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原著論文 総説 解説・ニュース 著書 その他

原著論文
[1] Okano T., Fukada Y., Artamonov I. D. and Yoshizawa T.
Purification of cone visual pigments from chicken retina.
Biochemistry, 28 :  8848-8856 (1989).
[2] Imamoto Y., Kandori H., Okano T., Fukada Y., Shichida Y. and Yoshizawa T.
Effect of chloride ion on the thermal decay process of the batho intermediate of iodopsin at low temperature.
Biochemistry, 28 :  9412-9416 (1989).
[3] Fukada Y., Okano T., Artamonov I. D. and Yoshizawa, T.
Chicken red-sensitive cone visual pigment retains a binding domain for transducin.
FEBS Lett., 246 :  69-72 (1989).
[4] Kuwata O., Imamot, Y., Okano T., Kokame K., Kojima D., Matsumoto H., Morodome A., Fukada Y., Shichida Y., Yasuda K., Shimura Y. and Yoshizawa, T.
The primary structure of iodopsin, a chicken red-sensitive cone pigment.
FEBS Lett., 272 :  128-132 (1990).
[5] Fukada Y., Okano T., Shichida Y., Yoshizawa T., Trehan A., Mead D., Denny M., Asato A. E. and Liu R. S.
Comparative study on the chromophore binding sites of rod and red-sensitive cone visual pigments by use of synthetic retinal isomers and analogues.
Biochemistry, 29 :  3133-3140 (1990).
[6] Fukada Y., Kokame K., Okano T., Shichida Y., Yoshizawa T., McDowell J. H., Hargrave P. A. and Palczewski K.
Phosphorylation of iodopsin, chicken red-sensitive cone visual pigment.
Biochemistry, 29 :  10102-10106 (1990).
[7] Okano T., Kojima D., Fukada Y., Shichida Y. and Yoshizawa T.
Primary structures of chicken cone visual pigments: vertebrate rhodopsins have evolved out of cone visual pigments.
PNAS, 89 :  5932-5936 (1992).
[8] Okano T., Fukada Y., Shichida Y. and Yoshizawa, T.
Photosensitivities of iodopsin and rhodopsins.
Photochem. Photobiol., 56 :  995-1001 (1992).
[9] Kojima, D., Okano, T., Fukada, Y., Shichida, Y., Yoshizawa, T. and Ebrey, T. G.
Cone visual pigments are present in gecko rod cells.
PNAS, 89 :  6841-6845 (1992).
[10] Okano T., Yoshizawa T. and Fukada, Y.
Pinopsin is a chicken pineal photoreceptive molecule.
Nature, 372 :  94-97 (1994).
[11] Morishita R., Nakayama H., Isobe T., Matsuda T., Hashimoto Y., Okano, T. and Fukada, Y.,
Primary structure of a γ subunit of G protein, γ12 and its phosphorylation by protein kinase C.
J. Biol. Chem., 270 :  29469-29475 (1995).
[12] Kojima D., Imai H., Okano T., Fukada Y., Crescitelli F., Yoshizawa T. and Shichida Y.
Purification and low temperature spectroscopy of gecko visual pigments green and blue.
Biochemistry, 34 :  1096-1106 (1995).
[13] Okano T., Yamazaki K., Kasahara T. and Fukada, Y.
Molecular cloning of heterotrimeric G-protein alpha-subunits in chicken pineal gland.
J. Mol. Evol., 44 :  S91-97 (1997).
[14] Okano T., Takanaka Y., Nakamura A., Hirunagi K., Adachi A., Ebihara S. and Fukada Y.
Immunocytochemical identification of pinopsin in pineal glands of chicken and pigeon.
Brain Res. Mol. Brain Res., 50 :  190-196 (1997).
[15] Hirunagi, K., Ebihara, S., Okano, T., Takanaka, Y. and Fukada, Y.
Immunoelectron-microscopic investigation of the subcellular localization of pinopsin
in the pineal organ of the chicken.
Cell. Tissue Res., 289 :  235-241 (1997).
[16] Yoshikawa T., Okano T., Oishi T. and Fukada Y.
A deep brain photoreceptive molecule in the toad hypothalamus.
FEBS Lett., 424 :  69-72 (1998).
[17] Wada Y., Okano T., Adachi A., Ebihara S. and Fukada Y.
Identification of rhodopsin in the pigeon deep brain.
FEBS Lett., 424 :  53-56 (1998).
[18] Takanaka Y., Okano T., Iigo M. and Fukada, Y.
Light-dependent expression of pinopsin gene in chicken pineal gland.
J. Neurochem., 70 :  908-913 (1998).
[19] Mizusawa K., Iigo M., Suetake H., Yoshiura Y., Gen K., Kikuchi K., Okano T., Fukada Y. and Aida, K.
Molecular cloning and characterization of a cDNA encoding the retinal arylalkylamine N-acetyltransferase of the rainbow trout, Oncorhynchus mykiss.
Zool. Sci., 15 :  345-351 (1998).
[20] Nakamura A., Kojima D., Imai H., Terakita A., Okano T., Shichida Y. and Fukada Y.
Chimeric nature of pinopsin between rod and cone visual pigments.
Biochemistry, 38 :  14738-14745 (1999).
[21] Yamao M., Araki M., Okano T., Fukada Y. and Oishi T.
Differentiation of pinopsin-immunoreactive cells in the developing quail pineal organ:
an in-vivo and in-vitro immunohistochemical study.
Cell. Tissue Res., 296 :  667-671 (1999).
[22] Wada Y., Okano T. and Fukada, Y.
Phototransduction molecules in the pigeon deep brain.
J. Comp. Neurol., 428 :  138-144 (2000).
[23] Sanada K., Hayashi Y., Harada Y., Okano T. and Fukada Y.
Role of circadian activation of mitogen-activated protein kinase in chick pineal clock oscillation.
J. Neurosci., 20 :  986-991 (2000).
[24] Okano K., Okano T., Yoshikawa T., Masuda A., Fukada Y. and Oishi,T.
Diversity of opsin immunoreactivities in the extraretinal tissues of four anuran amphibians.
J. Exp. Zool., 286 :  136-142 (2000).
[25] Matsushita A., Yoshikawa T., Okano T., Kasahara T. and Fukada Y.
Colocalization of pinopsin with two types of G-protein alpha-subunits in the chicken pineal gland.
Cell. Tissue Res., 299 :  245-251 (2000).
[26] Kasahara T., Okano T., Yoshikawa T., Yamazaki K. and Fukada, Y.
Rod-type transducin alpha-subunit mediates a phototransduction pathway in the chicken pineal gland.
J. Neurochem., 75 :  217-224 (2000).
[27] Okano T. and Fukada, Y.
Photoreceptors in pineal gland and brain: cloning, localization and overexpression.
Methods Enzymol., 316 :  278-291 (2000).
[28] Yoshikawa T., Okano T., Kokame K., Hisatomi O., Tokunaga F., Oishi T. and Fukada Y.
Immunohistochemical localization of opsins and alpha-subunit of transducin in the pineal complex and deep brain of the Japanese glass lizard, Takydromus tachydromoides.
Zool. Sci., 18 :  325-330 (2001).
[29] Hirota T., Kagiwada S., Kasahara T., Okano T., Murata M. and Fukada Y.
Effect of brefeldin A on melatonin secretion of chick pineal cells.
J. Biochem. (Tokyo), 129 :  51-59 (2001).
[30] Nakamura A., Kojima D., Okano T., Imai H., Terakita A., Shichida Y. and Fukada, Y.
Regulatory mechanism for the stability of the meta II intermediate of pinopsin.
J. Biochem. (Tokyo), 129 :  329-334 (2001).
[31] Doi M., Nakajima Y., Okano T. and Fukada, Y.
Light-induced phase-delay of the chicken pineal circadian clock is associated with the induction of cE4bp4,
a potential transcriptional repressor of cPer2 gene.
PNAS, 98 :  8089-8094 (2001).
[32] Okano T., Sasaki M. and Fukada Y.
Cloning of mouse BMAL2 and its daily expression profile in the suprachiasmatic nucleus:
a remarkable acceleration of Bmal2 sequence divergence after Bmal gene duplication.
Neurosci. Lett., 300 :  111-114 (2001).
[33] Yamamoto K., Okano T. and Fukada Y.
Chicken pineal Cry genes: light-dependent up-regulation of cCry1 and cCry2 transcripts.
Neurosci. Lett., 313 :  13-16 (2001).
[34] Okano T., Yamamoto K., Okano K., Hirota T., Kasahara T., Sasaki M., Takanaka Y. and Fukada, Y.
Chicken pineal clock genes: implication of BMAL2 as a bidirectional regulator in circadian clock oscillation.
Genes Cells, 6 :  825-836 (2001).
[35] Sanada K., Okano T. and Fukada Y.
Mitogen-activated protein kinase phosphorylates and negatively regulates
basic helix-loop-helix-PAS transcription factor BMAL1.
J. Biol. Chem., 277 :  267-271 (2002).
[36] Doi M., Nakajima Y., Okano T. and Fukada, Y.
Light-dependent changes in the chick pineal temperature and the expression of cHSP90alpha gene:
a potential contribution of in vivo temperature change to the photic-entrainment of the chick pineal circadian clock.
Zool. Sci., 19 :  633-641 (2002).
[37] Takanaka Y., Okano T., Yamamoto K. and Fukada, Y.
A negative regulatory element required for light-dependent pinopsin gene expression.
J. Neurosci., 22 :  4357-4363 (2002).
[38] Kasahara T., Okano T., Haga T. and Fukada, Y.
Opsin-G11-mediated signaling pathway for photic entrainment of the chicken pineal circadian clock.
J. Neurosci., 22 :  7321-7325 (2002).
[39] Hirota T., Okano T., Kokame K., Shirotani-Ikejima H., Miyata T. and Fukada, Y.
Glucose down-regulates Per1 and Per2 mRNA levels and induces circadian gene expression in cultured rat-1 fibroblasts.
J. Biol. Chem., 277 :  44244-44251 (2002).
[40] Doi M., Okano T., Yuovsky I., Sassone-Corsi P. and Fukada, Y.
Negative control of circadian clock regulator E4BP4 by casein kinase Ie-mediated phosphorylation.
Curr. Biol., 14 :  975-980 (2004).
[41] Kassai H., Aiba A., Nakao K., Nakamura K., Katsuki M., Xiong W.H., Yau K. W., Imai H., Shichida Y., Satomi Y., Takao T., Okano, T. and Fukada, Y.
Farnesylation of retinal transducin underlies its translocation during light adaptation.
Neuron, 47 :  529-539 (2005).
[42] Hatori M., Okano T., Nakajima Y., Doi M. and Fukada, Y.
Lcg is a light-inducible and clock-controlled gene expressed in the chicken pineal gland.
J. Neurochem., 96 :  1790-1800 (2006).
[43] Kubo Y., Akiyama M., Fukada Y. and Okano T.
Molecular cloning, mRNA expression and immunocytochemical localization of a putative blue-light photoreceptor CRY4 in the chicken pineal gland.
J. Neurochem., 97 :  1155-1165 (2006). doi:10.1111/j.1471-4159.2006.03826.x
[44] Wada Y., Sugiyama J., Okano T. and Fukada Y.
GRK1 and GRK7: Unique cellular distribution and widely different activities of opsin phosphorylation in the zebrafish rods and cones.
J. Neurochem., 98 :  824-837 (2006).
[45] Torii M., Kojima D., Okano T., Nakamura A., Terakita A., Shichida Y., Wada A. and Fukada Y.
Two isoforms of chicken melanopsins show blue light sensitivity.
FEBS Lett., 581 :  5327-5331 (2007).
[46] Nakao N., Yasuo S., Nishimura A., Yamamura T., Watanabe T., Anraku T., Okano T., Fukada Y., Sharp P.J., Ebihara S. and Yoshimura T.
Circadian clock gene regulation of steroidogenic acute regulatory protein gene expression
in preovulatory ovarian follicles.
Endocrinology, 148 :  3031-3038 (2007).
[47] Akiyama M., Okano K., Fukada Y. and Okano T.
Macrophage inhibitory cytokine MIC-1 is upregulated by short-wavelength light in cultured normal human dermal fibroblasts.
FEBS Lett., 583 :  933-937 (2009). doi:10.1016/j.febslet.2009.02.006
[48] Yoshitane H., Takao T., Satomi Y., Hien D.-N., Okano T. and Fukada Y.
Roles of CLOCK phosphorylation in suppression of E-box-dependent transcription.
Mol. Cell. Biol., 29 :  3675-3686 (2009).
[49] Sasaki M., Yoshitane, H., Du N.-H., Okano T. and Fukada Y.
Preferential inhibition of BMAL2:CLOCK activity by PER2 reemphasizes its negative role and a positive role of BMAL2 in the circadian transcription.
J. Biol. Chem., 286 :  25149-25159 (2009).
[50] Hirota T., Kon N., Itagaki T., Hoshina N., Okano T. and Fukada Y.
Transcriptional repressor TIEG1 regulates Bmal1 gene through GC box and controls circadian clockwork.
Genes Cells, 15 :  111-121 (2010).
[51] Kubo Y.*, Takeuchi T.*, Okano K. and Okano T. (*Equal contribution)
Cryptochrome genes are highly expressed in the ovary of the African clawed frog, Xenopus tropicalis.
PLoS ONE, 5 :  e9273 (2010). doi:10.1371/journal.pone.0009273
[52] Fukushiro M., Takeuchi T., Takeuchi Y., Hur S.-P., Sugama N., Takemura A., Kubo Y., Okano K. and Okano T.
Lunar phase-dependent expression of cryptochrome and a photoperiodic mechanism for lunar phase-recognition in a reef fish, goldlined spinefoot.
PLoS ONE, 6 :  e28643 (2011). doi:10.1371/journal.pone.0028643
[53] Takebe A., Furutani T., Wada T., Koinuma M., Kubo Y., Okano K. and Okano T.
Zebrafish respond to the geomagnetic field by bimodal and group-dependent orientation.
Scientific Reports, 2 :  Article number: 727 (2012). doi:10.1038/srep00727
[54] Watari R., Yamaguchi C., Zemba W., Kubo Y., Okano K. and Okano T.
Light-dependent structural change of chicken retinal Cryptochrome4.
J. Biol. Chem. 287 :  42634-42641 (2012). doi:10.1074/jbc.M112.395731
[55] Takeuchi T.*, Kubo Y.*, Okano K. and Okano T. (*Equal contribution)
Identification and characterization of cryptochrome4 in the ovary of western clawed frog Xenopus tropicalis.
Zool. Sci., 31 :  152-159 (2014). doi:10.2108/zsj.31.152
[56] Toda R., Okano K., Takeuchi Y., Yamauchi C., Fukushiro M., Takemura A. and Okano T.
Hypothalamic expression and moonlight-independent changes of Cry3 and Per4 implicate their roles in lunar clock oscillators of the lunar-responsive goldlined spinefoot.
PLoS ONE, 9 :  e109119 (2014). doi:10.1371/journal.pone.0109119
[57] Mitsui H., Maeda T., Yamaguchi C., Tsuji Y., Watari R., Kubo Y., Okano K. and Okano T.
Overexpression in yeast, photocycle, and in vitro structural change of an avian putative magnetoreceptor Cryptochrome4.
Biochemistry, 54 :  1908-1917 (2015). doi:10.1021/bi501441u
[58] Sakata R., Kabutomori R., Okano K., Mitsui H., Takemura A., Miwa T., Yamamoto H. and Okano T.
Rhodopsin in the dark hot sea: Molecular analysis of rhodopsin in a snailfish, Careproctus rhodomelas, Living near the deep-sea hydrothermal vent.
PLoS ONE, 10 :  e0135888 (2015). doi:10.1371/journal.pone.0135888
[59] Okano K., Ozawa S., Sato H., Kodachi S., Ito M., Miyadai T., Takemura A. and Okano T.
Light- and circadian-controlled genes respond to a broad light spectrum in Puffer Fish-derived Fugu eye cells.
Scientific Reports, 7 :  46150 (2017). doi:10.1038/srep46150
[60] Takeuchi Y., Kabutomori R., Yamauchi C., Miyagi H., Takemura A., Okano K. and Okano T.
Moonlight controls lunar-phasedependency and regular oscillation of clock gene expressions in a lunar-synchronized spawner fish, Goldlined spinefoot.
Scientific Reports, 8 :  6208 (2018). doi:10.1038/s41598-018-24538-1
[61] Miura K., Tsuji Y., Mitsui H., Oshima T., Noshi Y., Arisawa Y., Okano K. and Okano T.
THETA system allows one-step isolation of tagged proteins through temperature-dependent protein–peptide interaction.
Communications Biology, 2 :  207 (2019). doi:10.1038/s42003-019-0457-8
[62] Okano K., Saratani Y., Tamasawa A., Shoji Y., Toda R. and Okano T.
A photoperiodic time measurement served by the biphasic expression of Cryptochrome1ab in the zebrafish eye.
Scientific Reports, 10 :  5056 (2020). doi:10.1038/s41598-020-61877-4
[63] Saratani Y., Takeuchi Y., Okano K. and Okano T.
Clock gene expression in the eye exhibits circadian oscillation and light responsiveness but is not necessary for nocturnal locomotor activity of Japanese loach, Misgurnus anguillicaudatus
Zoological Science, 37 :  177-192 (2020).
[64] Takemura Y., Ito M., Shimizu Y., Okano K. and Okano T.
Adaptive Light: A lighting control method aligned with dark adaptation of human vision.
Scientific Reports, 10 :  11204 (2020). doi.org/10.1038/s41598-020-68119-7
英文総説
[1] Okano T., Fukada Y. and Yoshizawa T.
Molecular basis for tetrachromatic color vision.
Comp. Biochem. Physiol. B., 112:  405-414 (1995).
[2] Okano T. and Fukada Y.
Phototransduction cascade and circadian oscillator in chicken pineal gland.
J. Pineal. Res, 22 :  145-151 (1997).
[3] Okano T. and Fukada, Y.
Structure, gene expression, localization and functional implication of
chicken pineal photoreceptor pinopsin.
In: Circadian Clock and Entrainment (Hiroshige, T. and Honma, K. eds.). pp. 21-32.
Sapporo:  Hokkaido University Press :  21-32 (1998).
[4] Okano K., Yoshikawa T., Okano T., Seki T., Masuda A., Fukada Y. and Oishi T.
Immunocytochemical localization of visual pigments and HPLC analysis of retinal in the pineal,
deep brain and skin of several species of anuran amphibian.
In: Recent Progress in Molecular and Comparative Endocrinology
(Kwon, H. B., Joss, J. M. P. and Ishii, S. eds.). pp. 365-369 (1999).
[5] Okano T. and Fukada, Y.
Photoreception and circadian clock system of the chicken pineal gland.
Microsc. Res. Tech., 53 :  72-80 (2001).
[6] Fukada Y. and Okano, T.
Circadian clock system in the pineal gland.
Mol. Neurobiol., 25 :  1-12 (2002).
[7] Okano T. and Fukada, Y.
Chicktacking pineal clock.
J. Biochem. (Tokyo) 134 :  791-797 (2003).
[8] Yoshikawa T, Iigo M, Okano T, Fukada Y.
Roles of melatonin in photoperiodic gonadal response of birds.
Experimental Endocrinology and Reproductive Biology, Science Publishers: : (2008) 85-102, total 315 pages.
邦文総説
[1] 岡野俊行
生物リズムに関わる松果体の光受容蛋白質
比較生理生化学 Vol.12, No.3 , pp.260-269 (1995).
[2] 深田吉孝・岡野俊行
分子レベルにおける生物時計機構の解析
生化学 Vol.67 , pp.1137-1142 (1995).
[3] 岡野俊行・深田吉孝
脳は光を感じる第三の目
ニュートン Vol.15, No.11 , pp.102-107 (1995).
[4] 深田吉孝・岡野俊行
視物質の多様化と視覚の進化
細胞工学 Vol.14, No.9 , pp.1007-1014 (1995).
[5] 岡野俊行・深田吉孝
光受容蛋白質の分子進化
生物の科学 遺伝 Vol.49, No.12 , pp.28-34 (1995).
[6] 岡野俊行・深田吉孝
動物の体内時計
科学 Vol.67, No.1 , pp.48-56 (1997).
[7] 岡野俊行・深田吉孝
鳥類松果体細胞の概日時計システム
細胞工学 Vol.20, No.6 , pp.837-842 (2001).
[8] 三井広大・岡野俊行
動物が地磁気を感じる仕組みとは?
現代化学 No.545 , 東京化学同人 pp.44-48 (2016).
[9] 岡野俊行
光と生物—発色団と光受容タンパク質の機能-
化学と教育 講座:光と色と物質 日本化学会 第65巻 第6号 , (2017).
解説・ニュース
[1] 吉澤 透・岡野俊行
錐体の光感受性レチナール蛋白質アイオドプシンの精製とその局在
ビタミン Vol.64, No.10 , pp.614-615 (1990).
[2] 岡野俊行・七田芳則
錐体視物質の一次構造:ロドプシンは錐体視物質から進化した
生物物理 Vol.32, No.5 , pp.273-276 (1992).
[3] 岡野俊行・深田吉孝
脳内光受容体ピノプシンと生物時計
生物科学ニュース Vol.278 , 14-16 (1995).
[4] 深田吉孝・岡野俊行
生物時計の時刻合わせをする脳内タンパク質
生物の科学 遺伝 Vol.49, No.4 , pp.8-9 (1995).
[5] 岡野俊行・高中陽子
概日時計の同調因子ピノプシンの構造・機能・発現調節
生物物理 Vol.36, No.2 , pp.101-103 (1996).
[6] 岡野俊行
光と時刻を知る細胞
文部省重点領域研究「生体機能と設計分子《ニュース》」
DEPCOM Vol.1, No.3 , pp.22-28 (1998).
[7] 岡野俊行・深田吉孝
色覚の進化
生物の科学 遺伝 Vol.53, No.9 , pp.39-44 (1999).
[8] 笠原和起・岡野俊行
時計細胞の時刻を可視化する
バイオイメージング Vol.7 , pp.221-226 (1999).
[9] 岡野俊行・深田吉孝
脳内光レセプター
生物物理 Vol.39, No.4 , pp.246-249 (1999).
[10] 岡野俊行・深田吉孝
体内時計の時刻を調節する遺伝子の発見
生物の科学 遺伝 Vol.56, No.2 , pp.26-28 (2002).
[11] 吉川朋子・岡野俊行・深田吉孝
in vivoマイクロダイアリシス法を用いた鳥類の脳脊髄液中のメラトニン概日
リズムのラジオイムノアッセイ解析
東京大学アイソトープ総合センターニュース, Vol.36, No.3 , pp.12-14 (2002).
[12] 岡野俊行
オープンキャンパス2004: 理学部の取り組み
東京大学理学系研究科・理学部ニュース, Vol.32, No.4 , pp.2-4 (2004).
[13] 土居雅夫・岡野俊行
体内時計の時間調節を担うタンパク質リン酸化反応
生化学Vol.77, No.2 , pp.125-129 (2005).
[14] 岡野俊行、岡野恵子
マイコンを使って水棲動物の走光性実験を自動化する
日本比較生理生化学会編「研究者が教える動物実験」, 共立出版 (2015).
著書
[1] 吉澤 透・岡野俊行
視細胞における色受容:その分子機構と進化
視覚の進化と脳、第1章(三上 章允 編)
朝倉書店, pp.3-23 (1992).
[2] 深田吉孝・岡野俊行
視覚の分子生物学
図説・分子病態学
中外医学社, pp.400-409 (1995).
[3] 岡野俊行
試験監督のいない学校 (分担執筆)
東方出版, pp.26-29 (1996).
[4] 深田吉孝・岡野俊行
ピノプシンによる光シグナル伝達と生物時計
新臨床医のための分子医学シリーズ『細胞内情報伝達のしくみ』
羊土社, pp.28-39 (1996).
[5] 深田吉孝・岡野俊行
視覚異常症
図説・分子病態学(改訂版)
中外医学社, pp.382-387 (1998).
[6] 岡野俊行・深田吉孝
松果体:光受容.生物時計の分子生物学、第4章(海老原史樹文・深田吉孝 編)
シュプリンガーフェアラーク東京, pp.139-150 (1999).
[7] 深田吉孝・岡野俊行
視覚異常症
図説・分子病態学(第3版)
中外医学社 pp.378-384 (2003).
[8] 岡野俊行・深田吉孝
脊椎動物の時計システム.時計遺伝子の生物学、第1章(岡村均・深田吉孝 編)
シュプリンガーフェアラーク東京, pp.41-48 (2004).
[9] 深田吉孝・岡野俊行
視覚異常症、分子病態学 第4版
中外医学社, pp354-359 (2008).
[10] 岡野俊行、深田吉孝
第6章、概日リズムの分子機構
シリーズ21世紀の動物科学、 第9巻 動物の感覚とリズム
培風館, pp126-147 (2007).
[11] 岡野俊行
クリプトクロム
時間生物学辞典(分担執筆)
朝倉書店 (2008).
[12] 岡野俊行
クリプトクロムの光反応と生理機能
「動物の多様な生き方1 見える光、見えない光 」
共立出版(編集 日本比較生理生化学会), pp.114-133 (2009).
[13] 岡野俊行
新規12項目、修正196項目担当
岩波生物学辞典 第5版 (分担)
岩波書店 (2013)
[14] 岡野俊行
光と生命の事典(分担)
日本光生物学協会、朝倉書店 (2016)
その他
[1] Okano T., Yoshizawa T. and Fukada Y.
Cloning and characterization of pinopsin: A chicken pineal photoreceptive pigment.
Physiol Zoology 68 : 160 (1995).
[2] Kojima D., Imai H., Okano T., Fukada Y., Crescitelli F., Yoshizawa T. and Shichda Y.
Photobleaching processes of gecko visual pigments.
Physiol Zoology 68 : 162 (1995).
[3] Okano T. and Fukada Y.
Structure and localization of photoreceptive pigment in chicken pineal gland.
Exp. Eye. Res. 63 : S233 (1996).
[4] Okano T. and Fukada Y.
Molecular mechanisms of photic-entrainment of chicken pineal circadian clock.
J. Photosci 9 : 25-28 (2002).
[5] Okano T., Kasahara T. and Fukada, Y.
A novel phototransduction pathway in the pineal gland and retina.
J. Photosci 9 : 246-248 (2002).
[6] Okano K., Okano T., Oishi T. and Fukada, Y.
A long-day-stimulus induced the expression of c-Fos-like molecules in the hypothalamus of Japanese quail.
J. Photosci 9 : 255-257 (2002).
所属学会

日本生化学会、日本動物学会、日本生物物理学会、日本分子生物学会 日本比較生理生化学会、日本時間生物学会

活動歴
1996年 1月 ~ 1997年 12月 日本比較生理生化学会 行事幹事
1998年 1月 ~ 2001年 12月 日本比較生理生化学会 会計幹事
1998年 1月 ~ 2001年 12月 日本比較生理生化学会 評議員
2004年 1月 ~ 日本比較生理生化学会 評議員
受賞歴
1995年度 日本比較生理生化学会 奨励賞 (1995/07/18)
2002年度 米国光生物学会(American Society for Photobiology)
New Investigator Award (2002/7/16)
2005年度 科学技術分野の文部科学大臣表彰 若手科学者賞 (2005/04/20)
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