메뉴 건너뛰기




Volumn 35, Issue 7, 2011, Pages 799-807

A monoamine oxidase from scallop Chlamys farreri serving as an immunomodulator in response against bacterial challenge

Author keywords

Immunomodulation; Innate immunity; Monoamine; Monoamine oxidase (MAO); Scallop

Indexed keywords

ADRENALIN; AMINE OXIDASE (FLAVIN CONTAINING); CLORGYLINE; COMPLEMENTARY DNA; DOPAMINE; MESSENGER RNA; NORADRENALIN; RECOMBINANT AMINE OXIDASE (FLAVIN CONTAINING); SEROTONIN; UNCLASSIFIED DRUG;

EID: 79954697741     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2011.03.014     Document Type: Article
Times cited : (14)

References (51)
  • 1
    • 72649098099 scopus 로고    scopus 로고
    • Why should an immune response activate the stress response? Insights from the insects (the cricket Gryllus texensis)
    • Adamo S.A. Why should an immune response activate the stress response? Insights from the insects (the cricket Gryllus texensis). Brain Behav. Immun. 2010, 24(2):194-200.
    • (2010) Brain Behav. Immun. , vol.24 , Issue.2 , pp. 194-200
    • Adamo, S.A.1
  • 2
    • 38849125507 scopus 로고    scopus 로고
    • Effects of noradrenaline on immunological activity in Sydney rock oysters
    • Aladaileh S., Nair S.V., Raftos D.A. Effects of noradrenaline on immunological activity in Sydney rock oysters. Dev. Comp. Immunol. 2008, 32(6):627-636.
    • (2008) Dev. Comp. Immunol. , vol.32 , Issue.6 , pp. 627-636
    • Aladaileh, S.1    Nair, S.V.2    Raftos, D.A.3
  • 3
    • 67649610423 scopus 로고    scopus 로고
    • Membrane attachment facilitates ligand access to the active site in monoamine oxidase A
    • Apostolov R., Yonezawa Y., Standley D.M., Kikugawa G., Takano Y., Nakamura H. Membrane attachment facilitates ligand access to the active site in monoamine oxidase A. Biochemistry 2009, 48(25):5864-5873.
    • (2009) Biochemistry , vol.48 , Issue.25 , pp. 5864-5873
    • Apostolov, R.1    Yonezawa, Y.2    Standley, D.M.3    Kikugawa, G.4    Takano, Y.5    Nakamura, H.6
  • 4
    • 0024042954 scopus 로고
    • Cdna cloning of human-liver monoamine oxidase-a and oxidase-B-molecular-basis of differences in enzymatic-properties
    • Bach A.W.J., Lan N.C., Johnson D.L., Abell C.W., Bembenek M.E., Kwan S.W., et al. Cdna cloning of human-liver monoamine oxidase-a and oxidase-B-molecular-basis of differences in enzymatic-properties. Proc. Natl. Acad. Sci. U.S.A. 1988, 85(13):4934-4938.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , Issue.13 , pp. 4934-4938
    • Bach, A.W.J.1    Lan, N.C.2    Johnson, D.L.3    Abell, C.W.4    Bembenek, M.E.5    Kwan, S.W.6
  • 5
    • 33644874936 scopus 로고    scopus 로고
    • Oxidative stress by monoamine oxidase mediates receptor-independent cardiomyocyte apoptosis by serotonin and postischemic myocardial injury
    • Bianchi P., Kunduzova O., Masini E., Cambon C., Bani D., Raimondi L., et al. Oxidative stress by monoamine oxidase mediates receptor-independent cardiomyocyte apoptosis by serotonin and postischemic myocardial injury. Circulation 2005, 112(21):3297-3305.
    • (2005) Circulation , vol.112 , Issue.21 , pp. 3297-3305
    • Bianchi, P.1    Kunduzova, O.2    Masini, E.3    Cambon, C.4    Bani, D.5    Raimondi, L.6
  • 6
    • 3042774163 scopus 로고    scopus 로고
    • Molecular identification and expression of two non-P450 enzymes, monoamine oxidase A and flavin-containing monooxygenase 2, involved in phase I of xenobiotic biotransformation in the Pacific oyster, Crassostrea gigas
    • Boutet I., Tanguy A., Moraga D. Molecular identification and expression of two non-P450 enzymes, monoamine oxidase A and flavin-containing monooxygenase 2, involved in phase I of xenobiotic biotransformation in the Pacific oyster, Crassostrea gigas. BBA: Gene Struct. Expr. 2004, 1679(1):29-36.
    • (2004) BBA: Gene Struct. Expr. , vol.1679 , Issue.1 , pp. 29-36
    • Boutet, I.1    Tanguy, A.2    Moraga, D.3
  • 7
    • 10744231398 scopus 로고    scopus 로고
    • In vitro effects of LPS, IL-2, PDGF and CRF on haemocytes of Mytilus galloprovincialis Lmk
    • Cao A., Ramos-Martinez J.I., Barcia R. In vitro effects of LPS, IL-2, PDGF and CRF on haemocytes of Mytilus galloprovincialis Lmk. Fish Shellfish Immunol. 2004, 16(2):215-225.
    • (2004) Fish Shellfish Immunol. , vol.16 , Issue.2 , pp. 215-225
    • Cao, A.1    Ramos-Martinez, J.I.2    Barcia, R.3
  • 8
    • 34548129569 scopus 로고    scopus 로고
    • In hemocytes from Mytilus galloprovincialis Lmk., treatment with corticotropin or growth factors conditions catecholamine release
    • Cao A., Ramos-Martinez J.I., Barcia R. In hemocytes from Mytilus galloprovincialis Lmk., treatment with corticotropin or growth factors conditions catecholamine release. Int. Immunopharmacol. 2007, 7(11):1395-1402.
    • (2007) Int. Immunopharmacol. , vol.7 , Issue.11 , pp. 1395-1402
    • Cao, A.1    Ramos-Martinez, J.I.2    Barcia, R.3
  • 9
    • 24044462917 scopus 로고    scopus 로고
    • Expression regulation of MAO isoforms in monocytic cells in response to Th2 cytokines
    • Chaitidis P., Billett E., Kuban R.J., Ungethuem U., Kuhn H. Expression regulation of MAO isoforms in monocytic cells in response to Th2 cytokines. Med. Sci. Monit. 2005, 11(8):BR259-265.
    • (2005) Med. Sci. Monit. , vol.11 , Issue.8
    • Chaitidis, P.1    Billett, E.2    Kuban, R.J.3    Ungethuem, U.4    Kuhn, H.5
  • 10
    • 62949249358 scopus 로고    scopus 로고
    • Functional and molecular immune response of Mediterranean mussel (Mytilus galloprovincialis) haemocytes against pathogen-associated molecular patterns and bacteria
    • Costa M.M., Prado-Alvarez M., Gestal C., Li H., Roch P., Novoa B., et al. Functional and molecular immune response of Mediterranean mussel (Mytilus galloprovincialis) haemocytes against pathogen-associated molecular patterns and bacteria. Fish Shellfish Immunol. 2009, 26(3):515-523.
    • (2009) Fish Shellfish Immunol. , vol.26 , Issue.3 , pp. 515-523
    • Costa, M.M.1    Prado-Alvarez, M.2    Gestal, C.3    Li, H.4    Roch, P.5    Novoa, B.6
  • 11
    • 62249115660 scopus 로고    scopus 로고
    • Mitochondrial pathways for ROS formation and myocardial injury: the relevance of p66(Shc) and monoamine oxidase
    • Di Lisa F., Kaludercic N., Carpi A., Menabo R., Giorgio M. Mitochondrial pathways for ROS formation and myocardial injury: the relevance of p66(Shc) and monoamine oxidase. Basic Res. Cardiol. 2009, 104(2):131-139.
    • (2009) Basic Res. Cardiol. , vol.104 , Issue.2 , pp. 131-139
    • Di Lisa, F.1    Kaludercic, N.2    Carpi, A.3    Menabo, R.4    Giorgio, M.5
  • 12
    • 47249152398 scopus 로고    scopus 로고
    • The pH dependence of kinetic isotope effects in monoamine oxidase A indicates stabilization of the neutral amine in the enzyme-substrate complex
    • Dunn R.V., Marshall K.R., Munro A.W., Scrutton N.S. The pH dependence of kinetic isotope effects in monoamine oxidase A indicates stabilization of the neutral amine in the enzyme-substrate complex. FASEB J. 2008, 275(15):3850-3858.
    • (2008) FASEB J. , vol.275 , Issue.15 , pp. 3850-3858
    • Dunn, R.V.1    Marshall, K.R.2    Munro, A.W.3    Scrutton, N.S.4
  • 13
    • 66149173641 scopus 로고    scopus 로고
    • Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases
    • Edmondson D.E., Binda C., Wang J., Upadhyay A.K., Mattevi A. Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases. Biochemistry 2009, 48(20):4220-4230.
    • (2009) Biochemistry , vol.48 , Issue.20 , pp. 4220-4230
    • Edmondson, D.E.1    Binda, C.2    Wang, J.3    Upadhyay, A.K.4    Mattevi, A.5
  • 14
    • 34250862301 scopus 로고    scopus 로고
    • New insights into the structures and functions of human monoamine oxidases A and B
    • Edmondson D.E., DeColibus L., Binda C., Li M., Mattevi A. New insights into the structures and functions of human monoamine oxidases A and B. J. Neural Transm. 2007, 114(6):703-705.
    • (2007) J. Neural Transm. , vol.114 , Issue.6 , pp. 703-705
    • Edmondson, D.E.1    DeColibus, L.2    Binda, C.3    Li, M.4    Mattevi, A.5
  • 15
    • 34250862298 scopus 로고    scopus 로고
    • A link between monoamine oxidase-A and apoptosis in serum deprived human SH-SY5Y neuroblastoma cells
    • Fitzgerald J.C., Ufer C., Billett E.E. A link between monoamine oxidase-A and apoptosis in serum deprived human SH-SY5Y neuroblastoma cells. J. Neural Transm. 2007, 114(6):807-810.
    • (2007) J. Neural Transm. , vol.114 , Issue.6 , pp. 807-810
    • Fitzgerald, J.C.1    Ufer, C.2    Billett, E.E.3
  • 16
    • 36448968629 scopus 로고    scopus 로고
    • Monoamine oxidase-A modulates apoptotic cell death induced by staurosporine in human neuroblastoma cells
    • Fitzgerald J.C., Ufer C., De Girolamo L.A., Kuhn H., Billett E.E. Monoamine oxidase-A modulates apoptotic cell death induced by staurosporine in human neuroblastoma cells. J. Neurochem. 2007, 103(6):2189-2199.
    • (2007) J. Neurochem. , vol.103 , Issue.6 , pp. 2189-2199
    • Fitzgerald, J.C.1    Ufer, C.2    De Girolamo, L.A.3    Kuhn, H.4    Billett, E.E.5
  • 17
    • 17144455070 scopus 로고    scopus 로고
    • Differential substrate specificity of monoamine oxidase in the rat heart and renal cortex
    • Guimaraes J.T., Vindis C., Soares-Da-Silva P., Parini A. Differential substrate specificity of monoamine oxidase in the rat heart and renal cortex. Life Sci. 2003, 73(8):955-967.
    • (2003) Life Sci. , vol.73 , Issue.8 , pp. 955-967
    • Guimaraes, J.T.1    Vindis, C.2    Soares-Da-Silva, P.3    Parini, A.4
  • 18
    • 0030589009 scopus 로고    scopus 로고
    • The metabolism of tyramine by monoamine oxidase A/B causes oxidative damage to mitochondrial DNA
    • Hauptmann N., Grimsby J., Shih J.C., Cadenas E. The metabolism of tyramine by monoamine oxidase A/B causes oxidative damage to mitochondrial DNA. Arch Biochem. Biophys. 1996, 335(2):295-304.
    • (1996) Arch Biochem. Biophys. , vol.335 , Issue.2 , pp. 295-304
    • Hauptmann, N.1    Grimsby, J.2    Shih, J.C.3    Cadenas, E.4
  • 19
    • 0025321965 scopus 로고
    • Interaction of immunoactive monokines (interleukin 1 and tumor necrosis factor) in the bivalve mollusc Mytilus edulis
    • Hughes T.K., Smith E.M., Chin R., Cadet P., Sinisterra J., Leung M.K., et al. Interaction of immunoactive monokines (interleukin 1 and tumor necrosis factor) in the bivalve mollusc Mytilus edulis. Proc. Natl. Acad. Sci. U.S.A. 1990, 87(12):4426-4429.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , Issue.12 , pp. 4426-4429
    • Hughes, T.K.1    Smith, E.M.2    Chin, R.3    Cadet, P.4    Sinisterra, J.5    Leung, M.K.6
  • 20
    • 0346785248 scopus 로고    scopus 로고
    • Monoamine oxidase inhibition and CNS immunodeficiency infection
    • Koutsilieri E., Scheller C., ter Meulen V., Riederer P. Monoamine oxidase inhibition and CNS immunodeficiency infection. Neurotoxicology. 2004, 25(1-2):267-270.
    • (2004) Neurotoxicology. , vol.25 , Issue.1-2 , pp. 267-270
    • Koutsilieri, E.1    Scheller, C.2    ter Meulen, V.3    Riederer, P.4
  • 21
    • 0033781675 scopus 로고    scopus 로고
    • Circulating soluble vascular adhesion protein 1 accounts fear the increased serum monoamine oxidase activity in chronic liver disease
    • Kurkijarvi R., Yegutkin G.G., Gunson B.K., Jalkanen S., Salmi M., Adams D.H. Circulating soluble vascular adhesion protein 1 accounts fear the increased serum monoamine oxidase activity in chronic liver disease. Gastroenterology 2000, 119(4):1096-1103.
    • (2000) Gastroenterology , vol.119 , Issue.4 , pp. 1096-1103
    • Kurkijarvi, R.1    Yegutkin, G.G.2    Gunson, B.K.3    Jalkanen, S.4    Salmi, M.5    Adams, D.H.6
  • 22
    • 0035120079 scopus 로고    scopus 로고
    • Noradrenaline modulates hemocyte reactive oxygen species production via beta-adrenergic receptors in the oyster Crassostrea gigas
    • Lacoste A., Malham S.K., Cueff A., Poulet S.A. Noradrenaline modulates hemocyte reactive oxygen species production via beta-adrenergic receptors in the oyster Crassostrea gigas. Dev. Comp. Immunol. 2001, 25(4):285-289.
    • (2001) Dev. Comp. Immunol. , vol.25 , Issue.4 , pp. 285-289
    • Lacoste, A.1    Malham, S.K.2    Cueff, A.3    Poulet, S.A.4
  • 23
    • 0034997484 scopus 로고    scopus 로고
    • Noradrenaline modulates oyster hemocyte phagocytosis via a beta-adrenergic receptor-cAMP signaling pathway
    • Lacoste A., Malham S.K., Cueff A., Poulet S.A. Noradrenaline modulates oyster hemocyte phagocytosis via a beta-adrenergic receptor-cAMP signaling pathway. Gen. Comp. Endocrinol. 2001, 122(3):252-259.
    • (2001) Gen. Comp. Endocrinol. , vol.122 , Issue.3 , pp. 252-259
    • Lacoste, A.1    Malham, S.K.2    Cueff, A.3    Poulet, S.A.4
  • 24
    • 77957862827 scopus 로고    scopus 로고
    • A macrophage migration inhibitory factor like gene from scallop Chlamys farreri: involvement in immune response and wound healing
    • Li F., Huang S., Wang L., Yang J., Zhang H., Qiu L., et al. A macrophage migration inhibitory factor like gene from scallop Chlamys farreri: involvement in immune response and wound healing. Dev. Comp. Immunol. 2011, 35(1):62-71.
    • (2011) Dev. Comp. Immunol. , vol.35 , Issue.1 , pp. 62-71
    • Li, F.1    Huang, S.2    Wang, L.3    Yang, J.4    Zhang, H.5    Qiu, L.6
  • 25
    • 0034617302 scopus 로고    scopus 로고
    • Influence of FAD structure on its binding and activity with the C406A mutant of recombinant human liver monoamine oxidase A
    • Nandigama R.K., Edmondson D.E. Influence of FAD structure on its binding and activity with the C406A mutant of recombinant human liver monoamine oxidase A. J. Biol. Chem. 2000, 275(27):20527-20532.
    • (2000) J. Biol. Chem. , vol.275 , Issue.27 , pp. 20527-20532
    • Nandigama, R.K.1    Edmondson, D.E.2
  • 26
    • 56649089696 scopus 로고    scopus 로고
    • Functionally undefined gene, yggE, alleviates oxidative stress generated by monoamine oxidase in recombinant Escherichia coli
    • Ojima Y., Kawase D., Nishioka M., Taya M. Functionally undefined gene, yggE, alleviates oxidative stress generated by monoamine oxidase in recombinant Escherichia coli. Biotechnol. Lett. 2009, 31(1):139-145.
    • (2009) Biotechnol. Lett. , vol.31 , Issue.1 , pp. 139-145
    • Ojima, Y.1    Kawase, D.2    Nishioka, M.3    Taya, M.4
  • 27
    • 0031058465 scopus 로고    scopus 로고
    • Effect of PDGF and TGF-beta on the release of biogenic amines from invertebrate immunocytes and their possible role in the stress response
    • Ottaviani E., Caselgrandi E., Kletsas D. Effect of PDGF and TGF-beta on the release of biogenic amines from invertebrate immunocytes and their possible role in the stress response. FEBS Lett. 1997, 403(3):236-238.
    • (1997) FEBS Lett. , vol.403 , Issue.3 , pp. 236-238
    • Ottaviani, E.1    Caselgrandi, E.2    Kletsas, D.3
  • 28
    • 33746639596 scopus 로고    scopus 로고
    • Monoamine oxidase A and repressor R1 are involved in apoptotic signaling pathway
    • Ou X.M., Chen K., Shih J.C. Monoamine oxidase A and repressor R1 are involved in apoptotic signaling pathway. Proc. Natl. Acad. Sci. U.S.A. 2006, 103(29):10923-10928.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , Issue.29 , pp. 10923-10928
    • Ou, X.M.1    Chen, K.2    Shih, J.C.3
  • 29
    • 0032126626 scopus 로고    scopus 로고
    • Pharmacological analysis of monoamine synthesis and catabolism in the scallop, Placopecten magellanicus
    • Pani A.K., Croll R.P. Pharmacological analysis of monoamine synthesis and catabolism in the scallop, Placopecten magellanicus. Gen. Pharmacol. 1998, 31(1):67-73.
    • (1998) Gen. Pharmacol. , vol.31 , Issue.1 , pp. 67-73
    • Pani, A.K.1    Croll, R.P.2
  • 30
    • 58149123344 scopus 로고    scopus 로고
    • The effect of different grading equipment on stress levels assessed by catecholamine measurements in Pacific oysters, Crassostrea gigas (Thunberg)
    • Qu Y., Li X., Yu Y., Vandepeer M., Babidge P., Clarke S., et al. The effect of different grading equipment on stress levels assessed by catecholamine measurements in Pacific oysters, Crassostrea gigas (Thunberg). Aquacult. Eng. 2009, 40(1):11-16.
    • (2009) Aquacult. Eng. , vol.40 , Issue.1 , pp. 11-16
    • Qu, Y.1    Li, X.2    Yu, Y.3    Vandepeer, M.4    Babidge, P.5    Clarke, S.6
  • 31
    • 0035025788 scopus 로고    scopus 로고
    • Cellular localization of monoamine oxidase A and B in human tissues outside of the central nervous system
    • Rodriguez M.J., Saura J., Billett E.E., Finch C.C., Mahy N. Cellular localization of monoamine oxidase A and B in human tissues outside of the central nervous system. Cell Tissue Res. 2001, 304(2):215-220.
    • (2001) Cell Tissue Res. , vol.304 , Issue.2 , pp. 215-220
    • Rodriguez, M.J.1    Saura, J.2    Billett, E.E.3    Finch, C.C.4    Mahy, N.5
  • 33
    • 0028999344 scopus 로고
    • Cloning, sequencing and heterologous expression of the monoamine oxidase gene from Aspergillus niger
    • Schilling B., Lerch K. Cloning, sequencing and heterologous expression of the monoamine oxidase gene from Aspergillus niger. Mol. Gen. Genet. 1995, 247(4):430-438.
    • (1995) Mol. Gen. Genet. , vol.247 , Issue.4 , pp. 430-438
    • Schilling, B.1    Lerch, K.2
  • 34
    • 11144299596 scopus 로고    scopus 로고
    • Molecular characterization of monoamine oxidase in zebrafish (Danio rerio)
    • Setini A., Pierucci F., Senatori O., Nicotra A. Molecular characterization of monoamine oxidase in zebrafish (Danio rerio). Comp. Biochem. Phys. B 2005, 140(1):153-161.
    • (2005) Comp. Biochem. Phys. B , vol.140 , Issue.1 , pp. 153-161
    • Setini, A.1    Pierucci, F.2    Senatori, O.3    Nicotra, A.4
  • 35
  • 36
    • 0033358605 scopus 로고    scopus 로고
    • Monoamine oxidase in neuropsychiatry and behavior
    • Shih J.C., Thompson R.F. Monoamine oxidase in neuropsychiatry and behavior. Am. J. Hum. Genet. 1999, 65(3):593-598.
    • (1999) Am. J. Hum. Genet. , vol.65 , Issue.3 , pp. 593-598
    • Shih, J.C.1    Thompson, R.F.2
  • 37
    • 0018853019 scopus 로고
    • Hydrogen peroxide production by rat brain in vivo
    • Sinet P.M., Heikkila R.E., Cohen G. Hydrogen peroxide production by rat brain in vivo. J. Neurochem. 1980, 34(6):1421-1428.
    • (1980) J. Neurochem. , vol.34 , Issue.6 , pp. 1421-1428
    • Sinet, P.M.1    Heikkila, R.E.2    Cohen, G.3
  • 38
    • 44449117421 scopus 로고    scopus 로고
    • Structure of human monoamine oxidase A at 2.2-angstrom resolution: the control of opening the entry for substrates/inhibitors
    • Son S.Y., Ma A., Kondou Y., Yoshimura M., Yamashita E., Tsukihara T. Structure of human monoamine oxidase A at 2.2-angstrom resolution: the control of opening the entry for substrates/inhibitors. Proc. Natl. Acad. Sci. U.S.A. 2008, 105(15):5739-5744.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , Issue.15 , pp. 5739-5744
    • Son, S.Y.1    Ma, A.2    Kondou, Y.3    Yoshimura, M.4    Yamashita, E.5    Tsukihara, T.6
  • 39
    • 0035854354 scopus 로고    scopus 로고
    • Inhibition of brain monoamine oxidase activity by the generation of hydroxyl radicals-potential implications in relation to oxidative stress
    • Soto-Otero R., Mendez-Alvarez E., Hermida-Ameijeiras A., Sanchez-Sellero I., Cruz-Landeira A., Lamas M.L.R. Inhibition of brain monoamine oxidase activity by the generation of hydroxyl radicals-potential implications in relation to oxidative stress. Life Sci. 2001, 69(8):879-889.
    • (2001) Life Sci. , vol.69 , Issue.8 , pp. 879-889
    • Soto-Otero, R.1    Mendez-Alvarez, E.2    Hermida-Ameijeiras, A.3    Sanchez-Sellero, I.4    Cruz-Landeira, A.5    Lamas, M.L.R.6
  • 41
    • 35548958257 scopus 로고    scopus 로고
    • The catecholamine cytokine balance: interaction between the brain and the immune system
    • Szelenyi J., Vizi E.S. The catecholamine cytokine balance: interaction between the brain and the immune system. Ann. N. Y. Acad. Sci. 2007, 1113311-1113324.
    • (2007) Ann. N. Y. Acad. Sci. , pp. 1113311-1113324
    • Szelenyi, J.1    Vizi, E.S.2
  • 42
    • 40349105861 scopus 로고    scopus 로고
    • Morphologic, cytometric and functional characterisation of abalone (Haliotis tuberculata) haemocytes
    • Travers M.A., Mirella da Silva P., Le Goic N., Marie D., Donval A., Huchette S., et al. Morphologic, cytometric and functional characterisation of abalone (Haliotis tuberculata) haemocytes. Fish Shellfish Immunol. 2008, 24(4):400-411.
    • (2008) Fish Shellfish Immunol. , vol.24 , Issue.4 , pp. 400-411
    • Travers, M.A.1    Mirella da Silva, P.2    Le Goic, N.3    Marie, D.4    Donval, A.5    Huchette, S.6
  • 43
    • 68749107344 scopus 로고    scopus 로고
    • Mutagenic probes of the role of Ser209 on the cavity shaping loop of human monoamine oxidase A
    • Wang J., Harris J., Mousseau D.D., Edmondson D.E. Mutagenic probes of the role of Ser209 on the cavity shaping loop of human monoamine oxidase A. FASEB J. 2009, 276(16):4569-4581.
    • (2009) FASEB J. , vol.276 , Issue.16 , pp. 4569-4581
    • Wang, J.1    Harris, J.2    Mousseau, D.D.3    Edmondson, D.E.4
  • 44
    • 67349265232 scopus 로고    scopus 로고
    • Expressed sequence tags from the zhikong scallop (Chlamys farreri): discovery and annotation of host-defense genes
    • Wang L., Song L., Zhao J., Qiu L., Zhang H., Xu W., et al. Expressed sequence tags from the zhikong scallop (Chlamys farreri): discovery and annotation of host-defense genes. Fish Shellfish Immunol. 2009, 26(5):744-750.
    • (2009) Fish Shellfish Immunol. , vol.26 , Issue.5 , pp. 744-750
    • Wang, L.1    Song, L.2    Zhao, J.3    Qiu, L.4    Zhang, H.5    Xu, W.6
  • 45
    • 0043074444 scopus 로고    scopus 로고
    • Bivalve immunity: comparisons between the marine mussel (Mytilus edulis), the edible cockle (Cerastoderma edule) and the razor-shell (Ensis siliqua)
    • Wootton E.C., Dyrynda E.A., Ratcliffe N.A. Bivalve immunity: comparisons between the marine mussel (Mytilus edulis), the edible cockle (Cerastoderma edule) and the razor-shell (Ensis siliqua). Fish Shellfish Immunol. 2003, 15(3):195-210.
    • (2003) Fish Shellfish Immunol. , vol.15 , Issue.3 , pp. 195-210
    • Wootton, E.C.1    Dyrynda, E.A.2    Ratcliffe, N.A.3
  • 46
    • 0027245885 scopus 로고
    • Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines
    • Wu H.F., Chen K., Shih J.C. Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines. Mol. Pharmacol. 1993, 43(6):888-893.
    • (1993) Mol. Pharmacol. , vol.43 , Issue.6 , pp. 888-893
    • Wu, H.F.1    Chen, K.2    Shih, J.C.3
  • 47
    • 78049367917 scopus 로고    scopus 로고
    • Enzymological characteristic of monoamine oxidase from the visual ganglia of the Pacific squid Todarodes pacificus
    • Yagodina O.V. Enzymological characteristic of monoamine oxidase from the visual ganglia of the Pacific squid Todarodes pacificus. Dokl. Biochem. Biophys. 2009, 428(1):284-287.
    • (2009) Dokl. Biochem. Biophys. , vol.428 , Issue.1 , pp. 284-287
    • Yagodina, O.V.1
  • 48
    • 50149106793 scopus 로고    scopus 로고
    • A novel C1q-domain-containing protein from Zhikong scallop Chlamys farreri with lipopolysaccharide binding activity
    • Zhang H., Song L., Li C., Zhao J., Wang H., Qiu L., et al. A novel C1q-domain-containing protein from Zhikong scallop Chlamys farreri with lipopolysaccharide binding activity. Fish Shellfish Immunol. 2008, 25(3):281-289.
    • (2008) Fish Shellfish Immunol. , vol.25 , Issue.3 , pp. 281-289
    • Zhang, H.1    Song, L.2    Li, C.3    Zhao, J.4    Wang, H.5    Qiu, L.6
  • 49
    • 33748862602 scopus 로고    scopus 로고
    • Molecular cloning of an invertebrate goose-type lysozyme gene from Chlamys farreri, and lytic activity of the recombinant protein
    • Zhao J., Song L., Li C., Zou H., Ni D., Wang W., et al. Molecular cloning of an invertebrate goose-type lysozyme gene from Chlamys farreri, and lytic activity of the recombinant protein. Mol. Immunol. 2007, 44(6):1198-1208.
    • (2007) Mol. Immunol. , vol.44 , Issue.6 , pp. 1198-1208
    • Zhao, J.1    Song, L.2    Li, C.3    Zou, H.4    Ni, D.5    Wang, W.6
  • 50
    • 78650690614 scopus 로고    scopus 로고
    • A dopamine beta hydroxylase from Chlamys farreri and its induced mRNA expression in the haemocytes after LPS stimulation
    • Zhou Z., Wang L., Yang J., Zhang H., Kong P., Wang M., et al. A dopamine beta hydroxylase from Chlamys farreri and its induced mRNA expression in the haemocytes after LPS stimulation. Fish Shellfish Immunol. 2010, 30(1):154-162.
    • (2010) Fish Shellfish Immunol. , vol.30 , Issue.1 , pp. 154-162
    • Zhou, Z.1    Wang, L.2    Yang, J.3    Zhang, H.4    Kong, P.5    Wang, M.6
  • 51
    • 0026580106 scopus 로고
    • The insertion of monoamine oxidase-a into the outer-membrane of rat-liver mitochondria
    • Zhuang Z.P., Marks B., Mccauley R.B. The insertion of monoamine oxidase-a into the outer-membrane of rat-liver mitochondria. J. Biol. Chem. 1992, 267(1):591-596.
    • (1992) J. Biol. Chem. , vol.267 , Issue.1 , pp. 591-596
    • Zhuang, Z.P.1    Marks, B.2    Mccauley, R.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.