Kobayashi, T., Yamazaki, K., Shinada, J., Mizunuma, M., Furukawa, K., and Chuman, Y. Identification of Inhibitors of the Disease-Associated Protein Phosphatase Scp1 Using Antibody Mimetic Molecules. Int. J. Mol. Sci., 25(7), 3737, (2024) DOI: 10.3390/ijms25073737
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).
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)
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,
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Matsushima, A., Chuman, Y., Sato, S., Tominaga, Y., Shimohigashi, Y., and Shimohigashi,
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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
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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).
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Identification of receptor binding site of Nociceptin-14-15, the residue for high
receptor potentiation. Peptide Sci.2001, 109-112 (2002).
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Honda, T., Shigehiro, D., Okada, K., Shirasu, N., Chuman, Y., Fujita, T., Nose,
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the phenylalanine residues at positions 3-4 of endomorphine 2. Peptide
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Matsushima, A., Chuman, Y., Onoue, H., Ito, Y., Tomioka, K., Tominaga, Y., Shimohigashi,
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cricket Gryllus bimaculatus. Peptide Sci.2000, 63-66 (2001).
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cloning of circadian rhythm pacemaker neuropeptide PDF in Gryllus bimaculatus and
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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
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endomorphin 2 in opioid receptor binding. Peptide Sci.1999, 429-432
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receptor activation mechanism by incorporating the ligand peptide into the receptor; a d
opioid receptor tethereding enkephalin. Peptide Sci.1999, 425-428
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Shirasu, N., Okada, K., Chuman, Y., Fujita, T., Honda, T., Shigehiro, D., Nose, T., and
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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)
