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+-triggered bioluminescence in the oceanic squid Symplectoteuthis oualaniensis
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Tsuji, F.I.1
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0027763210
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Symplectoteuthis Bioluminescence (1). Structure and binding form of chromophore in photoprotein of a luminous squid
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a) Takahashi, H. and Isobe, M. (1993) Symplectoteuthis Bioluminescence (1). Structure and binding form of chromophore in photoprotein of a luminous squid. Bioorg. Med. Chem. Lett. 3, 2647-2652;
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Takahashi, H.1
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b) Takahashi, H. and Isobe, M. (1994) Photoprotein of luminous squid, Symplectoteuthis oualaniensis and reconstruction of the luminous system. Chem. Lett. 23, 843-846;
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Feng, M.C.7
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13C- dehydrocoelenterazine and NMR studies on the bioluminescence of a Symplectoteuthis model
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13C- dehydrocoelenterazine and NMR studies on the bioluminescence of a Symplectoteuthis model. Tetrahedron 56, 2629-2639.
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Two luminescent intermediates of coelenterazine analog, peroxide and dioxetanone, prepared by direct photo-oxygenation at low temperature
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a) Usami, K. and Isobe, M. (1995) Two luminescent intermediates of coelenterazine analog, peroxide and dioxetanone, prepared by direct photo-oxygenation at low temperature. Tetrahedron Lett. 36, 8613-8616;
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Low-temperature photooxygenation of coelenterate luciferin analog synthesis and proof of 1,2-dioxetanone as luminescence intermediate
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b) Usami, K. and Isobe, M. (1996) Low-temperature photooxygenation of coelenterate luciferin analog synthesis and proof of 1,2-dioxetanone as luminescence intermediate. Tetrahedron 52, 12061-12090.
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Usami, K.1
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A novel 60 kDa-photoprotein from oceanic sqiud (Symplectoteuthis oualaniensis) with sequence similarity to mammalian carbon-nitrogen hydrolase domains
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Fujii, T., Ahn, J.Y., Kuse, M., Mori, H., Matsuda, T. and Isobe, M. (2002) A novel 60 kDa-photoprotein from oceanic sqiud (Symplectoteuthis oualaniensis) with sequence similarity to mammalian carbon-nitrogen hydrolase domains. Biochem. Biophys. Res. Commun. 293, 874-879.
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Fujii, T.1
Ahn, J.Y.2
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Mori, H.4
Matsuda, T.5
Isobe, M.6
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10
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0035955156
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2-treated Cu,Zn-SOD protein with LC-ESI-Q-TOF-MS, MS/MS for the determination of the copper-binding site
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Kurahashi, T.1
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Isobe, M.4
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11
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56249091296
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JP Patent 2000-154786. Accession number of symplectin is AB447990. The S-S bondings are located between Cysteines 92-110, 129-137, and 380-385, respectively. The details of these informations are to be reported elsewhere in due course
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Isobe, M. and Matsuda, T. (2000) JP Patent 2000-154786. Accession number of symplectin is AB447990. The S-S bondings are located between Cysteines 92-110, 129-137, and 380-385, respectively. The details of these informations are to be reported elsewhere in due course.
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Isobe, M.1
Matsuda, T.2
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13
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Protein phosphatase inhibitory activity of tautomycin photoaffinity probes evaluated at femtomolar level
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Sydnes, M.O., Kuse, M., Kurono, M., Shimomura, A., Ohinata, H., Takai, A. and Isobe, M. (2008) Protein phosphatase inhibitory activity of tautomycin photoaffinity probes evaluated at femtomolar level. Bioorg. Med. Chem. 16, 1747-1755.
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Sydnes, M.O.1
Kuse, M.2
Kurono, M.3
Shimomura, A.4
Ohinata, H.5
Takai, A.6
Isobe, M.7
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14
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33749671351
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These conditions are essentially identical as reported in experimental part in Ref. 5 and following paper; Isobe, M., Kai, H., Kurahashi, T., Suwan, S., Pitchayawasin-T. S., Franz, T., Tani, N., Higashi, K. and Nishida, H. (2006) The molecular mechanism of the termination of insect diapause, Part 1: A timer protein, TIME-EA4, in the diapause eggs of the silkworm Bombyx mori is a Metallo-Glycoprotein. ChemBioChem. 7, 1590-1598.
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These conditions are essentially identical as reported in experimental part in Ref. 5 and following paper; Isobe, M., Kai, H., Kurahashi, T., Suwan, S., Pitchayawasin-T. S., Franz, T., Tani, N., Higashi, K. and Nishida, H. (2006) The molecular mechanism of the termination of insect diapause, Part 1: A timer protein, TIME-EA4, in the diapause eggs of the silkworm Bombyx mori is a Metallo-Glycoprotein. ChemBioChem. 7, 1590-1598.
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15
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56249100913
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These conditions are essentially identical as reported in Refs. 4 and 7.
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These conditions are essentially identical as reported in Refs. 4 and 7.
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