Data / Phylogeny / Species Specificity (出版サイトへのリンク) ● Publication site (DOI): 10.1023/a:1018755109757 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10626037 ● Summary page in Scopus @ Elsevier: 2-s2.0-0033405579 (DOI: 10.1023/a:1018755109757, PubMed: 10626037, Elsevier: Scopus)
9.	Junichi Fujimoto, chie Kanou, Yozo Eguchi and Yoshinori Matsuo : Adaptation to a starch environment and regulation of α-amylase in Drosophila., Biochemical Genetics, 37, 1-2, 53-62, 1999. (要約) The adaptation to glucose and starch foods in six species, D. melanogaster, D. virilis, D. saltans, D. funebris, D. levanonensis and D. americana, was studied by measuring productivity. D. melanogaster and D. virilis adapted more to the starch environment than to the glucose environment, while D. saltans adapted more to the glucose environment than to the starch environment. D. funebris, D. levanonensis, and D. americana did not distinctly adapt to either environment. In addition, the regulation of amylase in the six species was investigated by measuring the levels of amylase activity with glucose and starch food environments. The levels of amylase activity in D. levanonensis and D. saltans were substantially low, indicating that these species cannot utilize starch as a carbon source. The starch-adapted species, D. melanogaster and D. virilis, showed higher levels of amylase activity with the starch environment and higher inducibility. These results suggest that changing the regulation of amylase is important for the adaptation to a starch environment in Drosophila. (キーワード) Adaptation, Physiological / Animals / Drosophila / Enzyme Induction / Glucose / Species Specificity / Starch / alpha-Amylases (出版サイトへのリンク) ● Publication site (DOI): 10.1023/A:1018766017509 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10429832 ● Summary page in Scopus @ Elsevier: 2-s2.0-0033006572 (DOI: 10.1023/A:1018766017509, PubMed: 10429832, Elsevier: Scopus)
10.	Yozo Eguchi and Yoshinori Matsuo : Divergence of the regulation of α-amylase activity in Drosophila melanogaster, Drosophila funebris and Drosophila saltans., Biochemical Genetics, 37, 1-2, 41-52, 1999. (要約) The regulation of amylase activity in three Drosophila species, D. melanogaster, D. funebris and D. saltans, was analyzed by measuring the specific activity levels in four dietary environments, cornmeal, glucose, 5% starch, and 10% starch, at three developmental stages, i.e., the third-instar larval, pupal, and 2-day-old adult stages. The developmental profiles of amylase activity for the three Drosophila species showed that the level of activity was high at the larval and adult stages but substantially low at the pupal stage, suggesting that Drosophila does not utilize starch at the pupal stage. Divergence in the regulation of amylase was observed among the three Drosophila species on the following points. (1) The order of amylase specific activity was D. melanogaster > D. funebris > D. saltans. (2) The response pattern to the dietary environment varied among the species and changed during development. (3) The timing of the switch in the response pattern to the dietary environment during development was before pupation in D. funebris and D. saltans but after pupation in D. melanogaster. The significance of the divergence in the regulation of amylase activity for adaptation to a starch environment in Drosophila is discussed. (キーワード) Animals / Drosophila / Enzyme Induction / Larva / Species Specificity / alpha-Amylases (出版サイトへのリンク) ● Publication site (DOI): 10.1023/A:1018714000671 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10429831 ● Summary page in Scopus @ Elsevier: 2-s2.0-0033006571 (DOI: 10.1023/A:1018714000671, PubMed: 10429831, Elsevier: Scopus)
11.	Yoshinori Matsuo, Yutaka Tsuneoka, Yoshiyuki Ichikawa and Yasuhiro Watanabe : Genetic analysis of the CYP2D6 gene in patients with Parkinson' disease., Metabolism, 47, 1, 94-96, 1998. (要約) To further investigate the association between Parkinson's disease (PD) and genetic polymorphism of the CYP2D6 gene, a mutant allele (CVP2D6J) frequently observed in the Japanese population and related to EM/PM polymorphism (phenotypically, individuals are either extensive metabolizers [EM] or poor metabolizers [PM] of debrisoquine) was investigated. The CYP2D6J gene with a nucleotide substitution from C to T at position 188 (the HphI site in exon 1), which reduces CYP2D6 enzyme activity, was analyzed by polymerase chain reaction (PCR) and by digestion with HphI. No significant relationship was observed between PD patients and controls for this mutation. This suggests that the EM/PM polymorphism of CYP2D6 contributes little to the pathogenesis of PD. To further study the molecular basis for the relationship between PD and CYP2D6, the heterogeneity of CYP2D6 was investigated by combined genotype analysis of the two mutant CYP2D6 genes (ie, CYP2D6J, the HphI site mutation in exon 1, and CYP2D6L, the HhaI site mutation in exon 6). Although some characteristic patterns of the combined genotypes were observed in both PD patients and controls, a strong association between the heterogeneity of the CYP2D6 gene and PD was not shown by combined genotype analysis. (キーワード) Alleles / Cytochrome P-450 CYP2D6 / Debrisoquin / Deoxyribonucleases, Type II Site-Specific / Genotype / Humans / Japan / Mutation / Parkinson Disease / Polymerase Chain Reaction / Polymorphism, Genetic (出版サイトへのリンク) ● Publication site (DOI): 10.1016/S0026-0495(98)90199-8 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9440484 ● Summary page in Scopus @ Elsevier: 2-s2.0-0031951243 (DOI: 10.1016/S0026-0495(98)90199-8, PubMed: 9440484, Elsevier: Scopus)
12.	Yoshinori Matsuo and Tsuneyuki Yamazaki : Genetic factors on the second and third chromosomes responsible for the variation of amylase activity and inducibility in Drosophila melanogaster, Genetical Research, 70, 2, 97-103, 1997. (要約) Using second- or third-chromosome substitution lines of Drosophila melanogaster, the genetic variation of inducibility and amylase specific activities in three media (starch, normal and glucose) were investigated. Genetic factors on both the second and third chromosomes were responsible for the variation in amylase specific activity and inducibility. In glucose medium, the genetic variance of amylase specific activity estimated for the second-chromosome substitution lines was larger than that for the third-chromosome substitution lines; however, for starch medium and inducibility, the variance was larger for the third-chromosome substitution lines. High correlations for the second-chromosome substitution lines and low correlations for the third-chromosome substitution lines were observed for amylase specific activities in different media. These results suggest that the genetic factor(s) responsible for inducibility or amylase activity variation in an induced medium such as starch should be on the third chromosome and those in the non-induced medium such as glucose should be on the second chromosome. The functional roles of the factors on the second and third chromosomes would be the repression and induction of amylase, respectively. (キーワード) Animals / Chromosome Mapping / Chromosomes / Culture Media / Drosophila melanogaster / Enzyme Induction / Glucose / Insect Proteins / Starch / alpha-Amylases (出版サイトへのリンク) ● Publication site (DOI): 10.1017/S0016672397002887 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9449186 ● Search Scopus @ Elsevier (PMID): 9449186 ● Search Scopus @ Elsevier (DOI): 10.1017/S0016672397002887 (DOI: 10.1017/S0016672397002887, PubMed: 9449186)
13.	Yoshinori Matsuo, Aizo Furukawa, Yutaka Tsuneoka, J. Ono and Yoshiyuki Ichikawa : Characterization of the ferredoxin gene transcripts in bovine liver and brain., The International Journal of Biochemistry, 25, 7, 1065-1071, 1997. (要約) 1. To study the expression of a ferredoxin gene in extra-adrenocortical tissues, the amounts and structures of the ferredoxin gene transcripts in bovine liver and brain were studied and compared to those of that in adrenocortex. 2. The sizes and amounts of the ferredoxin mRNAs were analyzed by means of Northern blotting, RNA slot blotting and RT-PCR. 3. The nucleotide sequences were determined for 39 ferredoxin cDNA clones from bovine liver. 4. The results indicated that the sizes of the ferredoxin mRNAs in liver and brain were the same as that in adrenocortex, however, their amounts were approx 1/30th and less than the latter, respectively. 5. Although the multiple forms of ferredoxin cDNA, differing in the poly(A) addition sites, were also found in liver, a minor form of ferredoxin cDNA, produced through alternative promoter usage and splicing, could not be detected in liver. 6. The nucleotide sequences of all hepato-ferredoxin cDNA clones obtained were identical to that of a major type of adreno-ferredoxin. 7. These results showed that the expression level of the ferredoxin gene in different tissues was controlled by the amount of mRNA. (キーワード) Adrenal Cortex / Animals / Base Sequence / Brain / Cattle / DNA / Ferredoxins / Liver / Molecular Sequence Data / Polymerase Chain Reaction / RNA, Messenger (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8365547 ● Search Scopus @ Elsevier (PMID): 8365547 (PubMed: 8365547)
14.	松尾義則, 岩橋和彦 : アルコール関連障害とアルコール依存症アルコール代謝関連酵素ー検査法ー遺伝子構造解析法(Review), 日本臨牀(特別号), 55, 674-680, 1997年.
15.	Yoshinori Matsuo : Molecular evolution of the paired gene in Drosophila,Cloning and characterization of the partial paired gene from Drosophila willistoni, Biochemical Genetics, 34, 11-12, 415-420, 1996. (要約) A partial paired gene of Drosophila willistoni containing the paired box and extended homeo box was amplified by PCR and the nucleotide sequence of 1141 bp was determined. Comparison of the paired genes in D. willistoni and D. melanogaster showed that the proportions of identical nucleotide sites in the coding region and identical amino acid sites were 73.8 and 86.5%, respectively. The amino acid sites in the N-terminal region, the paired box, and the extended homeo box were 88.5, 95.3, and 98.6% identical in the two species. The rates of amino acid substitution for these regions were estimated to be 1.73 x 10(-9), 0.67 x 10(-9), and 0.19 x 10(-9)/site/year, respectively. In contrast, the connecting region between the two boxes has been highly diverged and evolved very rapidly, 18.3 x 10(-9)/site/year, suggesting almost no functional constraint in the connecting region. (キーワード) Amino Acid Sequence / Animals / Base Sequence / Cloning, Molecular / Codon / DNA-Binding Proteins / Drosophila / Drosophila Proteins / Evolution, Molecular / Genes, Homeobox / Genes, Insect / Homeodomain Proteins / Molecular Sequence Data / Restriction Mapping / Sequence Analysis, DNA / Sequence Homology, Amino Acid (出版サイトへのリンク) ● Publication site (DOI): 10.1007/BF00570122 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9126670 ● Summary page in Scopus @ Elsevier: 2-s2.0-0030430280 (DOI: 10.1007/BF00570122, PubMed: 9126670, Elsevier: Scopus)
16.	Yutaka Tsuneoka, Kouji Fukushima, Yoshinori Matsuo, Yoshiyuki Ichikawa and Yasuhiro Watanabe : Genotype analysis of the CYP2C19 gene in the Japanese population, Life Sciences, 59, 20, 1711-1715, 1996. (要約) A polymorphic CYP2C19 gene was analyzed in 233 Japanese subjects, including 63 with Parkinson's disease, 92 with chronic liver diseases (35 chronic hepatitis, 19 liver cirrhosis, 16 hepatocellular carcinoma, 10 primary biliary cirrhosis and 12 autoimmune hepatitis), 14 with lung cancer (squamous cell carcinoma) and 64 healthy subjects to determine the genotype distributions of the CYP2C19 gene and to investigate its involvement in the diseases. Among Japanese healthy subjects 14.1% are predicted to be poor metabolizers (PM) of mephenytoin. The frequencies of the m1 and the m2 mutations of the CYP2C19 gene in the healthy subjects were 21.9% and 11.7%, respectively. Though the number of patients was small, patients with lung cancer (squamous cell carcinoma) are believed to have reduced enzyme activities of CYP2C19. (キーワード) Aryl Hydrocarbon Hydroxylases / Carcinoma, Squamous Cell / Cytochrome P-450 CYP2C19 / Cytochrome P-450 Enzyme System / Genotype / Heterozygote / Homozygote / Humans / Japan / Liver Diseases / Lung Neoplasms / Mixed Function Oxygenases / Parkinson Disease / Polymorphism, Genetic (出版サイトへのリンク) ● Publication site (DOI): 10.1016/S0024-3205(96)00507-3 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8890945 ● Summary page in Scopus @ Elsevier: 2-s2.0-0030580125 (DOI: 10.1016/S0024-3205(96)00507-3, PubMed: 8890945, Elsevier: Scopus)
17.	Kazuhiko Iwahashi, Eisaku Okuyama, Aizo Furukawa, Kazuhiko Nakamura, Ryosuke Miyatake, Yoshinori Matsuo and Yoshiyuki Ichikawa : Novel 2-point linked mutations in the 5'-flanking region of human CYP2C18, Clinica Chimica Acta, 252, 2, 197-199, 1996. (キーワード) Aryl Hydrocarbon Hydroxylases / Base Sequence / Cytochrome P-450 Enzyme System / Humans / Molecular Sequence Data / Point Mutation / Polymerase Chain Reaction / Polymorphism, Single-Stranded Conformational (出版サイトへのリンク) ● Publication site (DOI): 10.1016/0009-8981(96)06345-0 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8853566 ● Summary page in Scopus @ Elsevier: 2-s2.0-0030606689 (DOI: 10.1016/0009-8981(96)06345-0, PubMed: 8853566, Elsevier: Scopus)
18.	Yutaka Tuneoka, Yoshinori Matsuo, Eisaku Okuyama, Yasuhiro Watanabe and Yoshiyuki Ichikawa : Genetic analysis of the cytochrome P-450IIC18(CYP2C18)gene and a novel member of the CYP2C subfamily, FEBS Letters, 384, 3, 281-284, 1996. (要約) The CYP2C18 gene was investigated in order to characterize its molecular basis in the CYP2C subfamily. A mutation of the CYP2C18 gene was identified at the 5'-flanking region of the gene, which could be detected by digestion with DdeI. The allele frequency of the mutant CYP2C18 gene was 21.4%. Genotypes of the polymorphic DdeI site of the CYP2C18 gene were found to be completely consistent with that of the polymorphic CYP2C19 gene (the m1 mutant). The CYP2C18 and CYP2C19 genes were suggested to be linked and located close together on the chromosome. Clones containing the 5'-flanking region of a member of the CYP2C subfamily were obtained from the PCR products from human genomic DNA. The nucleotide sequence of the clone proved to be 90.5% identical to the corresponding region of the CYP2C18 gene. This is very likely to be a novel member of the CYP2C subfamily. (キーワード) Alleles / Aryl Hydrocarbon Hydroxylases / Base Sequence / Cytochrome P-450 Enzyme System / Gene Frequency / Humans / Molecular Sequence Data / Mutation / Polymerase Chain Reaction / Polymorphism, Genetic / Polymorphism, Single-Stranded Conformational / Restriction Mapping / Sequence Analysis, DNA / Sequence Homology, Nucleic Acid (出版サイトへのリンク) ● Publication site (DOI): 10.1016/0014-5793(96)00329-8 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8617372 ● Summary page in Scopus @ Elsevier: 2-s2.0-0029865596 (DOI: 10.1016/0014-5793(96)00329-8, PubMed: 8617372, Elsevier: Scopus)
19.	Yoshinori Matsuo, Kazuhiko Nakamura, Eisaku Okuyama, Yasuhoko Watanabe and Yoshiyuki Ichikawa : Characterstics of Japanese alcoholics with the atypical aldehyde dehydrogenase 2*2. Acomparison of the genotypes of ALDH2,ADH2,ADH3,and cytochrome P-4502E1 between alcoholics and nonalcoholics., Alcohol.Clin.Exp.Res., 20, 52-55, 1996.
20.	Kazuhiko Nakamura, Kazuhiko Iwahashi, Yoshinori Matsuo, Ryosuke Miyatake, Yoshiyuki Ichikawa and Hirohi Suwaki : Characteristics of Japanese alcoholics with the atypical aldehyde dehydrogenase 22.I.Acomparison of the genotypes of ALDH2,ADH2,ADH3,and cytochrome P-4502E1 between alcoholics and nonalcoholics., Alcoholism, Clinical and Experimental Research, 20, 1, 52-55, 1996. (要約) We examined the genotypes of the aldehyde dehydrogenase (ALDH)-2, alcohol dehydrogenase (ADH)-2, ADH3, and P-4502E1 loci of 53 alcoholics and 97 nonalcoholics. All of the subjects fulfilled the DSM-III-R criteria for alcohol dependence. The control group consisted of 97 subjects who were either hospital staff or students. We also compared the frequencies of homozygous ALDH21/1 and heterozygous ALDH21/2 genotypes in alcoholics. Our study revealed differences in the allelic frequencies of the ALDH2, ADH2, and ADH3 loci between alcoholics and nonalcoholics. For alcoholics with both homozygous ALDH21/1 and heterozygous ALDH21/2 genotypes, it was found that ADH2 and ADH3 played important rates. Alcoholics with the heterozygous ALDH21/2 genotype showed a significantly higher frequency of ADH21/1 than ones with the homozygous ALDH21/1 genotype. We assume ADH21 plays an important role in the development of alcoholism in alcoholics with the heterozygous ALDH21/2 genotype. (キーワード) Adult / Alcohol Dehydrogenase / Alcoholism / Aldehyde Dehydrogenase / Alleles / Cytochrome P-450 CYP2E1 / Cytochrome P-450 Enzyme System / Ethnic Groups / Female / Gene Expression Regulation, Enzymologic / Genotype / Humans / Isoenzymes / Japan / Male / Middle Aged / Oxidoreductases, N-Demethylating / Polymorphism, Genetic (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8651462 ● Search Scopus @ Elsevier (PMID): 8651462 (PubMed: 8651462)
21.	Kazuhiko Iwahashi, Yoshinori Matsuo, Hiroshi Suwaki, Kazuhiko Nakamura and Yoshiyuki Ichikawa : CYP2E1 and ALDH2 genotypes and alcohol dependence in Japanese, Alcoholism Clin.Exp.Res., 19, 3, 564-566, 1995. (要約) The genotypes of the CYP2E1 and ALDH2 loci of alcoholic (alcohol dependence) and nonalcoholic (healthy) Japanese were investigated to examine the relationship between the polymorphism of CYP2E1 (C1/C2) and ALDH2 (ALDH21/ALDH22), and the susceptibility to alcoholism. There was no significant difference in C2 gene frequency between alcoholics (0.19) and nonalcoholics (controls) (0.20), whereas there was a significant difference in ALDH2 allele frequency, suggesting that, in Japanese, the C2 genotype of CYP2E1 may have nothing to do with the risk of developing alcohol dependence. However, the ALDH2*1 allele may influence drinking behavior and the development of alcohol dependence. Furthermore, racial interethnic differences in the frequency of the mutated allele of the CYP2E1 gene (C2) were found, like the ALDH2 gene. Japanese healthy controls showed a significantly higher frequency of the C2 allele than did Swedish healthy controls (0.05; reported by Persson et al., FEBS Lett. 319:207-211, 1993). (キーワード) Alcohol Drinking / Alcoholism / Aldehyde Dehydrogenase / Alleles / Cytochrome P-450 CYP2E1 / Cytochrome P-450 Enzyme System / Flushing / Gene Frequency / Genetics, Population / Genotype / Humans / Isoenzymes / Japan / Mitochondria, Liver / Oxidoreductases, N-Demethylating / Point Mutation / Polymorphism, Genetic / Risk Factors (出版サイトへのリンク) ● Publication site (DOI): 10.1111/j.1530-0277.1995.tb01549.x (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 7573775 ● Summary page in Scopus @ Elsevier: 2-s2.0-0029029495 (DOI: 10.1111/j.1530-0277.1995.tb01549.x, PubMed: 7573775, Elsevier: Scopus)
22.	Ryosuke Miyatake, Hirohi Suwaki, Kazuhiko Nakamura, Yoshinori Matsuo and Kazuhiko Iwahashi : CYP2E1 genotypes and serum LAP in Japanese Alcoholics, Life Sciences, 56, 13, 1121-1126, 1995. (要約) The genotypes of the ALDH2 and CYP2E1 loci of Japanese alcoholic patients were determined to investigate the susceptibility to alcoholic liver injury. In alcoholics with a liver-function disorder, a significant association was observed between the genotypes of the CYP2E1 loci and the serum level of a liver-derived enzyme, LAP. However, there was no significant association between the ALDH2 genotypes and liver dysfunction. (キーワード) Alcoholism / Aldehyde Dehydrogenase / Aldehyde Dehydrogenase, Mitochondrial / Alleles / Asian People / Cytochrome P-450 CYP2E1 / Genotype / Humans / Japan / Leucyl Aminopeptidase / Liver / Liver Diseases, Alcoholic (出版サイトへのリンク) ● Publication site (DOI): 10.1016/0024-3205(95)00049-C (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9001446 ● Summary page in Scopus @ Elsevier: 2-s2.0-0028954501 (DOI: 10.1016/0024-3205(95)00049-C, PubMed: 9001446, Elsevier: Scopus)
23.	中村和彦, 州脇寛, 松尾義則, 市川佳幸, 宮武良輔, 岩橋和彦 : アルコール依存症とALDH2,ADH2,ADH3,P-4502E1との関連について, アルコール研究と薬物依存, 30, 33-42, 1995年.
24.	Kazuhiko Iwahashi, Ryosuke Miyatake, Yutaka Tsuneoka, Yoshinori Matsuo, Yoshiyuki Ichikawa, Kiyoshi Hosokawa, Keiko Sato and Toshiyuki Hayabara : A novel cytochrome P-450IID6(CYPIID6) mutant gene associated with multiple system atrophy, Journal of Neurology, Neurosurgery, and Psychiatry, 58, 2, 263-264, 1995. (キーワード) Cytochrome P-450 CYP2D6 / Cytochrome P-450 Enzyme System / Humans / Mixed Function Oxygenases / Mutation / Nervous System Diseases / パーキンソン病 (Parkinson's disease) / Polymorphism, Genetic (出版サイトへのリンク) ● Publication site (DOI): 10.1136/jnnp.58.2.263 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 7876880 ● Summary page in Scopus @ Elsevier: 2-s2.0-0028946508 (DOI: 10.1136/jnnp.58.2.263, PubMed: 7876880, Elsevier: Scopus)
25.	Yoshinori Matsuo, Kazuhiko Iwahashi, Kazuhiko Nakamura, Hiroshi Suwaki and Yoshiyuki Ichikawa : Relationship between genetic polymorphism of CYP2E1 and ALDH2, and possible susceptibility to alcoholism., 29, 639-642, 1994.
26.	Yoshinori Matsuo, shozo yokoyama, Rebecca Ramsbotham and Ruth Yokoyama : Molecular characterization of a class IV human alcohol dehydrogenase gene(ADH7), FEBS Letters, 351, 3, 411-415, 1994.
27.	松尾義則, 宮武良輔, 州脇寛, 木下博之, 飴野清, 井尻厳, 石川安範 : エタノールおよびアルデヒドの代謝速度論的研究ーALDH2およびCYP2E1の遺伝子多型がアルコール代謝に及ぼす影響．, アルコール研究と薬物依存, 29, 190-194, 1994年.
28.	松尾義則, 岩橋和彦, 中村和彦, 州脇寛, 高城健司, 宮武良輔, 早原敏之, 細川清 : 抗てんかん薬PHTの代謝と神経系への副作用．, Neurosciences, 20, 181-184, 1994年.
29.	松尾義則, 中村和彦, 岩橋和彦, 州脇寛, 宮武良輔, 市川佳幸 : 非活性型アルデヒド脱水素酵素ALDH22を有するアルコール依存症の特徴ー他のアルコール代謝酵素との関連についてー．, アルコール研究と薬物依存, 29, 52-58, 1994年.
30.	Yoshinori Matsuo, Kazuhiko Iwahashi, Hiroshi Suwaki, yoshiyuki Ichikawa and Kiyoshi Hosokawa : Correspondence of increased debrisoquine 4 monooxygenase activity with seizure-susceptibility in Mongolian gerbils., Journal of the Neurological Sciences, 121, 1, 18-21, 1994. (要約) Four drug-metabolizing activities in Wistar rat and Mongolian gerbil liver microsomes were investigated to clarify the biochemical basis of convulsions. No significant associations were observed between the susceptibility to the tonic-clonic seizures in Mongolian gerbils and the drug-metabolizing enzymatic activities of p-nitroanisole O-demethylase, aminopyrine demethylase and benzo[a]pyrene-3-monooxygenase. However, a significant association was observed with the debrisoquine 4-monooxygenase (cytochrome P-450db1-linked monooxygenase system) activity, which is known to metabolize exogenous and endogenous parkinsonism-inducing neurotoxins such as MPTP and TIQ, and to activate carcinogens during the detoxication of xenobiotics. The mean activity of debrisoquine 4-monooxygenase in the seizure-sensitive group (male, 380; female, 350 pmol/h/mg protein) remained significantly higher (about 4-5 times) than that in the seizure-resistant group (male, 90; female, 80 pmol/h/mg protein). More Mongolian gerbils were extensive metabolizers of debrisoquine in the seizure-sensitive group than in the seizure-resistant group. These results suggest a possibility that the cytochrome P-450db1-linked monooxygenase system may activate the potential neurotoxins which are associated with tonic-clonic seizures in the Mongolian gerbil. (キーワード) Animals / Cytochrome P-450 CYP2D6 / Cytochrome P-450 Enzyme System / Electroencephalography / Female / Genetic Predisposition to Disease / Gerbillinae / Male / Mixed Function Oxygenases / Rats / Rats, Wistar / Seizures (出版サイトへのリンク) ● Publication site (DOI): 10.1016/0022-510X(94)90150-3 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8133306 ● Summary page in Scopus @ Elsevier: 2-s2.0-0028055123 (DOI: 10.1016/0022-510X(94)90150-3, PubMed: 8133306, Elsevier: Scopus)
31.	Yoshinori Matsuo, Mitsuru Orishiki, Mikio Nishioka and Yoshiyuki Ichikawa : In vitro administration of H2 blockers, cimetidine and ranitidine, reduced the contents of the cytochrome P-450IID(CYP2D) subfamily and their activities in rat liver microsomes., Int.J.Biochem., 26, 751-758, 1994.
32.	Yoshinori Matsuo, Kazuhiko Nakamura, Kazuhiko Iwahashi, Kiyoshi Hosokawa and Hiroshi Suwahashi : Presence of P-450 D subfamily in DA rat and bovine brains., Association Neurosciences., 19, 73-80, 1993.
33.	松尾義則, 常岡豊, 岩橋和彦, 竹内博明, 鈴木二郎, 市川佳幸 : シトクロームP-450ⅡD6の多型とパーキンソン病, 細胞工学, 12, 924-927, 1993年.
34.	Yoshinori Matsuo, Shuhei Tomita, Maki Tsujita, Toshitsugu Yubisui and Yoshiyuki Ichikawa : Identification of a microsomal retinoic acid synthase as a microsomal cytochrome P-450-linked monooxygenase system., The International Journal of Biochemistry, 25, 12, 1775-1784, 1993. (要約) 1. To characterize an enzyme which metabolizes retinal in liver microsomes, several properties of the enzymatic reaction from retinal to retinoic acid were investigated using rabbit liver microsomes. 2. The maximum pH of the reaction in the liver microsomes was 7.6. 3. The Km and Vmax values for all-trans, 9-cis and 13-cis-retinals were determined. 4. The reaction proceeded in the presence of NADPH and molecular oxygen. 5. The incorporation of one atom of molecular oxygen into retinal was confirmed by using oxygen-18, showing that the reaction comprised monooxygenation, not dehydrogenation. 6. The monooxygenase activity was inhibited by carbon monoxide, phenylisocyanide and anti-NADPH-cytochrome P-450 reductase IgG, but not by anti-cytochrome b5 IgG. 7. The enzymatic activity inhibited by carbon monoxide was photoreversibly restored by light of a wavelength of around 450 nm. 8. The retinal-induced spectra of liver microsomes with three isomeric retinals were type I spectra. 9. The microsomal monooxygenase activity induced by phenobarbital or ethanol were more effective than that by 3-methylcholanthrene, clotrimazole or beta-naphthoflavone. 10. These results showed that the monooxygenase reaction from retinal to retinoic acid in liver microsomes is catalyzed by a cytochrome P-450-linked monooxygenase system. (キーワード) Animals / Carbon Monoxide / Cytochrome P-450 Enzyme System / Enzyme Induction / Male / Microsomes, Liver / NADPH-Ferrihemoprotein Reductase / Nitriles / Oxygenases / Rabbits / Retinal Dehydrogenase / Substrate Specificity (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8138015 ● Search Scopus @ Elsevier (PMID): 8138015 (PubMed: 8138015)
35.	Yoshinori Matsuo, Kazuhiko Nakamura, Kazuhiko Iwahashi, Hiroshi Suwaki and Yoshiyuki Ichikawa : Improved methods for genotype determination at the ALDH2 locus using PCR by introducing the MBOII recognition site or conducting secondary PCR., Biochemistry and Molecular Biology International, 31, 3, 439-445, 1993.
36.	Yoshinori Matsuo, K. Taki, Kazuhiko Iwahashi, Hiroshi Suwaki and Kiyoshi Hosokawa : Side effects of phenytoin and the drug metabolism by cytochrome P-450 in DA rats., Association Neurosciences., 19, 173-181, 1993.
37.	松尾義則, 岩橋和彦, 中村和彦, 高城健司, 久郷敏明, 早原敏之, 細川清, 州脇寛 : 抗てんかん薬の代謝と神経系への副作用, 神経化学, 32, 280-281, 1993年.
38.	松尾義則, 中村和彦, 岩橋和彦, 州脇寛, 市川佳幸, 細川清, 市川正浩, 三船和史 : ALDH2のgenotypeの簡便な決定とアルコール依存症の特徴について．, 神経化学, 32, 68-69, 1993年.
39.	松尾義則, 岩橋和彦, 中村和彦, 州脇寛, 折野耕造 : フラッシング反応と飲酒パターンに及ぼすALDH2とCYP2E1の遺伝的多型, アルコール研究と薬物依存, 28, 395-399, 1993年.
40.	Yoshinori Matsuo, Yutaka Tsuneoka, Kazuhiko Iwahashi, H Takeuchi and Yoshiyuki Ichikawa : A novel cytochrome P-450 D6 mutant gene associated with Parkinson's disease., The Journal of Biochemistry, 114, 2, 263-266, 1993.
41.	松尾義則, 岩橋和彦, 細川清, 中村和彦, 早原敏之, 州脇寛 : シトクロームP-450db1における向精神薬代謝と薬物相互作用, 精神神経薬理, 15, 541-545, 1993年.
42.	Yoshinori Matsuo, Aizo Furukawa, Yutaka Tsuneoka, Junichiro Ono and Yoshiyuki Ichikawa : Characterization of the ferredoxin gene transcripts in bovine liver and brain., Int.J.Biochem, 25, 1065-1071, 1993.
43.	Yoshinori Matsuo, K. Taki, Kazuhiko Iwahashi, Yoshiyuki Ichikawa, T. Kugoh, Hiroshi Suwaki and Kiyoshi Hosokawa : Side effects of phenytoin related to the xenobiotics metabolism by cytochrome P-450-linked monooxygenase of liver microsomes in Dark Agouti rats., The Japanese Journal of Psychiatry and Neurology, 47, 2, 295-297, 1993. (キーワード) Animals / Cytochrome P-450 Enzyme System / Female / Inactivation, Metabolic / Male / Microsomes, Liver / Nerve Degeneration / Oxygenases / Phenytoin / Purkinje Cells / Rats / Rats, Inbred Strains / Sex Factors (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8271570 ● Search Scopus @ Elsevier (PMID): 8271570 (PubMed: 8271570)
44.	松尾義則, 岩橋和彦, 中村和彦, 常岡豊, 久郷敏明, 早原敏之, 州脇寛, 細川清 : シトクロームP-450db1の脳内分布, 日本脳研究会, 19, 57-60, 1993年.
45.	Yoshinori Matsuo, K Kurokohchi, H Yoneyama, Mikio Nishioka and Yoshiyuki Ichikawa : Interleukin 2-induction of cytochrome P450-linked monooxygenase systems of rat liver microsomes., Biochemical Pharmacology, 45, 3, 585-592, 1993. (要約) The effects of interleukin 2 (IL-2), a pivotal cytokine for generating an effective immune response, on rat liver microsomal cytochrome P450-linked monooxygenase systems were investigated by measuring the contents of cytochromes b5 and P450, and the activities of various xenobiotic-metabolizing enzymes [debrisoquine and bufuralol monooxygenases (CYP2D), 7-ethoxycoumarin O-deethylase, benzphetamine N-demethylase, aniline hydroxylase and p-nitroanisole N-demethylase]. The enzymatic activities except for p-nitroanisole N-demethylase and aniline hydroxylase were increased approximately to 1.3-fold of those of untreated liver microsomes following intraperitoneal injection of IL-2 (15 U/rat). However, the amount of immunoreactive b5 protein, and the activities of aniline hydroxylase and p-nitroanisole N-demethylase were not changed by injection of IL-2. To elucidate further the mechanism of the induction of CYP2D by IL-2, quantitative analyses of immunoreactive CYP2D protein and its mRNA were conducted by western blot and slot blot hybridization analyses. The results indicated that IL-2 induced an increase in the amounts of immunoreactive CYP2D protein and its mRNA. These enzymatic activities were thus up-regulated at the mRNA level. (キーワード) Animals / Cytochrome P-450 Enzyme System / Cytochromes b5 / Enzyme Induction / Gene Expression / Interleukin-2 / Isoenzymes / Male / Microsomes, Liver / Rats / Rats, Wistar / Xenobiotics (出版サイトへのリンク) ● Publication site (DOI): 10.1016/0006-2952(93)90131-F (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8442758 ● Search Scopus @ Elsevier (PMID): 8442758 ● Search Scopus @ Elsevier (DOI): 10.1016/0006-2952(93)90131-F (DOI: 10.1016/0006-2952(93)90131-F, PubMed: 8442758)
46.	Yoshinori Matsuo, Kazuhiko Iwahashi, Yutaka Tuneoka, Yoshiyuki Ichikawa, Kiyoshi Hosokawa and Hiroshi Suwaki : Histamine and l-methyI-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline are competitive inhibitors of debrisoquine 4-monooxygenase in rat liver., Arch.Toxicol., 67, 514-516, 1993.
47.	Yoshinori Matsuo, K Kurokohchi, H Yoneyama, Mikio Nishioka and Yoshiyuki Ichikawa : Effects of interleukin 1α on the activities and gene expressions of the cytochrome P450 D subfamily., Biochemical Pharmacology, 44, 8, 1669-1674, 1992.
48.	松尾義則, 岩橋和彦, 常岡豊, 中村和彦, 白杵豊之, 久郷敏明, 早原敏之, 州脇寛 : シトクロムP-450db1の脳内活性, 神経化学, 31, 122-123, 1992年.
49.	Yoshinori Matsuo, Yutaka Tsuneoka, R Higuchi and Yoshiyuki Ichikawa : Characterization of the cytochrome P-450 D subfamily in bovine liver:Nucleotide sequences and microheterogeneity., European Journal of Biochemistry, 208, 739-746, 1992.
50.	Yoshinori Matsuo, Kazuhiko Iwahashi and Yoshiyuki Ichikawa : Debrisoquine 4-monooxygenase and bufuralol 1'- monooxygenase activities in bovine and rabbit tissues., Biochemical Pharmacology, 43, 1911-1919, 1992.
51.	Yoshinori Matsuo, Kazuhiko Iwahashi, Yishinori Kawai and Yoshiyuki Ichikawa : Analysis of the transcripts of cytochrome P-450 D gene subfamily in bovine adrenal gland., Histochemistry, 97, 4, 319-322, 1992.
52.	Yoshinori Matsuo, Maki Tsujita, Kazuhiko Mizoguchi and Yoshiyuki Ichikawa : Expression cloning of a sheep adreno-ferredoxin using the polymerase chain reaction., FEBS Letters, 301, 2, 132-136, 1992.
53.	Yoshinori Matsuo, Shozo Yokoyama, Sumathi Rajasekharan and Ruth Yokoyama : Molecular structure of the human alcohol dehydrogenase 3 gene., Jpn.J.Genet., 67, 2, 167-171, 1992.
54.	Yoshinori Matsuo, Chiharu Shimizu, Syuhei Tomita, Akira Miyatake and Yoshiyuki Ichikawa : Determination of the amino acid sequence of adreno-ferredoxin from sheep adrenocortical mitochondria., The International Journal of Biochemistry, 24, 2, 281-288, 1992. (要約) 1. An adreno-ferredoxin was purified from sheep adrenocortical mitochondria. 2. Its amino acid composition and amino acid sequence were determined chemically. 3. It was found to be composed of 127 amino acid residues, including two tyrosyl residues. 4. The amino acid sequences of various ferredoxins of the two iron and two sulfur type were compared with respect to amino acid homology. (キーワード) Adrenal Cortex / Amino Acid Sequence / Amino Acids / Animals / Electrophoresis, Polyacrylamide Gel / Ferredoxins / Mitochondria / Molecular Sequence Data / Sheep (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 1733794 ● Search Scopus @ Elsevier (PMID): 1733794 (PubMed: 1733794)
55.	Yoshinori Matsuo, Syuhei Tomita, Yutaka Tsuneoka, Aizo Furukawa and Yoshiyuki Ichikawa : Molecular cloning and nucleotide sequences of bovine hepato-ferredoxin cDNA:Identical primary structures of hepato-and adreno-ferredoxins., Int.J.Biochem., 24, 289-295, 1992.
56.	Yoshinori Matsuo and Shozo Yokoyama : Cloning and sequencing of a processed pseudogene derived from a human class alcohol dehydrogenase gene., American Journal of Human Genetics, 46, 85-91, 1990.
57.	Yoshinori Matsuo, Ruth Yokoyama and Shozo Yokoyama : The genes for human alchol dehydrogenase β1 and β2 differ by only one nucletide., European Journal of Biochemistry, 183, 317-320, 1989.
58.	Yoshinori Matsuo and Tsuneyuki Yamazaki : Nucleotide variation and divergence in the histone multigene family in Drosophila melanogster., Genetics, 122, 87-97, 1989.
59.	Yoshinori Matsuo and Tsuneyuki Yamazaki : tRNA derived insertion element in histone gene repeating unit of Drosophila melanogaster., Nucleic Acids Research, 17, 225-238, 1989.
60.	Yoshinori Matsuo and Shozo Yokoyama : Molecular structure of the human alcohol dehydrogenase 1 gene., FEBS Letters, 243, 57-60, 1989.
61.	Yoshinori Matsuo, H. C. Langley, E. A. Shrimpton, Tsuneyuki Yamazaki, Naohiko Miyashita and F. C. Aquadro : Naturally occurring variation in the restriction map of the Amy region of Drosophila melanogaster., Genetics, 119, 619-629, 1988.
62.	Yoshinori Matsuo, Wataru Kugimiya, Youichi Kadokami and Kaoru Saigo : Nucleotide sequence of a retrotransposon 297 isolated from Drosophila simulans., Nucleic Acids Research, 14, 9521-9522, 1986.
63.	Yoshinori Matsuo and Tsuneyuki Yamazaki : Genetic analysis of natural populations of Drosophila melanogaster in Japan. .Differential regulation of duplicated amylase loci and degree of dominance of amylase activity in different environments., Jpn.J.Genet., 61, 543-558, 1986.
64.	Yoshinori Matsuo and Tsuneyuki Yamazaki : Genetic analysis of natural populations of Drosophila melanogaster in Japan. .Natural selection on the inducibility,but not on the structural genes,of amylase loci., Genetics, 108, 879-896, 1984.
65.	Kaoru Saigo, Wataru Kugimiya, Yoshinori Matsuo, Satoshi Inoue, Katuji Yoshioka and Shunji Yuki : Identification of the coding sequence for a reverse transcriptase-like enzyme in a transposable genetic element in Drosophila melanogaster., Nature, 312, 5995, 659-661, 1984. (要約) The largest group of transposable elements in Drosophila melanogaster, copia-like elements, share some important structural features with and are intimately related in evolution to vertebrate retroviruses. To further clarify the relationship between retroviruses and copia-like transposable elements, we set out to determine the complete nucleotide sequence of the genome of 17.6, which has long terminal repeats homologous in nucleotide sequence to those of avian leukaemia-sarcoma virus. We report here that 17.6 contains three long open reading frames comparable with gag, pol and env genes in retrovirus. At the level of amino acid sequence, the longest open reading frame of 17.6 includes a coding sequence similar to that for reverse transcriptase, suggesting a role for this enzyme in the life cycle of some Drosophila copia-like elements, analogous to the situation in retrovirus. (キーワード) Animals / Base Sequence / DNA Restriction Enzymes / DNA Transposable Elements / Drosophila melanogaster / RNA, Messenger / RNA-Directed DNA Polymerase / Retroviridae (出版サイトへのリンク) ● Publication site (DOI): 10.1038/312659a0 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 6209583 ● Search Scopus @ Elsevier (PMID): 6209583 ● Search Scopus @ Elsevier (DOI): 10.1038/312659a0 (DOI: 10.1038/312659a0, PubMed: 6209583)
66.	Yoshinori Matsuo and Tsuneyuki Yamazaki : Genetic analysis of natural populations of Drosophila melanogaster in Japan. .Genetic variability of inducing factors of amylase and fitness., Genetics., 108, 223-235, 1984.
67.	Yoshinori Matsuo, Masano Iwano, Kazue Hattori, Kaoru Saigo, Terumi Mukai and Tsuneyuki Yamazaki : Cloning of P-elements from P-and Q-strains in natural populations of Drosophila melanogaster in Japan., Jpn.J.Genet., 59, 403-409, 1984.
68.	松尾義則, 山崎常行 : 二倍体動物(ショウジョウバエ)および半数体植物(蛇苔)における遺伝的変異と進化, 病態生理, 3, 517-520, 1984年.
69.	Yoshinori Matsuo, Tsuneyuki Yamazaki, Yasuhisa Inoue and Yasubumi Matsuo : Genetic analysis of natural populations of Drosophila melanogaster in Japan. .Protein polymorphism,lethal gene,sterility gene,inversion polymorphism and linkage disequilibrium., Jpn.J.Genet., 59, 33-49, 1984.
70.	Tsuneyuki Yamazaki, Sinichi Kusakabe, Hidenori Tachida, Motoshi Ichinose, Hiroshi Yoshimaru, Yoshinori Matsuo and Terumi Mukai : Reexamination of diversifying selection of polymorphic allozymes genes by using population cages in Drosophila melanogaster., Proceedings of the National Academy of Sciences of the United States of America, 80, 18, 5789-5792, 1983.
71.	Yoshinori Matsuo and Tsuneyuki Yamazaki : Genetic variability and selection for inducibility at the amylase locus in Drosophila melanogaster., Jpn.J.Genet., 58, 383-386, 1983.

学術論文(紀要・その他):

1.	松尾義則 : ショウジョウバエホメオボックス遺伝子の進化, 生体の科学, 49, 531-541, 1998年.

総説・解説:

1.	Yoshinori Matsuo : Genomic structure and evolution of the histone gene family in Drosophila, Current Topics in Genetics, 2, 1-14, 2006.

国際会議:

1.	Yoshinori Matsuo : Genetic factors responsible for the variation of amylase activity and inducibility in Drosophila melanogaster, Fukuoka International Symposium of Population Genetics, Fukuoka, Aug. 1998.
2.	Yoshinori Matsuo, Shuhei Tomita, Maki Tujita, Shigetoshi Miura, Toshiji Yubisuki and Yoshiyuki Ichikawa : Identification of a microsomal retinoic acid synthase as a microsomal cytochrome P-450-linked monooxygenase system., 10th International Symposium on Microsomes&Drug Oxidations, Toront,Canada, Jul. 1994.
3.	Yoshinori Matsuo, Maki Tujita, Shuhei Tomita, Shigetoshi Miura and Yoshiyuki Ichikawa : Physicochemical properties of retinal oxidase purified from rabbit hepatic cytosol., International Symposium on Flavins and Flavoproteins, Berlin,Germany, 1994.
4.	Yoshinori Matsuo, Mitsuru Orishiki, Mikio Nishioka, Yutaka Tuneoka and yoshiyuki Ichikawa : Human CYP2D6 gene in chronic liver disease., Basel Liver Week,Falk Symposium No.70, Basel,Swizerland, Oct. 1992.

国内講演発表:

1.	松尾義則, 福田晶子, 中島祐子, 名古田のぞみ : D.americanaにおけるH1遺伝子を欠くヒストン遺伝子繰り返しユニットの解析, 日本遺伝学会第75回大会(東北大学), 2003年9月.
2.	松尾義則 : ショウジョウバエ遺伝子のコドン3番目におけるGC含量の進化とgenome-wideな要因の影響ーヒストン遺伝子の解析を中心として, 日本進化学会第5回大会(九州大学理学部), 2003年8月.
3.	松尾義則, 垣田満, 清水常典, 竹口美代, 細野裕希 : Drosophila melanogaster species subgroupのヒストン遺伝子繰り返しユニットの解析:D.sechellia,D.mauritiana,D.teissieri,D.orena., 日本遺伝学会第74回大会(九州大学), 2002年10月.
4.	垣田満, 清水恒典, 竹口美代, 細野裕希, 松尾義則 : Drosophila melanogaster species subgroupのヒストン遺伝子繰り返しユニットの解析:D.sechellia,D.mauritiana,D.teissieri,D.orena., 第74回日本遺伝学会, 2002年10月.
5.	松尾義則, 江本雅美, 永井マリヤ, 植田真由子, 小澤利勝 : Drosophila melanogaster species subgroup のヒストン遺伝子繰り返しユニットの解析:D.yakuba,D.erecta., 第73回日本遺伝学会(お茶の水女子大学), 2001年10月.
6.	江本雅美, 永井マリア, 植田真由子, 小沢利且, 松尾義則 : Drosophila melanogaster species subgroupのヒストン遺伝子繰り返しユニットの解析:D.yakuba, D.erecta., 第73回日本遺伝学会, 2001年10月.
7.	松尾義則 : ショウジョウバエの種間にみられるコドン使用頻度の違いと種に対するゲノム圧の解析, 第72回日本遺伝学会(京都大学), 2000年11月.
8.	松尾義則 : ショウジョウバエの種間にみられるコドン使用頻度の違いと種に対するゲノム圧の解析, 第72回日本遺伝学会, 2000年11月.
9.	松尾義則, 常本和伸 : Drosophila simulans のヒストン遺伝子繰り返しユニットの分子進化学的解析, 第2回日本進化学会(東京大学), 2000年10月.
10.	常本和伸, 松尾義則 : Drosophila simulansのヒストン遺伝子繰り返しユニットの分子進化学的解析, 第2回日本進化学会, 2000年10月.
11.	松尾義則 : ショウジョウバエのヒストン3遺伝子ファミリーのクローニングと分子進化, 第71回日本遺伝学会, 1999年9月.
12.	松尾義則 : ショウジョウバエのヒストン3遺伝子ファミリーのクローニングと分子進化, 第71回日本遺伝学会(広島大学理学部), 1999年9月.
13.	松尾義則, 堂本和伸, 小澤利且, 植田真由子, 江本雅美, 永井マリヤ : キイロショウジョウバエ(Drosophila melanogaster)の近縁種におけるヒストン遺伝子の解析, 日本動物学会中国四国支部大会(高知女子大), 1999年5月.
14.	松尾義則 : Drosophila melanogaster species subgroup におけるヒストン遺伝子群の分子進化, 日本動物学会中国四国支部大会(高知女子大), 1999年5月.
15.	常本和伸, 小沢利且, 植田真由子, 江本雅美, 永井マリア, 松尾義則 : キイロショウジョウバエ(Drosophila melanogaster)の近縁種におけるヒストン遺伝子の解析, 日本動物学会中国四国支部大会, 1999年5月.
16.	松尾義則 : Drosophila melanogaster species subgroupにおけるヒストン遺伝子群の分子進化, 日本動物学会中国四国支部大会, 1999年5月.
17.	松尾義則 : キイロショウジョウバエ近縁8種におけるヒストン3遺伝子ファミリーの分子進化, 70回日本遺伝学会, 1998年9月.
18.	松尾義則 : キイロショウジョウバエ近縁八種におけるヒストン3遺伝子ファミリーの分子進化, 第70回日本遺伝学会(北海道大学理学部), 1998年9月.
19.	Yoshinori Matsuo and Tsuneyuki Yamazaki : Genetic factors responsible for the variation of amylase activity and inducibility in Drosophila melanogaster, Fukuoka International Symposium of Population Genetics(Kyushu University), Aug. 1998.
20.	松尾義則 : D.melanogasterおよびD.hydeiにおけるヒストン3とヒストン4遺伝子ファミリーのコドン使用と分子進化, 第69回日本遺伝学会(横浜市立大学), 1997年11月.
21.	松尾義則, 森嵜一好 : キイロショウジョウバエにおける薬物代謝型P450遺伝子のmRNA の発現解析, 日本動物学会中国四国支部大会(愛媛大学理学部), 1997年5月.
22.	松尾義則, 江口陽三 : ショウジョウバエの発生段階におけるアミラーゼ遺伝子発現調節の解析, 日本動物学会中国四国支部大会(愛媛大学理学部), 1997年5月.
23.	松尾義則 : ショウジョウバエにおけるアミラーゼ酵素活性とスターチ環境への適応, 日本動物学会中国四国支部大会(愛媛大学理学部), 1997年5月.
24.	松尾義則, 山崎常行 : キイロショウジョウバエのアミラーゼ酵素活性と誘発能に影響を及ぼす第2および第3染色体上の遺伝因子の効果, 第68回日本遺伝学会(椙山女学園大), 1996年10月.
25.	松尾義則 : 生物の適応進化と遺伝的変異, 日本動物学会中国·四国地区大会47回大会シンポジウム(徳島大学), 1995年5月.
26.	松尾義則 : 生物の進化と分子の進化, 徳島生物学会第94回特別講演(徳島大学), 1994年11月.
27.	松尾義則, 宮武良輔, 岩橋和彦, 州脇寛, 中村和彦, 市川佳幸, 折野耕造 : アルコール依存症におけるCYP2E1の遺伝子型と血中LAP, 日本アルコール医学会, 1994年.
28.	松尾義則, 常岡豊, 市川佳幸, 中村道子, 鈴木二郎 : 薬物代謝酵素シトクロームP-450ⅡD6およびP-450ⅡC 18遺伝子の多型とパーキンソン病との関連性, 行動遺伝学会研究会第2回大会, 1994年.
29.	松尾義則, 常岡豊, 鈴木二郎, 市川佳幸 : シトクロムP-450ⅡC遺伝子の多型と疾患, 日本分子生物学会第16回大会, 1993年12月.
30.	松尾義則, 常岡豊, 大井勝代, 岩橋和彦, 市川佳幸 : ヒトのシトクロムP-450ⅡC遺伝子変異の検索, 日本分子生物学会第16回大会, 1993年12月.
31.	Yoshinori Matsuo, Yutaka Tuneoka and Yoshiyuki Itikawa : Association of the cytochrome P-450 D6(CYP2D6) gene polymorphism with some diseases., 日本薬理学会66回大会, Mar. 1993.
32.	Yoshinori Matsuo, Maki Tujita, syuhei Tomita, Shigetoshi Miura and Yoshiyuki Ichikawa : Physicochemical properties of retinal oxidase (cytosolic retinoic acid synthase)from rabbit hepatic cytosol., Eleventh International Symposium on Flavins and Flavoproteins, 1993.
33.	松尾義則, 常岡豊, 折敷満, 西岡幹夫, 鈴木二郎, 市川佳幸 : 肝疾患における薬物代謝酵素シトクロムP-450ⅡC遺伝子の解析, 日本肝臓学会東部会28回大会, 1993年.
34.	松尾義則, 折敷満, 市川佳幸, 西岡幹夫 : H2ブロッカー投与によるラット肝ミクロゾーム中シトクロムP-450ⅡD活性抑制について, 日本肝臓学会西部会28回大会, 1993年.
35.	松尾義則, 常岡豊, 岩橋和彦, 市川佳幸, 竹内博明 : 遺伝子病としてのパーキンソン病ーシトクロームP-450ⅡD6(CYP2D6)変異遺伝子の解析, 日本神経学会総会15回大会, 1993年.
36.	Yoshinori Matsuo, kazuhiko Iwaki, kazuhiko Nakamura, Toshiaki Kugo, Toshiyuki Hayabara, Kiyoshi Hosokawa and Hiroshi Suwaki : The relationship between the side effects of phenytoin and cytochrome P-450db 1 in DA rats., 生物学的精神医学会15回大会, 1993.
37.	松尾義則, 常岡豊, 岩橋和彦, 竹内博明, 市川佳幸 : パーキンソン病発症に関わる新しいシトクロームP-450ⅡD6(CYP2D6)変異遺伝子の解析, 日本分子生物学会第15回大会, 1992年12月.
38.	松尾義則, 常岡豊, 川口仁, 前田昌純, 市川佳幸 : 肺癌患者のシトクロムP-450ⅡD6(CYP2D6)遺伝子の解析, 日本肺癌学会33回大会, 1992年11月.
39.	松尾義則, 富田修平, 辻田麻紀, 指吸俊次, 井柳堯, 市川佳幸 : ミクロソーム型レチノイン酸合成酵素としてのシトクロムP-450依存性モノオキシゲナーゼ, 日本生化学学会第65回大会, 1992年10月.
40.	松尾義則, 常岡豊, 梅岡秀一, 岩橋和彦, 折敷満, 西岡幹夫, 市川佳幸 : 肝臓，肺の悪性疾患およびパーキンソン病患者のシトクロムP-450ⅡD6(CYP2D6)遺伝子の解析, 日本生化学会第65回大会, 1992年10月.
41.	松尾義則, 辻田麻紀, 溝口和博, 市川佳幸 : ヒツジのアドレノフェレドキシンの発現クローニング, 日本生化学会第65回大会, 1992年10月.
42.	松尾義則, 常岡豊, 市川佳幸 : 肝細胞癌患者ゲノムDNAのシトクロムP-450ⅡD6(CYP2D6)遺伝子の分子生物学的解析, 日本肝臓学会総会28回大会, 1992年6月.
43.	松尾義則, 折敷満, 西岡幹夫, 常岡豊, 市川佳幸 : 慢性肝疾患患者におけるゲノムDNAのシトクロームP-450ⅡD6(CYP2D6)遺伝子の解析, 日本肝臓学会西部会27回大会, 1992年.
44.	松尾義則, 中村和彦, 岩橋和彦, 常岡豊, 早原敏之, 州脇寛, 細川清 : シトクロームP ー450db1の脳内活性, 日本脳研究会19回大会, 1992年.
45.	松尾義則, 岩崎和彦, 常岡豊, 中村和彦, 早原敏之, 州脇寛, 細川清 : シトクロームP-450db1の脳内活性, 日本神経化学学会35回大会, 1992年.
46.	松尾義則, 高城健司, 岩橋和彦, 州脇寛, 細川清 : Phenytoinによる小脳失調の発生機序に関する酵素化学的考察, てんかん学会26回大会, 1992年.
47.	Yoshinori Matsuo, Kazuhiko Nakamura, Toshiaki kugo, Toshiyuki Hayabara, Kiyoshi Hosokawa and Hiroshi Suwaki : Cytochrome P-450db1 activity in bovine brain., 生物学的精神医学会14回大会, 1992.
48.	松尾義則, 富田修平, 市川佳幸 : レチノイドの酸化反応に関与するミクロソーム型シトクロムP-450モノオキシゲナーゼ系, レチノイドシンポジウム第3回, 1991年12月.
49.	松尾義則, 常岡豊, 樋口亮太, 市川佳幸 : ウシ肝臓ミクロソームのシトクロムP-450ⅡDcDNAの構造解析とパーキンソン病への臨床応用, 日本分子生物学会第14回大会, 1991年12月.
50.	松尾義則, 古川愛造, 常岡豊, 小野純一郎, 溝口和博, 市川佳幸 : ウシの肝臓フェレドキシンcDNAの解析, 日本分子生物学会第14回大会, 1991年12月.
51.	松尾義則, 岩橋和彦, 河合良訓, 市川佳幸 : シトクロームPー450ⅡDsubfamilyの解析:debrisoquine 4-hydroxylase及びbufuralol 1'-hydroxylaseの組織分布, 日本生化学会第64回大会, 1991年10月.
52.	松尾義則, 三浦成敏, 宮武明, 市川佳幸 : アドレノドキシンC-末端アミノ酸残基の多様性, 日本生化学学会第64回大会, 1991年10月.
53.	松尾義則, 常岡豊, 市川佳幸 : ウシ肝臓ミクロソームのシトクロムP-450ⅡDcDNAの構造解析とmicroheterogeneity, 日本生化学会第64回大会, 1991年10月.
54.	松尾義則, 米山弘人, 黒河内和貴, 西岡幹夫, 市川佳幸 : インターロイキン1-αのラット肝ミクロソームの薬物代謝活性に及ぼす影響について, 日本生化学会第64回大会, 1991年10月.
55.	松尾義則, 市川佳幸 : ウシの肝臓で発現しているフェレドキシン(ヘパトレドキシン)cDNAのクローニング, 日本生化学会第63回大会, 1990年9月.
56.	Yoshinori Matsuo and Shozo Yokoyama : Molecular structure of human alcohol dehydrogenase genes., 日本生化学会第62回大会, Nov. 1989.
57.	松尾義則, 山崎常行, 松木理恵, 仁田坂英二, 岩野政雄, 広瀬泰子 : キイロショウジョウバエの熱ショック耐性の遺伝的変異．, 日本遺伝学会57回大会, 1985年10月.
58.	松尾義則, 山崎常行 : キイロショウジョウバエのヒストン遺伝子の遺伝的変異と進化 Ⅰ.染色体内の遺伝的変異．, 日本遺伝学会57回大会, 1985年10月.
59.	松尾義則, 釘宮渉, 服部和枝, 門上洋一, 西郷薫, 山崎常行 : キイロショウジョウバエとその近縁種におけるCopia様因子297の解析．, 日本遺伝学会56回大会, 1984年11月.
60.	松尾義則, 井上郁子, 山崎常行 : キイロショウジョウバエのアミラーゼ誘発能に対する自然選択．, 日本動物学会九州地区大会37回大会, 1984年5月.
61.	松尾義則, 釘宮渉, 服部和枝, 門上洋一, 西郷薫, 山崎常行 : 塩基特異的挿入を行うDrosophilaのCopia様因子297の分子進化．, 日本動物学会九州地区大会37回大会, 1984年5月.
62.	松尾義則, 山崎常行 : キイロショウジョウバエにおけるアミラーゼ重複遺伝子座の遺伝的調節．, 日本遺伝学会55回大会(於東北大学), 1983年10月.
63.	松尾義則, 山崎常行 : キイロショウジョウバエの適応度におよぼすアミラーゼ遺伝子調節因子の影響．, 日本遺伝学会54回大会(於九州大学), 1982年10月.
64.	松尾義則, 山崎常行 : アミラーゼおよびアルコール脱水素酵素遺伝子座におけるアイソザイム多型と適応度．, 日本遺伝学会54回大会(於九州大学), 1982年10月.
65.	松尾義則, 山崎常行 : キイロショウジョウバエの適応度におよぼすアミラーゼ活性の影響．, 日本動物学会九州地区大会35回大会(於琉球大学), 1982年5月.
66.	松尾義則, 山崎常行 : 日本のキイロショウジョウバエの自然集団における連鎖不平衡．, 日本動物学会九州地区大会34回大会(於佐賀大学), 1981年5月.

科学研究費補助金 (KAKEN Grants Database @ NII.ac.jp)

ショウジョウバエのヒストン遺伝子における協調進化のメカニズムの解明 (研究課題/領域番号: 15570186 )
超分子ヘモグロビンの形成と適応進化 (研究課題/領域番号: 14540629 )
ショウジョウバエ近縁種のシトクロムP-450遺伝子群の構造解析と発現調節の研究 (研究課題/領域番号: 07640821 )
薬物代謝型シトクロムP-450の変異遺伝子と疾患 (研究課題/領域番号: 06770087 )
適応進化のメカニズムに関する分子集団遺伝学的研究 (研究課題/領域番号: 06304002 )
シトクロムP-450IIDの発現と疾患 (研究課題/領域番号: 05770082 )
レチノイン酸合成酵素であるシトクロムP-450モノオキシゲナーゼ系の特性 (研究課題/領域番号: 05670147 )
レチノイン酸合成酵素であるシトクロムP-450モノオキシゲナーゼ系の研究 (研究課題/領域番号: 04670164 )
シトクロムPー450の酵素化学的性質とシトクロムPー450の臓器特性 (研究課題/領域番号: 02217209 )
シトクロムP-450の酵素化学的並びに臓器特性 (研究課題/領域番号: 01635505 )
ミトコンドリア型シトクロムPー450依存性オキシゲナ-ゼ系の組織特性と生理機能 (研究課題/領域番号: 01570160 )
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名誉教授 : 松尾義則

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科学研究費補助金 (KAKEN Grants Database @ NII.ac.jp)

名誉教授 : 松尾 義則

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科学研究費補助金 (KAKEN Grants Database @ NII.ac.jp)

名誉教授 : 松尾義則