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Ayami Matsushima Last modified date:2018.09.04

Associate Professor / Organic and Biological Chemistry
Department of Chemistry
Faculty of Sciences


Graduate School
Undergraduate School
Administration Post
Other


E-Mail
Homepage
http://LSFB.scc.kyushu-u.ac.jp/
http://rsrc.scc.kyushu-u.ac.jp/
Academic Degree
Ph. D
Country of degree conferring institution (Overseas)
No
Field of Specialization
Biochemistry
Research
Research Interests
  • The Study on nociceptin receptor antagonist
    keyword : nociceptin, antagonist, agonist
    2010.04.
  • Studies on the mechanism in gene expression of nuclear receptors and the chemical risk assessments
    keyword : nuclear receptor, bisphenol A
    2005.04.
Academic Activities
Papers
1. Matsushima, A., A Novel Action of Endocrine-Disrupting Chemicals on Wildlife; DDT and Its Derivatives Have Remained in the Environment, Int. J. Mol. Sci., DOI:10.3390/ijms19051377, 19, 5, e1377, 2018.04.
2. Matsushima, A., Nishiimura, 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, 88, 2017.03.
3. Ayami Matsushima, Hiroyuki Nishimura, Yutaka Matsuyama, LIU XIAOHUI, Tomasso Costa, Yasuyuki Shimohigashi, Specific affinity-labeling of the nociceptin ORL1 receptor using a thiol-activated Cys(Npys)-containing peptide ligands, Biopolymers Peptide Science, 10.1002/bip.22792., 2016.03.
4. 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), 2016.03.
5. LIU XIAOHUI, Ayami Matsushima, Miki Shimohigashi, Yasuyuki Shimohigashi, A characteristic back support structure in the bisphenol A-binding pocket in the human nuclear receptor ERR, PLoS ONE, 10.1371/journal.pone.0101252, 9, e101252, 2014.06.
6. Jinglan Li, Hirokazu Nishimura, Ayami Matsushima, Yasuyuki Shimohigashi, N-Methylthioacetylation of RYYRIK-NH2 with enhanced specific binding affinity and high antagonist activity for nociceptin ORL1 receptor, Bioorg. Med. Chem., 10.1016/j.bmc.2014.09.049, 22, 5712-5716, 2014.05.
7. Shogo Inamine, Hirokazu Nishimura, Jinglan Li, Kaname Isozaki, Ayami Matsushima, Tomasso Costa, Yasuyuki Shimohigashi, Tritium-labelled isovaleryl-RYYRIK-NH2 as potential antagonist probe for ORL1 nociceptin receptor, Bioorg. Med. Chem., 10.1016/j.bmc.2014.09.049, 22, 5902-5909, 2014.05.
8. LIU XIAOHUI, Akina Fujiyama, Ayami Matsushima, Miki Shimohigashi, Yasuyuki Shimohigashi, α-Helix-Peptides Composing the human nuclear receptor ERRγ competitively provoke inhibition of functional homomeric dimerization., Biopolymers Peptide Science, 10.1002/bip.22795., 2014.03.
9. Ayami Matsushima, Hirokazu Nishimura, Shogo Inamine, Yasuyuki Shimohigashi, Identification of affinity binding site of Cys(Npys)-elongated RYYRIK peptide antagonist by means of Cys→Ala mutated ORL1 nociceptin receptors., Peptide Science 2012, 115-118, 2013.03, We have previously developed a peptidic affinity ligand for the ORL1 nociceptin receptor. It contains Cys(Npys) instead of isovareroyl of a pure antagonist peptide isovareroyl-RYYRIK-NH2. In this study, in order to identify the exact binding site of Cys(Npys), we performed affinity labeling experiments of a series of Cys→Ala mutated ORL1 receptors. A certain number of mutant receptors showed labeling effectiveness weaker than wild type receptor, suggesting that the recepor Cys was labeled by Cys(Npys)-RYYRIK-NH2..
10. Ayami Matsushima, Kerrianne Ryan, Yasuyuki Shimohigashi, Ian A. Meinertzhagen, An endocrine disruptor, bisphenol A, affects development in the protochordate Ciona intestinalis, Environ. Pollut., 10.1016/j.envpol.2012.10.015, 173, 257-263, 2013.02.
11. Liu X, Matsushima A, Nakamura M, Costa T, Nose T, 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., J. Biochem. , 10.1093/jb/mvs008, 151, 4, 403-415, 2012.04, Various lines of evidence have shown that bisphenol A (BPA) acts as an endocrine disruptor that affects various hormones even at merely physiological levels. We demonstrated recently that BPA binds strongly to human nuclear receptor estrogen-related receptor γ (ERRγ), one of 48 nuclear receptors. Based on X-ray crystal analysis of the ERRγ ligand-binding domain (LBD)/BPA complex, we demonstrated that ERRγ receptor residues, Glu275 and Arg316, function as the intrinsic-binding site of the phenol-hydroxyl group of BPA. If these phenol-hydroxyl↔Glu275 and Arg316 hydrogen bonds anchor the A-benzene ring of BPA, the benzene-phenyl group of BPA would be in a pocket constructed by specific amino acid side chain structures. In the present study, by evaluating the Ala-replaced mutant receptors, we identified such a ligand-binding pocket. Leu268, Leu271, Leu309 and Tyr326, in addition to the previously reported participants Glu275 and Arg316, were found to make a receptacle pocket for the A-ring, whereas Ile279, Ile310 and Val313 were found to assist or structurally support these residues. The results revealed that each amino acid residue is an essential structural element for the strong binding of BPA to ERRγ..
12. Matsushima, A., Nishimura, H., Inamine, S., Uemura, S., Shimohigashi, Y., Capturing of the free cysteine residue in the ligand-binding site by affinity labeling of the ORL1 nociceptin receptor., Bioorg. Med. Chem., 10.1016/j.bmc.2011.10.024 , 19, 7597–7602, 2011.09, All of the δ, μ, and κ opioid receptors have a free thiol group of the Cys residue in the ligand-binding site, although its functional role is not yet known. In order to examine whether or not a similar Cys is also present in the ORL1 nociceptin receptor, we attempted to identify it by affinity labeling using a specific antagonist peptide. We first treated ORL1-expressing COS-7 cell membrane preparations with the thiol-alkylation reagent N-ethylmaleimide (NEM) to perform a binding assay using [(3)H]nociceptin as a tracer and nociceptin, an ORL1 agonist, or Ac-Arg-Tyr-Tyr-Arg-Ile-Lys-NH(2), a nociceptin/ORL1 antagonist, as a competitor. It was suggested that ORL1 has a free Cys in its ligand-binding site, since the NEM treatment reduced the population of ligand-binding sites. This was further confirmed by affinity labeling using Cys(Npys)-Arg-Tyr-Tyr-Arg-Ile-Lys-NH(2) with the SNpys group that can react with a free thiol group, resulting in the formation of a disulfide bond. This affinity labeling was approximately 23 times more specific than NEM alkylation. The results revealed that the ORL1 nociceptin receptor does contain a free Cys residue in the ligand-binding site..
13. 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, 2010.05.
14. 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., Environ. Health Perspect., 2010.04.
15. 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, 2010.03.
16. 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 , 2010.03.
17. 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 γ (ERRγ)., Peptide Science 2009, 435–436, 2010.03.
18. 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, J. Biochem., , 146, 113-122, 2009.10.
19. 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 α-helix peptide in the estrogen-related receptor γ (ERRγ), Peptide Science 2008, 521-522, 2009.03.
20. 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., Biochem. Biophys. Res. Commun., 373, 408-413 (2008), 2008.12.
21. 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 Peptide Sci., 15, 949-955 (2008), 2008.08.
22. 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)., Environ. Health Perspect., 116, 32-38 (2008), 2008.01.
23. Li, J. Isozaki, K., Okada, K., Matsushima, A., Nose, T., Costa, T., and Shimohigashi, Y., Design Synthesis of Highly Potent Antagonist of ORL1 Nociceptin Receptor., Bioorg. Med. Chem., 16, 2635-2664 (2008), 2008.01.
24. 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), 2008.01.
25. 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), 2008.01.
26. 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), 2008.01.
27. 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), 2008.01.
28. 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, J. Biochem., 142, 517-524 (2007), 2007.10.
29. Liu, X., Matsushima, A., Okada, H., Tokunaga, T., Isozaki, K., and Shimohigashi, Y., Receptor binding characteristics of 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 , FEBS J., 274, 6340-6351 (2007), 2007.10.
30. Matsushima, A., Takano, K., Yoshida, T., Takeda, Y., Yokotani, S., Shimohigashi, Y., and Shimohigashi, M., Double-labeled 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, J. Biochem, 141, 867-877 (2007), 2007.06.
31. 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, (2006), 2006.12.
32. 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 cinstitutive activity, Toxicol. Lett., 195, 95-105 , 2006.11.
33. 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), 2006.03.
34. 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), 2006.03.
35. 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), 2005.03.
36. okotani, S., Matsushima, A., Nose, T., Morishita, F., and Shimohigashi Y., Bioactive Conformation of a D-Trp-Containing Cardioexcitatory Tripeptide Isolated from the Sea Hare Aplysia, Peptide Science 2004, 539-540 (2005), 2005.03.
37. 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), 2005.03.
38. 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), 2005.03.
39. Matsushima, S., 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 Pacemaker Neuropeptide PDF in Diptera, Lett., Peptide Sci., 10, 419-430 (2003), 2005.01.
40. Matsushima ., 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)., 2005.01.
41. 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, Zool. Sci., 10.2108/zsj.19.821, 19, 8, 821-828, 19, 821-828, 2002.12.
42. 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, J., Biochem., 131, 6, 895-903, 131, 895-903, 2002.11.
43. 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, Comp. Biochem. Physiol., 127, 374, 2002.03.
44. 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, 2002.03.
45. 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 , 2002.03.
46. 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, 2002.03.
47. 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, 2001.03.
48. Chuman, A., Matsushima, T., Nose, Y., Shimohigashi, and M., Shimohigashi, cDNA Cloning of Circadian Rhythm Pacemaker Neuropeptide PDF in Gryllus bimaculatus and Its Neuclear Localization, Peptide Science 2000, 59-62, 2001.03.
49. 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, 2001.03.
50. Matsushima, A., Cuman, Y., Sato, S., Shimohigashi, Y., Tominaga, Y., and Shimohigashi, M., cDNA cloning of a Circadian Rhythm Pacemaker Hormone PDF of theHouse Fly Musca domestica, Comp. Biochem. Physiol., 130, 876, 2001.02.
51. 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, Comp. Biochem. Physiol., 130, 874, 2001.02.
52. Matsushima, A., Fujita, T., 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, 2000.03.
53. Matsushima, A., Fujita, T., Okada, K., Shirasu, N., Nose, T., and Shimohigashi, Y., Exploration of the Role of Phenylalanine in the Thrombin Rwcwptor Tethered-Ligand Peptide by Substitution with a Series of Trifluorophenylalanines, Bull. Chem. Soc. Jpn, 10.1246/bcsj.73.2531, 73, 11, 2531-2538, 73, 2531-2538 , 2000.02.
54. 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, J. Biochem., 128, 2, 225-232, 128, 225-232, 2000.02.
55. 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 , 2000.02.
56. Fujita,T., Nose, T., Matsushima, A., Costa, T., and Shimohigashi, Y., Importance of Ligand Phe-phenyl Group for Activation of Thrombin Receptor, Peptide Science 1998, 33-36, 1999.03.
Presentations
1. 松島綾美, 環境ホルモン学会に参加して10年:10年間の核内受容体とリガンドの構造活性相関解析研究, 第19回環境ホルモン学会研究発表会, 2016.12.
2. 松島綾美, 核内受容体とハロゲン含有環境化学物質の精緻な構造活性相関, DV-Xα研究協会, 2016.12.
3. 松島 綾美, 西村裕一, 劉 暁輝, 武末祐貴, 松山祐昂, 下東 康幸, Comprehensive structural analysis of the nociceptin ORL1 receptor by means of virtual and experimental Ala-scanning combined methods, 第52回ペプチド討論会, 2015.11.
4. 劉 暁輝, 下東美樹, 松島 綾美, 下東 康幸, Protein constitutive peptide fragments to inhibit protein-protein interaction: Inhibitory peptides as molecular probe for clarification of human nuclear receptor activation mechanism, 第52回ペプチド討論会, 2015.11.
5. Ayami Matsushima, H. Nishimura, S. Inamine, 下東 康幸, Multiple and Simultaneous Cys→Ala Mutations of ORL1 Nociceptin Receptor to Identify the Affinity Binding site of Cys(Npys)-Elongated RYYRIK Peptide Antagonist., The 4th Asia-Pacific International Peptide Symposium / The 50th Japanese Peptide Symposium, 2013.11.
6. LIU XIAOHUI, A. Fujiyama, H. Nishimura, Ayami Matsushima, 下東 康幸, Constitutive α-Helix-peptides Required for Functional Dimerization of Estrogen-related Receptor γ (ERRγ), The 4th Asia-Pacific International Peptide Symposium / The 50th Japanese Peptide Symposium, 2013.11.
7. Ayami Matsushima, Structure activity relationships between nuclear receptors and newly developed bisphenol A derivatives, NIEHS Seminar, 2013.07.
8. Ayami Matsushima, Structure activity relationships between nuclear receptors and novel Bisphenol A derivative, "Crossing Boundaries with Informatics -from Basic Science to Social Infrastructure": US-Japan "Connections" Symposium for Women Leaders in Science, Technology and Engineering and Mathematics, 2013.07.
9. Exploration of high-affinity chemicals for nuclear receptors and their possible endocrine-disrupting effects as “inverse antagonists” .
10. Exploration of high-affinity chemicals for nuclear receptors and their possible endocrine-disrupting effects as “inverse antagonists” .
11. 松島 綾美, 下東 康幸, Extraordinary Strong Binding of Human Nuclear Receptor ERRγ with Endocrine-Disrupting Chemical BisphenolA, 第16回韓国ペプチド・タンパク質シンポジウム, 2012.11.
12. Exploration of high-affinity chemicals for nuclear receptors and their possible endocrine-disrupting effects as “inverse antagonists” .
13. Multiple Post-transcriptional Regulations in Circadian Pacemaker Neuropeptide pdf Gene.
14. Conformation Change of α-Helix Peptide for Sensing of Deactivation of Nuclear Receptor: Immunoassay Using Polyclonal Antibody Specific for the C-terminal -Helix 12 of Estrogen-related Receptor γ (ERRγ).
15. Structure-Activity Studies of FMRFamide-Related Peptides in Activating the Specific Receptor Present in the Housefly Musca domestica.
Awards
  • Elucidation of molecular mechanism of receptor activation using fluorine-containing aromatic ligands
  • Structure-function studies between the hormone-disrupting chemical bisphenols and the nuclear receptors