메뉴 건너뛰기




Volumn 40, Issue 2, 2014, Pages 584-594

The comparative proteomics analysis revealed the modulation of inducible nitric oxide on the immune response of scallop Chlamys farreri

Author keywords

Chlamys farreri; Immune response; Lipopolysaccharide (LPS); Nitric oxide (NO); Proteome

Indexed keywords

INDUCIBLE NITRIC OXIDE SYNTHASE; LIPOPOLYSACCHARIDE; NITRIC OXIDE; PROTEOME; S-METHYLISOTHIOPSEUDOURONIUM; THIOUREA DERIVATIVE;

EID: 84908288469     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2014.08.015     Document Type: Article
Times cited : (10)

References (69)
  • 1
    • 84866952466 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase aggresome formation is mediated by nitric oxide
    • Wang T., Xia Y. Inducible nitric oxide synthase aggresome formation is mediated by nitric oxide. Biochem Biophys Res Commun 2012, 426:386-389.
    • (2012) Biochem Biophys Res Commun , vol.426 , pp. 386-389
    • Wang, T.1    Xia, Y.2
  • 2
    • 0024208276 scopus 로고
    • Macrophage oxidation of l-arginine to nitrite and nitrate: nitric oxide is an intermediate
    • Marletta M.A., Yoon P.S., Iyengar R., Leaf C.D., Wishnok J.S. Macrophage oxidation of l-arginine to nitrite and nitrate: nitric oxide is an intermediate. Biochemistry 1988, 27:8706-8711.
    • (1988) Biochemistry , vol.27 , pp. 8706-8711
    • Marletta, M.A.1    Yoon, P.S.2    Iyengar, R.3    Leaf, C.D.4    Wishnok, J.S.5
  • 6
    • 0038236742 scopus 로고    scopus 로고
    • Heme proteins and nitric oxide (NO): the neglected, eloquent chemistry in NO redox signaling and regulation
    • Thomas D.D., Miranda K.M., Colton C.A., Citrin D., Espey M.G., Wink D.A. Heme proteins and nitric oxide (NO): the neglected, eloquent chemistry in NO redox signaling and regulation. Antioxid Redox Signal 2003, 5:307-317.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 307-317
    • Thomas, D.D.1    Miranda, K.M.2    Colton, C.A.3    Citrin, D.4    Espey, M.G.5    Wink, D.A.6
  • 7
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: structure, function and inhibition
    • Alderton W.K., Cooper C.E., Knowles R.G. Nitric oxide synthases: structure, function and inhibition. Biochem J 2001, 357:593-615.
    • (2001) Biochem J , vol.357 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 8
    • 0028902552 scopus 로고
    • Nitric oxide synthases: properties and catalytic mechanism
    • Griffith O.W., Stuehr D.J. Nitric oxide synthases: properties and catalytic mechanism. Annu Rev Physiol 1995, 57:707-736.
    • (1995) Annu Rev Physiol , vol.57 , pp. 707-736
    • Griffith, O.W.1    Stuehr, D.J.2
  • 9
    • 0029966119 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase, a modular enzyme formed by convergent evolution: structure studies of a cysteine thiolate-liganded heme protein that hydroxylates l-arginine to produce NO as a cellular signal
    • Masters B.S., McMillan K., Sheta E.A., Nishimura J.S., Roman L.J., Martasek P. Neuronal nitric oxide synthase, a modular enzyme formed by convergent evolution: structure studies of a cysteine thiolate-liganded heme protein that hydroxylates l-arginine to produce NO as a cellular signal. FASEB J 1996, 10:552-558.
    • (1996) FASEB J , vol.10 , pp. 552-558
    • Masters, B.S.1    McMillan, K.2    Sheta, E.A.3    Nishimura, J.S.4    Roman, L.J.5    Martasek, P.6
  • 10
    • 0028092958 scopus 로고
    • Nitric oxide synthases: roles, tolls, and controls
    • Nathan C., Xie Q.W. Nitric oxide synthases: roles, tolls, and controls. Cell 1994, 78:915-918.
    • (1994) Cell , vol.78 , pp. 915-918
    • Nathan, C.1    Xie, Q.W.2
  • 11
    • 84880789485 scopus 로고    scopus 로고
    • Ascallop nitric oxide synthase (NOS) with structure similar to neuronal NOS and its involvement in the immune defense
    • Jiang Q., Zhou Z., Wang L., Wang L., Yue F., Wang J., et al. Ascallop nitric oxide synthase (NOS) with structure similar to neuronal NOS and its involvement in the immune defense. PLoS One 2013, 8:e69158.
    • (2013) PLoS One , vol.8
    • Jiang, Q.1    Zhou, Z.2    Wang, L.3    Wang, L.4    Yue, F.5    Wang, J.6
  • 13
    • 0037227097 scopus 로고    scopus 로고
    • Nitric oxide contributes to induction of innate immune responses to gram-negative bacteria in Drosophila
    • Foley E., O'Farrell P.H. Nitric oxide contributes to induction of innate immune responses to gram-negative bacteria in Drosophila. Genes Dev 2003, 17:115-125.
    • (2003) Genes Dev , vol.17 , pp. 115-125
    • Foley, E.1    O'Farrell, P.H.2
  • 14
    • 77949888065 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the nitric oxide synthase gene from kuruma shrimp, Marsupenaeus japonicus
    • Inada M., Mekata T., Sudhakaran R., Okugawa S., Kono T., El Asely A.M., et al. Molecular cloning and characterization of the nitric oxide synthase gene from kuruma shrimp, Marsupenaeus japonicus. Fish Shellfish Immunol 2010, 28:701-711.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 701-711
    • Inada, M.1    Mekata, T.2    Sudhakaran, R.3    Okugawa, S.4    Kono, T.5    El Asely, A.M.6
  • 15
    • 77049117483 scopus 로고    scopus 로고
    • Molecular cloning and expression of NOS in shrimp, Litopenaeus vannamei
    • Yao C.L., Ji P.F., Wang Z.Y., Li F.H., Xiang J.H. Molecular cloning and expression of NOS in shrimp, Litopenaeus vannamei. Fish Shellfish Immunol 2010, 28:453-460.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 453-460
    • Yao, C.L.1    Ji, P.F.2    Wang, Z.Y.3    Li, F.H.4    Xiang, J.H.5
  • 16
    • 77954533065 scopus 로고    scopus 로고
    • An inducible nitric oxide synthase (NOS) is expressed in hemocytes of the spiny lobster Panulirus argus: cloning, characterization and expression analysis
    • Rodríguez-Ramos T., Carpio Y., Bolívar J., Espinosa G., Hernández-López J., Gollas-Galván T., et al. An inducible nitric oxide synthase (NOS) is expressed in hemocytes of the spiny lobster Panulirus argus: cloning, characterization and expression analysis. Fish Shellfish Immunol 2010, 29:469-479.
    • (2010) Fish Shellfish Immunol , vol.29 , pp. 469-479
    • Rodríguez-Ramos, T.1    Carpio, Y.2    Bolívar, J.3    Espinosa, G.4    Hernández-López, J.5    Gollas-Galván, T.6
  • 17
    • 0037363820 scopus 로고    scopus 로고
    • Nitric oxide production by carpet shell clam (Ruditapes decussatus) hemocytes
    • Tafalla C., Gomez-Leon J., Novoa B., Figueras A. Nitric oxide production by carpet shell clam (Ruditapes decussatus) hemocytes. Dev Comp Immunol 2003, 27:197-205.
    • (2003) Dev Comp Immunol , vol.27 , pp. 197-205
    • Tafalla, C.1    Gomez-Leon, J.2    Novoa, B.3    Figueras, A.4
  • 18
    • 36049027710 scopus 로고    scopus 로고
    • After the prestige oil spill modifications in NO production and other parameters related to the immune response were detected in hemocytes of Mytilus galloprovincialis
    • Novas A., Barcia R., Ramos-Martínez J.I. After the prestige oil spill modifications in NO production and other parameters related to the immune response were detected in hemocytes of Mytilus galloprovincialis. Aquat Toxicol 2007, 85:285-290.
    • (2007) Aquat Toxicol , vol.85 , pp. 285-290
    • Novas, A.1    Barcia, R.2    Ramos-Martínez, J.I.3
  • 19
    • 0033862794 scopus 로고    scopus 로고
    • Invitro production of superoxide and nitric oxide (as nitrite and nitrate) by Mytilus galloprovincialis haemocytes upon incubation with PMA or laminarin or during yeast phagocytosis
    • Arumugam M., Romestand B., Torreilles J., Roch P. Invitro production of superoxide and nitric oxide (as nitrite and nitrate) by Mytilus galloprovincialis haemocytes upon incubation with PMA or laminarin or during yeast phagocytosis. Eur J Cell Biol 2000, 79:513-519.
    • (2000) Eur J Cell Biol , vol.79 , pp. 513-519
    • Arumugam, M.1    Romestand, B.2    Torreilles, J.3    Roch, P.4
  • 20
    • 2542473579 scopus 로고    scopus 로고
    • Invitro production of peroxynitrite by haemocytes from marine bivalves: C-ELISA determination of 3-nitrotyrosine level in plasma proteins from Mytilus galloprovincialis and Crassostrea gigas
    • Torreilles J., Romestand B. Invitro production of peroxynitrite by haemocytes from marine bivalves: C-ELISA determination of 3-nitrotyrosine level in plasma proteins from Mytilus galloprovincialis and Crassostrea gigas. BMC Immunol 2001, 2:1.
    • (2001) BMC Immunol , vol.2 , pp. 1
    • Torreilles, J.1    Romestand, B.2
  • 21
    • 84871616586 scopus 로고    scopus 로고
    • The immunomodulation of inducible nitric oxide in scallop Chlamys farreri
    • Jiang Q., Zhou Z., Wang L., Shi X., Wang J., Yue F., et al. The immunomodulation of inducible nitric oxide in scallop Chlamys farreri. Fish Shellfish Immunol 2013, 34:100-108.
    • (2013) Fish Shellfish Immunol , vol.34 , pp. 100-108
    • Jiang, Q.1    Zhou, Z.2    Wang, L.3    Shi, X.4    Wang, J.5    Yue, F.6
  • 22
    • 0027787658 scopus 로고
    • Evidence for nitric oxide production and utilization as a bacteriocidal agent by invertebrate immunocytes
    • Ottaviani E., Paeman L.R., Cadet P., Stefano G.B. Evidence for nitric oxide production and utilization as a bacteriocidal agent by invertebrate immunocytes. Eur J Pharmacol Environ Toxicol Pharmacol 1993, 248:319-324.
    • (1993) Eur J Pharmacol Environ Toxicol Pharmacol , vol.248 , pp. 319-324
    • Ottaviani, E.1    Paeman, L.R.2    Cadet, P.3    Stefano, G.B.4
  • 23
    • 0032815497 scopus 로고    scopus 로고
    • Molluscan aquaculture in China
    • Guo X., Ford S.E., Zhang F. Molluscan aquaculture in China. JShellfish Res 1999, 18:19-31.
    • (1999) JShellfish Res , vol.18 , pp. 19-31
    • Guo, X.1    Ford, S.E.2    Zhang, F.3
  • 25
    • 81255127337 scopus 로고    scopus 로고
    • Comparative proteomic analysis of challenged Zhikong scallop (Chlamys farreri): a new insight into the anti-vibrio immune response of marine bivalves
    • Huan P., Wang H., Liu B. Comparative proteomic analysis of challenged Zhikong scallop (Chlamys farreri): a new insight into the anti-vibrio immune response of marine bivalves. Fish Shellfish Immunol 2011, 31:1186-1192.
    • (2011) Fish Shellfish Immunol , vol.31 , pp. 1186-1192
    • Huan, P.1    Wang, H.2    Liu, B.3
  • 26
    • 84891163064 scopus 로고    scopus 로고
    • The protein expression profile in hepatopancreas of scallop Chlamys farreri under heat stress and Vibrio anguillarum challenge
    • Sun Z., Yang C., Wang L., Wang X., Wang J., Yue F., et al. The protein expression profile in hepatopancreas of scallop Chlamys farreri under heat stress and Vibrio anguillarum challenge. Fish Shellfish Immunol 2014, 36:252-260.
    • (2014) Fish Shellfish Immunol , vol.36 , pp. 252-260
    • Sun, Z.1    Yang, C.2    Wang, L.3    Wang, X.4    Wang, J.5    Yue, F.6
  • 28
    • 84859699831 scopus 로고    scopus 로고
    • The gene ontology: enhancements for 2011
    • Consortium TGO
    • Consortium TGO The gene ontology: enhancements for 2011. Nucleic Acids Res 2012, 40:D559-D564.
    • (2012) Nucleic Acids Res , vol.40
  • 30
    • 84856834347 scopus 로고    scopus 로고
    • Regulation by S-nitrosylation of protein post-translational modification
    • Hess D.T., Stamler J.S. Regulation by S-nitrosylation of protein post-translational modification. JBiol Chem 2012, 287:4411-4418.
    • (2012) JBiol Chem , vol.287 , pp. 4411-4418
    • Hess, D.T.1    Stamler, J.S.2
  • 31
    • 79952009250 scopus 로고    scopus 로고
    • Aprimitive toll-like receptor signaling pathway in mollusk Zhikong scallop Chlamys farreri
    • Wang M., Yang J., Zhou Z., Qiu L., Wang L., Zhang H., et al. Aprimitive toll-like receptor signaling pathway in mollusk Zhikong scallop Chlamys farreri. Dev Comp Immunol 2011, 35:511-520.
    • (2011) Dev Comp Immunol , vol.35 , pp. 511-520
    • Wang, M.1    Yang, J.2    Zhou, Z.3    Qiu, L.4    Wang, L.5    Zhang, H.6
  • 32
    • 0042733592 scopus 로고    scopus 로고
    • SIGIRR, a negative regulator of toll-like receptor-interleukin 1 receptor signaling
    • Wald D., Qin J., Zhao Z., Qian Y., Naramura M., Tian L., et al. SIGIRR, a negative regulator of toll-like receptor-interleukin 1 receptor signaling. Nat Immunol 2003, 4:920-927.
    • (2003) Nat Immunol , vol.4 , pp. 920-927
    • Wald, D.1    Qin, J.2    Zhao, Z.3    Qian, Y.4    Naramura, M.5    Tian, L.6
  • 33
    • 21644477461 scopus 로고    scopus 로고
    • SIGIRR inhibits interleukin-1 receptor- and toll-like receptor 4-mediated signaling through different mechanisms
    • Qin J., Qian Y., Yao J., Grace C., Li X. SIGIRR inhibits interleukin-1 receptor- and toll-like receptor 4-mediated signaling through different mechanisms. JBiol Chem 2005, 280:25233-25241.
    • (2005) JBiol Chem , vol.280 , pp. 25233-25241
    • Qin, J.1    Qian, Y.2    Yao, J.3    Grace, C.4    Li, X.5
  • 34
    • 4444351205 scopus 로고    scopus 로고
    • Yeast Asc1p and mammalian RACK1 are functionally orthologous core 40S ribosomal proteins that repress gene expression
    • Gerbasi V.R., Weaver C.M., Hill S., Friedman D.B., Link A.J. Yeast Asc1p and mammalian RACK1 are functionally orthologous core 40S ribosomal proteins that repress gene expression. Mol Cell Biol 2004, 24:8276-8287.
    • (2004) Mol Cell Biol , vol.24 , pp. 8276-8287
    • Gerbasi, V.R.1    Weaver, C.M.2    Hill, S.3    Friedman, D.B.4    Link, A.J.5
  • 35
    • 52149108283 scopus 로고    scopus 로고
    • GβL regulates TNFα-induced NF-k{cyrillic}B signaling by directly inhibiting the activation of Ik{cyrillic}B kinase
    • Kim Y.L., Kim J.-E., Shin K.-J., Lee S., Ahn C., Chung J., et al. GβL regulates TNFα-induced NF-k{cyrillic}B signaling by directly inhibiting the activation of Ik{cyrillic}B kinase. Cell Signal 2008, 20:2127-2133.
    • (2008) Cell Signal , vol.20 , pp. 2127-2133
    • Kim, Y.L.1    Kim, J.-E.2    Shin, K.-J.3    Lee, S.4    Ahn, C.5    Chung, J.6
  • 36
    • 79951508964 scopus 로고    scopus 로고
    • Interaction of sesamol (3,4-methylenedioxyphenol) with tyrosinase and its effect on melanin synthesis
    • Mahendra Kumar C., Sathisha U.V., Dharmesh S., Rao A.G.A., Singh S.A. Interaction of sesamol (3,4-methylenedioxyphenol) with tyrosinase and its effect on melanin synthesis. Biochimie 2011, 93:562-569.
    • (2011) Biochimie , vol.93 , pp. 562-569
    • Mahendra Kumar, C.1    Sathisha, U.V.2    Dharmesh, S.3    Rao, A.G.A.4    Singh, S.A.5
  • 37
    • 84863223972 scopus 로고    scopus 로고
    • The phenoloxidase activity and antibacterial function of a tyrosinase from scallop Chlamys farreri
    • Zhou Z., Ni D., Wang M., Wang L., Wang L., Shi X., et al. The phenoloxidase activity and antibacterial function of a tyrosinase from scallop Chlamys farreri. Fish Shellfish Immunol 2012, 33:375-381.
    • (2012) Fish Shellfish Immunol , vol.33 , pp. 375-381
    • Zhou, Z.1    Ni, D.2    Wang, M.3    Wang, L.4    Wang, L.5    Shi, X.6
  • 38
    • 41549160174 scopus 로고    scopus 로고
    • ISG20L2, a novel vertebrate nucleolar exoribonuclease involved in ribosome biogenesis
    • Couté Y., Kindbeiter K., Belin S., Dieckmann R., Duret L., Bezin L., et al. ISG20L2, a novel vertebrate nucleolar exoribonuclease involved in ribosome biogenesis. Mol Cell Proteomics 2008, 7:546-559.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 546-559
    • Couté, Y.1    Kindbeiter, K.2    Belin, S.3    Dieckmann, R.4    Duret, L.5    Bezin, L.6
  • 39
    • 0038521287 scopus 로고    scopus 로고
    • ISG20, a new interferon-induced RNase specific for single-stranded RNA, defines an alternative antiviral pathway against RNA genomic viruses
    • Espert L., Degols G., Gongora C., Blondel D., Williams B.R., Silverman R.H., et al. ISG20, a new interferon-induced RNase specific for single-stranded RNA, defines an alternative antiviral pathway against RNA genomic viruses. JBiol Chem 2003, 278:16151-16158.
    • (2003) JBiol Chem , vol.278 , pp. 16151-16158
    • Espert, L.1    Degols, G.2    Gongora, C.3    Blondel, D.4    Williams, B.R.5    Silverman, R.H.6
  • 40
    • 34347226273 scopus 로고    scopus 로고
    • ISG20, an actor of the innate immune response
    • Degols G., Eldin P., Mechti N. ISG20, an actor of the innate immune response. Biochimie 2007, 89:831-835.
    • (2007) Biochimie , vol.89 , pp. 831-835
    • Degols, G.1    Eldin, P.2    Mechti, N.3
  • 41
    • 38349052952 scopus 로고    scopus 로고
    • Aprophenoloxidase from the Chinese mitten crab Eriocheir sinensis: gene cloning, expression and activity analysis
    • Gai Y., Zhao J., Song L., Li C., Zheng P., Qiu L., et al. Aprophenoloxidase from the Chinese mitten crab Eriocheir sinensis: gene cloning, expression and activity analysis. Fish Shellfish Immunol 2008, 24:156-167.
    • (2008) Fish Shellfish Immunol , vol.24 , pp. 156-167
    • Gai, Y.1    Zhao, J.2    Song, L.3    Li, C.4    Zheng, P.5    Qiu, L.6
  • 42
    • 84900403543 scopus 로고    scopus 로고
    • STAT3 regulation by S-nitrosylation: implication for inflammatory disease
    • Kim J., Won J.S., Singh A.K., Sharma A.K., Singh I. STAT3 regulation by S-nitrosylation: implication for inflammatory disease. Antioxid Redox Signal 2014, 20:2514-2527.
    • (2014) Antioxid Redox Signal , vol.20 , pp. 2514-2527
    • Kim, J.1    Won, J.S.2    Singh, A.K.3    Sharma, A.K.4    Singh, I.5
  • 46
    • 48249134102 scopus 로고    scopus 로고
    • Mediation, modulation, and consequences of membrane-cytoskeleton interactions
    • Doherty G.J., McMahon H.T. Mediation, modulation, and consequences of membrane-cytoskeleton interactions. Annu Rev Biophys 2008, 37:65-95.
    • (2008) Annu Rev Biophys , vol.37 , pp. 65-95
    • Doherty, G.J.1    McMahon, H.T.2
  • 47
    • 0026730739 scopus 로고
    • Confinement as a determinant of macromolecular structure and reactivity
    • Minton A.P. Confinement as a determinant of macromolecular structure and reactivity. Biophys J 1992, 63:1090-1100.
    • (1992) Biophys J , vol.63 , pp. 1090-1100
    • Minton, A.P.1
  • 48
    • 75749111318 scopus 로고    scopus 로고
    • Immune pathology associated with altered actin cytoskeleton regulation
    • Wickramarachchi D.C., Theofilopoulos A.N., Kono D.H. Immune pathology associated with altered actin cytoskeleton regulation. Autoimmunity 2010, 43:64-75.
    • (2010) Autoimmunity , vol.43 , pp. 64-75
    • Wickramarachchi, D.C.1    Theofilopoulos, A.N.2    Kono, D.H.3
  • 49
    • 0028945057 scopus 로고
    • Microtubules and microtubule-associated proteins
    • Mandelkow E., Mandelkow E.M. Microtubules and microtubule-associated proteins. Curr Opin Cell Biol 1995, 7:72-81.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 72-81
    • Mandelkow, E.1    Mandelkow, E.M.2
  • 50
    • 1542374026 scopus 로고    scopus 로고
    • Gamma tropomyosin gene products are required for embryonic development
    • Hook J., Lemckert F., Qin H., Schevzov G., Gunning P. Gamma tropomyosin gene products are required for embryonic development. Mol Cell Biol 2004, 24:2318-2323.
    • (2004) Mol Cell Biol , vol.24 , pp. 2318-2323
    • Hook, J.1    Lemckert, F.2    Qin, H.3    Schevzov, G.4    Gunning, P.5
  • 51
    • 0037031320 scopus 로고    scopus 로고
    • Actin dynamics: tropomyosin provides stability
    • Cooper J.A. Actin dynamics: tropomyosin provides stability. Curr Biol 2002, 12:R523-R525.
    • (2002) Curr Biol , vol.12
    • Cooper, J.A.1
  • 52
    • 37249019968 scopus 로고    scopus 로고
    • Tropomyosins as interpreters of the signalling environment to regulate the local cytoskeleton
    • O'Neill G.M., Stehn J., Gunning P.W. Tropomyosins as interpreters of the signalling environment to regulate the local cytoskeleton. Semin Cancer Biol 2008, 18:35-44.
    • (2008) Semin Cancer Biol , vol.18 , pp. 35-44
    • O'Neill, G.M.1    Stehn, J.2    Gunning, P.W.3
  • 53
    • 44949125487 scopus 로고    scopus 로고
    • Proteome of monocyte priming by lipopolysaccharide, including changes in interleukin-1beta and leukocyte elastase inhibitor
    • Pabst M., Pabst K., Handsman D., Beranova-Giorgianni S., Giorgianni F. Proteome of monocyte priming by lipopolysaccharide, including changes in interleukin-1beta and leukocyte elastase inhibitor. Proteome Sci 2008, 6:1-13.
    • (2008) Proteome Sci , vol.6 , pp. 1-13
    • Pabst, M.1    Pabst, K.2    Handsman, D.3    Beranova-Giorgianni, S.4    Giorgianni, F.5
  • 54
    • 0030602186 scopus 로고    scopus 로고
    • Nitric oxide induces ADP-ribosylation of actin in murine macrophages: association with the inhibition of pseudopodia formation, phagocytic activity, and adherence on a laminin substratum
    • Jun C.D., Han M.K., Kim U.H., Chung H.T. Nitric oxide induces ADP-ribosylation of actin in murine macrophages: association with the inhibition of pseudopodia formation, phagocytic activity, and adherence on a laminin substratum. Cell Immunol 1996, 174:25-34.
    • (1996) Cell Immunol , vol.174 , pp. 25-34
    • Jun, C.D.1    Han, M.K.2    Kim, U.H.3    Chung, H.T.4
  • 56
    • 0034634372 scopus 로고    scopus 로고
    • Survival for immunity: the price of immune system activation for bumblebee workers
    • Moret Y., Schmid-Hempel P. Survival for immunity: the price of immune system activation for bumblebee workers. Science 2000, 290:1166-1168.
    • (2000) Science , vol.290 , pp. 1166-1168
    • Moret, Y.1    Schmid-Hempel, P.2
  • 57
    • 0037218085 scopus 로고    scopus 로고
    • On the evolutionary ecology of specific immune defence
    • Schmid-Hempel P., Ebert D. On the evolutionary ecology of specific immune defence. Trends Ecol Evol 2003, 18:27-32.
    • (2003) Trends Ecol Evol , vol.18 , pp. 27-32
    • Schmid-Hempel, P.1    Ebert, D.2
  • 58
    • 33845866857 scopus 로고    scopus 로고
    • Inflammation and metabolic disorders
    • Hotamisligil G.S. Inflammation and metabolic disorders. Nature 2006, 444:860-867.
    • (2006) Nature , vol.444 , pp. 860-867
    • Hotamisligil, G.S.1
  • 59
  • 61
    • 37349110355 scopus 로고    scopus 로고
    • Metabolic adaptations through the PGC-1 alpha and SIRT1 pathways
    • Rodgers J.T., Lerin C., Gerhart-Hines Z., Puigserver P. Metabolic adaptations through the PGC-1 alpha and SIRT1 pathways. FEBS Lett 2008, 582:46-53.
    • (2008) FEBS Lett , vol.582 , pp. 46-53
    • Rodgers, J.T.1    Lerin, C.2    Gerhart-Hines, Z.3    Puigserver, P.4
  • 62
    • 33845399894 scopus 로고    scopus 로고
    • Resveratrol improves mitochondrial function and protects against metabolic disease by activating SIRT1 and PGC-1±
    • Lagouge M., Argmann C., Gerhart-Hines Z., Meziane H., Lerin C., Daussin F., et al. Resveratrol improves mitochondrial function and protects against metabolic disease by activating SIRT1 and PGC-1±. Cell 2006, 127:1109-1122.
    • (2006) Cell , vol.127 , pp. 1109-1122
    • Lagouge, M.1    Argmann, C.2    Gerhart-Hines, Z.3    Meziane, H.4    Lerin, C.5    Daussin, F.6
  • 63
    • 77955029360 scopus 로고    scopus 로고
    • Physiological and immune responses of zhikong scallop Chlamys farreri to the acute viral necrobiotic virus infection
    • Tang B., Liu B., Wang X., Yue X., Xiang J. Physiological and immune responses of zhikong scallop Chlamys farreri to the acute viral necrobiotic virus infection. Fish Shellfish Immunol 2010, 29:42-48.
    • (2010) Fish Shellfish Immunol , vol.29 , pp. 42-48
    • Tang, B.1    Liu, B.2    Wang, X.3    Yue, X.4    Xiang, J.5
  • 64
    • 84866746369 scopus 로고    scopus 로고
    • Immune response and energy metabolism of Chlamys farreri under Vibrio anguillarum challenge and high temperature exposure
    • Wang X., Wang L., Zhang H., Ji Q., Song L., Qiu L., et al. Immune response and energy metabolism of Chlamys farreri under Vibrio anguillarum challenge and high temperature exposure. Fish Shellfish Immunol 2012, 33:1016-1026.
    • (2012) Fish Shellfish Immunol , vol.33 , pp. 1016-1026
    • Wang, X.1    Wang, L.2    Zhang, H.3    Ji, Q.4    Song, L.5    Qiu, L.6
  • 65
    • 84862801494 scopus 로고    scopus 로고
    • Alternation of immune parameters and cellular energy allocation of Chlamys farreri under ammonia-N exposure and Vibrio anguillarum challenge
    • Wang X., Wang L., Yao C., Qiu L., Zhang H., Zhi Z., et al. Alternation of immune parameters and cellular energy allocation of Chlamys farreri under ammonia-N exposure and Vibrio anguillarum challenge. Fish Shellfish Immunol 2012, 32:741-749.
    • (2012) Fish Shellfish Immunol , vol.32 , pp. 741-749
    • Wang, X.1    Wang, L.2    Yao, C.3    Qiu, L.4    Zhang, H.5    Zhi, Z.6
  • 66
    • 0041352962 scopus 로고    scopus 로고
    • Sphase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component
    • Zheng L., Roeder R.G., Luo Y. Sphase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component. Cell 2003, 114:255-266.
    • (2003) Cell , vol.114 , pp. 255-266
    • Zheng, L.1    Roeder, R.G.2    Luo, Y.3
  • 67
    • 0026459818 scopus 로고
    • Proliferative dependent regulation of the glyceraldehyde-3-phosphate dehydrogenase/uracil DNA glycosylase gene in human cells
    • Meyer-Siegler K., Rahman-Mansur N., Wurzer J.C., Sirover M.A. Proliferative dependent regulation of the glyceraldehyde-3-phosphate dehydrogenase/uracil DNA glycosylase gene in human cells. Carcinogenesis 1992, 13:2127-2132.
    • (1992) Carcinogenesis , vol.13 , pp. 2127-2132
    • Meyer-Siegler, K.1    Rahman-Mansur, N.2    Wurzer, J.C.3    Sirover, M.A.4
  • 68
    • 0027518424 scopus 로고
    • Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase
    • Singh R., Green M.R. Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase. Science 1993, 259:365-368.
    • (1993) Science , vol.259 , pp. 365-368
    • Singh, R.1    Green, M.R.2
  • 69
    • 52449119928 scopus 로고    scopus 로고
    • The multifunctional protein glyceraldehyde-3-phosphate dehydrogenase is both regulated and controls colony-stimulating factor-1 messenger RNA stability in ovarian cancer
    • Zhou Y., Yi X., Stoffer J.B., Bonafe N., Gilmore-Hebert M., McAlpine J., et al. The multifunctional protein glyceraldehyde-3-phosphate dehydrogenase is both regulated and controls colony-stimulating factor-1 messenger RNA stability in ovarian cancer. Mol Cancer Res 2008, 6:1375-1384.
    • (2008) Mol Cancer Res , vol.6 , pp. 1375-1384
    • Zhou, Y.1    Yi, X.2    Stoffer, J.B.3    Bonafe, N.4    Gilmore-Hebert, M.5    McAlpine, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.