新潟大学理学部化学科生物化学研究室 中馬研究室

業績Publication

学術論文

  • Mizunuma, M., Suzuki, M., Kobayashi, T., Hara, Y., Kaneko, A., Furukawa, K., and Chuman, Y.*. Development of Mn2+-specific Biosensor Using G-quadruplex-based DNA. Int. J. Mol. Sci., 24(14), 11556, (2023), https://doi.org/10.3390/ijms241411556
  • Ikeura, M., Tashiro, H., Yamagata, Y., Saito, H., Kobayashi, T., Mizunuma, M., Yamazaki, K., Baba, K. Furukawa, K. and Chuman, Y.*. Development of Antibody-like Proteins Targeting the Oncogenic Ser/Thr Protein Phosphatase PPM1D. Processes, 10(8), 1501, (2022)
  • Mizunuma, M. †, Kaneko, A†., Imai, S., Furukawa, K. and Chuman, Y. Methods for Identification of Substrates/Inhibitors of FCP/SCP Type Protein Ser/Thr Phosphatases. Processes, 8(12), 1598, (2020)
  • Kaneko, A., Watari, M., Mizunuma, M., Saito, H., Furukawa, K. and Chuman, Y. Development of Specific Inhibitors for Oncogenic Phosphatase PPM1D by Using Ion-Responsive DNA Aptamer Library. Catalysts, 10(10), 1153, (2020)
  • Yoshida, T., Yamazaki, K., Imai, S., Banno, A., Kaneko, A., Furukawa, K. and Chuman, Y. Identification of a Specific Inhibitor of Human Scp1 Phosphatase Using the Phosphorylation Mimic Phage Display Method. Catalysts, 9(10), 842, (2019)
  • Ogasawara, S., Chuman, Y., Michiba, T., Kamada, R., Imagawa, T. and Sakaguchi, K. Inhibition of protein phosphatase PPM1D enhances retinoic acid-induced differentiation in human embryonic carcinoma cell line. J. Biochem., 165(6), 471-477, (2019)
  • Otsubo, K., Yoneda, T., Kaneko, A., Yagi, S., Furukawa, K., and Chuman, Y. Development of a Substrate Identification Method for Human Scp1 Phosphatase Using Phosphorylation Mimic Phage Display. Protein Pept. Lett. 25(1), 76-83. (2018)
  • Uchino, R., Sugiyama, S., Katagiri, M., Chuman, Y., and Furukawa, K. Non-farnesylated B-type lamin can tether chromatin inside the nucleus and its chromatin interaction requires the Ig-fold region. Chromosoma, 126(1),125-144. (2017) DOI 10.1007/s00412-016-0581-x
  • Kozakai, K., Kamada, R., Furuta, J., Kiyota, Y., Chuman, Y., and Sakaguchi, K. PPM1D controls nucleolar formation by up-regulating phosphorylation of nucleophosmin. Sci. Rep., 6, 33272. doi: 10.1038/srep33272 (2016)
  • Sakai, H., Watanabe, K., Kudoh, F., Kamada, R., Chuman, Y., Sakaguchi, K. Patterning nanofibrils through the templated growth of multiple modified amyloid peptides. Sci Rep. 6, 31993. doi: 10.1038/srep31993 (2016)
  • Kamada, R., Tano F., Kudoh, F., Kimura, N., Chuman, Y., Osawa, A., Namba, K., Tanino, K., Sakaguchi, K. Effective cellular morphology analysis for differentiation processes by a fluorescent 1,3a,6a-triazapentalene derivative probe in live cells. PLOS ONE, 11(8):e0160625
  • Ogasawara, S., Kiyota, Y., Chuman, Y., Kowata, A., Yoshimura, F., Tanino, K., Kamada, R., and Sakaguchi, K. Novel Inhibitors Targeting PPM1D Phosphatase Potently Suppress Cancer Cell Proliferation. Bioorg. Med. Chem., 23(19), 6246-6249, (2015) DOI: 10.1016/j.bmc.2015.08.042
  • Namba, K., Osawa, A., Nakayama, A., Mera, A., Tano, F., Chuman, Y., Sakuda, E., Taketsugu, T., Sakaguchi, K., Kitamura, N., and Tanino, K. Synthesis of Yellow and Red Fluorescent 1,3a,6a-Triazapentalene and Theoretical Investigation of Optical Properties. Chem. Sci., 6, 1083-1093, (2015) DOI: 10.1039/C4SC02780A
  • Xaviera, C.P., Melikova, M., Chuman, Y., Üren, A., Baljinnyam, B., Rubin, J.S. Secreted Frizzled-Related Protein Potentiation versus Inhibition of Wnt3a/β-catenin Signaling. Cell. Signal. 26,94-101, (2014)DOI: 10.1016/j.cellsig.2013.09.016
  • Chuman, Y., Ueyama, M., Sano, S, Wu, F, Kiyota, Y., Higashi, T., Osada, S., and Sakaguchi, K. Effects of E/Z Configuration of Fluoroalkene-containing HDAC Inhibitors on Selectivity for HDAC Isoforms. Chem. Lett. 42(8), 833-835, (2013) DOI: 10.1246/cl.130243
  • Sakai, H., Watanabe, K., Asanomi, Y., Kobayashi, Y., Chuman, Y., Shi, L., Masuda, T., Wyttenbach, T., Bowers, M.T., Uosaki, K., and Sakaguchi, K. Formation of Functionalized Nanowires by Control of Self-Assembly Using Multiple Modified Amyloid Peptides. Adv. Funct. Mater. 23(39), 4881-4887, (2013) DOI: 10.1002/adfm.201300577
  • Wada, J., Kamada, R., Imagawa, T., Chuman, Y., and Sakaguchi, K. Inhibition of tumor suppressor protein p53-dependent transcription by a tetramerization domain peptide via hetero-oligomerization Bioorg. Med. Chem. Lett. 22(8), 2780-2783, (2012) DOI: 10.1016/j.bmcl.2012.02.085
  • Yagi, H., Chuman, Y., Kozakai, Y., Imagawa, T., Takahashi, Y., Yoshimura, F., Tanino, K., and Sakaguchi, K. A Small Molecule Inhibitor of p53-inducible Protein Phosphatase PPM1D. Bioorg. Med. Chem. Lett. 22(1), 729-732, (2012) DOI: 10.1016/j.bmcl.2011.10.084
  • Chuman, Y., Iizuka, K., Honda, T., Onoue, H., Shimohigashi, Y., and Sakaguchi, K. Phosphatase assay for multi-phosphorylated substrates using phosphatase specific-motif antibody. J. Biochem., 150(3), 319–325, (2011) DOI: 10.1093/jb/mvr056
  • Martin-Manso, G., Calzada, M.J., Chuman, Y., Sipes, J.M., Xavier, C.P., Wolf, V., Kuznetsova, S.A., Rubin, J.S., and Roberts, D.D. sFRP-1 binds via its netrin-related motif to the N-module of thrombospondin-1 and blocks thrombospondin-1 stimulation of MDA-MB-231 breast carcinoma cell adhesion and migration. Arch. Biochem. Biophys., 509(2), 147-156, (2011) DOI: 10.1016/j.abb.2011.03.004
  • Nomura, T., Kamada, R., Ito, I., Sakamoto, K., Chuman, Y., Ishimori, K., Shimohigashi, Y., and Sakaguchi, K. Probing phenylalanine environments in oligomeric structures with pentafluorophenylalanine and cyclohexylalanine. Biopolymers, 95(6), 410-419, (2011) DOI: 10.1002/bip.21594
  • Kamada, R., Yoshino, W., Nomura, T., Chuman, Y., Imagawa, T., Suzuki, T., Sakaguchi, K. Enhancement of transcriptional activity of mutant p53 tumor suppressor protein through stabilization of tetramer formation by calix[6]arene derivatives. Bioorg. Med. Chem Lett., 20(15), 4412-4415, (2010) DOI: 0.1016/j.bmcl.2010.06.053
  • Asanomi, Y., Kobayashi, Y., Sakai, H., Masuda, T., Chen, X., Chuman, Y., Uosaki, K., Sakaguchi, K. Drastic Effects on Fibril Formation of Amyloid-beta Peptides by the Addition of Amino Acid Residue Units to the Termini Protein Pept. Lett.. 17(4), 458-463, (2010) DOI: 10.2174/092986610790963618
  • Osada, S., Sano, S., Ueyama, M., Chuman, Y., Kodama, H., and Sakaguchi, K. Fluoroalkene Modification of Mercaptoacetamide-based Histone Deacetylase Inhibitors Bioorg. Med. Chem. 18(2), 605-611, (2010) DOI: 10.1016/j.bmc.2009.12.005
  • Chuman, Y., Kurihashi, W., Mizukami, Y., Nashimoto, T., Yagi, H., and Sakaguchi, K. PPM1D430, a novel alternative splicing variant of the human PPM1D, can dephosphorylate p53 and exhibits specific tissue expression. J. Biochem., 145(1), 1-12, (2009) DOI: 10.1093/jb/mvn135
  • Kamada, R., Terai, T., Nomura, T., Chuman, Y., Imagawa, T., Sakaguchi, K. Effects of tumor-associated mutations in the p53 tetramerization domain on oligomerization state and transcriptional activity. Adv. Exp. Med. Biol., 611, 567-568, (2009).
  • Nomura, T., Kamada, R., Ito, I., Chuman, Y., Shimohigashi, Y., and Sakaguchi, K. Oxidation of methionine residue at hydrophobic core destabilizes p53 tetrameric structure. Biopolymers, 91(1), 78-84, (2009) DOI: 10.1002/bip.21594
  • Chuman, Y., Yagi, H., Fukuda, T., Nomura, T., Matsukizono, M., Shimohigashi, Y., and Sakaguchi K. Characterization of the Active Site and a Unique Uncompetitive Inhibitor of the PPM1-type Protein Phosphatase PPM1D. Protein Pept. Lett., 15, 938-948, (2008) DOI: 10.2174/092986608785849236
  • Polley, S., Guha, S., Roy, N.S., Kar, S., Sakaguchi, K., Chuman, Y., Swaminathan, V., and Roy, S. Differential Recognition of Phosphorylated Transactivation Domains of p53 by Different p300 Domains. J. Mol. Biol., 376, 8-12, (2008) DOI: 10.1016/j.jmb.2007.11.082
  • Honda, T., Shirasu, N., Isozaki, K., Kawano, M., Shigehiro, D., Chuman,Y., Fujita, T., Nose, T., and Shimohigashi, Y. Differential receptor binding characteristics of consecutive phenylalanines in m-opioid specific peptide ligand endomorphin-2. Bioorg. Med. Chem., 15, 3883-3888(2007) DOI: 10.1016/j.bmc.2007.03.009
  • Honda, T., Matsushima, A., Sumida, K., Chuman, Y., Sakaguchi, K., Onoue, H., Meinertzhagen, I.A., Shimohigashi, Y., 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. J. Comp. Neurol., 499, 404-421, (2006) DOI: 10.1002/cne.21112
  • Ambrosio, C., Molinari, P., Fanelli, F., Chuman, Y., Sbraccia, M., Ugur, O., and Costa, T. Different structural requirements for the constitutive and the agonist-induced activities of the beta 2-adrenergic receptor. J. Biol. Chem., 280, 23464-23474 (2005) DOI: 10.1074/jbc.M502901200
  • Chuman, Y., Uren, A., Cahill, J., Regan, C., Wolf, V., Kay, B.K., and Rubin, J.S. Identification of a peptide binding motif for secreted Frizzled-related protein-1. Peptides, 25, 1831-1838 (2004) DOI: 10.1016/j.peptides.2004.07.010
  • Häusler, K.D., Horwood, N.J., Chuman, Y., Fisher, J. L., Ellis, J., Martin, T.J., and Rubin, J.S., and Gillespie, M.T. Secreted Frizzled-Related Protein-1 Inhibits RANKL-Dependent Osteoclast Formation. J. Bone Miner. Res., 19, 1873-1881 (2004) DOI: 10.1359/JBMR.040807
  • 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. Zoolog, Sci., 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. J. Pept. Sci., 10, 82-91 (2004) DOI: 10.1002/psc.511
  • 2003年以前

  • Sato, S., Chuman, Y., Matsushima, A., Tominaga, Y., Shimohigashi, Y., Shimohigashi, M. A Circadian Neuropeptide, Pigment-Dispersing Factor-PDF, in the Last-Summer Cicada Meimuna opalifera: cDNA Cloning and Immunocytochemistry. Zoolog. Sci., 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 circadian neuropeptide designated as pigment-dispersing factor PDF in the cricket Gryllus bimaculatus. J. Biochem. 131, 895-903 (2002).
  • Okada, K., Sujaku, T., Chuman, Y., Nakashima, R., Nose, T., Costa, T., Yamada, Y., Yokoyama, M., Nagahisa, A., and Shimohigashi, Y. Highly potent nociceptin analog containing the Arg-Lys triple repeat. Biochem. Biophys. Res. Commun., 278, 493-498 (2000).
  • Honda, T., Shirasu, N., Chuman, Y., Okada, K., Fujita, T., Nose, T., and Shimohigashi, Y. The role of deltorphin II phenylalanine residue in binding to the d opioid receptor. Bull. Chem. Soc. Jpn., 73 (11), 2549-2552 (2000).
  • Chuman, Y., Nobuhisa, I., Ogawa, T., Deshimaru, M., Chijiwa, T., Tan, NH., Fukumaki, Y., Shimohigashi, Y., Ducancel, F., Boulain, JC., Menez, A., and Ohno, M. Regional and accelerated molecular evolution in group I snake venom gland phospholipase A2 isozymes. Toxicon, 38, 449-462 (2000).
  • Shirasu, N., Kuromizu. T., Nakao, H., Chuman, Y., Nose, T., Costa, T., and Shimohigashi, Y. Exploration of universal cysteines in the binding sites of three opioid receptor subtypes by disulfide-bonding affinity labeling with chemically activated thiol-containing dynorphin A analogs. J. Biochem., 126, 254-259 (1999).
  • Nobuhisa, I., Ogawa, T., Deshimaru, M., Chijiwa, T., Nakashima, K., Chuman, Y., Shimohigashi, Y., Fukumaki, Y., Hattori, S., and Ohno, M. Retrotransposable CR1-like elements in crotalinae snake genomes. Toxicon, 36, 915-920 (1998).
  • Chuman, Y., Yasunaga, T., Costa, T., and Shimohigashi, Y. Discrimination of a novel type of rat brain d opioid receptors by enkephalin analog containing structurally constrained cyclopropylphenylalanine (▽Phe). Biochem. Mol. Biol. Int., 42, 1227-1233 (1997).

著書,編書,翻訳書

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  • アプタマー創薬の現状と細胞膜 自動透過性DNAアプタマーの開発
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    月刊「細胞」,52 (5), 50-52, (2020) ISBN: 04127-05
  • 発がん関連酵素に対するDNAアプタマーを用いた新規阻害剤開発と応用
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    月刊「細胞」,51(3), 38-41, (2019)
  • 核酸アプタマーを用いた発がん関連酵素に対する新規阻害剤開発と応用
    金子 敦巳, 亘 美佑, 水沼 正昂, 中馬 吉郎
    アグリバイオ,2(13), 88-90, (2018), ISSN: 24325511
  • 発がん関連Ser/Thrホスファターゼに対する新規阻害剤と基質同定法の開発
    八木 誠也,金子 敦巳, 山崎 一樹,吉田 拓弥, 中馬 吉郎
    BIO Clinica, 33(6), 90-92, (2018) ISBN: 17601-06
  • 発がん関連Ser/Thrホスファターゼに対する新規阻害剤の開発
    金子 敦巳, 中馬 吉郎
    BIO Clinica, 33(1), 51-53, (2018)
  • Kaneko, A., Furukawa, K., Sakaguchi, K., and Chuman, Y. Inhibition of Oncogenic Phosphatase PPM1D by G-quadruplex DNA Aptamer in Cancer Cells. Peptide Sci. 2016, 23-24, (2017)
  • Yagi, S., Yoneda, T., Otsubo, K., Furukawa, K., and Chuman, Y., Characterization of Enzymatic Activity of FCP/SCP Type Ser/Thr Phosphatase Family. Peptide Sci. 2016, 225-226, (2017)
  • Otsubo, K., Furukawa K, Chuman, Y. Development of the Novel Substrate Identification Methodology for Ser/Thr Phosphatases Using Phosphorylation Mimic Phage Display Library. Peptide Sci. 2015, 271-272, (2016)
  • Kaneko, A., Eguchi, M., Furukawa, K., Kiyota, Y., Sakaguchi, K., and Chuman, Y., In Vitro Selection of G-quadruplex DNA Aptamers Targeting Ser/Thr Phosphatase PPM1D430. Peptide Sci. 2015, 315-316, (2016)
  • がん原遺伝子産物PPM1Dの細胞がん化機構および創薬を指向した阻害剤
    鎌田 瑠泉,中馬 吉郎,小境 夕紀,坂口 和靖
    生化学, 87(5), 531‒538(2015)
  • Sakaguchi, T., Janairo, J.I., Chuman, Y., Hara, K., Fukuoka, A., and Sakaguchi, K. Silver nanocrystals formed by oligomeric biomineralization peptide via p53 tetramerization domain. Peptide Sci. 2012, 57-58, (2013)
  • Shirahata, Y., Chuman, Y., Iwamuro, R., Janairo, J.I., Kiyota, Y., Yagi, H., Sakaguchi, K. Analysis of substrate preference of human PPM1 type Ser/Thr phosphatases. Peptide Sci. 2012, 403-404, (2013)
  • Sakai, H., Watanabe, K., Chuman, Y., Uosaki, K., Sakaguchi, K. Formation of functionalized nanowires using structure-controllable amyloid peptides. Peptide Sci. 2011, 23-24, (2012)
  • Kozakai, Y., Yagi, H., Teduka, Y., Chuman, Y., Sakaguchi, K. Analysis of interaction between p53 inducible protein phosphatase PPM1D and nucleolar protein. Peptide Sci. 2011, 43-44, (2012)
  • Janairo, J.I., Iwamuro, R., Kaya, S., Yagi, H., Chuman, Y., Imagawa, T., Sakaguchi, K. Probing the differential phosphothreonine and metal selectivity of human PPM1 phosphatase family. Peptide Sci. 2011, 245-246, (2012)
  • Wada, J., Kamada, R., Chuman, Y., Imagawa, T., Sakaguchi, K. Repression of p53 transcriptional activity by inhibitory peptide via heterotetramerization. Peptide Sci. 2011, 301-302, (2012)
  • Sakaguchi, T., Kamada, R., Chuman, Y., Sakaguchi, K. Nanostructure formed by biomineralization peptide oligomerized via p53 tetramerization. Peptide Sci. 2011, 345-346, (2012)
  • Yagi, H., Chuman, Y., Kozakai, Y., Imagawa, T., Sakaguchi, K. Involvement of PPM1D specific Pro-loop in regulatory mechanism of PPM1D phosphatase activity Peptide Sci. 2011, 373-374, (2012)
  • Sakai, H., Watanabe, K, Chuman, Y., Uosaki, K , Sakaguchi, K. Effective method for formation of functionalized nanowires using amyloid peptides. Abstracts of Papers of The American Chemical Society. 241, 237-INOR(2011)
  • Yagi, H., Chuman, Y., Yoshimura, F., Tanino, K., Sakaguchi, K. Novel chemical inhibitors specific for p53-inducible protein phosphatase PPM1D. Abstracts of Papers of The American Chemical Society. 241, 214-MEDI(2011)
  • Kamada, R., Nomura, T., Chuman, Y., Imagawa, T., Anderson, C.W. and Sakaguchi, K. Low threshold of destabilization for loss of tumor suppressor activity of p53: A quantitative analysis of p53 tetramelization domain mutants. Peptide Sci.2010, 149, (2011)
  • Sakai, H., Watanabe, K., Chuman, Y., and Sakaguchi, K. Controlling initiation position of amyloid nanowire using a gold nanoparticle. Peptide Sci.2010, 276, (2011)
  • Kozakai, Y., Yagi, H., Chuman, Y., Imagawa, T., and Sakaguchi, K. Dephosphorylation of nuclear protein nucleophosmin by protein phosphatase PPM1D. Peptide Sci.2010, 92, (2011)
  • Wada, J., Kamada, R., Chuman Y., Imagawa, T., and Sakaguchi, K. Repression of p53 transcriptional activity by p53 tetremerization domain peptide containing PTD and NLS domain. Peptide Sci.2010, 95, (2011)
  • Yagi, H., Chuman, Y., and Sakaguchi, K. Characterization of Two Novel and Potent Inhibitors Specific for p53-Inducible Protein Phosphatase PPM1D. Peptide Sci.2009, 455-456, (2010)
  • Sakaguchi, T., Kamada, R., Nomura, T., Chuman, Y., Imagawa, T., and Sakaguchi, K. Biomineralization Activity of Multivalent minTBP-1 Peptide Mediated by p53 Tetramerization Domain. Peptide Sci.2009, 411-412, (2010)
  • Watanabe, K., Sakai, H., Chen, X., Chuman, Y., and Sakaguchi, K. Development of Probed-SCAP Directed at Thiol Groups. Peptide Sci.2009, 407-408, (2010)
  • Kamada, R., Oshima, S., Chuman, Y., Imagawa, T., and Sakaguchi, K. Inhibition of p53 by Introducing Tetramerization Domain Peptide Fused with Polyvalent Cationic Sequence into Cells. Peptide Sci.2009, 319-320, (2010)
  • Chuman, Y., Kurihashi, W., Mizukami, Y., Nashimoto, T., Yagi, H., and Sakaguchi, K. PPM1D430, a Novel Alternative Splicing Variant of the Human PPM1D. Peptide Sci.2008, 531-532 (2009)
  • Nomura, T., Kamada, R., Chuman, Y., and Sakaguchi, K. Thermal Stability of p53 Tetramerization Domain Peptides Derived from Various Species. Peptide Sci.2008, 35-36 (2009)
  • Yagi, H., Chuman, Y., Yoshimura, F., Tanino, K., and Sakaguchi, K. Identification of Novel Chemical Inhibitors for p53-Inducible Protein Phosphatase PPM1D. Peptide Sci.2008, 385-386 (2009)
  • Sakai, H., Asanomi, Y., Kobayashi, Y., Chen, X., Chuman, Y., Masuda, T., Uosaki, K., and Sakaguchi, K. Extremely Long Nanofibrils of Functionalized Structure-Controlled-Amyloid Peptides Derived from Transthyretin. Peptide Sci.2008, 465-466 (2009)
  • Kamada, R., Terai, T., Nomura, T., Chuman, Y., Imagawa, T., and Sakaguchi, K. Correlation of Oligomeric Structure and Transcriptional Activity of p53 Mutants. Peptide Sci.2007, 69-70 (2008)
  • Nomura, T., Kamada, R., Chuman, Y., and Sakaguchi, K. Screening of Peptides to Stabilize the p53 Tetramer Formation from Phage Displayed Library. Peptide Sci.2007, 315-316 (2008)
  • Miyazaki, H., Kamada, R., Nomura, T., Chuman, Y., Imagawa, T., and Sakaguchi, K. Correlation between Expression Level in E. coli and Stability of Oligomeric Structure of the p53 Tetramerization Domain. Peptide Sci.2007, 317-318 (2008)
  • Kamada, R., Fukuda, K., Miyazaki, H., Nomura, T., Chuman, Y., Imagawa, T., Tanino, K., and Sakaguchi, K. Structural Photomodulation of Peptides with Azobenzoate Derivative in Peptide Backbone. Peptide Sci.2007, 447-448 (2008)
  • Chuman, Y., Fukuda, T., Yagi, H., and Sakaguchi, K. Function of Basic Loop in Substrate Recognition of Protein Phosphatase PPM1D. Peptide Sci.2006, 17-18 (2007)
  • Nomura, T., Chuman, Y., and Sakaguchi, K. Stabilization of p53 Tetrameric Structure by Polyol Compounds. Peptide Sci.2006, 131-132 (2007)
  • Kamada, R., Terai, T., Nomura, T., Chuman, Y., Imagawa, T., and Sakaguchi, K. Thermodynamic Stability of Mutant p53 Tetramerization Domain Peptides Associated with Human Tumors. Peptide Sci.2006, 293-294 (2007)
  • Fukuda, T., Chuman, Y., and Sakaguchi, K. Substrate Recognition of PP2C Family Phosphatase PPM1D. Peptide Sci.2005, 503-504 (2006)
  • Iizuka, K., Chuman, Y., Honda, T., Onoue, H., Shimohigashi, Y., and Sakaguchi, K. Characterization and Application of Monoclonal Antibody Specific for Ser(P)-Gln Phosphorylation Motif. Peptide Sci.2005, 499-502 (2006)
  • Nomura, T., Sakamoto, K., Kasai, Y., Chuman, Y., Ishimori, K., and Sakaguchi, K. Analysis of Stabilization by Substitution of Cyclohexylalanine for Phe341 in Hydrophobic Core of p53 Tetramer. Peptide Sci.2005, 399-402 (2006)
  • Asanomi, Y., Higashimoto, Y., Chuman, Y., Kaya, S., Imagawa, T., and Sakaguchi, K. Fibrillar and Granular Aggregation of G334V Mutant p53 Tetramer Peptide. Peptide Sci.2005, 397-398 (2006)
  • Nomura, T., Ito, I., Chuman, Y., Shimohigashi, Y., and Sakaguchi, K. Charactarization of superstable variant peptideof human p53 tetramerization domain. Peptide Sci.2004, 423-426 (2005)
  • Kasai, Y., Kaya, S., Chuman, Y., and Sakaguchi, K. Stability and folding mechanism for Trp-contaning peptides of p53 tetramerization domain. Peptide Sci.2004, 419-422 (2005)
  • Yamamoto, T., Chuman, Y., Kaya, S., Imagawa, T., and Sakaguchi, K. DNA binding of peptide with single helix-hairpin-helix motif. Peptide Sci.2004, 517-520 (2005)
  • Asanomi, Y., Takakusagi, S., Chuman, Y., Kaya, S., Imagawa, T., Uosaki, K., and Sakaguchi, K. Mechanism of amyloid-like fibrillar aggregation of mutant peptide of p53 tetramerization domain. Peptide Sci.2004, 313-316 (2005)
  • Takeda, Y., Shirasu, N., Sato, S., Matsushima, A., Chuman, Y., Tominaga, Y., Shimohigashi, M., and Shimohogashi, Y. Triplicate Alternative Splicings that Produce Multiple Variants of the PERIOD Protein in the Silk Moth Bombym mori by Deletion/Insertion of Peptides. Peptide Sci.2004, 203-206 (2005)
  • Chuman, Y., Üren, A., Häusler, K.D., Horwood, N.J., Ellis J., Lengel, C., Wolf, V., Gillespie, M.T., Kay, B., and Rubin, J.S. Identification of Novel Binding Motif for Secreted Frizzled-Related Protein-1. Peptide Sci.2004, 91-94 (2005)
  • Honda, T., Chuman, Y., Matsushima, T., Asai, D., Sumida, K., 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 Sci.2003, 81-84 (2004)
  • Okada, K., Kawano, M., Isozaki, K., Chuman, Y., Fujita, T., Nose, T., Costa, T., and Shimohigashi, Y. Identification of receptor residues functioning for activation of ORL1 nociceptin receptor by site-directed mutagenesis. Peptide Sci.2002, 261-264 (2003)
  • Honda, T., Chuman, Y., Matushima, A., Asai, D., Nose, T., Sakaguchi, K., Onoue, H., Tominaga, Y., Shimohigashi, Y., and Shimohigashi, M. Localization profiles of the precursor protein of circadian rhythm pacemaker hormone PDF in Gryllus brain. Peptide Sci. 2002, 433-436 (2003)
  • Kawano, M., Okada, K., Kim1, YH., Honda, T., Fujita, T., Chuman, Y., Nose, T., Costa, T., and Shimohigashi, Y. The attempt to identify the binding sites of nociceptin antagonist Ac-RYYRIK-NH2 in ORL1 receptor. Peptide Sci.2002, 253-256 (2003)
  • Asai, D., Tokunaga, T., Matsushima, A., Sato, S., Chuman, Y., Nose, T., Tominaga, Y., Shimohigashi, Y., and Shimohigashi, M. Design and preparation of universal anti-PERIOD antibodies and their immunoresponses. Peptide Sci.2001, 399-402 (2002).
  • Kawano, M., Honda, T., Okada, K., Chuman, Y., Nose, T., Sakaguchi, K., Costa, T., and Shimohigashi, Y. Structure-activity studies on the Nociceptine peptidic antagonist Ac-RYYRIK-NH2. Peptide Sci.2001, 185-188 (2002).
  • Tokunaga, T., Ohtani, M., Matsushima, A., Chuman, Y., Nose, T., Shimohigashi, M., Aimoto, S., and Shimohigashi, Y. Contractile activity of Drosophila FMRFamide-related peptides in the Meretrix lusoria heart muscle. Peptide Sci.2001, 167-170 (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 hormonepeptide receptor. Peptide Sci.2001, 159-162 (2002).
  • Fujita, T., Fukahori, F., Tokunaga, T., Chuman, Y., Riitano, D., Nose, T., Costa, T., and Shimohigashi, Y. Receptor binding site for the Phe-2-phenyl group of thrombin receptor-tehered ligand peptide:analyses by Ala/Thr mutant receptor. Peptide Sci.2001, 157-158 (2002).
  • Sato, S., Matsushima, A., Chuman, Y., Tominaga, Y., Shimohigashi, Y., and Shimohigashi, M. cDNA cloning of PDF peptide precursors in house fly and last summer cicada. Peptide Sci.2001, 139-142 (2002).
  • Okada, K., Chuman, Y., Fujita, T., Kawano, M., Nose, T., Costa, T., and Shimohigashi, Y. Identification of receptor binding site of Nociceptin-14-15, the residue for high receptor potentiation. Peptide Sci.2001, 109-112 (2002).
  • Okada, K., Chuman, Y., Nakashima, R., Fujita, T., Nose, T., Costa, T., and Shimohigashi, Y. Synergistic potentiation of nociceptin by simultaneous incorporation of basic amino acids at the consecutive positions 14-15. Peptide Sci.2000, 143-146 (2001).
  • Honda, T., Shigehiro, D., Okada, K., Shirasu, N., Chuman, Y., Fujita, T., Nose, T., Sakaguchi, K., and Shimohigashi, Y. Differential receptor binding characteristics of the phenylalanine residues at positions 3-4 of endomorphine 2. Peptide Sci.2000, 139-142 (2001).
  • Matsushima, A., Chuman, Y., Onoue, H., Ito, Y., Tomioka, K., Tominaga, Y., Shimohigashi, Y., Shimohigashi, M. Gene expression of a circadian pacemaker hormone peptide PDF in cricket Gryllus bimaculatus. Peptide Sci.2000, 63-66 (2001).
  • Chuman, Y., Matsushima, A., Nose, T., Shimohigashi, Y., and Shimohigashi, M. cDNA cloning of circadian rhythm pacemaker neuropeptide PDF in Gryllus bimaculatus and its nuclear localization. Peptide Sci.2000, 59-62 (2001).
  • Chuman, Y. and Shimohigashi, Y.  Opioid peptides and nociceptive peptides. J. Clinical and Exp. Med., 195 (9), 595-599 (2000).
  • Shimohigashi, Y., Okada, K., Nakashima, R., Chuman, Y., Nose, T., and Costa, T. Highly potent nociceptin analogs. Akabori Conference, 8, 126-131 (2000).
  • Okada, K., Chuman, Y., Nakashima, R., Nose, T., Costa, T., and Shimohigashi, Y. Leucine-14 of nociceptin is a structural element in the CH/p interaction with the receptor aromatic residue. Peptide Sci.1999, 433-436 (2000).
  • Honda, T., Shigehiro, D., Shirasu, N., Chuman, Y., Fujita, T., Nose, T., and Shimohigashi, Y. The mode of molecular interaction of Phe-3 deltorphin II and endomorphin 2 in opioid receptor binding. Peptide Sci.1999, 429-432 (2000).
  • Chuman, Y., Riitano, D., Sbraccia, C., Costa, T., and Shimohigashi., Y. Analysis of receptor activation mechanism by incorporating the ligand peptide into the receptor; a d opioid receptor tethereding enkephalin. Peptide Sci.1999, 425-428 (2000).
  • Shirasu, N., Okada, K., Chuman, Y., Fujita, T., Honda, T., Shigehiro, D., Nose, T., and Shimohigashi, Y. Receptor interaction mode of the Phe-phenyl group of opioid peptides. Peptide Sci.1999, 25-28 (2000).
  • Chuman, Y., Yasunaga, T., Costa, T., and Shimohigashi, Y. A novel type of rat brain d opioid receptors differentiated by cyclopropylphenylalanine-containing enkephalin analog. Peptide Sci.- Present and Future, 207-209 (1999).
  • アミノ酸リシンに新たな翻訳後修飾-リシンスクシニル化がタンパク質の”性質“を変える 中馬吉郎 化学, 66, 64-65 (2011)
  • 鎮痛および疼痛にかかわる神経ペプチド 中馬吉郎, 下東康幸 医学のあゆみ, 195(9), 595-599 (2000).

特許関連

  • 発明名称: 核酸アプタマー及びその使用
    登録番号: 特許第7255852号
    登 録 日: 令和5年4月3日
  • 名称:細胞内分子を標的とした細胞膜透過型核酸アプタマー
    出願番号:特願2019-096035 (2019)
    PCT出願:PCT/JP2020/20119 (2020)
    JST特許出願支援制度(PCT出願)採択
  • 名称:発がん原因酵素を標的としたイオン応答性DNAアプタマー
    出願番号:特願2019-045938 (2019)
  • 名称: Monoclonal antibody specifically recognizing modification site after translation of p53 and kit for assaying modification site containing the same
    出願番号:11/910,313 (United states patent)
  • 名称:「プロテインホスファターゼ阻害剤」
    出願番号:特願2008-262646, PCT出願PCT/JP2009/005128,国際公開番号:WO2010041401 A1 (日米英独仏中計6か国)
  • 名称:p53翻訳後修飾部位を特異的に認識するモノクローナル抗体、及びその抗体を含む修飾部位測定キット
    出願国:PCT出願
    出願番号:PCT/JP2006/306921,特願2007-511193)

受賞関係

  • 名称:Fellows Award for Research Excellence (FARE) 2003 (National Institutes of Health) 2002年10月
  • 名称:2010年度(第18回) JB論文賞、2010年10月25日