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Volumn 6, Issue 7, 2005, Pages 557-574

Spatial and temporal coordination of expression of immune response genes during Pseudomonas infection of horseshoe crab, Carcinoscorpius rotundicauda

Author keywords

Expressed sequence tags (ESTs); Immune response gene clusters; Pseudomonas infection; Spatial and temporal immune gene expression; Transcript profiling

Indexed keywords

ACUTE DISEASE; ANIMAL TISSUE; APOPTOSIS; ARTICLE; CONTROLLED STUDY; DOWN REGULATION; EXPRESSED SEQUENCE TAG; GENE CLUSTER; GENE EXPRESSION REGULATION; GRAM NEGATIVE INFECTION; HEPATOPANCREAS; IMMUNE RESPONSE; IMMUNITY; IMMUNOMODULATION; LIMULUS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SIGNAL TRANSDUCTION; STRESS; UNINDEXED SEQUENCE; UPREGULATION;

EID: 27844477305     PISSN: 14664879     EISSN: 14765470     Source Type: Journal    
DOI: 10.1038/sj.gene.6364240     Document Type: Article
Times cited : (33)

References (79)
  • 1
    • 0346157290 scopus 로고    scopus 로고
    • Innate immunity: An overview
    • Beutler B. Innate immunity: An overview. Mol Immunol 2004; 40: 845-859.
    • (2004) Mol. Immunol. , vol.40 , pp. 845-859
    • Beutler, B.1
  • 2
    • 0034210449 scopus 로고    scopus 로고
    • How does the immune system distinguish self from nonself?
    • discussion 257-344
    • Medzhitov R, Janeway Jr CA. How does the immune system distinguish self from nonself? Semin Immunol 2000; 12: 185-188; discussion 257-344.
    • (2000) Semin. Immunol. , vol.12 , pp. 185-188
    • Medzhitov, R.1    Janeway Jr., C.A.2
  • 3
    • 0032994485 scopus 로고    scopus 로고
    • Induction and regulation of antimicrobial peptides in Drosophila
    • Engstrom Y. Induction and regulation of antimicrobial peptides in Drosophila. Dev Comp Immunol 1999; 23: 345-358.
    • (1999) Dev. Comp. Immunol. , vol.23 , pp. 345-358
    • Engstrom, Y.1
  • 4
    • 0031446642 scopus 로고    scopus 로고
    • Drosophila host defense: Differential induction of antimicrobial peptide genes after infection by various classes of microorganisms
    • Lemaitre B, Reichhart JM, Hoffmann JA. Drosophila host defense: differential induction of antimicrobial peptide genes after infection by various classes of microorganisms. Proc Natl Acad Sci USA 1997; 94: 14614-14619.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14614-14619
    • Lemaitre, B.1    Reichhart, J.M.2    Hoffmann, J.A.3
  • 6
    • 0035940514 scopus 로고    scopus 로고
    • Genome-wide analysis of the Drosophila immune response by using oligonucleotide microarrays
    • De Gregorio E, Spellman PT, Rubin GM, Lemaitre B. Genome-wide analysis of the Drosophila immune response by using oligonucleotide microarrays. Proc Natl Acad Sci USA 2001; 98: 12590-12595.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12590-12595
    • De Gregorio, E.1    Spellman, P.T.2    Rubin, G.M.3    Lemaitre, B.4
  • 7
    • 0037013856 scopus 로고    scopus 로고
    • The Toll and Imd pathways are the major regulators of the immune response in Drosophila
    • De Gregorio E, Spellman PT, Tzou P, Rubin GM, Lemaitre B. The Toll and Imd pathways are the major regulators of the immune response in Drosophila. EMBO J 2002; 21: 2568-2579.
    • (2002) EMBO J. , vol.21 , pp. 2568-2579
    • De Gregorio, E.1    Spellman, P.T.2    Tzou, P.3    Rubin, G.M.4    Lemaitre, B.5
  • 9
    • 0027328307 scopus 로고
    • Two forms of factor C from the amoebocytes of Carcinoscorpius rotundicauda: Purification and characterisation
    • Ding JL, Navas MAr, Ho B. Two forms of factor C from the amoebocytes of Carcinoscorpius rotundicauda: Purification and characterisation. Biochim Biophys Acta 1993; 1202: 149-156.
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 149-156
    • Ding, J.L.1    Navas, MAr.2    Ho, B.3
  • 10
    • 0029257172 scopus 로고
    • Molecular cloning and sequence analysis of factor C cDNA from the Singapore horseshoe crab, Carcinoscorpius rotundicauda
    • Ding JL, Navas III MA, Ho B. Molecular cloning and sequence analysis of factor C cDNA from the Singapore horseshoe crab, Carcinoscorpius rotundicauda. Mol Mar Biol Biotechnol 1995; 4: 90-103.
    • (1995) Mol. Mar. Biol. Biotechnol. , vol.4 , pp. 90-103
    • Ding, J.L.1    Navas III, M.A.2    Ho, B.3
  • 11
    • 1442302316 scopus 로고    scopus 로고
    • Current genome-wide analysis on serine proteases in innate immunity
    • Ding JL, Wang LH, Ho B. Current genome-wide analysis on serine proteases in innate immunity. Curr Genomics 2004; 5: 147-155.
    • (2004) Curr. Genomics , vol.5 , pp. 147-155
    • Ding, J.L.1    Wang, L.H.2    Ho, B.3
  • 12
    • 0031934614 scopus 로고    scopus 로고
    • New types of clotting factors and defense molecules found in horseshoe crab hemolymph: Their structures and functions
    • Iwanaga S, Kawabata S, Muta T. New types of clotting factors and defense molecules found in horseshoe crab hemolymph: Their structures and functions. J Biochem (Tokyo) 1998; 123: 1-15.
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 1-15
    • Iwanaga, S.1    Kawabata, S.2    Muta, T.3
  • 13
    • 0343092000 scopus 로고    scopus 로고
    • High-affinity LPS binding domain(s) in recombinant factor C of a horseshoe crab neutralizes LPS-induced lethality
    • Tan NS, Ho B, Ding JL. High-affinity LPS binding domain(s) in recombinant factor C of a horseshoe crab neutralizes LPS-induced lethality. FASEB J 2000; 14: 859-870.
    • (2000) FASEB J. , vol.14 , pp. 859-870
    • Tan, N.S.1    Ho, B.2    Ding, J.L.3
  • 14
    • 3042853063 scopus 로고    scopus 로고
    • The C-reactive protein: A predominant LPS-binding acute phase protein responsive to Pseudomonas infection
    • Ng ML, Tan SH, Ho B, Ding JL. The C-reactive protein: A predominant LPS-binding acute phase protein responsive to Pseudomonas infection. J Endotoxin Res 2004; 10: 163-174.
    • (2004) J. Endotoxin. Res. , vol.10 , pp. 163-174
    • Ng, M.L.1    Tan, S.H.2    Ho, B.3    Ding, J.L.4
  • 15
    • 0034806998 scopus 로고    scopus 로고
    • High therapeutic index of factor C Sushi peptides: Potent antimicrobials against Pseudomonas aeruginosa
    • Yau YH, Ho B, Tan NS, Ng ML, Ding JL. High therapeutic index of factor C Sushi peptides: Potent antimicrobials against Pseudomonas aeruginosa. Antimicrob Agents Chemother 2001; 45: 2820-2825.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 2820-2825
    • Yau, Y.H.1    Ho, B.2    Tan, N.S.3    Ng, M.L.4    Ding, J.L.5
  • 16
    • 13444269022 scopus 로고    scopus 로고
    • The ancient origin of the complement system
    • Zhu Y, Thangamani S, Ho B, Ding JL. The ancient origin of the complement system. EMBO J 2005; 24: 382-394.
    • (2005) EMBO J. , vol.24 , pp. 382-394
    • Zhu, Y.1    Thangamani, S.2    Ho, B.3    Ding, J.L.4
  • 17
    • 0032992548 scopus 로고    scopus 로고
    • Role of lectins in the innate immunity of horseshoe crab
    • Kawabata S, Iwanaga S. Role of lectins in the innate immunity of horseshoe crab. Dev Comp Immunol 1999; 23: 391-400.
    • (1999) Dev. Comp. Immunol. , vol.23 , pp. 391-400
    • Kawabata, S.1    Iwanaga, S.2
  • 18
    • 0034924843 scopus 로고    scopus 로고
    • The contribution of proteinase inhibitors to immune defense
    • Armstrong PB. The contribution of proteinase inhibitors to immune defense. Trends Immunol 2001; 22: 47-52.
    • (2001) Trends Immunol. , vol.22 , pp. 47-52
    • Armstrong, P.B.1
  • 19
    • 0036467504 scopus 로고    scopus 로고
    • The molecular basis of innate immunity in the horseshoe crab
    • Iwanaga S. The molecular basis of innate immunity in the horseshoe crab. Curr Opin Immunol 2002; 14: 87-95.
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 87-95
    • Iwanaga, S.1
  • 20
    • 0029845634 scopus 로고    scopus 로고
    • Toward the development of a gene index to the human genome: An assessment of the nature of high-throughput EST sequence data
    • Aaronson JS, Eckman B, Blevins RA, Borkowski JA, Myerson J, Imran S et al. Toward the development of a gene index to the human genome: An assessment of the nature of high-throughput EST sequence data. Genome Res 1996; 6: 829-845.
    • (1996) Genome Res. , vol.6 , pp. 829-845
    • Aaronson, J.S.1    Eckman, B.2    Blevins, R.A.3    Borkowski, J.A.4    Myerson, J.5    Imran, S.6
  • 22
    • 0037363719 scopus 로고    scopus 로고
    • Identification of immunorelevant genes from greater wax moth (Galleria mellonella) by a subtractive hybridization approach
    • Seitz V, Clermont A, Wedde M, Hummel M, Vilcinskas A, Schlatterer K et al. Identification of immunorelevant genes from greater wax moth (Galleria mellonella) by a subtractive hybridization approach. Dev Comp Immunol 2003; 27: 207-215.
    • (2003) Dev. Comp. Immunol. , vol.27 , pp. 207-215
    • Seitz, V.1    Clermont, A.2    Wedde, M.3    Hummel, M.4    Vilcinskas, A.5    Schlatterer, K.6
  • 23
    • 0029991653 scopus 로고    scopus 로고
    • TDB: New databases for biological discovery
    • White O, Kerlavage AR. TDB: New databases for biological discovery. Methods Enzymol 1996; 266: 27-40.
    • (1996) Methods Enzymol. , vol.266 , pp. 27-40
    • White, O.1    Kerlavage, A.R.2
  • 24
    • 0027394999 scopus 로고
    • The limulus clotting reaction
    • Iwanaga S. The limulus clotting reaction. Curr Opin Immunol 1993; 5: 74-82.
    • (1993) Curr. Opin. Immunol. , vol.5 , pp. 74-82
    • Iwanaga, S.1
  • 25
    • 3042523021 scopus 로고    scopus 로고
    • Structure and function of coagulogen, a clottable protein in horseshoe crabs
    • Osaki T, Kawabata S. Structure and function of coagulogen, a clottable protein in horseshoe crabs. Cell Mol Life Sci 2004; 61: 1257-1265.
    • (2004) Cell Mol. Life Sci. , vol.61 , pp. 1257-1265
    • Osaki, T.1    Kawabata, S.2
  • 26
    • 0242551421 scopus 로고    scopus 로고
    • Tissue transglutaminase mRNA expression in apoptotic cell death
    • Volokhina EB, Hulshof R, Haanen C, Vermes I. Tissue transglutaminase mRNA expression in apoptotic cell death. Apoptosis 2003; 8: 673-679.
    • (2003) Apoptosis , vol.8 , pp. 673-679
    • Volokhina, E.B.1    Hulshof, R.2    Haanen, C.3    Vermes, I.4
  • 27
    • 0032560573 scopus 로고    scopus 로고
    • 'Tissue' transglutaminase in cell death: A downstream or a multifunctional upstream effector?
    • Melino G, Piacentini M. 'Tissue' transglutaminase in cell death: A downstream or a multifunctional upstream effector? FEBS Lett 1998; 430: 59-63.
    • (1998) FEBS Lett. , vol.430 , pp. 59-63
    • Melino, G.1    Piacentini, M.2
  • 28
    • 0027525969 scopus 로고
    • Limulus hemocyte transglutaminase. Its purification and characterization, and identification of the intracellular substrates
    • Tokunaga F, Yamada M, Miyata T, Ding YL, Hiranaga-Kawabata M, Muta T et al. Limulus hemocyte transglutaminase. Its purification and characterization, and identification of the intracellular substrates. J Biol Chem 1993; 268: 252-261.
    • (1993) J. Biol. Chem. , vol.268 , pp. 252-261
    • Tokunaga, F.1    Yamada, M.2    Miyata, T.3    Ding, Y.L.4    Hiranaga-Kawabata, M.5    Muta, T.6
  • 29
    • 0035920142 scopus 로고    scopus 로고
    • Functional conversion of hemocyanin to phenoloxidase by horseshoe crab antimicrobial peptides
    • Nagai T, Osaki T, Kawabata S. Functional conversion of hemocyanin to phenoloxidase by horseshoe crab antimicrobial peptides. J Biol Chem 2001; 276: 27166-27170.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27166-27170
    • Nagai, T.1    Osaki, T.2    Kawabata, S.3
  • 30
    • 0037424354 scopus 로고    scopus 로고
    • Processing of an antibacterial peptide from hemocyanin of the freshwater crayfish Pacifastacus leniusculus
    • Lee SY, Lee BL, Soderhall K. Processing of an antibacterial peptide from hemocyanin of the freshwater crayfish Pacifastacus leniusculus. J Biol Chem 2003; 278: 7927-7933.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7927-7933
    • Lee, S.Y.1    Lee, B.L.2    Soderhall, K.3
  • 31
    • 0027123107 scopus 로고
    • Molecular and cellular biology of blood coagulation
    • Furie B, Furie BC. Molecular and cellular biology of blood coagulation. N Engl J Med 1992; 326: 800-806.
    • (1992) N. Engl. J. Med. , vol.326 , pp. 800-806
    • Furie, B.1    Furie, B.C.2
  • 32
    • 0019364862 scopus 로고
    • The proteolytic activation systems of complement
    • Reid KB, Porter RR. The proteolytic activation systems of complement. Annu Rev Biochem 1981; 50: 433-464.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 433-464
    • Reid, K.B.1    Porter, R.R.2
  • 33
    • 0038466373 scopus 로고
    • The role of proteases in macrophage physiology
    • Reich E, Rifkin DB, Shaw E Cold Spring Harbr Press: Cold Spring Harbor
    • Cohn Z. The role of proteases in macrophage physiology. In: Reich E, Rifkin DB, Shaw E (eds). Proteases and Biological Control. Cold Spring Harbr Press: Cold Spring Harbor, 1975.
    • (1975) Proteases and Biological Control
    • Cohn, Z.1
  • 34
    • 0002669303 scopus 로고
    • Proteases and matrix degradation
    • Kelly WN, Harris ED, Sledge RS Saunders: Philadelphia
    • Werb Z. Proteases and matrix degradation. In: Kelly WN, Harris ED, Sledge RS (eds). Textbook of Rheumatology. Saunders: Philadelphia, 1993.
    • (1993) Textbook of Rheumatology
    • Werb, Z.1
  • 35
    • 0037184084 scopus 로고    scopus 로고
    • Modular arrangement and secretion of a multidomain serine protease. Evidence for involvement of proline-rich region and N-glycans in the secretion pathway
    • Wang J, Tan NS, Ho B, Ding JL. Modular arrangement and secretion of a multidomain serine protease. Evidence for involvement of proline-rich region and N-glycans in the secretion pathway. J Biol Chem 2002; 277: 36363-36372.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36363-36372
    • Wang, J.1    Tan, N.S.2    Ho, B.3    Ding, J.L.4
  • 36
    • 1442272618 scopus 로고    scopus 로고
    • Transcriptional regulation of limulus Factor C: Repression of an NF B motif modulates its responsiveness to bacterial lipopolysaccharide
    • Wang LH, Ho B, Ding JL. Transcriptional regulation of limulus Factor C: repression of an NF B motif modulates its responsiveness to bacterial lipopolysaccharide. J Biol Chem 2003; 278: 49428-49437.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49428-49437
    • Wang, L.H.1    Ho, B.2    Ding, J.L.3
  • 37
    • 0041707780 scopus 로고    scopus 로고
    • Molecular cloning, structure and bait region splice variants of alpha2-macroglobulin from the soft tick Ornithodoros moubata
    • Saravanan T, Weise C, Sojka D, Kopacek P. Molecular cloning, structure and bait region splice variants of alpha2-macroglobulin from the soft tick Ornithodoros moubata. Insect Biochem Mol Biol 2003; 33: 841-851.
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 841-851
    • Saravanan, T.1    Weise, C.2    Sojka, D.3    Kopacek, P.4
  • 39
    • 0022039432 scopus 로고
    • Proteinase inhibitory activity released from the horseshoe crab blood cell during exocytosis
    • Armstrong PB, Quigley JP. Proteinase inhibitory activity released from the horseshoe crab blood cell during exocytosis. Biochim Biophys Acta 1985; 827: 453-459.
    • (1985) Biochim. Biophys. Acta , vol.827 , pp. 453-459
    • Armstrong, P.B.1    Quigley, J.P.2
  • 40
    • 0023955490 scopus 로고
    • Interaction between lipopolysaccharide and intracellular serine protease zymogen, factor C, from horseshoe crab (Tachypleus tridentatus) hemocytes
    • Nakamura T, Tokunaga F, Morita T, Iwanaga S. Interaction between lipopolysaccharide and intracellular serine protease zymogen, factor C, from horseshoe crab (Tachypleus tridentatus) hemocytes. J Biochem (Tokyo) 1988; 103: 370-374.
    • (1988) J. Biochem. (Tokyo) , vol.103 , pp. 370-374
    • Nakamura, T.1    Tokunaga, F.2    Morita, T.3    Iwanaga, S.4
  • 41
    • 0025899931 scopus 로고
    • A novel trypsin inhibitor from the hemolymph of the horseshoe crab Limulus polyphemus
    • Donovan MA, Lane TM. A novel trypsin inhibitor from the hemolymph of the horseshoe crab Limulus polyphemus. J Biol Chem 1991; 266: 2121-2125.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2121-2125
    • Donovan, M.A.1    Lane, T.M.2
  • 42
    • 0036588702 scopus 로고    scopus 로고
    • The inhibitors of the tissue factor: Factor VII pathway
    • Golino P. The inhibitors of the tissue factor: Factor VII pathway. Thromb Res 2002; 106: V257-V265.
    • (2002) Thromb. Res. , vol.106
    • Golino, P.1
  • 43
    • 0028985590 scopus 로고
    • A limulus intracellular coagulation inhibitor type 2. Purification, characterization, cDNA cloning, and tissue localization
    • Miura Y, Kawabata S, Wakamiya Y, Nakamura T, Iwanaga S. A limulus intracellular coagulation inhibitor type 2. Purification, characterization, cDNA cloning, and tissue localization. J Biol Chem 1995; 270: 558-565.
    • (1995) J. Biol. Chem. , vol.270 , pp. 558-565
    • Miura, Y.1    Kawabata, S.2    Wakamiya, Y.3    Nakamura, T.4    Iwanaga, S.5
  • 46
    • 0036562563 scopus 로고    scopus 로고
    • Platelet-activating factor acetylhydrolase (PAF-AH)
    • Arai H, Koizumi H, Aoki J, Inoue K. Platelet-activating factor acetylhydrolase (PAF-AH). J Biochem (Tokyo) 2002; 131: 635-640.
    • (2002) J. Biochem. (Tokyo) , vol.131 , pp. 635-640
    • Arai, H.1    Koizumi, H.2    Aoki, J.3    Inoue, K.4
  • 47
    • 0034739453 scopus 로고    scopus 로고
    • Platelet-activating factor acetyl-hydrolases in health and disease
    • Tjoelker LW, Stafforini DM. Platelet-activating factor acetyl-hydrolases in health and disease. Biochim Biophys Acta 2000; 1488: 102-123.
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 102-123
    • Tjoelker, L.W.1    Stafforini, D.M.2
  • 48
    • 0030972976 scopus 로고    scopus 로고
    • Native recombinant cyclophilins A, B, and C degrade DNA independently of peptidylprolyl cis-trans-isomerase activity. Potential roles of cyclophilins in apoptosis
    • Montague JW, Hughes Jr FM, Cidlowski JA. Native recombinant cyclophilins A, B, and C degrade DNA independently of peptidylprolyl cis-trans-isomerase activity. Potential roles of cyclophilins in apoptosis. J Biol Chem 1997; 272: 6677-6684.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6677-6684
    • Montague, J.W.1    Hughes Jr., F.M.2    Cidlowski, J.A.3
  • 49
    • 0034045947 scopus 로고    scopus 로고
    • Mechanisms of action of cyclosporine
    • Matsuda S, Koyasu S. Mechanisms of action of cyclosporine. Immunopharmacology 2000; 47: 119-125.
    • (2000) Immunopharmacology , vol.47 , pp. 119-125
    • Matsuda, S.1    Koyasu, S.2
  • 50
    • 0033770487 scopus 로고    scopus 로고
    • Expression of SpC3, the sea urchin complement component, in response to lipopolysaccharide
    • Clow LA, Gross PS, Shih CS, Smith LC. Expression of SpC3, the sea urchin complement component, in response to lipopolysaccharide. Immunogenetics 2000; 51: 1021-1033.
    • (2000) Immunogenetics , vol.51 , pp. 1021-1033
    • Clow, L.A.1    Gross, P.S.2    Shih, C.S.3    Smith, L.C.4
  • 51
    • 0036216769 scopus 로고    scopus 로고
    • Phagocytosis of microbes: Complexity in action
    • Underhill DM, Ozinsky A. Phagocytosis of microbes: Complexity in action. Annu Rev Immunol 2002; 20: 825-852.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 825-852
    • Underhill, D.M.1    Ozinsky, A.2
  • 52
    • 0037374138 scopus 로고    scopus 로고
    • Recognition and clearance of apoptotic cells: A role for complement and pentraxins
    • Nauta AJ, Daha MR, van Kooten C, Roos A. Recognition and clearance of apoptotic cells: A role for complement and pentraxins. Trends Immunol 2003; 24: 148-154.
    • (2003) Trends Immunol. , vol.24 , pp. 148-154
    • Nauta, A.J.1    Daha, M.R.2    van Kooten, C.3    Roos, A.4
  • 53
    • 0034913274 scopus 로고    scopus 로고
    • Drosophila immunity: Two paths to NF-kappaB
    • Khush RS, Leulier F, Lemaitre B. Drosophila immunity: Two paths to NF-kappaB. Trends Immunol 2001; 22: 260-264.
    • (2001) Trends Immunol. , vol.22 , pp. 260-264
    • Khush, R.S.1    Leulier, F.2    Lemaitre, B.3
  • 54
    • 0037178731 scopus 로고    scopus 로고
    • A conserved p38 MAP kinase pathway in Caenorhabditis elegans innate immunity
    • Kim DH, Feinbaum R, Alloing G, Emerson FE, Garsin DA, Inoue H et al. A conserved p38 MAP kinase pathway in Caenorhabditis elegans innate immunity. Science 2002; 297: 623-626.
    • (2002) Science , vol.297 , pp. 623-626
    • Kim, D.H.1    Feinbaum, R.2    Alloing, G.3    Emerson, F.E.4    Garsin, D.A.5    Inoue, H.6
  • 55
    • 0030236418 scopus 로고    scopus 로고
    • Signal transduction during exocytosis in Limulus polyphemus granulocytes
    • Solon E, Gupta AP, Gaugler R. Signal transduction during exocytosis in Limulus polyphemus granulocytes. Dev Comp Immunol 1996; 20: 307-321.
    • (1996) Dev. Comp. Immunol. , vol.20 , pp. 307-321
    • Solon, E.1    Gupta, A.P.2    Gaugler, R.3
  • 57
    • 0043092063 scopus 로고    scopus 로고
    • Surface coat remodeling during differentiation of Trypanosoma brucei
    • Gruszynski AE, DeMaster A, Hooper NM, Bangs JD. Surface coat remodeling during differentiation of Trypanosoma brucei. J Biol Chem 2003; 278: 24665-24672.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24665-24672
    • Gruszynski, A.E.1    DeMaster, A.2    Hooper, N.M.3    Bangs, J.D.4
  • 58
    • 0028342952 scopus 로고
    • Signal transmission between the plasma membrane and nucleus of T lymphocytes
    • Crabtree GR, Clipstone NA. Signal transmission between the plasma membrane and nucleus of T lymphocytes. Annu Rev Biochem 1994; 63: 1045-1083.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 1045-1083
    • Crabtree, G.R.1    Clipstone, N.A.2
  • 59
    • 0030918084 scopus 로고    scopus 로고
    • Horseshoe crab coagulogen is an invertebrate protein with a nerve growth factor-like domain
    • Bergner A, Muta T, Iwanaga S, Beisel HG, Delotto R, Bode W. Horseshoe crab coagulogen is an invertebrate protein with a nerve growth factor-like domain. Biol Chem 1997; 378: 283-287.
    • (1997) Biol. Chem. , vol.378 , pp. 283-287
    • Bergner, A.1    Muta, T.2    Iwanaga, S.3    Beisel, H.G.4    Delotto, R.5    Bode, W.6
  • 61
    • 0035179629 scopus 로고    scopus 로고
    • Molecular mechanisms of bacteria induced apoptosis
    • Grassme H, Jendrossek V, Gulbins E. Molecular mechanisms of bacteria induced apoptosis. Apoptosis 2001; 6: 441-445.
    • (2001) Apoptosis , vol.6 , pp. 441-445
    • Grassme, H.1    Jendrossek, V.2    Gulbins, E.3
  • 62
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • Newmeyer DD, Ferguson-Miller S. Mitochondria: Releasing power for life and unleashing the machineries of death. Cell 2003; 112: 481-490.
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 63
    • 0142049202 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization and superoxide production during apoptosis. A single-cell analysis
    • Dussmann H, Kogel D, Rehm M, Prehn JH. Mitochondrial membrane permeabilization and superoxide production during apoptosis. A single-cell analysis. J Biol Chem 2003; 278: 12645-12649.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12645-12649
    • Dussmann, H.1    Kogel, D.2    Rehm, M.3    Prehn, J.H.4
  • 64
    • 0028853547 scopus 로고
    • Electron transfer and proton pumping in cytochrome oxidase
    • Brunori M, Wilson MT. Electron transfer and proton pumping in cytochrome oxidase. Biochimie 1995; 77: 668-676.
    • (1995) Biochimie , vol.77 , pp. 668-676
    • Brunori, M.1    Wilson, M.T.2
  • 65
    • 0034026576 scopus 로고    scopus 로고
    • The complete mitochondrial DNA sequence of the horseshoe crab Limulus polyphemus
    • Lavrov DV, Boore JL, Brown WM. The complete mitochondrial DNA sequence of the horseshoe crab Limulus polyphemus. Mol Biol Evol 2000; 17: 813-824.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 813-824
    • Lavrov, D.V.1    Boore, J.L.2    Brown, W.M.3
  • 67
    • 17544404224 scopus 로고    scopus 로고
    • Reactive oxygen and reactive nitrogen intermediates in innate and specific immunity
    • Bogdan C, Rollinghoff M, Diefenbach A. Reactive oxygen and reactive nitrogen intermediates in innate and specific immunity. Curr Opin Immunol 2000; 12: 64-76.
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 64-76
    • Bogdan, C.1    Rollinghoff, M.2    Diefenbach, A.3
  • 68
    • 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 JC, Cadenas E. The metabolism of tyramine by monoamine oxidase A/B causes oxidative damage to mitochondrial DNA. Arch Biochem Biophys 1996; 335: 295-304.
    • (1996) Arch. Biochem. Biophys. , vol.335 , pp. 295-304
    • Hauptmann, N.1    Grimsby, J.2    Shih, J.C.3    Cadenas, E.4
  • 70
    • 0032932201 scopus 로고    scopus 로고
    • SAG, a novel zinc RING finger protein that protects cells from apoptosis induced by redox agents
    • Duan H, Wang Y, Aviram M, Swaroop M, Loo JA, Bian J et al. SAG, a novel zinc RING finger protein that protects cells from apoptosis induced by redox agents. Mol Cell Biol 1999; 19: 3145-3155.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 3145-3155
    • Duan, H.1    Wang, Y.2    Aviram, M.3    Swaroop, M.4    Loo, J.A.5    Bian, J.6
  • 71
    • 0029582852 scopus 로고
    • Superoxide anion generation in Drosophila during melanotic encapsulation of parasites
    • Nappi AJ, Vass E, Frey F, Carton Y. Superoxide anion generation in Drosophila during melanotic encapsulation of parasites. Eur J Cell Biol 1995; 68: 450-456.
    • (1995) Eur. J. Cell Biol. , vol.68 , pp. 450-456
    • Nappi, A.J.1    Vass, E.2    Frey, F.3    Carton, Y.4
  • 72
    • 0028263070 scopus 로고
    • Structure and function of glutathione S-transferases
    • Wilce MC, Parker MW. Structure and function of glutathione S-transferases. Biochim Biophys Acta 1994; 1205: 1-18.
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 1-18
    • Wilce, M.C.1    Parker, M.W.2
  • 73
    • 0038647490 scopus 로고    scopus 로고
    • Selenium and selenoproteins in the brain and brain diseases
    • Chen J, Berry MJ. Selenium and selenoproteins in the brain and brain diseases. J Neurochem 2003; 86: 1-12.
    • (2003) J. Neurochem. , vol.86 , pp. 1-12
    • Chen, J.1    Berry, M.J.2
  • 75
    • 0035189577 scopus 로고    scopus 로고
    • Regulatory roles of thioredoxin in oxidative stress-induced cellular responses
    • Nishinaka Y, Masutani H, Nakamura H, Yodoi J. Regulatory roles of thioredoxin in oxidative stress-induced cellular responses. Redox Rep 2001; 6: 289-295.
    • (2001) Redox. Rep. , vol.6 , pp. 289-295
    • Nishinaka, Y.1    Masutani, H.2    Nakamura, H.3    Yodoi, J.4
  • 76
    • 0034571008 scopus 로고    scopus 로고
    • Molecular chaperones and the aging process
    • Soti C, Csermely P. Molecular chaperones and the aging process. Biogerontology 2000; 1: 225-233.
    • (2000) Biogerontology , vol.1 , pp. 225-233
    • Soti, C.1    Csermely, P.2
  • 78
    • 0031826869 scopus 로고    scopus 로고
    • Searching DNA databases for similarities to DNA sequences: When is a match significant?
    • Anderson I, Brass A. Searching DNA databases for similarities to DNA sequences: When is a match significant? Bioinformatics 1998; 14: 349-356.
    • (1998) Bioinformatics , vol.14 , pp. 349-356
    • Anderson, I.1    Brass, A.2


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