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Volumn 163, Issue 1, 2012, Pages 1-25

Structure, biosynthesis and possible function of tunichromes and related compounds

Author keywords

Defense reactions; Dehydrodopamine; Quinone methides; Tunic formation; Tunicates

Indexed keywords

ANTIBIOTIC AGENT; BIOMATERIAL; CELENAMIDE A; CELENAMIDE B; CELENAMIDE C; CELENAMIDE D; CELENAMIDE E; CLAVANIN DERIVATIVE; DEHYDRO N ACYLDOPAMINE; DOPAMINE DERIVATIVE; HALOCYAMINE; IRON; MONOMER; MONOPHENOL MONOOXYGENASE; MORULIN PM; OLIGOPEPTIDE; PLICATAMIDE; STORNIAMIDE DERIVATIVE; STYELIN DERIVATIVE; TUNICHROME DERIVATIVE; TUNICHROME MM 1; TUNICHROME MM 2; TUNICHROME PM 1; TUNICHROME PM 2; TUNICHROME PM 3; TUNICHROME QUINONE METHIDE; TUNICHROME SP1; TYROSINE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VANADIUM;

EID: 84862988670     PISSN: 10964959     EISSN: 18791107     Source Type: Journal    
DOI: 10.1016/j.cbpb.2012.05.005     Document Type: Review
Times cited : (31)

References (194)
  • 1
    • 77956182067 scopus 로고    scopus 로고
    • Reexamination of the mechanisms of oxidative transformations of the insect cuticular sclerotizing precursor, 1,2-dehydro-N-acetyldopamine
    • Abebe A., Zheng D., Evans J., Sugumaran M. Reexamination of the mechanisms of oxidative transformations of the insect cuticular sclerotizing precursor, 1,2-dehydro-N-acetyldopamine. Insect Biochem. Mol. Biol. 2010, 40:650-659.
    • (2010) Insect Biochem. Mol. Biol. , vol.40 , pp. 650-659
    • Abebe, A.1    Zheng, D.2    Evans, J.3    Sugumaran, M.4
  • 2
    • 0006643454 scopus 로고
    • The intracellular pH of the blood cells of the tunicate Boltenia ovifera
    • Agudelo M.I., Kustin K., McLeod G.C. The intracellular pH of the blood cells of the tunicate Boltenia ovifera. Comp. Biochem. Physiol. A 1983, 75:211-214.
    • (1983) Comp. Biochem. Physiol. A , vol.75 , pp. 211-214
    • Agudelo, M.I.1    Kustin, K.2    McLeod, G.C.3
  • 3
    • 0018711065 scopus 로고
    • Clionamide, a major metabolite of the sponge Cliona celata grant
    • Andersen R.J., Stonard R.J. Clionamide, a major metabolite of the sponge Cliona celata grant. Can. J. Chem. 1979, 57:2325-2328.
    • (1979) Can. J. Chem. , vol.57 , pp. 2325-2328
    • Andersen, R.J.1    Stonard, R.J.2
  • 4
    • 0000409039 scopus 로고
    • Phenoloxidase characterization in vacuolar hemocytes from the solitary ascidian Styela plicata
    • Arizza V., Cammarata M., Tomasino M.C., Parrinello N. Phenoloxidase characterization in vacuolar hemocytes from the solitary ascidian Styela plicata. J. Invertebr. Pathol. 1995, 66:297-302.
    • (1995) J. Invertebr. Pathol. , vol.66 , pp. 297-302
    • Arizza, V.1    Cammarata, M.2    Tomasino, M.C.3    Parrinello, N.4
  • 5
    • 0344908530 scopus 로고
    • The formation of dopa by the exposure of tyrosine solutions to ultraviolet radiation
    • Arnow L.E. The formation of dopa by the exposure of tyrosine solutions to ultraviolet radiation. J. Biol. Chem. 1937, 120:151-155.
    • (1937) J. Biol. Chem. , vol.120 , pp. 151-155
    • Arnow, L.E.1
  • 6
    • 0025097969 scopus 로고
    • Halocyamines: novel antibacterial tetrapeptide-like structures isolated from the hemocytes of the solitary ascidian Halocynthia roretzi
    • Azumi K., Yokosawa H., Ishii S. Halocyamines: novel antibacterial tetrapeptide-like structures isolated from the hemocytes of the solitary ascidian Halocynthia roretzi. Biochemistry 1990, 29:159-165.
    • (1990) Biochemistry , vol.29 , pp. 159-165
    • Azumi, K.1    Yokosawa, H.2    Ishii, S.3
  • 7
    • 0025135257 scopus 로고
    • Inhibitory effect of halocyamine, an antimicrobial substance from ascidian hemocytes, on the growth of fish viruses and marine bacteria
    • Azumi K., Yoshimizu M., Suzuki S., Ezura Y., Yokosawa H. Inhibitory effect of halocyamine, an antimicrobial substance from ascidian hemocytes, on the growth of fish viruses and marine bacteria. Experientia 1990, 46:1066-1068.
    • (1990) Experientia , vol.46 , pp. 1066-1068
    • Azumi, K.1    Yoshimizu, M.2    Suzuki, S.3    Ezura, Y.4    Yokosawa, H.5
  • 9
    • 67649247128 scopus 로고    scopus 로고
    • Immunobiology of compound ascidians, with particular reference to Botryllus schlosseri: state of the art
    • Ballarin L. Immunobiology of compound ascidians, with particular reference to Botryllus schlosseri: state of the art. Invertebr. Surviv. J. 2008, 5:54-74.
    • (2008) Invertebr. Surviv. J. , vol.5 , pp. 54-74
    • Ballarin, L.1
  • 10
    • 84862984150 scopus 로고    scopus 로고
    • Ascidian cytotoxic cells: state of the art and research perspectives
    • Ballarin L. Ascidian cytotoxic cells: state of the art and research perspectives. Invertebr. Surviv. J. 2012, 9:1-6.
    • (2012) Invertebr. Surviv. J. , vol.9 , pp. 1-6
    • Ballarin, L.1
  • 11
    • 0001827875 scopus 로고
    • Phenoloxidase in the colonial ascidian Botryllus schlosseri (Urochordata: Ascidiacea)
    • Ballarin L., Cima F., Sabbadin A. Phenoloxidase in the colonial ascidian Botryllus schlosseri (Urochordata: Ascidiacea). Anim. Biol. 1994, 3:41-48.
    • (1994) Anim. Biol. , vol.3 , pp. 41-48
    • Ballarin, L.1    Cima, F.2    Sabbadin, A.3
  • 12
    • 0031796855 scopus 로고    scopus 로고
    • Phenoloxidase and cytotoxicity in the compound ascidian, Botryllus schlosseri
    • Ballarin L., Cima F., Sabbadin A. Phenoloxidase and cytotoxicity in the compound ascidian, Botryllus schlosseri. Dev. Comp. Immunol. 1998, 22:479-492.
    • (1998) Dev. Comp. Immunol. , vol.22 , pp. 479-492
    • Ballarin, L.1    Cima, F.2    Sabbadin, A.3
  • 13
    • 0035716770 scopus 로고    scopus 로고
    • Morula cells as the major immunomodulatory hemocytes in ascidians: evidences from the colonial species Botryllus schlosseri
    • Ballarin L., Franchini A., Ottaviani E., Sabbadin A. Morula cells as the major immunomodulatory hemocytes in ascidians: evidences from the colonial species Botryllus schlosseri. Biol. Bull. 2001, 201:59-64.
    • (2001) Biol. Bull. , vol.201 , pp. 59-64
    • Ballarin, L.1    Franchini, A.2    Ottaviani, E.3    Sabbadin, A.4
  • 18
    • 0018715474 scopus 로고
    • Ultrastructural localization of vanadium in the blood cells of Ascidiacea
    • Botte L., Scippa S., de Vincentiis M. Ultrastructural localization of vanadium in the blood cells of Ascidiacea. Experientia 1979, 35:1228-1230.
    • (1979) Experientia , vol.35 , pp. 1228-1230
    • Botte, L.1    Scippa, S.2    de Vincentiis, M.3
  • 20
    • 0000641503 scopus 로고
    • Isolation and structure of tunichrome B-1, a reducing blood pigment from the tunicate Ascidia nigra L
    • Bruening R.C., Oltz E.M., Furukawa J., Nakanishi K. Isolation and structure of tunichrome B-1, a reducing blood pigment from the tunicate Ascidia nigra L. J. Am. Chem. Soc. 1985, 107:5298-5300.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 5298-5300
    • Bruening, R.C.1    Oltz, E.M.2    Furukawa, J.3    Nakanishi, K.4
  • 21
    • 0022675662 scopus 로고
    • Isolation of tunichrome B-1, a reducing blood pigment of the sea squirt, Ascidia nigra
    • Bruening R.C., Oltz E.M., Furukawa J., Nakanishi K., Kustin K. Isolation of tunichrome B-1, a reducing blood pigment of the sea squirt, Ascidia nigra. J. Nat. Prod. 1986, 49:193-204.
    • (1986) J. Nat. Prod. , vol.49 , pp. 193-204
    • Bruening, R.C.1    Oltz, E.M.2    Furukawa, J.3    Nakanishi, K.4    Kustin, K.5
  • 22
    • 0003600825 scopus 로고
    • Sinauer Associates, Sunderland, MA.
    • Brusca R.C., Brusca G.J. Invertebrates 1990, Sinauer Associates, Sunderland, MA, 922 pp.
    • (1990) Invertebrates , pp. 922
    • Brusca, R.C.1    Brusca, G.J.2
  • 23
    • 0035140529 scopus 로고    scopus 로고
    • Molecular evolution of the arthropod hemocyanin superfamily
    • Burmester T. Molecular evolution of the arthropod hemocyanin superfamily. Mol. Biol. Evol. 2001, 18:184-195.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 184-195
    • Burmester, T.1
  • 24
    • 1242277861 scopus 로고    scopus 로고
    • Evolutionary history and diversity of arthropod hemocyanins
    • Burmester T. Evolutionary history and diversity of arthropod hemocyanins. Micron 2004, 35:121-122.
    • (2004) Micron , vol.35 , pp. 121-122
    • Burmester, T.1
  • 25
    • 0035079852 scopus 로고    scopus 로고
    • Reactivity of peptidyl tyrosine to hydroxylation and crosslinking
    • Burzio L.A., Waite J.H. Reactivity of peptidyl tyrosine to hydroxylation and crosslinking. Protein Sci. 2001, 10:735-740.
    • (2001) Protein Sci. , vol.10 , pp. 735-740
    • Burzio, L.A.1    Waite, J.H.2
  • 26
    • 0036629205 scopus 로고    scopus 로고
    • The other topa: formation of 3,4,5-trihydroxyphenylalanine in peptides
    • Burzio L.A., Waite J.H. The other topa: formation of 3,4,5-trihydroxyphenylalanine in peptides. Anal. Biochem. 2002, 306:108-114.
    • (2002) Anal. Biochem. , vol.306 , pp. 108-114
    • Burzio, L.A.1    Waite, J.H.2
  • 27
    • 47949087372 scopus 로고    scopus 로고
    • The crosslinking and antimicrobial properties of tunichrome
    • Cai M., Sugumaran M., Robinson W.E. The crosslinking and antimicrobial properties of tunichrome. Comp. Biochem. Physiol. B 2008, 151:110-117.
    • (2008) Comp. Biochem. Physiol. B , vol.151 , pp. 110-117
    • Cai, M.1    Sugumaran, M.2    Robinson, W.E.3
  • 29
    • 0005789228 scopus 로고
    • Cytotoxic activity of Styela plicata hemocytes against mammalian cell targets: II. Properties of the in vitro reaction against human tumor cell lines
    • Cammarata M., Candore G., Arizza V., Caruso C., Parrinello N. Cytotoxic activity of Styela plicata hemocytes against mammalian cell targets: II. Properties of the in vitro reaction against human tumor cell lines. Anim. Biol. 1995, 4:139-144.
    • (1995) Anim. Biol. , vol.4 , pp. 139-144
    • Cammarata, M.1    Candore, G.2    Arizza, V.3    Caruso, C.4    Parrinello, N.5
  • 32
    • 0001732168 scopus 로고
    • Nuclear magnetic resonance spectrum of living tunicate blood cells and the structure of the native vanadium chromogen
    • Carlson R.M.K. Nuclear magnetic resonance spectrum of living tunicate blood cells and the structure of the native vanadium chromogen. Proc. Natl. Acad. Sci. 1975, 72:2217-2221.
    • (1975) Proc. Natl. Acad. Sci. , vol.72 , pp. 2217-2221
    • Carlson, R.M.K.1
  • 34
    • 1642463826 scopus 로고    scopus 로고
    • The prophenoloxidase-activating system in invertebrates
    • Cerenius L., Söderhäll K. The prophenoloxidase-activating system in invertebrates. Immunol. Rev. 2004, 198:116-126.
    • (2004) Immunol. Rev. , vol.198 , pp. 116-126
    • Cerenius, L.1    Söderhäll, K.2
  • 35
    • 44649197623 scopus 로고    scopus 로고
    • The proPO-system: pros and cons for its role in invertebrate immunity
    • Cerenius L., Lee B.L., Söderhäll K. The proPO-system: pros and cons for its role in invertebrate immunity. Trends Immunol. 2008, 29:263-271.
    • (2008) Trends Immunol. , vol.29 , pp. 263-271
    • Cerenius, L.1    Lee, B.L.2    Söderhäll, K.3
  • 36
    • 0000757188 scopus 로고
    • Ortho-diphenoloxidase system of ascidians
    • Chaga O.Y. Ortho-diphenoloxidase system of ascidians. Tsitologiya 1980, 22:619-625.
    • (1980) Tsitologiya , vol.22 , pp. 619-625
    • Chaga, O.Y.1
  • 37
    • 0033816833 scopus 로고    scopus 로고
    • Purification, characterization and molecular cloning of prophenoloxidases from Sarcophaga bullata
    • Chase M.R., Raina K., Bruno J., Sugumaran M. Purification, characterization and molecular cloning of prophenoloxidases from Sarcophaga bullata. Insect Biochem. Mol. Biol. 2000, 30:953-967.
    • (2000) Insect Biochem. Mol. Biol. , vol.30 , pp. 953-967
    • Chase, M.R.1    Raina, K.2    Bruno, J.3    Sugumaran, M.4
  • 38
    • 0000501984 scopus 로고
    • The biochemistry of vanadium
    • Chasteen N.D. The biochemistry of vanadium. Struct. Bond. 1983, 53:105-138.
    • (1983) Struct. Bond. , vol.53 , pp. 105-138
    • Chasteen, N.D.1
  • 40
    • 4544292891 scopus 로고    scopus 로고
    • Analysis of the Henze precipitate from the blood cells of the ascidian Phallusia mammillata
    • Ciancio A., Scippa S., Nette G., de Vincentiis M. Analysis of the Henze precipitate from the blood cells of the ascidian Phallusia mammillata. Naturwissenschaften 2004, 91:366-370.
    • (2004) Naturwissenschaften , vol.91 , pp. 366-370
    • Ciancio, A.1    Scippa, S.2    Nette, G.3    de Vincentiis, M.4
  • 42
    • 0017715897 scopus 로고
    • Studies on the fibrous components of the test of Ciona intestinalis Linnaeus. I. Cellulose-like polysaccharide
    • De Leo G., Patricolo E., D'Ancona Lunetta G. Studies on the fibrous components of the test of Ciona intestinalis Linnaeus. I. Cellulose-like polysaccharide. Acta Zool. 1977, 58:135-141.
    • (1977) Acta Zool. , vol.58 , pp. 135-141
    • De Leo, G.1    Patricolo, E.2    D'Ancona Lunetta, G.3
  • 43
    • 0019869093 scopus 로고
    • Accumulation of vanadium by tunicate blood cells occurs via a specific anion transport system
    • Dingley A.L., Kustin K., Macara I.G., McLeod G.C. Accumulation of vanadium by tunicate blood cells occurs via a specific anion transport system. Biochim. Biophys. Acta 1981, 649:493-502.
    • (1981) Biochim. Biophys. Acta , vol.649 , pp. 493-502
    • Dingley, A.L.1    Kustin, K.2    Macara, I.G.3    McLeod, G.C.4
  • 45
    • 77950518275 scopus 로고    scopus 로고
    • Insect multicopper oxidases: diversity, properties and physiological roles
    • Dittmer N.T., Kanost M.R. Insect multicopper oxidases: diversity, properties and physiological roles. Insect Biochem. Mol. Biol. 2010, 40:179-188.
    • (2010) Insect Biochem. Mol. Biol. , vol.40 , pp. 179-188
    • Dittmer, N.T.1    Kanost, M.R.2
  • 46
    • 0000444745 scopus 로고
    • Ferreascidin: a highly aromatic protein containing 3,4-dihydroxypphenylalanine from the blood cells of a stolidobranch ascidian
    • Dorsett L.C., Hawkins C.J., Grice J.A., Lavin M.F., Merefield P.M., Parry D.L., Ross I.L. Ferreascidin: a highly aromatic protein containing 3,4-dihydroxypphenylalanine from the blood cells of a stolidobranch ascidian. Biochemistry 1987, 26:8078-8082.
    • (1987) Biochemistry , vol.26 , pp. 8078-8082
    • Dorsett, L.C.1    Hawkins, C.J.2    Grice, J.A.3    Lavin, M.F.4    Merefield, P.M.5    Parry, D.L.6    Ross, I.L.7
  • 47
    • 0001291713 scopus 로고
    • The blood cells of the ascidian, Phallusia mammillata
    • Endean R. The blood cells of the ascidian, Phallusia mammillata. Q. J. Microsc. Sci. 1960, 101:177-197.
    • (1960) Q. J. Microsc. Sci. , vol.101 , pp. 177-197
    • Endean, R.1
  • 48
    • 0011452022 scopus 로고
    • Interactions between vanadate and 1,2-aromatic diols. Complex formation and oxidation-reduction
    • Ferguson J.H., Kustin K. Interactions between vanadate and 1,2-aromatic diols. Complex formation and oxidation-reduction. Inorg. Chem. 1979, 18:3349-3357.
    • (1979) Inorg. Chem. , vol.18 , pp. 3349-3357
    • Ferguson, J.H.1    Kustin, K.2
  • 49
    • 0034716135 scopus 로고    scopus 로고
    • Defining chemical species in complex environments using K-edge X-ray absorption spectroscopy: vanadium in intact blood cells and Henze solution from the tunicate Ascidia ceratodes
    • Frank P., Hodgson K.O. Defining chemical species in complex environments using K-edge X-ray absorption spectroscopy: vanadium in intact blood cells and Henze solution from the tunicate Ascidia ceratodes. Inorg. Chem. 2000, 39:6018-6027.
    • (2000) Inorg. Chem. , vol.39 , pp. 6018-6027
    • Frank, P.1    Hodgson, K.O.2
  • 50
    • 33845375845 scopus 로고
    • Vanadyl ion EPR as a non-invasive probe of pH in intact vanadocytes from Ascidia ceratodes
    • Frank P., Carlson R.M.K., Hodgson K.O. Vanadyl ion EPR as a non-invasive probe of pH in intact vanadocytes from Ascidia ceratodes. Inorg. Chem. 1986, 25:470-478.
    • (1986) Inorg. Chem. , vol.25 , pp. 470-478
    • Frank, P.1    Carlson, R.M.K.2    Hodgson, K.O.3
  • 51
    • 0023651151 scopus 로고
    • A large reservoir of sulfate and sulfonate resides within plasma cells from Ascidia ceratodes, revealed by X-ray absorption near-edge structure spectroscopy
    • Frank P., Hedman B., Carlson R.M.K., Tyson T.A., Roe A.L., Hodgson K.O. A large reservoir of sulfate and sulfonate resides within plasma cells from Ascidia ceratodes, revealed by X-ray absorption near-edge structure spectroscopy. Biochemistry 1987, 26:4975-4979.
    • (1987) Biochemistry , vol.26 , pp. 4975-4979
    • Frank, P.1    Hedman, B.2    Carlson, R.M.K.3    Tyson, T.A.4    Roe, A.L.5    Hodgson, K.O.6
  • 52
    • 0000920046 scopus 로고
    • Interaction of vanadium and sulfate in blood cells from the tunicate Ascidia ceratodes: observations using X-ray absorption edge structure and EPR spectroscopies
    • Frank P., Hedman B., Carlson R.M.K., Hodgson K.O. Interaction of vanadium and sulfate in blood cells from the tunicate Ascidia ceratodes: observations using X-ray absorption edge structure and EPR spectroscopies. Inorg. Chem. 1994, 33:3794-3803.
    • (1994) Inorg. Chem. , vol.33 , pp. 3794-3803
    • Frank, P.1    Hedman, B.2    Carlson, R.M.K.3    Hodgson, K.O.4
  • 53
    • 0000123194 scopus 로고
    • Nature and ligation of vanadium within whole blood cells and Henze solution from the tunicate Ascidia ceratodes, as investigated by using X-ray absorption spectroscopy
    • Frank P., Kustin K., Robinson W.E., Linebaugh L., Hodgson K.O. Nature and ligation of vanadium within whole blood cells and Henze solution from the tunicate Ascidia ceratodes, as investigated by using X-ray absorption spectroscopy. Inorg. Chem. 1995, 34:5942-5949.
    • (1995) Inorg. Chem. , vol.34 , pp. 5942-5949
    • Frank, P.1    Kustin, K.2    Robinson, W.E.3    Linebaugh, L.4    Hodgson, K.O.5
  • 54
    • 0032544659 scopus 로고    scopus 로고
    • Vanadium K-edge X-ray absorption spectroscopy reveals species differences within the same ascidian genera
    • Frank P., Hodgson K.O., Kustin K., Robinson W.E. Vanadium K-edge X-ray absorption spectroscopy reveals species differences within the same ascidian genera. J. Biol. Chem. 1998, 273:24498-24503.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24498-24503
    • Frank, P.1    Hodgson, K.O.2    Kustin, K.3    Robinson, W.E.4
  • 55
    • 40649092296 scopus 로고    scopus 로고
    • The uptake and fate of vanadyl ion in ascidian blood cells and a detailed hypothesis for the mechanism and location of biological vanadium reduction. A visible and X-ray absorption spectroscopy study
    • Frank P., Carlson E.J., Carlson R.M.K., Hedman B., Hodgson K.O. The uptake and fate of vanadyl ion in ascidian blood cells and a detailed hypothesis for the mechanism and location of biological vanadium reduction. A visible and X-ray absorption spectroscopy study. J. Inorg. Biochem. 2008, 102:809-823.
    • (2008) J. Inorg. Biochem. , vol.102 , pp. 809-823
    • Frank, P.1    Carlson, E.J.2    Carlson, R.M.K.3    Hedman, B.4    Hodgson, K.O.5
  • 56
    • 0033391991 scopus 로고    scopus 로고
    • Purification and partial characterization of phenoloxidase from the colonial ascidian Botryllus schlosseri
    • Frizzo A., Guidolin L., Ballarin L., Sabbadin A. Purification and partial characterization of phenoloxidase from the colonial ascidian Botryllus schlosseri. Mar. Biol. 1999, 135:483-488.
    • (1999) Mar. Biol. , vol.135 , pp. 483-488
    • Frizzo, A.1    Guidolin, L.2    Ballarin, L.3    Sabbadin, A.4
  • 57
    • 0012448724 scopus 로고    scopus 로고
    • Immunolocalization of phenoloxidase in the vacuoles of the compound ascidian Botryllus schlosseri morula cells
    • Frizzo A., Guidolin L., Ballarin L., Balden B., Sabbadin A. Immunolocalization of phenoloxidase in the vacuoles of the compound ascidian Botryllus schlosseri morula cells. Ital. J. Zool. 2000, 67:273-276.
    • (2000) Ital. J. Zool. , vol.67 , pp. 273-276
    • Frizzo, A.1    Guidolin, L.2    Ballarin, L.3    Balden, B.4    Sabbadin, A.5
  • 58
    • 77956736173 scopus 로고
    • The physiology of ascidians
    • Academic Press, London
    • Goodbody I. The physiology of ascidians. Advances in Marine Biology 1974, vol. 12:1-149. Academic Press, London.
    • (1974) Advances in Marine Biology , vol.12 , pp. 1-149
    • Goodbody, I.1
  • 59
    • 0344089900 scopus 로고
    • Human and other animal cellulose
    • Hall D.A., Saxl H. Human and other animal cellulose. Nature 1960, 187:547-550.
    • (1960) Nature , vol.187 , pp. 547-550
    • Hall, D.A.1    Saxl, H.2
  • 60
    • 0029112663 scopus 로고
    • Proenzyme of Manduca sexta phenol oxidase: purification, activation, substrate specificity of the active enzyme and molecular cloning
    • Hall M., Scott T., Sugumaran M., Söderhäll K., Law J.H. Proenzyme of Manduca sexta phenol oxidase: purification, activation, substrate specificity of the active enzyme and molecular cloning. Proc. Natl. Acad. Sci. 1995, 92:7764-7768.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 7764-7768
    • Hall, M.1    Scott, T.2    Sugumaran, M.3    Söderhäll, K.4    Law, J.H.5
  • 61
    • 0031817504 scopus 로고    scopus 로고
    • Ascidian phenoloxidase: its release from hemocytes, isolation, characterization and physiological roles
    • Hata S., Azumi K., Yokosawa H. Ascidian phenoloxidase: its release from hemocytes, isolation, characterization and physiological roles. Comp. Biochem. Physiol. B 1998, 119:769-776.
    • (1998) Comp. Biochem. Physiol. B , vol.119 , pp. 769-776
    • Hata, S.1    Azumi, K.2    Yokosawa, H.3
  • 64
    • 84941831900 scopus 로고
    • Unterschungen uber das blut der ascidien. I. Mitteilung. Die vanadiumverbindung der blutkorperchen
    • Henze M. Unterschungen uber das blut der ascidien. I. Mitteilung. Die vanadiumverbindung der blutkorperchen. Hoppe Seylers Z. Physiol. Chem. 1911, 72:494-501.
    • (1911) Hoppe Seylers Z. Physiol. Chem. , vol.72 , pp. 494-501
    • Henze, M.1
  • 65
    • 0001629640 scopus 로고
    • Unterschungen uber das blut der ascidien. II. Mitteilung
    • Henze M. Unterschungen uber das blut der ascidien. II. Mitteilung. Hoppe Seylers Z. Physiol. Chem. 1912, 79:215-228.
    • (1912) Hoppe Seylers Z. Physiol. Chem. , vol.79 , pp. 215-228
    • Henze, M.1
  • 66
    • 84862996694 scopus 로고
    • Unterschungen uber das blut der ascidien. III. Mitteilung
    • Henze M. Unterschungen uber das blut der ascidien. III. Mitteilung. Z. Physiol. Chem. 1913, 86:340-344.
    • (1913) Z. Physiol. Chem. , vol.86 , pp. 340-344
    • Henze, M.1
  • 67
    • 0026101282 scopus 로고
    • Valency of vanadium in the vanadocytes of Ascidia gemmata separated by density-gradient centrifugation
    • Hirata J., Michibata H. Valency of vanadium in the vanadocytes of Ascidia gemmata separated by density-gradient centrifugation. J. Exp. Zool. 1991, 257:160-165.
    • (1991) J. Exp. Zool. , vol.257 , pp. 160-165
    • Hirata, J.1    Michibata, H.2
  • 68
    • 0013545501 scopus 로고
    • Synthesis of unprotected (±)-tunichrome An-1, a tunicate blood pigment
    • Horenstein B.A., Nakanishi K. Synthesis of unprotected (±)-tunichrome An-1, a tunicate blood pigment. J. Am. Chem. Soc. 1989, 111:6242-6246.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 6242-6246
    • Horenstein, B.A.1    Nakanishi, K.2
  • 69
    • 1642308130 scopus 로고    scopus 로고
    • Putative phenoloxidases in the tunicate Ciona intestinalis and the origin of the arthropod hemocyanin superfamily
    • Immesberger A., Burmester T. Putative phenoloxidases in the tunicate Ciona intestinalis and the origin of the arthropod hemocyanin superfamily. J. Comp. Physiol. B 2004, 174:169-180.
    • (2004) J. Comp. Physiol. B , vol.174 , pp. 169-180
    • Immesberger, A.1    Burmester, T.2
  • 70
    • 42549092546 scopus 로고    scopus 로고
    • Chemistry of mixed melanogenesis: pivotal roles of dopaquinone
    • Ito S., Wakamatsu K. Chemistry of mixed melanogenesis: pivotal roles of dopaquinone. Photochem. Photobiol. 2008, 84:582-592.
    • (2008) Photochem. Photobiol. , vol.84 , pp. 582-592
    • Ito, S.1    Wakamatsu, K.2
  • 71
    • 20444506858 scopus 로고    scopus 로고
    • Recent advances in the innate immunity of invertebrate animals
    • Iwanaga S., Lee B.L. Recent advances in the innate immunity of invertebrate animals. J. Biochem. Mol. Biol. 2005, 38:128-150.
    • (2005) J. Biochem. Mol. Biol. , vol.38 , pp. 128-150
    • Iwanaga, S.1    Lee, B.L.2
  • 72
    • 0027463054 scopus 로고
    • In vitro phenoloxidase activity in the blood of Ciona intestinalis and other ascidians
    • Jackson A.D., Smith V.J., Peddie C.M. In vitro phenoloxidase activity in the blood of Ciona intestinalis and other ascidians. Dev. Comp. Immunol. 1993, 17:97-108.
    • (1993) Dev. Comp. Immunol. , vol.17 , pp. 97-108
    • Jackson, A.D.1    Smith, V.J.2    Peddie, C.M.3
  • 73
    • 0025374783 scopus 로고
    • A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine amine oxidase
    • Jane S.M., Mu D., Wemmer D., Smith A.I., Kaur S., Malby D., Burlingame A.I., Klinman J.P. A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine amine oxidase. Science 1990, 248:981-987.
    • (1990) Science , vol.248 , pp. 981-987
    • Jane, S.M.1    Mu, D.2    Wemmer, D.3    Smith, A.I.4    Kaur, S.5    Malby, D.6    Burlingame, A.I.7    Klinman, J.P.8
  • 74
    • 36549029991 scopus 로고
    • Comparative studies on the in vitro response of bacteria to invertebrate body fluids. II. Aplysia californica (Sea Hare) and Ciona intestinalis (Tunicate)
    • Johnson P.T., Chapman F.A. Comparative studies on the in vitro response of bacteria to invertebrate body fluids. II. Aplysia californica (Sea Hare) and Ciona intestinalis (Tunicate). J. Invertebr. Pathol. 1970, 16:259-267.
    • (1970) J. Invertebr. Pathol. , vol.16 , pp. 259-267
    • Johnson, P.T.1    Chapman, F.A.2
  • 75
    • 0001401444 scopus 로고
    • Intracellular sites of activity in the histogenesis of tunicate vanadocytes
    • Kalk M. Intracellular sites of activity in the histogenesis of tunicate vanadocytes. Q. J. Microsc. Sci. 1963, 104:483-493.
    • (1963) Q. J. Microsc. Sci. , vol.104 , pp. 483-493
    • Kalk, M.1
  • 76
    • 0033393526 scopus 로고    scopus 로고
    • Direct reduction from vanadium (V) to vanadium (IV) by NADPH in the presence of EDTA. A consideration of the reduction and accumulation of vanadium in the ascidian blood cells
    • Kanamori K., Sakurai M., Kinoshita T., Uyama T., Ueki T., Michibata H. Direct reduction from vanadium (V) to vanadium (IV) by NADPH in the presence of EDTA. A consideration of the reduction and accumulation of vanadium in the ascidian blood cells. J. Inorg. Biochem. 1999, 77:157-161.
    • (1999) J. Inorg. Biochem. , vol.77 , pp. 157-161
    • Kanamori, K.1    Sakurai, M.2    Kinoshita, T.3    Uyama, T.4    Ueki, T.5    Michibata, H.6
  • 78
    • 0034648298 scopus 로고    scopus 로고
    • The Haber-Weiss reaction and mechanism of toxicity
    • Kehrer J.P. The Haber-Weiss reaction and mechanism of toxicity. Toxicology 2000, 149:43-50.
    • (2000) Toxicology , vol.149 , pp. 43-50
    • Kehrer, J.P.1
  • 79
    • 0025600973 scopus 로고
    • Synthesis of the tunichromes Mm-1 and Mm-2, blood pigments of the iron-assimilating tunicate, Molgula manhattensis
    • Kim D., Li Y., Horenstein B.A., Nakanishi K. Synthesis of the tunichromes Mm-1 and Mm-2, blood pigments of the iron-assimilating tunicate, Molgula manhattensis. Tetrahedron Lett. 1990, 31:7119-7122.
    • (1990) Tetrahedron Lett. , vol.31 , pp. 7119-7122
    • Kim, D.1    Li, Y.2    Horenstein, B.A.3    Nakanishi, K.4
  • 80
    • 33845225475 scopus 로고
    • Isolation of unstable tunichromes from tunicate blood via protection-deprotection
    • Kim D., Li Y., Nakanishi K. Isolation of unstable tunichromes from tunicate blood via protection-deprotection. J. Chem. Soc. Chem. Commun. 1991, 1991:9-10.
    • (1991) J. Chem. Soc. Chem. Commun. , vol.1991 , pp. 9-10
    • Kim, D.1    Li, Y.2    Nakanishi, K.3
  • 81
  • 82
    • 0041806802 scopus 로고    scopus 로고
    • Determination of the through-bond carbon-carbon and carbon-proton connectivities of the native celluloses in the solid state
    • Kono H., Erata T., Takai M. Determination of the through-bond carbon-carbon and carbon-proton connectivities of the native celluloses in the solid state. Macromolecules 2003, 36:5131-5138.
    • (2003) Macromolecules , vol.36 , pp. 5131-5138
    • Kono, H.1    Erata, T.2    Takai, M.3
  • 83
    • 0017101786 scopus 로고
    • The kinetics of the reduction of cytochrome c by the superoxide anion radical
    • Koppenol W.H., van Buuren K.J., Butler J., Braams R. The kinetics of the reduction of cytochrome c by the superoxide anion radical. Biochim. Biophys. Acta 1976, 449:157-168.
    • (1976) Biochim. Biophys. Acta , vol.449 , pp. 157-168
    • Koppenol, W.H.1    van Buuren, K.J.2    Butler, J.3    Braams, R.4
  • 84
    • 0001168958 scopus 로고
    • Interaction of catechol and catechol derivatives with dioxovanadium(V). I. Kinetics of complex formation in acidic media
    • Kustin K., Liu S.-T., Nicolini C., Toppen D.L. Interaction of catechol and catechol derivatives with dioxovanadium(V). I. Kinetics of complex formation in acidic media. J. Am. Chem. Soc. 1974, 96:7410-7415.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 7410-7415
    • Kustin, K.1    Liu, S.-T.2    Nicolini, C.3    Toppen, D.L.4
  • 85
    • 0001275818 scopus 로고
    • Interaction of catechol and catechol derivatives with dioxovanadium (V). II. Kinetics of ligand oxidation
    • Kustin K., Nicolini C., Toppen D.L. Interaction of catechol and catechol derivatives with dioxovanadium (V). II. Kinetics of ligand oxidation. J. Am. Chem. Soc. 1974, 96:7416-7420.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 7416-7420
    • Kustin, K.1    Nicolini, C.2    Toppen, D.L.3
  • 86
    • 0000342247 scopus 로고
    • Tunichromes, vanadium, and vacuolated blood cells in tunicates
    • Kustin K., Robinson W.E., Smith M.J. Tunichromes, vanadium, and vacuolated blood cells in tunicates. Invertebr. Reprod. Dev. 1990, 17:129-139.
    • (1990) Invertebr. Reprod. Dev. , vol.17 , pp. 129-139
    • Kustin, K.1    Robinson, W.E.2    Smith, M.J.3
  • 87
  • 89
    • 0025165288 scopus 로고
    • The intracellular pH of tunicate blood cells: Ascidia ceratodes whole blood, morula cells, vacuoles and cytoplasm
    • Lee S., Nakanishi K., Kustin K. The intracellular pH of tunicate blood cells: Ascidia ceratodes whole blood, morula cells, vacuoles and cytoplasm. Biochim. Biophys. Acta 1990, 1033:311-317.
    • (1990) Biochim. Biophys. Acta , vol.1033 , pp. 311-317
    • Lee, S.1    Nakanishi, K.2    Kustin, K.3
  • 90
    • 0001505184 scopus 로고    scopus 로고
    • Styelins, broad-spectrum antimicrobial peptides from the solitary tunicate, Styela clava
    • Lee I.H., Cho Y., Lehrer R.I. Styelins, broad-spectrum antimicrobial peptides from the solitary tunicate, Styela clava. Comp. Biochem. Physiol. B 1997, 118:515-521.
    • (1997) Comp. Biochem. Physiol. B , vol.118 , pp. 515-521
    • Lee, I.H.1    Cho, Y.2    Lehrer, R.I.3
  • 91
    • 1842373858 scopus 로고    scopus 로고
    • Effects of pH and salinity on the antimicrobial properties of clavanins
    • Lee I.H., Cho Y., Lehrer R.I. Effects of pH and salinity on the antimicrobial properties of clavanins. Infect. Immun. 1997, 65:2898-2903.
    • (1997) Infect. Immun. , vol.65 , pp. 2898-2903
    • Lee, I.H.1    Cho, Y.2    Lehrer, R.I.3
  • 92
    • 0000330275 scopus 로고    scopus 로고
    • Enzymatic and non-enzymatic pathways to formation of DOPA-modified PEG hydrogels
    • Lee B.P., Dalsin J.L., Messersmith P.B. Enzymatic and non-enzymatic pathways to formation of DOPA-modified PEG hydrogels. Polym. Prepr. 2001, 42:151-152.
    • (2001) Polym. Prepr. , vol.42 , pp. 151-152
    • Lee, B.P.1    Dalsin, J.L.2    Messersmith, P.B.3
  • 93
    • 0037968647 scopus 로고    scopus 로고
    • Plicatamide, an antimicrobial octapeptide from Styela plicata hemocytes
    • Lehrer R.I. Plicatamide, an antimicrobial octapeptide from Styela plicata hemocytes. J. Biol. Chem. 2003, 278:13546-13553.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13546-13553
    • Lehrer, R.I.1
  • 94
    • 0035057952 scopus 로고    scopus 로고
    • Clavanins and styelins, alpha-helical antimicrobial peptides from the hemocytes of Styela clava
    • Lehrer R.I., Lee I.H., Menzel L., Waring A., Zhao C. Clavanins and styelins, alpha-helical antimicrobial peptides from the hemocytes of Styela clava. Adv. Exp. Med. Biol. 2001, 484:71-76.
    • (2001) Adv. Exp. Med. Biol. , vol.484 , pp. 71-76
    • Lehrer, R.I.1    Lee, I.H.2    Menzel, L.3    Waring, A.4    Zhao, C.5
  • 95
    • 0042203502 scopus 로고    scopus 로고
    • Natural peptide antibiotics from tunicates: structures, functions and potential uses
    • Lehrer R.I., Tincu J.A., Taylor S.W., Menzel L.P., Waring A.J. Natural peptide antibiotics from tunicates: structures, functions and potential uses. Integr. Comp. Biol. 2003, 43:313-322.
    • (2003) Integr. Comp. Biol. , vol.43 , pp. 313-322
    • Lehrer, R.I.1    Tincu, J.A.2    Taylor, S.W.3    Menzel, L.P.4    Waring, A.J.5
  • 96
    • 0005838113 scopus 로고
    • Cytotoxic activity of Styela plicata hemocytes against mammalian cell targets: I. Properties of the in vitro reaction against erythrocytes
    • Lipari L., Cammarata M., Arizza V., Parrinello D. Cytotoxic activity of Styela plicata hemocytes against mammalian cell targets: I. Properties of the in vitro reaction against erythrocytes. Anim. Biol. 1995, 4:131-137.
    • (1995) Anim. Biol. , vol.4 , pp. 131-137
    • Lipari, L.1    Cammarata, M.2    Arizza, V.3    Parrinello, D.4
  • 97
    • 0018508886 scopus 로고
    • Isolation, properties and structural studies on a compound from tunicate blood cells that may be involved in vanadium accumulation
    • Macara I.G., McLeod G.C., Kustin K. Isolation, properties and structural studies on a compound from tunicate blood cells that may be involved in vanadium accumulation. Biochem. J. 1979, 181:457-465.
    • (1979) Biochem. J. , vol.181 , pp. 457-465
    • Macara, I.G.1    McLeod, G.C.2    Kustin, K.3
  • 99
    • 0022498770 scopus 로고
    • Optimization of hydroxylation of tyrosine and tyrosine-containing peptides by mushroom tyrosinase
    • Marumo K., Waite J.H. Optimization of hydroxylation of tyrosine and tyrosine-containing peptides by mushroom tyrosinase. Biochim. Biophys. Acta 1986, 872:98-103.
    • (1986) Biochim. Biophys. Acta , vol.872 , pp. 98-103
    • Marumo, K.1    Waite, J.H.2
  • 100
    • 0025956444 scopus 로고
    • Biochemical and energetic composition, population biology, and chemical defense of the Antarctic ascidian Cnemidocarpa verrucosa Lesson
    • McClintock J.B., Heine J., Slattery M., Weston J. Biochemical and energetic composition, population biology, and chemical defense of the Antarctic ascidian Cnemidocarpa verrucosa Lesson. J. Exp. Mar. Biol. Ecol. 1991, 147:163-175.
    • (1991) J. Exp. Mar. Biol. Ecol. , vol.147 , pp. 163-175
    • McClintock, J.B.1    Heine, J.2    Slattery, M.3    Weston, J.4
  • 102
    • 0008612937 scopus 로고
    • New aspects of accumulation and reduction of vanadium ions in ascidians, based on concerted investigation from both a chemical and biological viewpoint
    • Michibata H. New aspects of accumulation and reduction of vanadium ions in ascidians, based on concerted investigation from both a chemical and biological viewpoint. Zool. Sci. 1989, 6:639-647.
    • (1989) Zool. Sci. , vol.6 , pp. 639-647
    • Michibata, H.1
  • 103
    • 79952281951 scopus 로고    scopus 로고
    • Advances in research on the accumulation, redox behavior, and function of vanadium in ascidians
    • Michibata H., Ueki T. Advances in research on the accumulation, redox behavior, and function of vanadium in ascidians. BioMol. Concepts 2010, 1:97-107.
    • (2010) BioMol. Concepts , vol.1 , pp. 97-107
    • Michibata, H.1    Ueki, T.2
  • 104
    • 84989656815 scopus 로고
    • Separation of vanadocytes: determination and characterization of vanadium ion in the separated blood cells of the ascidian, Ascidia ahodori
    • Michibata H., Hirata J., Uesaka M., Numakunai T., Sakurai H. Separation of vanadocytes: determination and characterization of vanadium ion in the separated blood cells of the ascidian, Ascidia ahodori. J. Exp. Zool. 1987, 244:33-38.
    • (1987) J. Exp. Zool. , vol.244 , pp. 33-38
    • Michibata, H.1    Hirata, J.2    Uesaka, M.3    Numakunai, T.4    Sakurai, H.5
  • 105
    • 0002228066 scopus 로고
    • Vanadium-containing blood cells (vanadocytes) show no fluorescence due to the tunichrome in the ascidian, Ascidia sydneiensis samea
    • Michibata H., Uyama T., Hirata J. Vanadium-containing blood cells (vanadocytes) show no fluorescence due to the tunichrome in the ascidian, Ascidia sydneiensis samea. Zool. Sci. 1990, 7:55-61.
    • (1990) Zool. Sci. , vol.7 , pp. 55-61
    • Michibata, H.1    Uyama, T.2    Hirata, J.3
  • 106
    • 84989636827 scopus 로고
    • Isolation of highly acidic and vanadium-containing blood cells from among several types of blood cells in Ascidiidae species by density-gradient centrifugation
    • Michibata H., Iwata Y., Hirata J. Isolation of highly acidic and vanadium-containing blood cells from among several types of blood cells in Ascidiidae species by density-gradient centrifugation. J. Exp. Zool. 1991, 257:306-313.
    • (1991) J. Exp. Zool. , vol.257 , pp. 306-313
    • Michibata, H.1    Iwata, Y.2    Hirata, J.3
  • 107
    • 0002287042 scopus 로고
    • Evolution in ascidians
    • George Allen and Unwin, Ltd., London, H. Barnes (Ed.)
    • Millar R.H. Evolution in ascidians. Some Contemporary Studies in Marine Science 1966, 519-534. George Allen and Unwin, Ltd., London. H. Barnes (Ed.).
    • (1966) Some Contemporary Studies in Marine Science , pp. 519-534
    • Millar, R.H.1
  • 108
    • 0003008016 scopus 로고
    • The biology of ascidians
    • Academic Press, London
    • Millar R.H. The biology of ascidians. Advances in Marine Biology 1971, vol. 9:1-100. Academic Press, London.
    • (1971) Advances in Marine Biology , vol.9 , pp. 1-100
    • Millar, R.H.1
  • 109
    • 0034129232 scopus 로고    scopus 로고
    • Origin of the Henze solution/precipitate from morula cells of the blood of the ascidian Phallusia mammillata
    • Nette G., Scippa S., de Vincentiis M. Origin of the Henze solution/precipitate from morula cells of the blood of the ascidian Phallusia mammillata. Naturwissenschaften 2000, 87:220-224.
    • (2000) Naturwissenschaften , vol.87 , pp. 220-224
    • Nette, G.1    Scippa, S.2    de Vincentiis, M.3
  • 110
    • 0032723494 scopus 로고    scopus 로고
    • 5,6-Dihydroxyindoles in the Fenton reaction: a model study of the role of melanin precursors in oxidative stress and hyperpigmentary processes
    • Novellino L., Napolitano A., Prota G. 5,6-Dihydroxyindoles in the Fenton reaction: a model study of the role of melanin precursors in oxidative stress and hyperpigmentary processes. Chem. Res. Toxicol. 1999, 12:985-992.
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 985-992
    • Novellino, L.1    Napolitano, A.2    Prota, G.3
  • 111
    • 33845278462 scopus 로고
    • The tunichromes. A class of reducing blood pigments from sea squirts: isolation, structures and vanadium chemistry
    • Oltz E.M., Bruening R.C., Smith M.J., Kustin K., Nakanishi K. The tunichromes. A class of reducing blood pigments from sea squirts: isolation, structures and vanadium chemistry. J. Am. Chem. Soc. 1988, 110:6162-6172.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 6162-6172
    • Oltz, E.M.1    Bruening, R.C.2    Smith, M.J.3    Kustin, K.4    Nakanishi, K.5
  • 113
    • 0026987504 scopus 로고
    • Complex formation of tunichrome Mm-2 with ferrous and ferric ions
    • Paik Y.-S. Complex formation of tunichrome Mm-2 with ferrous and ferric ions. Arch. Pharm. Res. 1992, 15:269-271.
    • (1992) Arch. Pharm. Res. , vol.15 , pp. 269-271
    • Paik, Y.-S.1
  • 114
    • 0343058970 scopus 로고    scopus 로고
    • Storniamides A-D: alkaloids from a patagonian sponge, Cliona sp.
    • Palermo J.A., Brasco M.F.R., Seldes A.M. Storniamides A-D: alkaloids from a patagonian sponge, Cliona sp. Tetrahedron 1996, 52:2727-2734.
    • (1996) Tetrahedron , vol.52 , pp. 2727-2734
    • Palermo, J.A.1    Brasco, M.F.R.2    Seldes, A.M.3
  • 115
  • 116
    • 0005882581 scopus 로고
    • Cytotoxic activity of invertebrate hemocytes with preliminary findings on the tunicate Ciona intestinalis
    • Parrinello N., Arizza V. Cytotoxic activity of invertebrate hemocytes with preliminary findings on the tunicate Ciona intestinalis. Boll. Zool. 1992, 59:183-189.
    • (1992) Boll. Zool. , vol.59 , pp. 183-189
    • Parrinello, N.1    Arizza, V.2
  • 117
    • 0025005095 scopus 로고
    • Fine structural observations of the granulocytes involved in the tunic inflammatory-like reaction of Ciona intestinalis (Tunicata)
    • Parrinello N., De Leo G., Di Bella M.A. Fine structural observations of the granulocytes involved in the tunic inflammatory-like reaction of Ciona intestinalis (Tunicata). J. Invertebr. Pathol. 1990, 56:181-189.
    • (1990) J. Invertebr. Pathol. , vol.56 , pp. 181-189
    • Parrinello, N.1    De Leo, G.2    Di Bella, M.A.3
  • 118
    • 0043210537 scopus 로고    scopus 로고
    • Phenoloxidases in ascidian hemocytes: characterization of the prophenoloxidase activating system
    • Parrinello N., Arizza V., Chinnici C., Parrinello D., Cammarata M. Phenoloxidases in ascidian hemocytes: characterization of the prophenoloxidase activating system. Com. Biochem. Physiol. B 2003, 135:583-591.
    • (2003) Com. Biochem. Physiol. B , vol.135 , pp. 583-591
    • Parrinello, N.1    Arizza, V.2    Chinnici, C.3    Parrinello, D.4    Cammarata, M.5
  • 119
    • 0000170376 scopus 로고
    • Distribution of tunichrome in the Ascidiacea
    • Parry D.L., Brand S.G., Kustin K. Distribution of tunichrome in the Ascidiacea. Bull. Mar. Sci. 1992, 50:302-306.
    • (1992) Bull. Mar. Sci. , vol.50 , pp. 302-306
    • Parry, D.L.1    Brand, S.G.2    Kustin, K.3
  • 120
    • 0018566683 scopus 로고
    • Studies on the fibrous components of the test of Ciona intestinalis Linnaeus. II. Collagen-elastin-like protein
    • Patricolo E., De Leo G. Studies on the fibrous components of the test of Ciona intestinalis Linnaeus. II. Collagen-elastin-like protein. Acta Zool. 1979, 60:259-269.
    • (1979) Acta Zool. , vol.60 , pp. 259-269
    • Patricolo, E.1    De Leo, G.2
  • 121
    • 0027918508 scopus 로고
    • In vitro spontaneous cytotoxic activity against mammalian target cells by the hemocytes of the solitary ascidian, Ciona intestinalis
    • Peddie C.M., Smith V.J. In vitro spontaneous cytotoxic activity against mammalian target cells by the hemocytes of the solitary ascidian, Ciona intestinalis. J. Exp. Zool. 1993, 267:616-623.
    • (1993) J. Exp. Zool. , vol.267 , pp. 616-623
    • Peddie, C.M.1    Smith, V.J.2
  • 122
    • 0028155652 scopus 로고
    • Mechanism of cytotoxic activity by hemocytes of the solitary ascidian, Ciona intestinalis
    • Peddie C.M., Smith V.J. Mechanism of cytotoxic activity by hemocytes of the solitary ascidian, Ciona intestinalis. J. Exp. Zool. 1994, 270:335-342.
    • (1994) J. Exp. Zool. , vol.270 , pp. 335-342
    • Peddie, C.M.1    Smith, V.J.2
  • 123
    • 0000403817 scopus 로고
    • The localization of inorganic elements, particularly vanadium and sulfur, in hemolymph from the ascidians Ascidia mentula (Muller) and Ascidiella aspersa (Muller)
    • Pirie B.J.S., Bell M.V. The localization of inorganic elements, particularly vanadium and sulfur, in hemolymph from the ascidians Ascidia mentula (Muller) and Ascidiella aspersa (Muller). J. Exp. Mar. Biol. Ecol. 1984, 74:187-194.
    • (1984) J. Exp. Mar. Biol. Ecol. , vol.74 , pp. 187-194
    • Pirie, B.J.S.1    Bell, M.V.2
  • 124
    • 77951243863 scopus 로고    scopus 로고
    • Characterization of a novel type of oxidative decarboxylase involved in the biosynthesis of the styryl moiety of chondrochloren from an acylated tyrosine
    • Rachid S., Revemann O., Dauth C., Kazmaier U., Muller R. Characterization of a novel type of oxidative decarboxylase involved in the biosynthesis of the styryl moiety of chondrochloren from an acylated tyrosine. J. Biol. Chem. 2010, 285:12482-12489.
    • (2010) J. Biol. Chem. , vol.285 , pp. 12482-12489
    • Rachid, S.1    Revemann, O.2    Dauth, C.3    Kazmaier, U.4    Muller, R.5
  • 125
    • 0344143856 scopus 로고
    • Physico-chemical investigations on animal cellulose (tunicin)
    • Rånby B.G. Physico-chemical investigations on animal cellulose (tunicin). Ark. Kemi 1952, 4:241-248.
    • (1952) Ark. Kemi , vol.4 , pp. 241-248
    • Rånby, B.G.1
  • 126
    • 0028168040 scopus 로고
    • 1,2-Dehydro-N-β-alanyldopamine as a new intermediate in insect cuticular sclerotization
    • Ricketts D., Sugumaran M. 1,2-Dehydro-N-β-alanyldopamine as a new intermediate in insect cuticular sclerotization. J. Biol. Chem. 1994, 269:22217-22221.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22217-22221
    • Ricketts, D.1    Sugumaran, M.2
  • 128
    • 21344458362 scopus 로고    scopus 로고
    • Rejection patterns in botryllid ascidian immunity: the first tier of allorecognition
    • Rinkevich B. Rejection patterns in botryllid ascidian immunity: the first tier of allorecognition. Can. J. Zool. 2005, 83:101-121.
    • (2005) Can. J. Zool. , vol.83 , pp. 101-121
    • Rinkevich, B.1
  • 129
    • 84986468578 scopus 로고
    • 14C]glucose into the tunic of the ascidian, Ciona intestinalis (Linnaeus)
    • 14C]glucose into the tunic of the ascidian, Ciona intestinalis (Linnaeus). J. Exp. Zool. 1983, 225:187-195.
    • (1983) J. Exp. Zool. , vol.225 , pp. 187-195
    • Robinson, W.E.1    Kustin, K.2    McLeod, G.C.3
  • 130
    • 0021155483 scopus 로고
    • Tunichrome content in the blood cells of the tunicate, Ascidia callosa Stimpson, as an indicator of vanadium distribution
    • Robinson W.E., Agudelo M.I., Kustin K. Tunichrome content in the blood cells of the tunicate, Ascidia callosa Stimpson, as an indicator of vanadium distribution. Comp. Biochem. Physiol. A 1984, 78:667-673.
    • (1984) Comp. Biochem. Physiol. A , vol.78 , pp. 667-673
    • Robinson, W.E.1    Agudelo, M.I.2    Kustin, K.3
  • 131
    • 0022653287 scopus 로고
    • The influence of tunichrome and other reducing compounds on tunic and fin formation in embryonic Ascidia callosa Stimpson
    • Robinson W.E., Kustin K., Cloney R.A. The influence of tunichrome and other reducing compounds on tunic and fin formation in embryonic Ascidia callosa Stimpson. J. Exp. Zool. 1986, 237:63-72.
    • (1986) J. Exp. Zool. , vol.237 , pp. 63-72
    • Robinson, W.E.1    Kustin, K.2    Cloney, R.A.3
  • 133
    • 0021060318 scopus 로고
    • Preliminary investigations on the possible antimicrobial properties of tunicate blood cell vanadium
    • Rowley A.F. Preliminary investigations on the possible antimicrobial properties of tunicate blood cell vanadium. J. Exp. Zool. 1983, 227:319-322.
    • (1983) J. Exp. Zool. , vol.227 , pp. 319-322
    • Rowley, A.F.1
  • 134
    • 85008503623 scopus 로고    scopus 로고
    • Diverse strategies of protein sclerotization in marine invertebrates: structure-property relationships in natural biomaterials
    • Rubin D.J., Miserez A., Waite J.H. Diverse strategies of protein sclerotization in marine invertebrates: structure-property relationships in natural biomaterials. Adv. Insect Physiol. 2010, 38:75-133.
    • (2010) Adv. Insect Physiol. , vol.38 , pp. 75-133
    • Rubin, D.J.1    Miserez, A.2    Waite, J.H.3
  • 135
    • 0030011379 scopus 로고    scopus 로고
    • Reactions between vanadium ions and biogenic reductants of tunicates: spectroscopic probing for complexation and redox products in vitro
    • Ryan D.E., Grant K.B., Nakanishi K., Frank P., Hodgson K.O. Reactions between vanadium ions and biogenic reductants of tunicates: spectroscopic probing for complexation and redox products in vitro. Biochemistry 1996, 35:8651-8661.
    • (1996) Biochemistry , vol.35 , pp. 8651-8661
    • Ryan, D.E.1    Grant, K.B.2    Nakanishi, K.3    Frank, P.4    Hodgson, K.O.5
  • 136
    • 0029899612 scopus 로고    scopus 로고
    • Reactions between tunichrome Mm-1, a tunicate blood pigment, and vanadium ions in acidic and neutral media
    • Ryan D.E., Grant K.B., Nakanishi K. Reactions between tunichrome Mm-1, a tunicate blood pigment, and vanadium ions in acidic and neutral media. Biochemistry 1996, 35:8640-8650.
    • (1996) Biochemistry , vol.35 , pp. 8640-8650
    • Ryan, D.E.1    Grant, K.B.2    Nakanishi, K.3
  • 137
    • 0026029533 scopus 로고
    • α,β-Dehydro-3,4-dihydroxy phenylalanine derivatives: rate and mechanism of formation
    • Rzepecki L.M., Waite J.H. α,β-Dehydro-3,4-dihydroxy phenylalanine derivatives: rate and mechanism of formation. Arch. Biochem. Biophys. 1991, 285:27-36.
    • (1991) Arch. Biochem. Biophys. , vol.285 , pp. 27-36
    • Rzepecki, L.M.1    Waite, J.H.2
  • 138
    • 0026028299 scopus 로고
    • α,β-Dehydro-3,4-dihydroxy phenylalanine derivatives: potential sclerotization intermediates in natural composite materials
    • Rzepecki L.M., Nagafuchi T., Waite J.H. α,β-Dehydro-3,4-dihydroxy phenylalanine derivatives: potential sclerotization intermediates in natural composite materials. Arch. Biochem. Biophys. 1991, 285:17-26.
    • (1991) Arch. Biochem. Biophys. , vol.285 , pp. 17-26
    • Rzepecki, L.M.1    Nagafuchi, T.2    Waite, J.H.3
  • 140
    • 0024962064 scopus 로고
    • O-Quinone/quinone methide isomerase: a novel enzyme preventing the destruction of self-matter by phenoloxidase generated quinones during immune response in insects
    • Saul S.J., Sugumaran M. o-Quinone/quinone methide isomerase: a novel enzyme preventing the destruction of self-matter by phenoloxidase generated quinones during immune response in insects. FEBS Lett. 1989, 249:155-158.
    • (1989) FEBS Lett. , vol.249 , pp. 155-158
    • Saul, S.J.1    Sugumaran, M.2
  • 141
    • 0024978566 scopus 로고
    • N-acetyldopamine quinone methide/1,2-dehydro-N-acetyldopamine tautomerase. A new enzyme involved in sclerotization of insect cuticle
    • Saul S.J., Sugumaran M. N-acetyldopamine quinone methide/1,2-dehydro-N-acetyldopamine tautomerase. A new enzyme involved in sclerotization of insect cuticle. FEBS Lett. 1989, 255:340-344.
    • (1989) FEBS Lett. , vol.255 , pp. 340-344
    • Saul, S.J.1    Sugumaran, M.2
  • 142
    • 0025036539 scopus 로고
    • 4-Alkyl-o-quinone/2-hydroxy-p-quinone methide isomerase from the larval hemolymph of Sarcophaga bullata. I. Purification and characterization of enzyme-catalyzed reaction
    • Saul S.J., Sugumaran M. 4-Alkyl-o-quinone/2-hydroxy-p-quinone methide isomerase from the larval hemolymph of Sarcophaga bullata. I. Purification and characterization of enzyme-catalyzed reaction. J. Biol. Chem. 1990, 265:16992-16999.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16992-16999
    • Saul, S.J.1    Sugumaran, M.2
  • 143
    • 0000837156 scopus 로고
    • Ultrastructure and X-ray microanalysis of blood cells of Ascidia malaca
    • Scippa S., Botte L., de Vincentiis M. Ultrastructure and X-ray microanalysis of blood cells of Ascidia malaca. Acta Zool. 1982, 63:121-131.
    • (1982) Acta Zool. , vol.63 , pp. 121-131
    • Scippa, S.1    Botte, L.2    de Vincentiis, M.3
  • 144
    • 0021959861 scopus 로고
    • X-ray microanalytical studies on cryofixed blood cells of the ascidian Phallusia mammillata. I. Elemental composition of morula cells
    • Scippa S., Botte L., Zierold K., de Vincentiis M. X-ray microanalytical studies on cryofixed blood cells of the ascidian Phallusia mammillata. I. Elemental composition of morula cells. Cell Tissue Res. 1985, 239:459-461.
    • (1985) Cell Tissue Res. , vol.239 , pp. 459-461
    • Scippa, S.1    Botte, L.2    Zierold, K.3    de Vincentiis, M.4
  • 145
    • 0000098678 scopus 로고
    • Morphology and genetics of rejection reactions between oozoids from the tunicate Botryllus schlosseri
    • Scofield V.L., Nagashima L.S. Morphology and genetics of rejection reactions between oozoids from the tunicate Botryllus schlosseri. Biol. Bull. 1983, 165:733-744.
    • (1983) Biol. Bull. , vol.165 , pp. 733-744
    • Scofield, V.L.1    Nagashima, L.S.2
  • 146
    • 0020076489 scopus 로고
    • Protochordate allorecognition is controlled by a MHC-like gene system
    • Scofield V.L., Schlumpberger J.M., West L.A., Weissman I.L. Protochordate allorecognition is controlled by a MHC-like gene system. Nature 1982, 295:499-502.
    • (1982) Nature , vol.295 , pp. 499-502
    • Scofield, V.L.1    Schlumpberger, J.M.2    West, L.A.3    Weissman, I.L.4
  • 147
    • 0036941777 scopus 로고    scopus 로고
    • Involvement of quinones and phenoloxidase in the allorejection reaction in a colonial ascidian Botrylloides simodensis: histochemical and immunological study
    • Shirae M., Ballarin L., Frizzo A., Saito Y., Hirose E. Involvement of quinones and phenoloxidase in the allorejection reaction in a colonial ascidian Botrylloides simodensis: histochemical and immunological study. Mar. Biol. 2002, 141:659-665.
    • (2002) Mar. Biol. , vol.141 , pp. 659-665
    • Shirae, M.1    Ballarin, L.2    Frizzo, A.3    Saito, Y.4    Hirose, E.5
  • 149
    • 0001330758 scopus 로고
    • Chemical defenses of ascidians against predators
    • Stoecker D. Chemical defenses of ascidians against predators. Ecology 1980, 61:1327-1334.
    • (1980) Ecology , vol.61 , pp. 1327-1334
    • Stoecker, D.1
  • 150
    • 33847085333 scopus 로고
    • Celenamides A and B, linear peptide alkaloids from the sponge Cliona celata
    • Stonard R.J., Andersen R.J. Celenamides A and B, linear peptide alkaloids from the sponge Cliona celata. J. Org. Chem. 1980, 45:3687-3691.
    • (1980) J. Org. Chem. , vol.45 , pp. 3687-3691
    • Stonard, R.J.1    Andersen, R.J.2
  • 151
    • 0001255796 scopus 로고
    • Linear peptide alkaloids from the sponge Cliona celata (Grant). Celenamides C and D
    • Stonard R.J., Andersen R.J. Linear peptide alkaloids from the sponge Cliona celata (Grant). Celenamides C and D. Can. J. Chem. 1980, 58:2121-2126.
    • (1980) Can. J. Chem. , vol.58 , pp. 2121-2126
    • Stonard, R.J.1    Andersen, R.J.2
  • 152
    • 0022500671 scopus 로고
    • Tyrosinase catalyzes an unusual oxidative decarboxylation of 3,4-dihydroxymandelate
    • Sugumaran M. Tyrosinase catalyzes an unusual oxidative decarboxylation of 3,4-dihydroxymandelate. Biochemistry 1986, 25:4489-4492.
    • (1986) Biochemistry , vol.25 , pp. 4489-4492
    • Sugumaran, M.1
  • 153
    • 77956736927 scopus 로고    scopus 로고
    • Unified mechanism for sclerotization of insect cuticle
    • Sugumaran M. Unified mechanism for sclerotization of insect cuticle. Adv. Insect Physiol. 1998, 27:229-334.
    • (1998) Adv. Insect Physiol. , vol.27 , pp. 229-334
    • Sugumaran, M.1
  • 154
    • 84862998531 scopus 로고    scopus 로고
    • Different modes of activation of prophenoloxidase
    • SOS Publications, Fair Haven NJ, A. Wiesner, B. Dunphy, V.J. Marmaras, I. Morishima, M. Sugumaran, M. Yamakawa (Eds.)
    • Sugumaran M. Different modes of activation of prophenoloxidase. Techniques in Insect Immunology 1998, 193-204. SOS Publications, Fair Haven NJ. A. Wiesner, B. Dunphy, V.J. Marmaras, I. Morishima, M. Sugumaran, M. Yamakawa (Eds.).
    • (1998) Techniques in Insect Immunology , pp. 193-204
    • Sugumaran, M.1
  • 155
    • 0034660346 scopus 로고    scopus 로고
    • Oxidation chemistry of 1,2-dehydro-N-acetyldopamines: direct evidence for the formation of 1,2-dehydro-N-acetyldopamine quinone
    • Sugumaran M. Oxidation chemistry of 1,2-dehydro-N-acetyldopamines: direct evidence for the formation of 1,2-dehydro-N-acetyldopamine quinone. Arch. Biochem. Biophys. 2000, 378:404-410.
    • (2000) Arch. Biochem. Biophys. , vol.378 , pp. 404-410
    • Sugumaran, M.1
  • 156
    • 0035058105 scopus 로고    scopus 로고
    • Control mechanisms of prophenoloxidase cascade in insects
    • Sugumaran M. Control mechanisms of prophenoloxidase cascade in insects. Adv. Exp. Med. and Biol. 2001, 484:289-298.
    • (2001) Adv. Exp. Med. and Biol. , vol.484 , pp. 289-298
    • Sugumaran, M.1
  • 157
    • 0035999729 scopus 로고    scopus 로고
    • Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects
    • Sugumaran M. Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects. Pigment Cell Res. 2002, 15:2-9.
    • (2002) Pigment Cell Res. , vol.15 , pp. 2-9
    • Sugumaran, M.1
  • 158
    • 69449105246 scopus 로고    scopus 로고
    • Complexities of cuticular pigmentation in insects
    • Sugumaran M. Complexities of cuticular pigmentation in insects. Pigment Cell Melanoma Res. 2009, 22:523-525.
    • (2009) Pigment Cell Melanoma Res. , vol.22 , pp. 523-525
    • Sugumaran, M.1
  • 159
    • 77957963448 scopus 로고    scopus 로고
    • Chemistry of cuticular sclerotization
    • Sugumaran M. Chemistry of cuticular sclerotization. Adv. Insect Physiol. 2010, 39:151-209.
    • (2010) Adv. Insect Physiol. , vol.39 , pp. 151-209
    • Sugumaran, M.1
  • 160
    • 0025528469 scopus 로고
    • On the latency and nature of phenoloxidase present in the left colleterial gland of the cockroach. Periplaneta americana
    • Sugumaran M., Nellaiappan K. On the latency and nature of phenoloxidase present in the left colleterial gland of the cockroach. Periplaneta americana. Arch. Insect Biochem. Physiol. 1990, 15:165-181.
    • (1990) Arch. Insect Biochem. Physiol. , vol.15 , pp. 165-181
    • Sugumaran, M.1    Nellaiappan, K.2
  • 161
    • 0025923448 scopus 로고
    • Lysolecithin - a potent activator of prophenoloxidase from the hemolymph of the lobster, Homarus americanas
    • Sugumaran M., Nellaiappan K. Lysolecithin - a potent activator of prophenoloxidase from the hemolymph of the lobster, Homarus americanas. Biochem. Biophys. Res. Commun. 1991, 176:1371-1376.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 1371-1376
    • Sugumaran, M.1    Nellaiappan, K.2
  • 162
    • 0029206656 scopus 로고
    • Model sclerotization studies. 3. Cuticular enzyme catalyzed oxidation of peptidyl model tyrosine and dopa derivatives
    • Sugumaran M., Ricketts D. Model sclerotization studies. 3. Cuticular enzyme catalyzed oxidation of peptidyl model tyrosine and dopa derivatives. Arch. Insect Biochem. Physiol. 1995, 28:17-32.
    • (1995) Arch. Insect Biochem. Physiol. , vol.28 , pp. 17-32
    • Sugumaran, M.1    Ricketts, D.2
  • 163
    • 78650673521 scopus 로고    scopus 로고
    • Bioactive dehydrotyrosyl and dehydrodopyl compounds of marine origin
    • Sugumaran M., Robinson W.E. Bioactive dehydrotyrosyl and dehydrodopyl compounds of marine origin. Mar. Drugs 2010, 8:2906-2935.
    • (2010) Mar. Drugs , vol.8 , pp. 2906-2935
    • Sugumaran, M.1    Robinson, W.E.2
  • 164
    • 0025764070 scopus 로고
    • Quinone methide as a new intermediate in eumelanin biosynthesis
    • Sugumaran M., Semensi V. Quinone methide as a new intermediate in eumelanin biosynthesis. J. Biol. Chem. 1991, 266:6073-6078.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6073-6078
    • Sugumaran, M.1    Semensi, V.2
  • 165
    • 0023645278 scopus 로고
    • Tyrosinase-catalyzed unusual oxidative dimerization of 1,2-dehydro-N-acetyldopamine
    • Sugumaran M., Dali H., Semensi V., Hennigan B. Tyrosinase-catalyzed unusual oxidative dimerization of 1,2-dehydro-N-acetyldopamine. J. Biol. Chem. 1987, 262:10546-10549.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10546-10549
    • Sugumaran, M.1    Dali, H.2    Semensi, V.3    Hennigan, B.4
  • 166
    • 84990485091 scopus 로고
    • On the nature of nonenzymatic and enzymatic oxidation of the putative sclerotizing precursor, 1,2-dehydro-N-acetyldopamine
    • Sugumaran M., Hennigan B., Semensi V., Dali H. On the nature of nonenzymatic and enzymatic oxidation of the putative sclerotizing precursor, 1,2-dehydro-N-acetyldopamine. Arch. Insect Biochem. Physiol. 1988, 8:89-100.
    • (1988) Arch. Insect Biochem. Physiol. , vol.8 , pp. 89-100
    • Sugumaran, M.1    Hennigan, B.2    Semensi, V.3    Dali, H.4
  • 167
    • 0024806426 scopus 로고
    • Unusual intramolecular cyclization and side chain desaturation of carboxyethyl-o-benzoquinone derivatives
    • Sugumaran M., Dali H., Kundzicz H., Semensi V. Unusual intramolecular cyclization and side chain desaturation of carboxyethyl-o-benzoquinone derivatives. Bioorg. Chem. 1989, 17:443-453.
    • (1989) Bioorg. Chem. , vol.17 , pp. 443-453
    • Sugumaran, M.1    Dali, H.2    Kundzicz, H.3    Semensi, V.4
  • 168
    • 0024978514 scopus 로고
    • Nonenzymatic transformations of enzymatically generated N-acetyl dopamine quinone and isomeric dihydrocaffeiyl methylamide quinone
    • Sugumaran M., Semensi V., Dali H., Saul S.J. Nonenzymatic transformations of enzymatically generated N-acetyl dopamine quinone and isomeric dihydrocaffeiyl methylamide quinone. FEBS Lett. 1989, 255:345-349.
    • (1989) FEBS Lett. , vol.255 , pp. 345-349
    • Sugumaran, M.1    Semensi, V.2    Dali, H.3    Saul, S.J.4
  • 170
    • 0026727777 scopus 로고
    • Evidence for the formation of a quinone methide during the oxidation of the insect cuticular sclerotizing precursor, 1,2-dehydro-N-acetyldopamine
    • Sugumaran M., Semensi V., Kalyanaraman B., Bruce J.M., Land E.J. Evidence for the formation of a quinone methide during the oxidation of the insect cuticular sclerotizing precursor, 1,2-dehydro-N-acetyldopamine. J. Biol. Chem. 1992, 267:10355-10361.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10355-10361
    • Sugumaran, M.1    Semensi, V.2    Kalyanaraman, B.3    Bruce, J.M.4    Land, E.J.5
  • 171
    • 0026567052 scopus 로고
    • Mechanistic studies on tyrosinase catalysed oxidative decarboxylation of 3,4-dihydroxymandelic acid
    • Sugumaran M., Dali H., Semensi V. Mechanistic studies on tyrosinase catalysed oxidative decarboxylation of 3,4-dihydroxymandelic acid. Biochem. J. 1992, 281:353-357.
    • (1992) Biochem. J. , vol.281 , pp. 353-357
    • Sugumaran, M.1    Dali, H.2    Semensi, V.3
  • 172
    • 40549085299 scopus 로고    scopus 로고
    • Deciphering deuterostome phylogeny: molecular, morphological and palaeontological perspectives
    • Swalla B.J., Smith A.B. Deciphering deuterostome phylogeny: molecular, morphological and palaeontological perspectives. Philos. Trans. R. Soc. 2008, 363:1557-1568.
    • (2008) Philos. Trans. R. Soc. , vol.363 , pp. 1557-1568
    • Swalla, B.J.1    Smith, A.B.2
  • 175
    • 24044497630 scopus 로고    scopus 로고
    • A genome wide survey of genes for enzymes involved in pigment synthesis in an ascidian Ciona intestinalis
    • Takeuchi K., Satou Y., Yamamoto H., Satoh N. A genome wide survey of genes for enzymes involved in pigment synthesis in an ascidian Ciona intestinalis. Zool. Sci. 2005, 22:723-734.
    • (2005) Zool. Sci. , vol.22 , pp. 723-734
    • Takeuchi, K.1    Satou, Y.2    Yamamoto, H.3    Satoh, N.4
  • 176
    • 0001198219 scopus 로고
    • Self or non-self discrimination in ascidians
    • Taneda Y., Saito Y., Watanabe H. Self or non-self discrimination in ascidians. Zool. Sci. 1985, 2:433-442.
    • (1985) Zool. Sci. , vol.2 , pp. 433-442
    • Taneda, Y.1    Saito, Y.2    Watanabe, H.3
  • 177
    • 0025931350 scopus 로고
    • Oxidation of peptidyl 3,4-dihydroxyphenylalanine analogues: implications for the biosynthesis of tunichromes and related oligopeptides
    • Taylor S.W., Molinski T.F., Rzepecki L.M., Waite J.H. Oxidation of peptidyl 3,4-dihydroxyphenylalanine analogues: implications for the biosynthesis of tunichromes and related oligopeptides. J. Nat. Prod. 1991, 54:918-922.
    • (1991) J. Nat. Prod. , vol.54 , pp. 918-922
    • Taylor, S.W.1    Molinski, T.F.2    Rzepecki, L.M.3    Waite, J.H.4
  • 178
    • 0028005466 scopus 로고
    • Vanadium in ascidians: changes in vanadium coordination and oxidation state upon cell lysis
    • Taylor S.W., Hawkins C.J., Parry D.L., Swinehart J.H., Hanson G.R. Vanadium in ascidians: changes in vanadium coordination and oxidation state upon cell lysis. J. Inorg. Biochem. 1994, 56:97-116.
    • (1994) J. Inorg. Biochem. , vol.56 , pp. 97-116
    • Taylor, S.W.1    Hawkins, C.J.2    Parry, D.L.3    Swinehart, J.H.4    Hanson, G.R.5
  • 179
    • 0029560564 scopus 로고
    • Novel 3,4-di- and 3,4,5-trihydroxy phenylalanine-containing polypeptides from the blood cells of the ascidians Ascidia ceratodes and Molgula manhattensis
    • Taylor S.W., Ross M.M., Waite J.H. Novel 3,4-di- and 3,4,5-trihydroxy phenylalanine-containing polypeptides from the blood cells of the ascidians Ascidia ceratodes and Molgula manhattensis. Arch. Biochem. Biophys. 1995, 324:228-240.
    • (1995) Arch. Biochem. Biophys. , vol.324 , pp. 228-240
    • Taylor, S.W.1    Ross, M.M.2    Waite, J.H.3
  • 180
    • 0001246667 scopus 로고    scopus 로고
    • New perspectives in the chemistry and biochemistry of the tunichromes and related compounds
    • Taylor S.W., Kammerer B., Bayer E. New perspectives in the chemistry and biochemistry of the tunichromes and related compounds. Chem. Rev. 1997, 97:333-346.
    • (1997) Chem. Rev. , vol.97 , pp. 333-346
    • Taylor, S.W.1    Kammerer, B.2    Bayer, E.3
  • 182
    • 0034623953 scopus 로고    scopus 로고
    • Styelin D, an extensively modified antimicrobial peptide from ascidian hemocytes
    • Taylor S.W., Craig A.F., Fischer W.H., Park M., Lehrer R.I. Styelin D, an extensively modified antimicrobial peptide from ascidian hemocytes. J. Biol. Chem. 2000, 275:38417-38426.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38417-38426
    • Taylor, S.W.1    Craig, A.F.2    Fischer, W.H.3    Park, M.4    Lehrer, R.I.5
  • 184
    • 0036201034 scopus 로고    scopus 로고
    • Tunichrome Sp-1: new pentapeptide tunichrome from the hemocytes of Styela plicata
    • Tincu J.A., Taylor S.W. Tunichrome Sp-1: new pentapeptide tunichrome from the hemocytes of Styela plicata. J. Nat. Prod. 2002, 65:377-378.
    • (2002) J. Nat. Prod. , vol.65 , pp. 377-378
    • Tincu, J.A.1    Taylor, S.W.2
  • 185
    • 0034643280 scopus 로고    scopus 로고
    • Plicatamide: a lead to the biosynthetic origins of the tunichromes?
    • Tincu J.A., Craig A.G., Taylor S.W. Plicatamide: a lead to the biosynthetic origins of the tunichromes?. Biochem. Biophys. Res. Commun. 2000, 270:421-424.
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 421-424
    • Tincu, J.A.1    Craig, A.G.2    Taylor, S.W.3
  • 188
    • 0035851403 scopus 로고    scopus 로고
    • Effects of tributyltin and other metals on the phenoloxidase activating system of the tunicate, Styela plicata
    • Tujula N., Radford J., Nair S.V., Raftos D.A. Effects of tributyltin and other metals on the phenoloxidase activating system of the tunicate, Styela plicata. Aquat. Toxicol. 2001, 55:191-201.
    • (2001) Aquat. Toxicol. , vol.55 , pp. 191-201
    • Tujula, N.1    Radford, J.2    Nair, S.V.3    Raftos, D.A.4
  • 189
    • 0001290908 scopus 로고
    • Structural study of the vanadium complex in living ascidian blood cells by X-ray absorbance spectrometry
    • Tullius T.D., Gillum W.O., Carlson R.M.K., Hodgson K.O. Structural study of the vanadium complex in living ascidian blood cells by X-ray absorbance spectrometry. J. Am. Chem. Soc. 1980, 102:5670-5676.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 5670-5676
    • Tullius, T.D.1    Gillum, W.O.2    Carlson, R.M.K.3    Hodgson, K.O.4
  • 190
    • 84862981312 scopus 로고
    • Structure des fibres celluloso-proteiques de la tunique de Halocynthia papillosa Gün. (Ascidiacea Stolodobranchiata)
    • Van Dalle Y., Goffinet G., Godeaux J. Structure des fibres celluloso-proteiques de la tunique de Halocynthia papillosa Gün. (Ascidiacea Stolodobranchiata). Bull. Soc. Roy. Liège. 1988, 57:59-68.
    • (1988) Bull. Soc. Roy. Liège. , vol.57 , pp. 59-68
    • Van Dalle, Y.1    Goffinet, G.2    Godeaux, J.3
  • 191
    • 0025160176 scopus 로고
    • The phylogeny and chemical diversity of quinone tanned glues and varnishes
    • Waite J.H. The phylogeny and chemical diversity of quinone tanned glues and varnishes. Comp. Biochem. Physiol. 1990, 97:19-29.
    • (1990) Comp. Biochem. Physiol. , vol.97 , pp. 19-29
    • Waite, J.H.1
  • 192
    • 0019798541 scopus 로고
    • Quantitative measurement by microdensitometry of tyrosinase (dopa oxidase) development in whole small ascidian embryos
    • Whittaker J.R. Quantitative measurement by microdensitometry of tyrosinase (dopa oxidase) development in whole small ascidian embryos. Histochemistry 1981, 71:349-359.
    • (1981) Histochemistry , vol.71 , pp. 349-359
    • Whittaker, J.R.1
  • 193
    • 0019578706 scopus 로고
    • Cytochrome c reduction by semiquinone radicals can be indirectly inhibited by superoxide dismutase
    • Winterbourn C.C. Cytochrome c reduction by semiquinone radicals can be indirectly inhibited by superoxide dismutase. Arch. Biochem. Biophys. 1981, 209:159-167.
    • (1981) Arch. Biochem. Biophys. , vol.209 , pp. 159-167
    • Winterbourn, C.C.1
  • 194
    • 0000334355 scopus 로고
    • Urochordates
    • Academic Press, London
    • Wright R.K. Urochordates. Invertebrate Blood Cells 1981, vol. 2:565-626. Academic Press, London.
    • (1981) Invertebrate Blood Cells , vol.2 , pp. 565-626
    • Wright, R.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.