論文

2024年

Hu, Z., Shirane, K., Aramaki, K., Leproux, P., Inoko, A., Kano, H.*, Matsushima, A.*,: Intracellular vacuoles induced by hypo-osmotic stress visualized by coherent anti-Stokes Raman scattering (CARS) spectroscopic imaging, Applied Physics Express, in press, DOI:35848/1882-0786/ad63f0

Kamikawa, T., Hashimoto, A., Yamazaki, N., Adachi, J., Matsushima, A., Kikuchi, K., Hori, Y. Bioisostere-conjugated fluorescent probes for live-cell protein imaging without non-specific organelle accumulation. Chem. Sci. 15, 8097–8105 (2024). DOI:10.1039/d3sc06957e

Qiu, Y., Sajidah, E.S., Kondo, S., Narimatsu, S., andira, M.I., Higashiguchi, Y., Nishide, G., Taoka, A., Hazawa, M., Inaba, Y., Inoue, H., Matsushima, A., Okada, Y, Nakada, M., Ando, T., Lim, K.*, and Wong, R.W.*: An efficient method for isolating and purifying nuclei from mice brain for single-molecule imaging using high-speed atomic force microscopy. Cells 13, 279 (2024). DOI:3390/cells13030279

2023年

Matsushima, A.*: Novel estrogen receptor inhibitory mechanism for halogen-containing endocrine-disrupting chemicals discovered by computer simulation. J. Synth. Org. Chem., Jpn. 81, 1103–1109 (2023). DOI:10.5059/yukigoseikyokaishi.81.1103

Suyama, K., Kesamaru, H., Okubo, T., Kasatani, K., Tomohara, K., Matsushima, A., Nose, T.*: High cytotoxicity of a degraded TBBPA, dibromobisphenol A, through apoptotic and necrosis pathways. Heliyon, 9(1), e130003 (2023). DOI:10.1016/j.heliyon.2023.e13003

2022年

Choi, J., Oh, T. G., Jung, H., Park, K.-Y., Shin, H., Jo, T., Kang, D., Chanda, D., Hong, S., Kim, J., Hwang, H., Ji, M., Jung, M., Hoji, S., Matsushima, A., Kim, P., Mun, J., Paik, M., Cho, S., Lee, I., Whitcomb, D.C., Greer, P., Blobner, B., Goodarzi, M.O., Pandol, S.J., Rotter, J.I., North American Pancreatitis Study 2 (NAPS2) Consortium, Fan, W., Bapat, S.P., Zheng, Y., Liddle, C., Yu, R.T., Atkins, A.R., Downes, M., Yoshihara, E., Evans, R.M., Suh, J.M. (2022). Estrogen-Related Receptor γ maintains pancreatic acinar cell function and identity by regulating cellular metabolism. Gastroenterology, 163(1) 239-256 (2022). http://doi.org/10.1053/j.gastro.2022.04.013

Matsushima, A.*, Teramoto, T., and Kakuta, Y.* :Crystal structure of endocrine-disrupting chemical bisphenol A and estrogen-related receptor γ. Journal of Biochemistry, 171(1), 23–25. (2022). http://doi.org/10.1093/jb/mvab145

2021年

Iwamoto, M., Masuya, T., Hosose, M., Tagawa, K., Ishibash, T., Yoshihara, E., Michael Downes, M., Evans, R.M., and Matsushima, A.* :Bisphenol A derivatives act as novel coactivator binding inhibitors for estrogen receptor β. Journal of Biological Chemistry, 297(5), 101173 (2021). DOI:10.1016/j.jbc.2021.101173

Asai, D., Inoue, N., Sugiyama, M., Fujita, T., Matsuyama, Y., Liu, X., Matsushima, A., Nose, T., Costa, T., Shimohigashi, Y. Direct evidence of edge-to-face CH/π interaction for PAR-1 thrombin receptor activation. Bioorganic & Medicinal Chemistry, 51, 116498. (2021). DOI:10.1016/j.bmc.2021.116498

2020年

Suyama, K., Kaneko, S., Kesamaru, H., Liu, X., Matsushima, A., Kakuta, Y., Okubo, T., Kasatani, K., and Nose, T.* : Evaluation of the influence of halogenation on the binding of bisphenol A to the estrogen-related receptor γ. Chemical Research in Toxicology, 33, 889–902, (2020). DOI:10.1021/acs.chemrestox.9b00379

Ohga, H.*, Akase, F., Sakanoue, R., Matsushima, A., Ohta, K., & Matsuyama, M. : Alanine scanning and characterization of core peptides in Scombridae fish family for construction of Kiss1 super analog. General and Comp. Endocrinology, 288, 113356 (2020). DOI:10.1016/j.ygcen.2019.113356

2019年

Masuya, T., Iwamoto, M., Liu, X., and Matsushima, A.* : Discovery of novel oestrogen receptor α agonists and antagonists by screening a revisited privileged structure moiety for nuclear receptors. Scientific Reports, 9, 9954 (2019). DOI:10.1038/s41598-019-46272-y

Matsushima, A.*, Sese, J., & Koyanagi, K. O. : Biosynthetic short neuropeptides: A rational theory based on experimental results for the missing pain‐relief opioid endomorphin precursor gene. ChemBioChem, 20, 2054-2058 (2019). DOI:10.1002/cbic.201900317.

Liu, X., Sakai, H., Nishigori, M., Suyama, K., Nawaji, T., Ikeda, S., Nishigouchi, M., Okada, H., Matsushima, A., Nose T., Shimohigashi, M., Shimohigashi, Y.*: Receptor-binding affinities of bisphenol A and its next-generation analogs for human nuclear receptors. Toxicology and Applied Pharmacology, 377, 114610 (2019). DOI:10.1016/j.taap.2019.114610.

2018年

Matsushima, A.*:A Novel Action of Endocrine-Disrupting Chemicals on Wildlife; DDT and Its Derivatives Have Remained in the Environment. Int. J. Mol. Sci. 19(5) , e1337 (2018).

2017年

Matsushima, A., Nishimura, H., Matsuyama, Y., Liu, X., and Shimohigashi. Y.: Docking simulation to elucidate the labeled cysteine residue of the nociception receptor ORL1 using a Cys(Npys)-containing peptide ligand. Peptide Science 2016, 87-88 (2017).

2016年

Matsushima, A.,* Nishimura, H., Matsuyama, Y., Liu, X., Tommaso Costa, T., and Shimohigashi, Y.: Specific affinity-labeling of the nociceptin ORL1 receptor using a thiol-activated Cys(Npys)-containing peptide ligands. Biopolymers Peptide Science, 106, 406 – 469 (2016) DOI:10.1002/bip.22792.
Liu, X., Fujiyama, A., Matsushima, A., Shimohigashi, M., and Shimohigashi, Y.*: α-Helix-peptides composing the human nuclear receptor ERRγ competitively provoke inhibition of functional homomeric dimerization. Biopolymers Peptide Science, 106, 547 – 554 (2016) DOI: 10.1002/bip.22795.

2015年

Matsushima, A.,* Nishimura, H., Matsuyama, Y., Liu, X., Tommaso Costa, T., and Shimohigashi, Y.: Specific affinity-labeling of the nociceptin ORL1 receptor using a thiol-activated Cys(Npys)-containing peptide ligands. Biopolymers Peptide Science, in press, DOI:10.1002/bip.22792.

2014年

Liu, X., Matsushima, A., Shimohigashi, M., and Shimohigashi, Y.*: A characteristic back support structure in the bisphenol A-binding pocket in the human nuclear receptor ERRγ. PLoS ONE, 9, e101252 (2014).  DOI:10.1371/journal.pone.0101252.

Li, J., Nishimura, H., Matsushima, A., and Shimohigashi, Y.*: N-methylthioacetylation of RYYRIK-NH2 with enhanced specific binding affinity and high antagonist activity for nociceptin ORL1 receptor, Bioorganic & Medicinal Chemistry, 22, 5721-5726 (2014).

Inamine, S., Nishimura, N., Li, J., Isozaki, K., Matsushima, A., Costa , T., and Shimohigashi, Y.*: Tritium-Labelled isovaleryl-RYYRIK-NH2 as potential antagonist probe for ORL1 nociceptin receptor. Bioorganic & Medicinal Chemistry, 22, 5902-5909 (2014).  DOI:10.1016/j.bmc.2014.09.018.

2013年

Matsushima, A.,* Ryan, K., Shimohigashi, Y., Meinertzhagen, Ian A.: An endocrine disruptor, bisphenol A, affects development in the protochordate Ciona intestinalis: Hatching rates and swimming behavior alter in a dose-dependent manner. Environ. Pollut. 173, 257-263 (2013).

2012年

Liu, X., Matsushima, A., Nakamura, M., Costa, T., Nose, T., and Shimohigashi, Y.*: Fine spatial assembly for construction of the phenol-binding pocket to capture bisphenol A in the human nuclear receptor estrogen-related receptor γ. Journal of Biochemistry, 151(4), 403-415 (2012). DOI: 10.1093/jb/mvs008.

2011年

Arase, S., Ishii, K., Igarashi, K., Aisaki, K., Yoshio, Y., Matsushima, A., Shimohigashi ,Y., Arima, K., Kanno, J., Sugimura, Y. *: Endocrine disrupter bisphenol A increases in situ estrogen production in the mouse urogenital sinus. Biology of Reproduction, 84, 734-742 (2011). DOI: 10.1095/biolreprod.110.087502.

Hassaneen, E., El-Din Sallam, A., Abo-Ghalia, A., Moriyama, Y., Karpova, S.G., Abdelsalam, S., Matsushima, A., Shimohigashi, Y., and Tomioka, K. *: Pigment-dispersing factor affects nocturnal activity rhythms, photic entrainment and the free-running period of the circadian clock in the cricket Gryllus bimaculatus, Journal of Biological Rhythms, 26, 3-13 (2011). DOI:10.1177/0748730410388746.

2010年

Liu, X., Matsushima, A., Okada, H., and Shimohigashi, Y.*: Distinction of the binding modes for human nuclear receptor ERRγ between bisphenol A and 4-hydroxytamoxifen. J. Biochem., 148, 247-254 (2010). DOI:10.1093/jb/mvq056.

Matsushima, A., Liu, X., Okada, H., Shimohigashi, M., and Shimohigashi, Y.*: Bisphenol AF is a full agonist for the estrogen receptor ERα, but a highly specific antagonist for ERβ. Environmental Health Perspectives, 118, 1267-1272 (2010). DOI:10.1289/ehp.0901819.

2009年

Isozaki, K., Li, J., Okada, K., Nishimura H., Matsushima, A., Nose, T., Costa, T., Shimohigashi, Y.*: Spare interactions of highly potent [Arg14,Lys15]nociceptin for cooperative induction of ORL1 receptor activation. Bioorganic & Medicinal Chemistry, 17, 7904–7908 (2009). DOI: 10.1016/j.bmc.2009.10.026.

Takeda, Y., Liu, X., Sumiyoshi, M., Matsushima, A., Shimohigashi, M., and Shimohigashi, Y.*: Placenta expressing the greatest quantity of bisphenol A receptor ERRγ among the human reproductive tissues: predominant expression of type-1 ERRγ isoform. Journal of Biochemistry, 146, 113-122 (2009). DOI:10.1093/jb/mvp049.

Nishimura, H., Li, J., Isozaki, K., Okada, K., Matsushima, A., Nose, T., Costa, T., and Shimohigashi, Y.*: Discriminatory synergistic effect of Trp-substitutions in superagonist [(Arg/Lys)14, (Arg/Lys)15]nociceptin on ORL1 receptor binding and activation. Bioorganic & Medicinal Chemistry, 17, 5683–5687 (2009). DOI:10.1016/j.bmc.2009.06.015.

2008年

Yokotani, S., Nose, T., Horiuchi, Y., Matsushima, A., and Shimohigashi, Y.*: Radar chart deviation analysis of prion protein amino acid composition defines characteristic structural abnormalities of the N-terminal octapeptide tandem repeat. Protein and Peptide Letters, 15, 949-955 (2008). DOI:10.2174/092986608785849182.

Matsushima, A., Teramoto, T., Okada, H., Liu, X., Tokunaga, T., Kakuta, Y., and Shimohigashi, Y.*: ERRγ tethers strongly bisphenol A and 4-α-cumylphenol in an induced-fit manner. Biochemical and Biophysical Research Communications, 373, 408-413 (2008). DOI:10.1016/j.bbrc.2008.06.050

Matsushima, A., Shimohigashi, Y.*: A strategy to explore the target receptor of endocrine disruptors: Estrogen-related receptor γ (ERRγ) as a genuine acceptor of bisphenol A. Alternatives to Animal Testing and Experimentation.AATEX journal, 14, special issue, 495-497 (2008).

Li, J. Isozaki, K., Okada, K., Matsushima, A., Nose, T., Costa, T., and Shimohigashi, Y.*: Designed modification of partial agonist of ORL1 nociceptin receptor for conversion into highly potent antagonist. Bioorganic & Medicinal Chemistry, 16, 2635-2664 (2008). DOI: 10.1016/j.bmc.2007.11.043.

Okada, H., Tokunaga, T., Lui, X., Takayanagi, S., Matsushima, A., and Shimohigashi, Y.*: Direct evidence revealing structural elements essential for the high binding ability of bisphenol A to human estrogen-related receptor γ (ERRγ). Environmental Health Perspectives, 116, 32-38 (2008). DOI: 10.1289/ehp.1058.

2007年

Liu, X., Matsushima, A., Okada, H., Tokunaga, T., Isozaki, K., and Shimohigashi, Y.*: Receptor binding characteristics of the endocrine disruptor bisphenol A: Chief and corroborative hydrogen bonds of bisphenol A phenol-hydroxyl group with Arg316 and Glu275 residues in the human nuclear receptor of estrogen-related receptor γ (ERRγ). FEBS Journal, 274, 6340-6351 (2007). DOI:10.1111/j.1742-4658.2007.06152.x.

Matsushima, A., Kakuta, Y., Teramoto, T., Koshiba, T., Liu, X., Okada, H., Tokunaga, T., Kawabata, S., Kimura, M., and Shimohigashi, Y.*: Structural evidence for endocrine disruptor bisphenol A binding to human nuclear receptor ERRγ. Journal of Biochemistry, 142, 517-524 (2007). DOI: 10.1093/jb/mvm158.

Matsushima, A., Takano, K., Yoshida, T., Takeda, Y., Yokotani, S., Shimohigashi, Y., and Shimohigashi, M.*: Double-labelled in situ hybridization reveals the lack of co-localization of mRNAs for the circadian neuropeptide PDF and FMRFamide in brains of the flies Musca domestica and Drosophila melanogaster. Journal of Biochemistry, 141, 867-877 (2007). DOI: 10.1093/jb/mvm094.

2006年

Takayanagi, S., Tokunaga, T., Liu, X., Okada, H., Matsushima, A., and Shimohigashi, Y.*: Endocrine disruptor bisphenol A strongly binds to human estrogen-related receptor γ (ERRγ) with high constitutive activity. Toxicology Letters, 195, 95-105 (2006). DOI: 10.1016/j.toxlet.2006.08.012.

Honda, T., Matsushima, A., Sumida K., Chuman Y., Sakaguchi K., Onoue H., Meinertzhagen I.A., Shimohigashi Y., and Shimohigashi, M.*: Structural isoforms of the circadian neuropeptide PDF expressed in the optic lobes of the cricket Gryllus bimaculatus: Immunocytochemical evidence from specific monoclonal antibodies. Journal of Comparative Neurology, 499, 404-421 (2006). DOI:10.1002/cne.21112

2004年

Takeda, Y., Chuman, Y., Shirasu, N., Sato, S., Matsushima, A., Kaneki, A., Tominaga, Y., Shimohigashi, Y., and Shimohigashi, M.*:Structural analysis and identification of novel isoforms of the circadian clock gene period in the silk moth Bombyx mori. Zoological Science, 21, 903-915 (2004). DOI:10.2108/zsj.21.903.

Matsushima, A., Sato, S., Chuman, Y., Takeda, Y., Yokotani, S., Nose, T., Tominaga, Y., Shimohigashi, M., and Shimohigashi, Y.*: cDNA cloning of the housefly pigment-dispersing factor (PDF) precursor protein and its peptide comparison among the insect circadian neuropeptides. Journal of Peptide Science., 10, 82-91 (2004). DOI:10.1002/psc.511.

2003年

Matsushima, A., Yokotani, S., Sato, S., Kaneki, A., Takeda, Y., Chuman, Y., Ozaki, M., Asai, D., Nose, T., Onoue, H., Ito, Y., Tominaga, Y., Shimohigashi, Y., and Shimohigashi, M.*: Molecular cloning and circadian expression profile of  insect neuropeptide PDF in black blowfly, Phormia regina. Letters in Peptide Science, 10, 419-430 (2003). DOI: 10.1007/BF02442573

2002年

Soto, S., Chuman, Y., Matsushima, A., Tominaga, K., Shimohigashi, Y., and Shimohigashi, M.*: A circadian neuropeptide, pigment-dispersing factor-PDF, in the last-summer cicada Meimuna opalifera: cDNA cloning and immunocytochemistry. Zoological Science, 19, 821-828 (2002). DOI:10.2108/zsj.19.821.

Chuman, Y., Matsushima, A., Sato, S., Tomioka, K., Tominaga, Y., Meinertzhagen, I.A., Shimohigashi, Y., and Shimohigashi, M.*: cDNA cloning and nuclear localization of the circadian neuropeptide designated as pigment-dispersing factor PDF in the cricket Gryllus bimaculatus. Journal of Biochemistry, 131, 895-903 (2002). DOI:10.1093/oxfordjournals.jbchem.a003180

2000年

Fujita, T., Nose, T., Matsushima, A., Okada, K., Asai, D., Yamauchi, Y., Shirasu, N., Honda, T., Shigehiro, D., and Shimohigashi, Y.*: Synthesis of complete set of L-difluorophenylalanines, L-(F2)Phe, as molecular explorers for the CH/π  interaction between peptide ligand and receptor. Tetrahedron Letters, 41, 923-927 (2000). DOI: 10.1016/S0040-4039(99)02191-7

Matsushima, A., Fujita, T., Okada, K., Shirasu, N., Nose, T., and Shimohigashi, Y.*: Exploration of the role of phenylalanine in the thrombin receptor tethered-ligand peptide by substitution with a series of trifluorophenylalanines. Bulletin of the Chemical Society of Japan, 73, 2531-2538 (2000). DOI: 10.1246/bcsj.73.2531.

Matsushima, A., Fujita, T., Okada, K., Nose, T., and Shimohigashi, Y.*: Edge-to-face CH/π interaction between ligand Phe-phenyl and receptor aromatic group in thrombin receptor activation. Journal of Biochemistry, 128, 225-232 (2000). DOI: 10.1093/oxfordjournals.jbchem.a022745.


プロシーディング(査読 有)

2022年

Hosose, M., Shirane, K., Ishibashi, T., Ito, K., Tagawa, K., and Matsushima, A.: Neuropeptide gene expression in the fetal mouse brain exposed to an endocrine-disrupting chemical, Peptide Science 2021, 99-100 (2022).

2021年

Tagawa, K., Suyama, K., Kesamaru, H., Masuya, T., Nose, T., Matsushima, A. Design and synthesis of a universal coactivator peptide binding to the estrogen receptor and Nurr1. Peptide Science 2020, 123-124 (2021).

2019年

Masuya, T., Tada, Y., Lui, A., and Matsushima, A.: Evaluation of the binding ability of an orphan nuclear receptor nurr1 to synthetic peptides. Peptide Science 2018, 113 (2019).

2018年

Sugiyama, M., Fujita, T., Liu, X., Yutaka, M., Matsushima, A., Shimohigashi, M., and Shimohigashi, Y.: Phe 27139 of Thronbin Receptor PAR-1 is a specific target of Phe-2-phenl group of its tethered ligand. Peptide Science 2017, 94-95 (2018).

Liu, X., Nakagawa, H., Sugiyama, M., Matsushima, A., Shimohigashi, M., and Shimohigashi, Y.: Homodimer function of human nuclear receptor ERRa evidenced using a-helix peptides in the dimer interface. Peptide Science 2017, 190-191 (2018).

Liu, X., Shimohigashi, M., Sugiyama, M., Matsushima, A., and Shimohigashi, Y.: Mutual co-work between nuclear receptor ERa and ERRg requires their homodimerization. Peptide Science 2017, 198-199 (2018).

2017年

Matsushima, A., Nishimura, H., Matsuyama, Y., Liu, X., and Shimohigashi. Y.: Docking simulation to elucidate the labeled cysteine residue of the nociception receptor ORL1 using a Cys(Npys)-containing peptide ligand. Peptide Science 2016, 87-88 (2017).

2016年

Matsushima, A., Nishiimura, H., Liu, X., Takesue, Y., Matsuyama, Y., and Shimohigashi. Y.: Comprehensive structural analysis of the nociceptin ORL1 receptor by means of virtual and experimental Ala-scanning combinated methods. Peptide Science 2015, 149-150 (2016).

Takesue, Y., Nishimura, H., Liu, X., Matsushima, A., and Shimohigashi. Y.: Functional role of the Phe-Phe stacking microswitch in the ORL1 nociceptin receptor activation. Peptide Science 2015, 147-148 (2016).

Tokumaru, A., Matsuo, A., Umeno, S., Matsuyama, Y., Nakamura, M., Sumiyoshi, M., Liu, X., Matsushima, A., Shimohigashi, M., and Shimohigashi, Y.: Expression analysis of neuropeptide PDF mRNA in the hypoactive and hyperactive fruit flies Drosophila melanogaster. Peptide Science 2015, 317-318 (2016).

Matsuyama, Y., Nishimura H., Liu, X., Matsushima, A., and Shimohigashi. Y.: Comparative analysis of the ligand binding domain secondary structures of human nuclear receptors. Peptide Science 2015, 337-338 (2016).

Sugiyama, M., Motomatsu, Y., Matsuyama, Y., Kajiyama, S., Kameda, T., Saito, T., Uchimura, E., Liu, X., Matsushima, A., and Shimohigashi. Y.: SCN Circadian rhythm signal transduction neuropeptides evoke hypoactive phenotype differently in male and female mice. Peptide Science 2015, 53-54 (2016).

Motomatsu, Y., Nishimura, H., Matsusyama, Y., Liu, X., Matsushima, A., and Shimohigashi. Y.: ORL1 Nociceptin receptor response of opioid peptides derived from proenkephalin precursor protein. Peptide Science 2015, 181-182 (2016).

Sakito, S., Liu, X., Fujiyama, A., Matsushima, A., and Shimohigashi. Y.: Do the estrogen receptors function as a homodimer? experimental validation of homodimerization by inhibitory peptides. Peptide Science 2015, 335-336 (2016).

2015年

Liu, X., Matsushima, A., and Shimohigashi. Y.: A novel method identify and quantify the coactivator proteins that couple with human nuclear receptor: the use of interacting interface a-helix peptide for quantitative inhibition. Peptide Science 2014, 347-348 (2015).

Takesue, Y., Nishimura, H., Liu, X., Matsushima, A., and Shimohigashi. Y.: GPCR functional role of Phe-269 and Phe-221 in the molecular switching of ORL1 nociceptin receptor activation. Peptide Science 2014, 203-204 (2015).

Umeno, S., Matsuo, A., Matsuyama, Y., Nakamura, M., Koga, K., Liu, X., Matsushima, A., Shimohigashi, M., and Shimohigashi, Y.: Bisphenol A-induced substantial peak decay of Drosophila circadian neuropeptide hugin mRNA expression. Peptide Science 2014, 41-42 (2015).

Matsuyama, Y., Nishimura H., Liu, X., Matsushima, A., and Shimohigashi. Y.: Structural and molecular evolutionary analysis of the ligand-binding domain of forty-eight human nuclear receptors. Peptide Science 2014, 347-348 (2015).

Sugiyama, M., Kajiyama, S., Saito, T., Uchimura, E., Motomatsu, Y., Matsuo, A., Matsushima, A., and Shimohigashi. Y.: Alternative polyadenylation analyses of neuropeptide genes in bisphenol A-exposed hypoactive mouse brain. Peptide Science 2014, 345-346 (2015).

Motomatsu, Y., Nishimura, H., Matsumoto, Y., Kuramitsu, Y., Inamine, S., Matsushima, A., and Shimohigashi. Y.: Receptor selectivity and specificity of a series of opioid peptides latent in the proenkephalin precursor protein. Peptide Science 2014, 205-206 (2015).

Nishimura, H., Li, J., Isozaki, K., Takesue, Y., Liu, X., Shimohigashi, M., Inamine, S., Matsushima, A., and Shimohigashi. Y.: The molecular switching of ORL1 nociceptin receptor in activation/inactivation. Peptide Science 2014, 201-202 (2015).

Matsushima, A., Koyanagi, O.K., Nishimura, H., Inamine, S., Motomatsu, Y., and Shimohigashi. Y.: An in silico genomic search of endomorphin-like opioid peptides. Peptide Science 2014, 281-282 (2015).

2014年

Nishimura, H., Li, J., Isozaki, K., Abe, Y., Inamine, S., Matsushima, A., Costa, T., and Shimohigashi, Y.: Functionally Essential Amino Acid Residues in ORL1 Nociceptin Receptor for Ligand-stimulated Receptor Activation. Peptide Science 2013, 333-334 (2014).

Matsuo, A., Umeno, S., Matsuyama, Y., Nakamura, M., Takeda, Y., Sumiyoshi, M., Liu, X., Matsushima, A., Shimohigashi, M., and Shimohigashi, Y.: Bisphenol A-induced Epigenetic Mutations in Circadian Pacemaker Neuropeptide mRNAs of Hyperactive Drosophila Fruit Flies. Peptide Science 2013, 457-458 (2014).

Matsushima, A., Nishimura, H., Inamine, S., and Shimohigashi, Y.: Multiple and Simultaneous Cys→Ala Mutations of ORL1 Nociceptin Receptor to Identify the Affinity Binding site of Cys(Npys)-Elongated RYYRIK Peptide Antagonist. Peptide Science 2013, 413-414 (2014).

Liu, X., Nishimura, H., Fujiyama, A., Matsushima, A., and Shimohigashi, Y.: Constitutive α-Helix-peptides Required for Functional Dimerization of Estrogen-related Receptor γ (ERRγ). Peptide Science 2013, 429-430 (2014).

Sugiyama, M., Matsuo, A., Saito, T., Uchimura, E., Liu, X., Matsushima, A., and Shimohigashi, Y.: Expression and Mutation Analyses of Brain Neuropeptide Genes of Rndocrine-disrupting Bisphenol A-exposed Hypoactive Mouse. Peptide Science 2013, 453-454 (2014).

Kuramitsu, Y., Nishimura, H., Nakamura, R., Suyama, K., Matsushima, A., Nose, T., and Shimohigashi, Y.: Structure-activity Studies on the Halogenated Phe-containing Neuropeptide Substance P Analogs. Peptide Science 2013, 319-320 (2014).

Umeno, S., Matsuo, A., Matsuyama, Y., Nakamura, M., Takeda, Y., Sumiyoshi, M., Liu, X., Matsushima, A., Shimohigashi, M., and Shimohigashi, Y.: Influence Analysis of the Circadian Evening Pacemaker Neuropeptide hugg Gene in the Bisphenol A-exposed Fruit Fly Drosophila Brain. Peptide Science 2013, 455-456 (2014).

Motomatsu, Y., Nishimura, H., Matsumoto, Y., Inamine, S., Kuramitsu, Y., Matsushima, A., and Shimohigashi, Y.: Specific Role of Phe Residues in Opioid Peptide Met-enkephalin- Arg-Phe in Binding to All Three Opioid Receptors. Peptide Science 2013, 317-318 (2014).

Matsuyama, Y., Liu, X., Nishimura, H., Matsushima, A., and Shimohigashi, Y.: Three-dimensional Docking Modeling to Human Nuclear Receptors for Exploration of Bisphenol-A Targeting Receptors. Peptide Science 2013,459-460 (2014).

2013年

Nishio, K., Nishimura, H., Suyama, K., Matsushima, A., Nose, T., and Shimohigashi, Y.: Halogenated Phe-containing endomorphin-2 analogs with mixed agonist and antagonist activities. Peptide Science 2012, 25-26 (2013).

Matsuo, A., Nakamura, M., Takeda, Y., Matsuyama, Y., Sumiyoshi, M., Liu, X., Matsushima, A. Shimohigashi, M., and Shimohigashi, Y.: The impact of bisphenol A-feeding on the Drosophila neuropeptide PDF mRNA structure. Science 2012, 75-76 (2013).

Nishimura, H., Inamine, S., Li, J. Matsushima, A., and Shimohigashi, Y.: Exploration of pharmacological chaperone for rescue of misfolded and/or unfolded ORL1 nociceptin receptor proteins. Peptide Science 2012, 115-118 (2013).

Matsushima, A., Nishimura, H., Inamine, S., and Shimohigashi, Y.: Identification of affinity binding site of Cys(Npys)-elongated RYYRIK peptide antagonist by means of Cys®Ala mutated ORL1 nociceptin receptors. Peptide Science 2012, 207-208 (2013).

Kuramitsu, Y., Nishimura, H., Nakamura, R., Suyama, K., Matsushima, A., Nose, T., and Shimohigashi, Y.: High-precision binding assay procedure of tachykinin receptor NK-1 for highly potent Substance P analogs. Peptide Science 2012, 213-214 (2013).

Inamine, S., Nishimura, H., Li, J., Matsushima, A. Costa, T., and Shimohigashi, Y.: Two different binding modes of peptide library-based antagonist acyl-RYYRIK amide in the orl1 nociceptin receptor. Peptide Science 2012, 229-230 (2013).

Matsuyama, Y., Liu, X., Nishimura, H., Matsushima, A., Nose, T., and  Shimohigashi, Y. : Bisphenol-binding pocket of constitutively active nuclear receptor CAR: Docking modeling for close-packing. Peptide Science 2012, 401-402 (2013).

2012年

Inamine, S., Nishimura, H., Li, J., Matsushima, A., Nose, T., Costa, T., and Shimohigashi Y.: Receptor Binding Characteristics of Tritium-labeled Pure antagonist Peptide for Hyperalgesic nociceptin ORL1 receptor. Peptide Science 2011, 183-184 (2012).

Matsushima, A., Nishimura, H., Inamine, S., Uemura, S., and Shimohigashi Y.: Affinity labeling of the ORL1 nociceptin receptor by Cys(Npys)-elongated RYYRIK peptide antagonist. Peptide Science 2011, 179-180 (2012).

Nishio, K., Hishimura, H., Suyama, K., Abe, Y., Matsushima, A., Nose, T., and Shimohigashi Y.: Effects ofthe halogenation of Phe-phenyl group of two consecutive residues in endomorphin-2 on the interaction with the m–opioid receptors. Peptide Science 2011, 171-172 (2012).

Nishimura, H., Li, J., Isozaki, K., Abe, Y., Inamine, S., Matsushima, A., Nose, T.,  Costa, T., and Shimohigashi Y.: Structural essentials of hyperalgesic nococeptin ORL1 receptor for ligand binding and receptor activation. Peptide Science 2011, 33-34 (2012).

2011年

Sato, K., Horiuchi, Y., Matsushima, A., and Shimohigashi, Y.: QCM-analyses of the intermolecular interaction between prion protein N-terminal domains having increased number of octapeptide repeat. Peptide Science 2010, 128 (2011).

Inamine, S., Li, J., Nishimura, , Matsushima, A., Nose, T., Costa, T. and Shimohigashi, Y.: Exploration of the binding site of ORL1 nociceptin receptor antagonist. Peptide Science 2010, 167 (2011).

Nishimura, H., Li, J., Inokuchi, N., Koikawa, S., Matsushima, A., Nose, T., Costa, T. and Shimohigashi, Y.: The Trp residue of opioid receptor TM5 present at the cell membrane interface is a molecular anchor for full activation. Peptide Science 2010 , 175 (2011).

2010年

Liu, X., Matsushima, A., Okada, H., and Shimohigashi, Y.: Functional role of the C-terminal Helix 12 peptide in the receptor activation mechanism of estrogen-related receptor g (ERRg). Peptide Science 2009, 435–436 (2010).

Sato, K., Horiuchi, Y., Matsushima, A., and shimohigashi, Y.: The preparation and purification of prion protein N-terminal domain with fluctuations in the number of octapeptide repeat. Peptide Science 2009, 433–434 (2010).

Li, J., Isozaki, K., Matsushima, A., Nose, T., Costa, T., and Shimoohigashi, Y.: Structure-function analysis of nociceptin receptor ORL1 by the site-directed mutagenesis. Peptide Science 2009, 219–220 (2010).

Shimohigashi, M., Itoh, T.Q., Honda, T., Saito, M., Koga, K., Takahashi, K., Matsushima, A., Ueda, R., Tanimura T., Shimohigashi, Y., and Matsumoto A.: The role of the peptide PAP coded in pdf Peptide Science 2009, 217–218 (2010).

Horiuchi, Y., Matsushima, A., and Shimohigashi, Y.: The direct measure of intermolecular interaction of prion protein N-terminal octapeptide repeats by the quarts crystal microbalance (QCM). Peptide Science 2009, 207–208 (2010).

Kawanaka, C., Matsushima, A., Takeda, Shimohigashi, Y., M., and Shimohigashi, Y.: Identification of circadian neuropeptide PDF mRNA isoforms in the housefly Musca domestica. Peptide Science 2009, 145–146 (2010).

Nishimura, H., Li, J., Inokuchi, N., Koikawa, A., Matsuhima, A., Nose, T., Costa, T., and Shimohigashi, Y.: The functional role of Trp present at the cell membrane interface in the opioid receptor activation. Peptide Science 2009, 23–24 (2010).

2009年

Takeda, Y., Liu, X., Sumiyoshi, M., Matsushima, A., Shimohigashi, Y. and Shimohigashi, M.: Bisphenol A-specific nuclear receptor ERRg: structure-function analysis of the two novel isoforms lacking vital peptide fragment in the ligand binding domain. Peptide Science 2008, 517-518 (2009).

Ikeda, S., Matsushim, A., and Shimohigashi, Y.: ERa/ERRa nuclear receptor heterodimer directly linked by a flag peptide. Peptide Science 2008, 511-512 (2009).

Horiuchi, Y., Hattori, E., Yokotani, S., Matsushima, A., and Shimohigashi, Y.: Molecular recognition of prion protein via its N-terminal octapeptide repeat Structure. Peptide Science 2008, 513-516 (2009).

Matsushima, A., Okada, H., Liu, X., Tokunaga, T., Teramoto, T., Kakuta, Y., Shimohigashi, Y.: Induced-fit type ligand binding guided by free-rotatory Leu residue present in the 7th a-helix peptide in the estrogen-related receptor g (ERRg). Peptide Science 2008, 521-522 (2009).

2008年

Hattori, E., Yokotani, S., Horiuchi, Y., Matsushima, A., and Shimohigashi, Y.: The effect of amino acid substitution on oligomerization of octapeptide repeat structure in prion protein. Peptide Science 2007, 239-242 (2008).

Matsushima, A., Koretsune, Y., Kaneki, A., Isozaki, K., Shimohigashi, M., and Shimohigashi, Y.: Structural requirement of housefly FMRFamide peptides in its receptor activation. Peptide Science 2007,313-314 (2008).

Takeda, Y., Koga, K., Matsushima, A., Shimohigashi, M., and Shimohigashi, Y.: The output mechanism of circadian pacemaker neuropeptide PDF in the regulation of bimodal locomotor distribution. Peptide Science 2007, 65-68 (2008).

Li, J. Isozaki, K., Matsushima, A., Nose, T., Costa, T., and Shimohigashi, Y.: Optimization of the N-terminal group of Ac-RYYRIK-NH2 as ORL1 receptor antagonist. Peptide Science 2007, 257-260 (2008).

2007年

Tokunaga, T., Liu, X., Okada, H., Matsushima, A., Nose, T., Shimohigashi, M., and Shimohigashi, Y.: Conformation change of a-helix peptide for sensing of deactivation of nuclear peceptor: Immunoassay using polyclonal antibody specific for the C-terminal a-helix 12 of estrogen-related receptor g (ERRg). Peptide Science 2006, 176, (2007).

Kaneki, A., Yoshida, T., Isozaki, K., Matsushima A., Shimohigashi, M., and Shimohigashi, Y.: Molecular cloning and in situ hybridization of circadian neuropeptide PDF receptor in the fruit fly Drosophila melanogaster. Peptide Science 2006, 263, (2007).

Koga, K., Yakayama, Y., Hiramura, D., Takeda, Y., kaneki, A., Matsushima, A., Shimohigashi, Y., and Shimoshigashi, M.: Immunological confirmation of circadian-related neuropeptide PDF-isoform peptide in the cricket Gryllus bimaculatus. Peptide Science 2006, 262, (2007).

Takeda, Y., Sumiyuki, M., Koga, K., Ito, M., Matsushima, A., Shimohigashi, Y., and Shimohigashi, M.: Multiple post-transcriptional regulations in circadian pacemaker neuropeptide pdf gene. Peptide Science 2006, 260, (2007).

Matsushima, A. Koretsune, Y., Kaneki, A. Isozaki, K., Shimohigashi, M., and Shimohigashi, Y.: Structure-activity studies of FMRFamide-related peptides in activating the specific receptor present in the housefly Musca domestica. Peptide Science 2006, 174, (2007).

2006年

Honda, T., Matsushima, A., Hiramura, D., Sumida, K., Takeda, Y., Sato, S., Meinertzhagen I.A., Shimohigashi, Y., and Shimohigashi, M.: Immunological evidences of circadian neuropeptide PDF isoform present at the lamina outer cells and varicose network in the optic lobes of the cricket Gryllus bimaculatus. Peptide Science 2005, 181-184 (2006).

Koga, K., Sato S., Horiuchi Y., Matsushima, A., and Shimohigashi, Y.: Design and synthesis of a-helix peptide binding to prion protein N-terminal octarepeat domain. Peptide Science 2005, 209-210 (2006)

Okada, H., Tokunaga, T., Shirasu N., Matsushima, A., Nose, T., and Shimohigashi Y.: a-helix peptides for bio-panning in the phage display method to obtain the antibodies specific for conformation-change nuclear receptors. Peptide Science 2005, 291-294 (2006).

Yokotani, S., Honda, T., Kawano, M., Matsuhima A., and Shimohigashi, Y.: Monoclonal antibody sensing assay for conformation change induced by metal binding to prion protein N-terminal octarepear domain. Peptide Science 2005, 455-456 (2006).,

Sato, S., Jonathan C., Corrins, Takeda, Y., Kaneki, A., Matsushima, A., Shimohigashi, Y., and Shimohigashi, M.: Identification of novel isoforms of the circadian neuropeptide PDF in the silk moth Bombyx mori and their expression in brain. Peptide Science 2005, 99-100 (2006).

Matsushima, A., Horiuchi, Y., Yokotani, S., Kawano, M., and Shimohigashi, Y.: Specific dimerization of prion protein N-terminal domain. Peptide Science 2005, 457-458 (2006).

2005年

Shimohigasi M., Honda T., Matsushima A., Sumida K., Meinertzhagen, I.A., Shimohigasi Y., and Tominaga Y.: Immunocytochemical studies on the circadian neuropeptide PDF in the Cricket Gryllus bimaculatus. Peptide Science 2004, 339-342 (2005).

Sumida, K., Honda, T., Matsushima, A., Tominaga, Y., Shimohigashi, Y., and Shimohigashi, M.: Immunocytochemical identification of mature peptide formation for the circadian neuromodulator PDF in the housefly Musca domestica. Peptide Science 2004, 347-350 (2005).

Kawano, M., Honda, T., Horiuchi, Y., Yokotani, S., Matsushima, A., Nose, T., and Shimohigashi, Y.: Conformation change-senseing assay using monoclonal antibody for N-terminal octapeptide repreat region of prion protein. Peptide Science 2004, 355-356 (2005).

Takeda, Y., Shirasu, N., Sato, S., Matsushima, A., Chuman, Y., Tominaga, Y., Shimohigashi, M., and Shimohigashi, M.: Triplicate alternative splicings that produce multiple variants of the PERIOD protein in the silk moth Bombyx mori by deletion/Insertion of peptides. Peptide Science 2004, 203-206 (2005).

Liu, X., Matsushima, A., Shirasu, N., Tominaga, Y., Shimohigashi, M., Shimohigashi, Y., and Nose, T.: Structural characteristics of Drosophila estrogen-related receptor ligand binding domain to capture the peptide and non-peptide ligands. Peptide Science 2004, 303-304 (2005).

Sato, S., Sumida, K., Hiramura, D., Matsushima, A., Tominaga, Y., Shimohigashi, Y., and Shimohigashi, M. : cDNA cloning and mRNA expression of the circadian neuropeptide PDF in the silk moth Bombyx mori. Peptide Science 2004, 197-200 (2005).

Yokotani, S., Matsushima, A., Nose, T., Morishita, F., and Shimohigashi Y.: Bioactive conformation of a D-Trp-containing cardioexcitatory tripeptide isolated from the sea hare Peptide Science 2004, 539-540 (2005).

Horiuchi, Y., Kawano, M., Yokotani, S., Honda, T., Matsushima, A., Nose, T., and Shimohigashi, Y.: Structural characteristics of the N-Terminal octapeptide repeat region of Prion protein in self-polymerization. Peptide Science 2004, 317-318 (2005).

Matsushima A., Yokotani, S., Koretsune, Y., Meinertzhagen, I.A., Tominaga, Y., Shimohigashi, M., and Shimohigashi, Y.: FMRFamide-related peptides in the nervous system of the housefly Musca domestica: cDNA cloning and actions on clam heart contraction. Peptide Science 2004, 157-160 (2005).

2004年

Kawano, M., Horiuchi, Y., Honda, T., Yokotani, S., Matushima, A, Nose, T., and Shimohigashi, Y.: Structural requirements of the N-terminal octapeptide repeat of prion protein. Peptide Science 2003,375-378 (2004).

Kaneki, A., Matsushima, A., Takeda, Y., Yokotani, S., Ozaki, M., Shimohigashi, M., and Shimohigashi, Y.: Primary structure analysis of circadian neuropeptide PDF and precursors in insect cicadae and flies. Peptide Science 2003, 483-486 (2004).

Yokotani, S., Matsushima, A., Nose, T., Shimohigashi, Y., and Morishita, F.: Effect of the Phe-Phenyl H-F subsutitution in the sea hare Aplysia neuropeptide H-Asn-d-Phe-NH2 on the conformation and contraction activity. Peptide Science 2003, 459-462 (2004).

Takeda, Y., Shirasu, N., Sato, S., Matsushima, A., Chuman, Y., Shimohigashi, M., and Shimohigashi, Y.: Two distinctly different isoforms with/without pentapeptide fragment in the silk moth clock protein peptide. Peptide Science 2003, 473-476 (2004).

Honda, T., Chuman, Y., Matsushima, A., Nose, T., Sakaguchi, K., Onoue, H., Tominaga, Y., Shimohigashi, Y., and Shimohigashi, M.: Localization profiles of circadian neuropeptide PDF in brain of the cricket Gryllus bimaculatus. Peptide Science 2003, 81-84 (2004).

Matsushima, A., Yokotani, S., Shimohigashi, Y., Tominaga, Y., Shimohibashi, M.: cDNA cloning and in situ hybridization studies of sulfated peptide, sulfakinin, on housefly Musca domestica. Peptide Science 2003, 459-462 (2004).

2003年

Sato, S., Oka, H., Matsushima, A., Tominaga, Y., Shimohigashi, Y., and Shimohigashi, M.: Structural analysis of PERIOD-PAS domain binding regions in insect clock protein TIMELESS. Peptide Science 2002, 429-432 (2003).

Tokunaga, T., Ohtani, M., Matsushima, A., Nose, T., Shimohigashi, Y., Aimoto, S., and Shimohigashi, Y.: The Structure-activity studies of Drosophila FMRFamide-related peptides. Peptide Science 2002, 265-268 (2003).

Honda, T., Chuman, Y., Matsushima, A., Asai, D., Nose, T., Sakaguchi, K., Onoue, H., Tominaga, Y., Shimohigashi, Y., and Shimohigashi, Y.: Localization profiles of the precursor protein of circadian rhythm pacemaker hormone PDF in Gryllus Peptide Science 2002, 433-436 (2003).

Matsushima, A., Nose, T., Tomioka, K., Shimohigashi, M., and Shimohigashi, Y.: Structural characterization of the house fly PDF, a circadian rhythm pacemaker hormone. Peptide Science 2002, 333-336 (2003).

2002年

Asai, D., Tokunaga, T., Matsushima, A., Sato, S., Chuman, Y., Nose, T., Tominaga, Y., Shimohigashi, Y., and Shiimohigashi, M.: Design and preparation of universal anti-PERIOD antibodies and their immunoresponses. Peptide Science 2001, 399-402 (2002).

Tokunaga, T., Ohtani, M., Matsushima, A., Chuman, Y., Nose, T., Shimohigashi, Y., Aimoto, S., and Shimohigashi, Y.: Contractile activity of Drosophila FMRFamide-related peptides in the Meretrix Lusoria heart muscle. Peptide Science 2001, 167-170 (2002).

Sato, S., Matsushima, A., Chuman, Y., Tominaga, K., Shimohigashi, Y., and Shimohigashi, M.: cDNA cloning of PDF peptide precursors in housefly and last summer cicada. Peptide Science 2001, 139-142 (2002).

Matsushima, A., Chuman, Y., Sato, S., Tominaga, Y., Shimohigashi, Y., and Shimohigashi M.: Structure and function of nuclear localization signal peptide present in circadian rhythm hormone peptide precursor. Peptide Science 2001, 159-162 (2002).

Chuman, Y., Matsushima, A., Shimohigashi, Y., and Shimohigashi M.: Circadian rhythm pacemaker neuropeptide ‘PDF’ in nocturnal insect cricket gryllus bimaculatus: cDNA cloning, mRNA expression, and nuclear localization. American Peptide Society 2001, 797-798 (2002).

2001年

Shimohigashi, Y., Chuman, Y., Matsushima, A., Onoue, H., Ito, Y., Tomioka, K., Shimohigashi, M., and Tominaga Y.: Molecular cloning and gene expression of a circadian neuropeptide, PDF, in the cricket Gryllus bimaculatus. Comp. Biochem. Physiol., 127, 374 (2001).

Fujita, T., Inoue, N., Matsuhima, A., Nose, T., Costa, T., and Shimohigashi, Y.: Activity Enhancement by Introduction of two different halogen atoms into Phe-2-phenyl group of thrombin receptor tetherd-ligand analogs. Peptide Science 2000, 135-138 (2001).

Chuman, A., Matsushima, Nose, T., Y., Shimohigashi, and M., Shimohigashi, Y.: cDNA Cloning of circadian rhythm pacemaker neuropeptide PDF in Gryllus bimaculatus and its neuclear localization. Peptide Science 2000, 59-62 (2001).

Matsushima, A., Chuman, Y., Onoue, H., Ito, Y., Tomioka, K., Tominaga, Y., Shimohigashi, Y., and Shimohigashi M.: Gene expression of a circadian pacemaker hormone peptide PDF in cricket Gryllus bimaculatus. Peptide Science 2000, 63-66 (2001).

Sato, S., Chuman, Y., Matsushima, A., Shimohigashi, Y., Tominaga, Y., and Shimohigashi, M.: PERIOD clock protein of the summer cicada Meimuna opalifera: cDNA cloning and structural analysis. Biochem. Physiol., 130, 874 (2001).

Matsushima, A., Cuman, Y., Sato, S., Shimohigashi, Y., Tominaga, Y., and Shimohigashi, M.: cDNA cloning of a circadian rhythm pacemaker hormone PDF of the house fly Musca domestica. Comp. Biochem. Physiol., 130, 876 (2001).

2000年

Matsushima, A., Fujita, , Okada, K., Yamauchi, Y., Nose, T., and Shimohigashi, Y.: Chemical syntheses of phenylalanine derivatives containing halogenated benzene ring as structural explorers for elucidation of molecular mechanisms of receptor interactions. Peptide Science 1999, 141-142 (2000).

Fujita, , Nose, T., Matsushima, A., Costa, T., and Shimohigashi, Y.: Highly potent peptide ligands for thrombin receptor. Peptide Science 1999, 421-424 (2000).

1999年

Fujita,T., Nose, , Matsushima, A., Costa, T., and Shimohigashi, Y.: Importance of ligand Phe-phenyl group for activation of thrombin receptor. Peptide Science 1998, 33-36 (1999).


プロシーディング(査読 無)、その他

2022年

松島綾美: 解説 ビスフェノール類が環境ホルモンとして作用する機構を解明―コンピュータシミュレーションを駆使して見出した複雑な作用、化学(化学同人) 77, No. 3, p 23-26 (2022).

2019年

枡屋宇洋、岩本雅樹、劉 暁輝、松島綾美*: 内分泌撹乱物質から薬ができるかも知れないー新規な創薬シードと期待される三環系ビスフェノール、Endocrine Disrupter NEWS LETTER Vol. 21, No. 1, p 2 (2019).

2017年

劉 暁輝、松島綾美下東康幸*: 乳がん細胞における内分泌撹乱物質ビスフェノールのエストロゲン受容体応答、月刊 細胞 the cell(ニューサイエンス)Vol. 49, No. 7 p 47-51 (2017).

「無意識のバイアス – Unconscious Bias – を知っていますか?」男女共同参画学協会連絡会著(2017)の作成に従事。(https://www.djrenrakukai.org/doc_pdf/2019/UnconsciousBias_leaflet.pdf

2016年

松島綾美*核内受容体が示す有害化学物質ビスフェノール応答、生化学、 88, No. 6, pp. 733-743 (2016).

松島綾美*:新世代ビスフェノールと核内受容体の構造活性相関解析研究〜ハロゲン原子を含有するリガンドとその受容体〜、生命科学ニュースレター、 52、pp. 20-25 (2016).

松島綾美*:若手科学者に聞く〜未来に貢献する科学者をめざして〜-奨励賞受賞者からのコメント-、http://www.jbsoc.or.jp/column/h28-5.html

劉 暁輝、松島綾美下東康幸*: 内分泌撹乱物質ビスフェノールの乳がん細胞におけるエストロゲン受容体応答、月刊 細胞 the cell(ニューサイエンス)Vol.48, No. 7, p 41-45 (2016).

2015年

劉 暁輝、松島綾美下東康幸*: 乳がん細胞におけるビスフェノールのエストロゲン様活性、BIO Clinica(北隆館)Vol. 30, No. 10, p 90 (2015).

2013年

下東康幸、劉 暁輝、松島綾美: ビスフェノールの核内受容体応答の分子メカニズム、Endocrine Disrupter NEWS LETTER Vol. 15, No. 4, p 5 (2013).

2011年

松島綾美: 注目の論文、キレートの傘を被った女性ホルモン-結晶構造解析で受容体にある通路も推定、化学(化学同人)Vol. 66, No. 12, p 2 (2011).

2007年

松島綾美、下東康幸: エストロゲン関連受容体γ型(ERRγ):ビスフェノールAが非常に強く結合する自発活性化型核内受容体の発見、Endocrine Disrupter NEWS LETTER Vol. 10, No. 3, p 2 (2007).

松島綾美:理学部化学科に進学してから現在まで.科学の未来は女性が開く〜輝く人生を目指して〜 文部科学省女子中高生理系進路選択支援事業『女子中高生向け「理系への招待」—同窓会組織との連携による理系進学者ロールモデル明示プラン—』(九州大学)啓発資料冊子p. 16 (2007).

2004年

松島綾美:5th Australian Peptide Conferenceへの参加報告Peptide Newsletter JAPAN, No.51, P. 8 (2004).

2001年

松島綾美、下東康幸、下東美樹:昆虫の概日リズムペースメーカーペプチドホルモンPDF、比較生理生化学 18(3), 159-166 (2001).