Kyushu University Academic Staff Educational and Research Activities Database
List of Papers
Takeru Nose Last modified date:2019.05.13

Professor / Division for Experimental Natural Science / Faculty of Arts and Science

1. Keitaro Suyama, Daiki Tatsubo, Wataru Iwasaki, Masaya Miyazaki, Yuhei Kiyota, Ichiro Takahashi, Iori Maeda, Takeru Nose, Enhancement of self-aggregation properties of linear elastin-derived short peptides by simple cyclization
strong self-aggregation properties of cyclo[FPGVG]n, consisting only of natural amino acids, Biomacromolecules, 10.1021/acs.biomac.8b00353, 19, 8, 3201-3211, 2018.02, Elastin-like peptides (ELP) consist of distinctive repetitive sequences, such as (VPGVG)n, exhibit temperature-dependent reversible self-assembly (coacervation), and have been considered to be useful for the development of thermo-responsive materials. Further fundamental studies evaluating coacervative properties of novel nonlinear ELPs could present design concepts for new thermo-responsive materials. In this study, we prepared novel ELPs, cyclic (FPGVG)n (cyclo[FPGVG]n, n = 1-5), and analyzed its self-assembly properties and structural characteristics. Cyclo[FPGVG]n (n = 3-5) demonstrated stronger coacervation capacity than the corresponding linear peptides. The coacervate of cyclo[FPGVG]5 was able to retain water-soluble dye molecules at 40°C, which implied that cyclo[FPGVG]5 could be employed as a base material of DDS (Drug Delivery System) matrices and other biomaterials. The results of molecular dynamics simulations and circular dichroism measurements suggested that a certain chain length was required for cyclo[FPGVG]n to demonstrate alterations in molecular structure that were critical to the exhibition of coacervation..
2. Daiki Tatsubo, Keitaro Suyama, Masaya Miyazaki, Iori Maeda, Takeru Nose, Stepwise Mechanism of Temperature-Dependent Coacervation of the Elastin-like Peptide Analogue Dimer, (C(WPGVG)3)2, Biochemistry, 10.1021/acs.biochem.7b01144, 57, 10, 1582-1590, 2018.03.
3. Iori Maeda, Shohei Kai, Suguru Taniguchi, Asako Inoue, Hujun Li, Hitoshi Kesamaru, Takeru Nose, Angiotensin I Converting Enzyme-inhibiting Peptides Purified from Elastase-degraded Elastin Prepared from Pig Aorta, Current Enzyme Inhibition, 10.2174/1573408013666170912113121, 14, 67-74, 2018.03.
4. Daiki Tatsubo, Misako Kodama, Keiji Sato, Keitaro Suyama, Iori Maeda, and Takeru Nose, Effects of Salts and pH on Coacervation of Short Elastin-Like Peptide (FPGVG)5, Peptide Science 2017, 62-63, 2018.03.
5. Hujun Li, Asako Inoue, Suguru Taniguchi, Tomohiko Yukutake, Keitaro Suyama, Takeru Nose, Iori Maeda, Multifunctional biological activities of water extract of housefly larvae (Musca domestica), PharmaNutrition, 10.1016/j.phanu.2017.09.001, 5, 4, 119-126, 2017.12, Many types of insects have been used as foods and protein sources. In this study, we investigated the usefulness of housefly larvae (Musca domestica) based on their amino acid composition and multifunctional biological activities. First, the utility of the amino acid composition of housefly larvae was evaluated by amino acid analysis. Notably, the housefly larvae contained sufficient amounts of all essential amino acids, and the amino acid composition was similar to that of hen eggs. Second, we prepared housefly larvae water extract (HLWE) using the decoction method and explored the biological activities of the extract for potential application of the extract as a functional food. HLWE showed significant antioxidant activity (75.4% at 5.00 mg/mL), angiotensin-I-converting enzyme (ACE) inhibitory activity (half-maximal inhibitory concentration [IC50] = 0.430 mg/mL), and dipeptidyl peptidase-IV (DPP-IV) inhibitory activity ([IC50] = 3.52 mg/mL). We found that the low-molecular-weight constituents (<6 kDa) in HLWE contributed to antioxidant and ACE-inhibitory activities, whereas the high-molecular-weight constituents (>6 kDa) contributed to DPP-IV inhibition. Our results suggested that housefly larvae may provide a useful source of multifunctional protein..
6. Keitaro Suyama, Hitoshi Kesamaru, Daiki Tatsubo, Takeru Nose, Coacervation Property and Structural Analysis of Cyclic Analogs of Elastin-derived Peptide (FPGVG)n , Peptide Science 2016, 101-102, 2017.03.
7. Daiki Tatsubo, Keitaro Suyama, Takeru Nose, Analysis of structural requirement for coacervation property of elastin model peptide dimers, Peptide Science 2016, 13-14, 2017.03.
8. Asako Inoue, Tomohiro Hikima, Suguru Taniguchi, Takeru Nose, Iori Maeda, Investigation of water-soluble elastin as a multifunctional cosmetic material: Moisturizing and whitening effects, JOURNAL OF COSMETIC SCIENCE, 10.1002/psc.2837, 68, 1-13, 2017.01.
9. 山口容子, Steve Peigneur, 劉 俊驛, Shiho Uemura, Takeru Nose, Selvanayagam Nirthanan, Ponnampalam Gopalakrishnakone, Jan Tytgat, 佐藤一紀, Role of individual disulfide bridges in the conformation and activity of spinoxin (α-KTx6.13), a potassium channel toxin from Heterometrus spinifer scorpion venom, Toxicon, 10.1016/j.toxicon.2016.09.013, 122, 31-38, 2016.11.
10. Steve Peigneur, 山口容子, Chihiro Kawano, Takeru Nose, Selvanayagam Nirthanan, Ponnampalam Gopalakrishnakone, Jan Tytgat, 佐藤一紀, Active Sites of Spinoxin, a Potassium Channel Scorpion Toxin, Elucidated by Systematic Alanine Scanning, Biochemistry, 10.1021/acs.biochem.6b00139, 55, 21, 2927-2935, 2016.05.
11. Keitaro Suyama, Suguru Taniguchi, Daiki Tatsubo, Iori Maeda, Takeru Nose, Dimerization effects on coacervation property of an elastin-derived synthetic peptide (FPGVG)5, Journal of Peptide Science, 10.1002/psc.2876, 22, 236-243, 2016.03.
12. Keitaro Suyama, Hitoshi Kesamaru, Daiki Tatsubo, Takeru Nose, Coacervation Properties and Structural Analysis of Aminobenzoyl-labeled Fluorescent Elastin-derived Peptides, Peptide Science 2015, 293-294, 2016.03.
13. Daiki Tatsubo, Keitaro Suyama, Takeru Nose, Fluorescence Analysis Using a Molecular Probe 1,8-ANS for Elucidation of the Molecular Mechanisms Underlying Coacervation of a Tryptophan-containing Elastin derived Dimeric Peptide, Peptide Science 2015, 95-96, 2016.03.
14. Suguru Taniguchi, Noriko Watanabe, Takeru Nose, Iori Maeda, Development of short and highly potent self-assembling elastin-derived pentapeptide repeats containing aromatic amino acid residues, JOURNAL OF PEPTIDE SCIENCE, 10.1002/psc.2837, 22, 1, 36-42, 2016.01.
15. Iori Maeda, Suguru Taniguchi, Noriko Watanabe, Asako Inoue, Yuko Yamazaki, Takeru Nose, Design of Phenylalanine-Containing Elastin-Derived Peptides Exhibiting Highly Potent Self-Assembling Capability , Protein & Peptide Letters, 10.2174/092986652210150821170703, 22, 10, 939-939, 2015.08, In this study, we developed a series of Phe-containing elastin-derived peptide-analogs, (Phe-Pro-Gly-Val-Gly)n (n = 1–5) and analyzed their reversible coacervation properties. Compared to the native elastin-derived repeating peptide sequence ((Val-Pro-Gly-Val-Gly)10), one of the Phecontaining 5-mer repeating peptide sequences ((Phe-Pro-Gly-Val-Gly)5) clearly exhibited stronger coacervation properties. The coacervation of (Phe-Pro-Gly-Val-Gly)5 is nearly the same as that of polypeptides (Val-Pro-Gly-Val-Gly)n (n > 40). Although large molecular weights (>10,000 Da) are generally required for the coacervation of elastin-derived peptides, (Phe-Pro-Gly-Val-Gly)5 exhibited reversible coacervation properties despite its low molecular weight (MW = 2,305 Da). High performance liquid chromatography (HPLC) and circular dichroism (CD) analysis revealed that (Phe-Pro-Gly-Val-Gly)5 has high hydrophobicity and an ordered structure with a type II β-turn, which contributes to the strong coacervation ability of the peptide. In addition, (Phe-Pro-Gly-Val-Gly)5 exhibited an effective particle size distribution (60–70 nm) at body temperature (37°C) and a dispersed small particle size similar to that of the monomer peptides at low temperatures. These properties, along with its small size and simple design, render the peptide suitable for use in biomaterials, including drug-delivery carriers..
16. Steve Peigneur, 山口容子, Chihiro Kawano, Takeru Nose, Selvanayagam Nirthanan, Ponnampalam Gopalakrishnakone, Jan Tytgat, 佐藤一紀, Structure-function relationships of spinoxin, a peptide neurotoxin from scorpion venom, Peptide Science 2014, 55-56, 2015.03.
17. Keitaro Suyama, Daiki Tatsubo, Suguru Taniguchi, Hitoshi Kesamaru, Iori Maeda, Takeru Nose, Coacervation property and structural analysis of synthetic dimer peptides of aromatic amino acid containing elastin-derived peptides, Peptide Science 2014, 323-324, 2015.03.
18. Iori Maeda, Suguru Taniguchi, Takeru Nose, Identification of an Elastin-derived Peptide Degrade in Human Blood After Oral Ingestion of Elastin, Peptide Science 2014, 305-306, 2015.03.
19. KIKAN education KADAI-KYOGAKU (interdisciplinary collaborative learning of social issues).
20. Keitaro Suyama, Suguru Taniguchi, Iori Maeda, Daiki Tatsubo, Takeru Nose, Coacervation Property and Secondary Structure of Synthetic Dimer Peptides of Elastin-Derived Pentapeptide Repeats, Peptide Science 2013, 277-278, 2014.03.
21. Yumi Kuramitsu, Hirokazu Nishimura, Ryo Nakamura, Keitaro Suyama, Ayami Matsushima, Takeru Nose, Yasuyuki Shimohigashi, Structure-Activity Studies on the Halogenated Phe-containing Neuropeptide Substance P Analogs, Peptide Science 2013, 319-320, 2014.03.
22. Asako Inoue, Suguru Taniguchi, Yuko Yamasaki, Masakazu Furuta, Takeru Nose, Iori Maeda, Preparing of Phenylalanine Containing Elastin-Derived Pentapeptide Based Biomaterials , Peptide Science 2013, 431-432, 2014.03.
23. Suguru Taniguchi, Noriko Watanabe, Takao Hattori, Taishi Inatomi, Asako Inoue, Yuko Yamasaki, Takeru Nose, Iori Maeda, Coacervation Properties of Short Elastin-Derived Pentapeptide Analogues Containing Aromatic Amino Acids, Peptide Science 2013, 433-434, 2014.03.
24. Iori Maeda, Suguru Taniguchi, Junko Ebina, Noriko Watanabe, Takao Hattori, Takeru Nose, Comparison between Coacervation Property and Secondary Structure of Synthetic Peptides, Ile-containing Elastin-derived Pentapeptide Repeats, Protein & Peptide Letters, 10.2174/0929866511320080007 , 20, 8, 905-910, 2013.08, A series of Ile-containing elastin-derived peptide-analogs, (Ile-Pro-Gly-Val-Gly)n (n=7–10) possessing remarkable and reversible coacervation property were newly synthesized. In comparison with the known elastin-derived peptideanalogs, which were so-called polypeptides, the obtained 35 to 50 mer peptides, (IPGVG)n (n=7–10) were significantly low molecular sized-polypeptides. However, they clearly exhibited coacervation property as same as the polypeptides did. Because of their low molecular size, spectrographic analyses of (IPGVG)n (n=7–10) became feasible to carry out. As results of secondary structural analyses by CD and FT-IR, it was found that the coacervation property of the peptides is clearly attributed to the ordered secondary-structures, mainly, type II β–turn..
25. Nishio K, Nishimura H, Suyama K, Matsushima A, Nose T, Shimohigashi, Halogenated Phe-containing endomorphin-2 analogs with mixed agonist and antagonist activities, Peptide Science 2012, 25-26, 2013.03.
26. Y. Kuramitsu, H. Nishimura, R. Nakamura, K. Suyama, A. Matsushima, T. Nose, Y. Shimohigashi, High-precision binding assay procedure of tachykinin receptor NK-1 for highly potent Substance P analogs, Peptide Science 2012, 213-214, 2013.03.
27. Maniwa Y., Inoue A., Watanabe N., Ogino Y., Yamasaki Y., Nose T., Maeda I., Coacervation properties of hydrophobic elastin-derived pentapeptide analogues, Peptide Science 2012, 391-392, 2013.03.
28. Y. Matsuyama, X. Liu, H. Nishimura, A. Matsushima, T. Nose, Y. Shimohigashi, Bisphenol-binding pocket of constitutively active nuclear receptor CAR: Docking modeling for close-packing, Peptide Science 2012, 401-402, 2013.03.
29. Mitsuhiro Nishigori, Takeru Nose, Yasuyuki Shimohigashi, Highly Potent Binding and Inverse Agonist Activity of Bisphenol A Derivatives for Retinoid-related Orphan Nuclear Receptor RORg, Toxicol. Lett.,, 212, 2, 205-211, 2012.05.
30. Asanomi Y, Koga Y, Miyazaki M, Nose T, Kodama H, and Maeda H., Protease-immobilized Microreactor for Rapid and Site-specific Affinity Tag Cleavage, Peptide Science 2011, 395-396, 2012.03.
31. Nishimura H, Li J, Isozaki K, Abe Y, Inamine S, Matsushima A, Nose T, Costa T, and Shimohigashi Y, Structural Essentials of Hyperalgesic Nociceptin ORL1 Receptor for Ligand Binding and Receptor Activation, Peptide Science 2011, 33-34, 2012.03.
32. Nakamura R, Nishimura H, Suyama K, Nose T, and Shimohigashi Y, The Effects of Halogenation of Phe-phenyl Group of Two Consecutive Phe Residues Present in Neuropeptide Substance P on its Specific Receptor Interaction, Peptide Science 2011, 157-158, 2012.03.
33. Nishio K, Nishimura H, Suyama K, Abe Y, Matsushima A, Nose T, Shimohigashi Y, Effects of the Halogenation of Phe-phenyl Group of Two Consecutive Residues in endomorphin-2 on the Interaction with the μ-opioid receptors, Peptide Science 2011, 171-172, 2012.03.
34. Ito N, Nishimura H, Matsushima A, Nose T, Costa T, and Shimohigashi Y, Structural Analysis of Delta Opioid Receptor Dimer by Bivalent Deltorphin II Analogs, Peptide Science 2011, 173-174, 2012.03.
35. 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, 2012.03.
36. Abe Y, Matsuo T, Nishimura H, Li J, Nose T, Costa T, and Shimohigashi Y, Functional Analysis of a Histidine Residue Essential for Receptor Activation of Delta Opioid Receptor

 , Peptide Science 2011, 185-186, 2012.03.
37. Matsuo A, Nishimura H, Nakamura M, Koga K, Sumiyoshi M, Matsushima A, Nose T, Shimohigashi M, and Shimohigashi Y, Structural Characteristics of Thr-Gly Dipeptide Repeat in the Drosophila Clock Protein PERIOD, Peptide Science 2011, 351-352, 2012.03.
38. 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 ERRγ, J. Biochem.  , 10.1093/jb/mvs008, 151, 4, 403-415, 2012.01, [URL], 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..
39. Maeda I., Fukumoto Y., Nose T., Shimohigashi Y., Nezu T., Terada Y., Kodama H., Kaibara K., and Okamoto K., Structural Requirements Essential for Elastin Coacervation: Favorable Spatial Arrangements of Valine Ridges on the Three-dimensional Structure of Elastin-derived Polypeptide (VPGVG)n, J. Pept. Sci., 10.1002/psc.1394, 17, 11, 735-743, 2011.06, [URL], The elastin precursor tropoelastin possesses a number of polymeric peptides with repeating 3–9 mer sequences. One of these is the pentapeptide Val-Pro-Gly-Val-Gly (VPGVG) present in almost all animal species, and its polymer (VPGVG)n coacervates just as does tropoelastin. In the present study, in order to explore the structural requirements essential for coacervation, (VPGVG)n and its shortened repeat analogs (VPGV)n, (VPG)n, and (PGVG)n were synthesized and their structural properties were investigated. In our turbidity measurements, (VPGVG)n demonstrated complete reversible coacervation in agreement with previous findings. The Gly5-deleted polymer (VPGV)n also achieved self-association, though the onset of self-association occurred at a lower temperature. However, the dissociation of (VPGV)n upon temperature lowering was found to occur in a three-step process; the Vali4-Vali+11 structure arising in the VPGV polypeptide appeared to perturb the dissociation. No self-association was observed for (VPG)n or (PGVG)n repeats. Spectroscopic measurements by CD, FT-IR, and 1H-NMR showed that the (VPGV)n and (VPG)n both assumed ordered structures similar to that of (VPGVG)n. These results demonstrated that VPGVG is a structural element essential to achieving the β-spiral structure required for self-association followed by coacervation, probably due to the ideal spatial arrangement of the hydrophobic Val residues. .
40. Nishimura H., Li J., Inokuchi N., Koikawa S., Nose T., Matsushima A., Costa T., and Shimohigashi Y., A Trp Residue of Opioid Receptor TM5 is Present at the Cell Membrane Interface as a Molecular Anchor for Full Activation, Peptide Science 2010, 175, 2011.03.
41. Inamine S, Li J, Nishimura H, Matsushima A, Nose T, Costa T, and Shimohigashi Y, Exploration of the Binding Site of ORL1 Nociceptin Receptor Antagonist, Peptide Science 2010, 167, 2011.03.
42. Nishimura H., Li J., Inokuchi N., Koikawa S., Matsushima A., Nose T., Costa T., Shimohigashi Y., The functional role of Trp present at the cell membrane interface in the opioid receptor activation, Peptide Science 2009, 23-24 (2010), 2010.03.
43. Li J., Isozaki K., Matsushima A., Nose T., Costa T., Shimohigashi Y., Structure-function analysis of nociceptin receptor ORL1 by the site-directed mutagenesis, Peptide Science 2009, 219-222 (2010), 2010.03.
44. Nose T., Tokunaga T., Shimohigashi Y., The agonist/antagonist differential-docking screening (AADS) method for exploration of the estrogen receptor-binding chemicals, Peptide Science 2009, 463-464 (2010), 2010.03.
45. 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, Bioorg. Med. Chem.,, 17, 23, 7904-7908, 2009.12.
46. Nose T., Tokunaga T., and Shimohigashi Y., Exploration of endocrine-disrupting chemicals on estrogen receptor α by the agonist/antagonist differential-docking screening (AADS) method: 4-(1-Adamantyl)phenol as a potent endocrine disruptor candidate, Toxicol. Lett.,, in press, 2009.11.
47. Nishimura H., Li J., Isozaki K., Okada K., Matsushima A., Nose T., Costa T., Shimohigashi Y., Discriminatory synergistic effect of Trp-substitutions in superagonist [(Arg/Lys)(14), (Arg/Lys)(15)]nociceptin on ORL1 receptor binding and activation., Bioorg. Med. Chem.,, 17(15), 5683-5687 (2009)., 2009.08.
48. Li J., Isozaki K., Nose T., Costa T., Shimohigashi Y., Essential Amino Acid Residues in the ORL1 Receptor Transmembrane Domains for Receptor Activation, Peptide Science 2008, 33-34 (2009), 2009.01.
49. Matsuo T., Abe Y., Li J., Isozaki K., Nose T., Shimohigashi Y., Histidines as Structurally Essential Residue for the Delta Opioid Receptor Activation, Peptide Science 2008, 263-264 (2009), 2009.01.
50. Koga K., Nose T., Horiuchi Y., Shimohigashi Y., Molecular Mechanism of alpha-Helix Peptide That Inhibits Intermolecular Interaction of Prion Protein N-Terminal Tetrarepeaat Domain, Peptide Science 2008, 265-266 (2009), 2009.01.
51. Nishimura H., Li J., Isozaki K., Okada K., Nose T., Costa T., Shimohigashi Y., The Effects of Arg→Trp and Lys →Trp Substitutions for Arg-Lys14-15 Residues in a Superagonist [Arg-Lys14-15]-Nociceptin on the ORL1 Receptor Binding and Activation, Peptide Science 2008, 267-268 (2009), 2009.01.
52. Yokotani S., Nose T., Horiuchi Y., Matsushima A., and Shimohigashi Y., Radar Chart Deviation Analysis of Prion Protein Amino Acid Composition Defines Characteristics Structural Abnomalities of the N-Terminal Octapeptide Tandem Repeat, Protein Pept. Lett.,, 15(9), 949-955 (2008)., 2008.10.
53. 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, Bioorg. Med. Chem.,, 16(5), 2635-2644 (2008)., 2008.10.
54. Okada K., Isozaki K., Li J., Matsushima A., Nose T., Costa T., and Shimohigashi Y., Synergistic Effect of Basic Residues at Positions 14-15 of Nociceptin on Binding Affinity and Receptor Activation, Bioorg. Med. Chem.,, 16(20), 9261-9267 (2008)., 2008.09.
55. Takeru Nose, Yasuyuki Shimohigashi, A docking modelling rationally predicts strong binding of bisphenol A to estrogen-related receptor γ , Protein and Peptide Letters, 15, 290-296, 2008.03.
56. M. Nishigori, T. Nose, X. Liu, T. Tokunaga, Y. Shimohigashi, The Conformation Change-Sensing Antibodies for Retinoid-Related Orphan Receptor Family, Peptide Science 2007, 491-492, 2008.03.
57. N. Inokuchi, K. Isozaki, Y. Tsuda, Y. Okada, S. Osada, T. Nose, T. Costa, Y. Shimohigashi, Differential Receptor Recognition by Dmt-Containing Enlephalin Dimers Cross-Linked by Phenylenediamines, Peptide Science 2007, 303-306, 2008.03.
58. K. Isozaki, J. Li, T. Nose, T. Costa, Y. Shimohigashi, The Molecular Mechanism of ORL1 Nociceptin Receptor in Activation: Residual Essential in the Sixth Transmembrane Domain, Peptide Science 2007, 289-292, 2008.03.
59. Y. Horiuchi, T. Nose, Y. Abe, Y. Shimohigashi, F. Morishita, Structural Analysis of Excitatory Neuropeptides TEP-1 and TEP-2 Isolated from the Prosobraanch Gastopod Thais clavigera, Peptide Science 2007, 273-276, 2008.03.
60. J. Li, K. Isozaki, A. Matsushima, T. Nose, T. Costa, Y. Shimohigashi, Optimization of the N-terminal Group of Ac-RYYRIL-NH2 as ORL1 Receptor Antagonist, Peptide Science 2007, 257-260, 2008.03.
61. I. Maeda, Y. Fukumoto, T. Nose, Y. Shimohigashi, T. Nezu, Y. Terada, H. Kodama, K. Kaibara, K. Okamoto, Structural Profiles for Coaservation of Elastin-derived Polypeptides, Peptide Science 2007, 219-222, 2008.03.
62. Jinglan Li, Kaname Isozaki, Kazushi Okada, Ayami Matsushima, Takeru Nose, Tommaso Costa and Yasuyuki Shimohigashia, Designed modification of partial agonist of ORL1 nociceptin receptor for conversion into highly potent antagonist, Bioorganic and Medicinal Chemistry, 16, 2635-2644, 2007.11.
63. K. Isozaki, K. Okada, S. Koikawa, T. Nose, T. Costa, and Y. Shimohigashi, Residual Roles of Hydrophobic Amino Acids in the Fifth Transmembrane Domain of ORL1 Receptor in Its Activation, Peptide Science 2006, 11, 2006.11.
64. J. Li, K. Isozaki, K. Okada, T. Nose, T. Costa, and Y. Shimohigashi, Synthesis of Pure Antagonist of ORL1 Nociceptin Receptor, Peptide Science 2006, 175, 2006.11.
65. T. Tokunaga, X. Liu, H. Okada, A. Mastushima, T. Nose, M. Shimohigashi, and Y. Shimohigashi, Conformation Change of α-Helix Peptide for Sensing of Deactivation of Nuclear Receptor: Immunoassay Using Polyclonal Antibody Specific for the C-terminal α-Helix 12 of Estrogen-related Receptor γ (ERRγ) , Peptide Science 2006, 177, 2006.11.
66. T. Tokunaga, H. Okada, T. Nose, and Y. Shimohigashi, Conformation Sensing Assay Using Polyclonal Antibody Specific for the C-terminal α-helix of Glucocorticoid Receptor and Progesterone Receptor, Peptide Science 2005, 291-294, 2006.03.
67. H. Okada, T. Tokunaga, N. Shirasu, T. Nose, and Y. Shimohigashi, α-Helix peptides for bio-panning in the phage display method to obtain the antibodies specific for conformation-change in nuclear receptors, Peptide Science 2005, 475-478, 2006.03.
68. K. Isozaki, J. Funama, T. Nose, T. Coosta, and Y. Shimohigashi, Continuous Activation of the δ-opioid Receptor by Affinity Labeling, Peptide Science 2005, 475-478, 2006.03.
69. J. Funama, K. Isozaki, T. Nose, T. Coosta, and Y. Shimohigashi, Enkephalin Dimers Cross-linked by Diaminobenzene for Homodimeric Opioid Receptors Expressed in COS-7 Cells, Peptide Science 2005, 475-478, 2006.03.
70. A. Matsushima, S. Yokotani, X.H. Lui, K. Sumida, T. Honda, S. Sato, A. Kaneki, Y. Takeda, Y. Chuman, M. Ozaki, D. Asai, T. Nose, H. Onoue, Y. Ito, Y. Tominaga, Y. Shimohigashi, and M. Shimohigashi, Molecular cloning and circadian expression profile of insect neuropeptide PDF in black blowfly, Phormia regina, Lett. Peptide Sci., 10.1007/BF02442573, 10, 5-6, 419-430, 10 (5-6), 419-430, 2004.05.
71. A. Matsushima, S. Sato, Y. Chuman, Y. Takeda, S. Yokotani, T. Nose, Y. Tomioka, M. Shimohigashi, and Y. Shimohigashi, cDNA Cloning of the Housefly Pigment-Dispersing Factor (PDF) Precursor Protein and Its Peptide Comparison among the Insect Circadian Neuropeptides, J. Peptide Sci., 10.1002/psc.511, 10, 2, 82-91, 10 (2) 82-91, 2004.02.
72. Y. In, S. Kishima, K. Minoura, T. Nose, Y. Shimohigashi, and T. Ishida, Aggregation feature of fluorine-substituted benzene rings and intermolecular C-H center dot center dot center dot F interaction: Crystal structure analyses of mono- and trifluoro-L-phenylalanines, Chem. Pharm. Bull.,, 10.1248/cpb.51.1258, 51, 11, 1258-1263, 51 (11), 1258-1263, 2003.11.
73. K. Isozaki, H. Fukahori, T. Honda, N. Shirasu, K. Okada, T. Nose, K. Sakaguchi, and Y. Shimohigashi, Site-directed affinity-labeling of delta opioid receptors by SNpys-containing enkephalin and dynorphin analogues, Lett. Peptide Sci.,, 10.1007/BF02442583, 10, 5-6, 511-522, 10 (5-6), 511-522, 2003.05.
74. M. Kawano, K. Okada, T. Honda, T. Nose, K. Sakaguchi, T. Costa, and Y. Shimohigashi, Structural Requirements of Nociceptin Antagonist Ac-RYYRIK-NH2 for Receptor Binding, J. Peptide Sci.,, 10.1002/psc.415, 8, 10, 561-569, 8 (10), 561-569, 2002.10.
75. A. Tani, T. Ogawa, T. Nose, N. N. Nikandrov, M. Deshimaru, T. Chijiwa, C.-C. Chang, Y. Fukumaki, and M. Ohno, Characterization, Primary Structure and Molecular Evolution of Anticoagulant Protein from Agkistrodon actus Venom, Toxicon, 10.1016/S0041-0101(01)00289-6, 40, 6, 803-813, 40 (6) 803-813, 2002.06.
76. A. Matsushima, T. Fujita, K. Okada, N. Shirasu, T. Nose, and Y. Shimohigashi, Exploration of the Role of Phenylalanine in the Thrombin Receptor Tethered-Ligand by Substitution with a Series of Trifluorophenylalanines, Bull. Chem. Soc. Jpn., 10.1246/bcsj.73.2531, 73, 11, 2531-2538, 73(11), 2531-2538, 2000.11.
77. K. Okada, T. Sujaku, Y. Chuman, R. Nakashima, T. Nose, T. Costa, Y. Yamada, M. Yokoyama, A. Nagahisa, and Y. Shimohigashi, Highly potent Nociceptin Analog Containing the Arg-Lys Triple Repeat, Biochem. Biophys. Res. Commun., 10.1006/bbrc.2000.3822, 278, 2, 493-498, 278(2), 493-498, 2000.11.
78. H. Kawasaki, T. Nose, T. Muta, S. Iwanaga, Y. Shimohigashi, and S. Kawabata, Head-to-Tail Polymerization of Coagulin, a Clottable Protein of the Horseshoe Crab, J. Biol. Chem., 10.1074/jbc.M006856200, 275, 45, 35297-35301, 275(45), 35297-3530, 2000.11.
79. T. Honda, N. Shirasu,Y. Chuman, K. Okada, T. Fujita, T. Nose, and Y. Shimohigashi, The Role of Deltorphin II Phenylalanine Residue in Binding to the δ Opioid Receptor, Bull. Chem. Soc. Jpn., 10.1246/bcsj.73.2549, 73, 11, 2549-2552, 73(11), 2549-2552, 2000.11.
80. T. Fujita, T. Nose, A. Matsushima, K. Okada, D. Asai, Y. Yamauchi, N. Shirasu, T. Honda, D. Shigehiro, and Y. Shimohigashi, Synthesis of a Complete Set of L-difluorophenylalanines, L-(F-2)Phe, as Molecular Explorers for the CH/π Interaction between Peptide Ligand and Receptor , Tetrahedron Lett., 10.1016/S0040-4039(99)02191-7, 41, 6, 923-927, 41(6), 923-927, 2000.06.
81. A. Matsushima, T. Fujita, T. Nose, and Y. Shimohigashi, Edge-to-face CH/π Interaction between Ligand Phe-phenyl and Receptor Aromatic Group in the Thrombin Receptor Activation, J. Biochem., 128, 2, 225-232, 128(2), 225-232, 2000.02.
82. D. Asai, Y. Tahara, M. Nakai, Y. Yakabe, M. Takatsuki, T. Nose, T. Shinmyozu, and Y. Shimohigashi, Structural Essentials of Xenoestrogen Dialkyl Phthalates to Bind to the Estrogen Receptors, Toxicology Lett., 10.1016/S0378-4274(00)00253-8, 118, 1-2, 1-8, 118(1-2), 1-8 (2000)., 2000.01.
83. K. Okada, T. Sujaku, R. Nakashima, T. Nose, Y. Yamada, M. Yokoyama, A. Nagahisa, and Y. Shimohigashi, Effects of Substitution of Hydrophobic Amino Acid by Tryptophan on Receptor Binding and Biological Activity of Neuropeptide Nociceptin, Bull. Chem. Soc. Jpn., 10.1246/bcsj.72.1899, 72, 8, 1899-1904, 72(8), 1899-1904, 1999.08.
84. Y. Shimohigashi, T. Nose, Y. Yamauchi, and I. Maeda, Design of Serine Protease Inhibitors with Conformation Restricted by Amino Acid Side Chain-Side Chain CH/π Interaction, Biopolymers, 10.1002/(SICI)1097-0282(1999)51:1<9::AID-BIP3>3.0.CO;2-5, 51, 1, 9-17, 51, 9-17., 1999.06.
85. S. Tanabe, Y. Shimohigashi, Y. Nakayama, T. Makino, T. Fujita, T. Nose, G. Tsujimoto, T. Yokokura, M. Naito, T. Tsuruo, and T. Terasaki, In Vivo and In Vitro Evidences of Blood-Brain Barrier Transport of a Novel Cationic Arginine-Vasopressin Fragment 4-9 Analogue, J. Pharmacol. Exp. Ther.,, 290, 2, 561-568, 290(2), 561-568, 1999.08.
86. T. Fujita, M. Nakajima, Y. Inoue, T. Nose, and Y. Shimohigashi, A novel Molecular Design of Thrombin Receptor Antagonist, Bioorg. Med. Chem. Lett., 10.1016/S0960-894X(99)00202-4, 9, 10, 1351-1356, 9, 1351-1356, 1999.05.
87. T. Fujita, T. Nose, M. Nakajima, Y. Inoue, T. Costa, and Y. Shimohigashi, Design and Syntheses of para-Fluorophenylalanine Amide Derivatives as Thrombin Receptor Antagonist, J. Biochem., 126, 1, 174-179, 126(1), 174-179, 1999.01.
88. N. Shirasu, T. Kuromizu, H. Nakao, Y. Chuman, T. Nose, T. Costa, and Y. Shimohigashi, Exploration of Universal Cysteines in the Binding Site of Three Opioid Receptor Subtypes by Disulfide-Bonding Affinity Labeling with Chemically Activated Thiol-containing Dynorphin A Analogs, J. Biochem.,, 126, 1, 254-259, 126(1), 254-259, 1999.01.
89. Nose, T., Satoh, Y., Fujita, T., Ohno, M., Nakajima, M., Inoue, Y., Ogino, Y., Costa, T., and Shimohigashi, Y, The Role of Arginine in Thrombin Receptor Tethered-Ligand Peptide in Intramolecular Receptor Binding and Self-activation, Bull. Chem. Soc. Jpn.,, 10.1246/bcsj.71.1661, 71, 7, 1661-1665, 71(7), 1661-1665, 1998.07.
90. A. Kashima, Y. Inoue, S. Sugio, I. Maeda, T. Nose, and Y. Shimohigashi, X-ray Crystal Structure of a Dipeptide-Chymotrypsin Complex in an Inhibitory Interaction, Eur. J. Biochem., 10.1046/j.1432-1327.1998.2550012.x, 255, 1, 12-23, 255(1), 12-23, 1998.07.
91. T. Nose, T. Fujita, M. Nakajima, Y. Inoue, T. Costa, and Y. Shimohigashi, Interaction Mode of the Phe-phenyl Group of Thrombin Receptor Tethered-ligand SFLLRNP in Receptor Activation, J. Biochem., 124, 2, 354-358, 124(2), 354-358, 1998.02.
92. I. Maeda, S. Taniguchi, J. Ebina, N. Watanabe, T. Hattori, T. Nose, Comparison between Coacervation Property and Secondary Structure of Synthetic Peptides, Ile-containing Elastin-derived Pentapeptide Repeats, Protein and Peptide Letters.