메뉴 건너뛰기




Volumn 271, Issue 10, 2004, Pages 1924-1937

A (1→3)-β-D-glucan recognition protein from the sponge Suberites domuncula: Mediated activation of fibrinogen-like protein and epidermal growth factor gene expression

Author keywords

D glucan binding protein; Epidermal growth factor; Fungi; Sponges; Symbiosis

Indexed keywords

BETA 1,3 GLUCAN; CARBOHYDRATE; CELL PROTEIN; CELL SURFACE RECEPTOR; CURDLAN; EPIDERMAL GROWTH FACTOR; FIBRINOGEN; LAMINARAN; PROTEIN ANTIBODY; PROTEIN TYROSINE KINASE; BETA GLUCAN; BETA-1,3-GLUCAN; CARRIER PROTEIN; EPIDERMAL GROWTH FACTOR PRECURSOR; GLUCAN; GLUCAN BINDING PROTEINS; GLUCAN-BINDING PROTEINS; LECTIN; PROTEIN PRECURSOR; RECOMBINANT PROTEIN;

EID: 2442685244     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04102.x     Document Type: Article
Times cited : (72)

References (79)
  • 3
    • 0036314931 scopus 로고    scopus 로고
    • Drugs from the seas - Current status and microbiological implications
    • Proksch, P., Edrada, R.A. & Ebel, R. (2002) Drugs from the seas - current status and microbiological implications. Appl. Microbiol. Biotechnol. 59, 125-134.
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 125-134
    • Proksch, P.1    Edrada, R.A.2    Ebel, R.3
  • 5
    • 17644439084 scopus 로고    scopus 로고
    • Origin of the metazoan immune system: Identification of the molecules and their functions in sponges
    • Müller, W.E.G. & Müller, I.M. (2003) Origin of the metazoan immune system: identification of the molecules and their functions in sponges. Integr. Comp. Biol. 43, 281-292.
    • (2003) Integr. Comp. Biol. , vol.43 , pp. 281-292
    • Müller, W.E.G.1    Müller, I.M.2
  • 6
    • 0042357386 scopus 로고    scopus 로고
    • Emergence and disappearance of an immune molecule, an antimicrobial lectin, in basal Metazoa: The tachylectin family
    • Schröder, H.C., Ushijima, H., Krasko, A., Gamulin, V., Schütze, J., Müller, I.M. & Müller, W.E.G. (2003) Emergence and disappearance of an immune molecule, an antimicrobial lectin, in basal Metazoa: the tachylectin family. J. Biol. Chem. 278, 32810-32817.
    • (2003) J. Biol. Chem. , vol.278 , pp. 32810-32817
    • Schröder, H.C.1    Ushijima, H.2    Krasko, A.3    Gamulin, V.4    Schütze, J.5    Müller, I.M.6    Müller, W.E.G.7
  • 8
    • 72949147617 scopus 로고
    • Identification of a reticulo-endothelial simulating agent in zymosan
    • Riggi, S.J. & Luzio, N.R. (1961) Identification of a reticulo-endothelial simulating agent in zymosan. Am. J. Physiol. 200, 297-305.
    • (1961) Am. J. Physiol. , vol.200 , pp. 297-305
    • Riggi, S.J.1    Luzio, N.R.2
  • 9
    • 0025196351 scopus 로고
    • Curdlan, (1→3)-β-D-glucan from Alcaligenes faecalis var. myxogenes IFO13140, activates the alternative complement pathway by heat treatment
    • Matsushita, M. (1990) Curdlan, (1→3)-β-D-glucan from Alcaligenes faecalis var. myxogenes IFO13140, activates the alternative complement pathway by heat treatment. Immunol. Lett. 26, 95-97.
    • (1990) Immunol. Lett. , vol.26 , pp. 95-97
    • Matsushita, M.1
  • 10
    • 0031224949 scopus 로고    scopus 로고
    • Down-regulation of tumor necrosis factor-α, moderate reduction of interferon-1β, but not interleukin-6 or interleukin-10, by glucan immunmodulators curdlan sulfate and lentinan
    • Masihi, K.N., Madaj, K., Hintelmann, H., Gast, G. & Kaneko, Y. (1997) Down-regulation of tumor necrosis factor-α, moderate reduction of interferon-1β, but not interleukin-6 or interleukin-10, by glucan immunmodulators curdlan sulfate and lentinan. Int. J. Immunopharmacol. 19, 463-468.
    • (1997) Int. J. Immunopharmacol. , vol.19 , pp. 463-468
    • Masihi, K.N.1    Madaj, K.2    Hintelmann, H.3    Gast, G.4    Kaneko, Y.5
  • 11
    • 0001027436 scopus 로고
    • Manufacture of algal chemicals. III. Laboratory-scale isolation of laminarin from brown marine algae
    • Black, W.A.P., Cornhill, W.J., Dewar, E.T. & Woodward, F.N. (1951) Manufacture of algal chemicals. III. Laboratory-scale isolation of laminarin from brown marine algae. J. Appl. Chem. 1, 505-517.
    • (1951) J. Appl. Chem. , vol.1 , pp. 505-517
    • Black, W.A.P.1    Cornhill, W.J.2    Dewar, E.T.3    Woodward, F.N.4
  • 12
    • 0032544658 scopus 로고    scopus 로고
    • Identification and cloning of a glucan- and lipopolysaccharide-binding protein from Eisenia foetida earthworm involved in the activation of prophenoloxidase cascade
    • Beschin, A., Bilej, M., Hanssens, F., Raymakers, J., Van Dyck, E., Revets, H., Brys, L., Gomez, J., De Baetselier, P. & Timmermans, M. (1998) Identification and cloning of a glucan- and lipopolysaccharide-binding protein from Eisenia foetida earthworm involved in the activation of prophenoloxidase cascade. J. Biol. Chem. 273, 24948-24954.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24948-24954
    • Beschin, A.1    Bilej, M.2    Hanssens, F.3    Raymakers, J.4    Van Dyck, E.5    Revets, H.6    Brys, L.7    Gomez, J.8    De Baetselier, P.9    Timmermans, M.10
  • 13
    • 0343415656 scopus 로고    scopus 로고
    • A lipopolysaccharide-and beta-1,3-glucan-binding protein from hemocytes of the freshwater crayfish Pacifastacus leniusculus. Purification, characterization, and cDNA cloning
    • Lee, S.Y., Wang, R. & Söderhall, K. (2000) A lipopolysaccharide-and beta-1,3-glucan-binding protein from hemocytes of the freshwater crayfish Pacifastacus leniusculus. Purification, characterization, and cDNA cloning. J. Biol. Chem. 275, 1337-1343.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1337-1343
    • Lee, S.Y.1    Wang, R.2    Söderhall, K.3
  • 14
    • 0036802550 scopus 로고    scopus 로고
    • The effect of soluble β-1,3-glucan and lipopolysaccharide on cytokine production and coagulation activation in whole blood
    • Engstad, C.S., Engstad, R.E., Olsen, J.O. & Østerud, B. (2002) The effect of soluble β-1,3-glucan and lipopolysaccharide on cytokine production and coagulation activation in whole blood. Int. Immunopharmacol. 2, 1585-1597.
    • (2002) Int. Immunopharmacol. , vol.2 , pp. 1585-1597
    • Engstad, C.S.1    Engstad, R.E.2    Olsen, J.O.3    Østerud, B.4
  • 16
    • 0030770048 scopus 로고    scopus 로고
    • Wound activation of prototoxins in the marine sponge Aplysina aerophoba
    • Ebel, R., Brenzinger, M., Kunze, A., Gross, H. & Proksch, P. (1997) Wound activation of prototoxins in the marine sponge Aplysina aerophoba. J. Chem. Ecol. 23, 1451-1462.
    • (1997) J. Chem. Ecol. , vol.23 , pp. 1451-1462
    • Ebel, R.1    Brenzinger, M.2    Kunze, A.3    Gross, H.4    Proksch, P.5
  • 17
    • 0036634213 scopus 로고    scopus 로고
    • The lipopolysaccharide and beta-1,3-glucan binding protein gene is upregulated in white spot virus-infected shrimp (Penaeus stylirostris)
    • Roux, M.M., Pain, A., Klimpel, K.R. & Dhar, A.K. (2002) The lipopolysaccharide and beta-1,3-glucan binding protein gene is upregulated in white spot virus-infected shrimp (Penaeus stylirostris). J. Virol. 76, 7140-7149.
    • (2002) J. Virol. , vol.76 , pp. 7140-7149
    • Roux, M.M.1    Pain, A.2    Klimpel, K.R.3    Dhar, A.K.4
  • 18
    • 0030867913 scopus 로고    scopus 로고
    • Molecular immune responses of the mosquito Anopheles gambiae to bacteria and malaria parasites
    • Dimopoulos, G., Richman, A., Muller, H.M. & Kafatos, F.C. (1997) Molecular immune responses of the mosquito Anopheles gambiae to bacteria and malaria parasites. Proc. Natl Acad. Sci. USA 94, 11508-11513.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11508-11513
    • Dimopoulos, G.1    Richman, A.2    Muller, H.M.3    Kafatos, F.C.4
  • 19
    • 0029900086 scopus 로고    scopus 로고
    • Molecular cloning of the first metazoan beta-1,3 glucanase from eggs of the sea urchin Strongylocentrotus purpuratus
    • Bachman, E.S. & McClay, D.R. (1996) Molecular cloning of the first metazoan beta-1,3 glucanase from eggs of the sea urchin Strongylocentrotus purpuratus. Proc. Natl Acad. Sci. USA 93, 6808-6813.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6808-6813
    • Bachman, E.S.1    McClay, D.R.2
  • 21
    • 0035827589 scopus 로고    scopus 로고
    • Cloning and characterization of novel ficolins from the solitary ascidian, Halocynthia roretzi
    • Kenjo, A., Takahashi, M., Matsushita, M., Endo, Y., Nakata, M., Mizuochi, T. & Fujita, T. (2001) Cloning and characterization of novel ficolins from the solitary ascidian, Halocynthia roretzi. J. Biol. Chem. 276, 19959-19965.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19959-19965
    • Kenjo, A.1    Takahashi, M.2    Matsushita, M.3    Endo, Y.4    Nakata, M.5    Mizuochi, T.6    Fujita, T.7
  • 22
    • 0037184115 scopus 로고    scopus 로고
    • Activation of macrophages by linear (1→3)-β-D-glucans
    • Kataoka, K., Muta, T., Yamazaki, S. & Takeshige, K. (2002) Activation of macrophages by linear (1→3)-β-D-glucans. J. Biol. Chem. 277, 36825-36831.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36825-36831
    • Kataoka, K.1    Muta, T.2    Yamazaki, S.3    Takeshige, K.4
  • 24
    • 1842378643 scopus 로고    scopus 로고
    • Early evolution of metazoan serine/threonine- and tyrosine kinases: Identification of selected kinases in marine sponges
    • Kruse, M., Müller, I.M. & Müller, W.E.G. (1997) Early evolution of metazoan serine/threonine- and tyrosine kinases: identification of selected kinases in marine sponges. Mol. Biol. Evol. 14, 1326-1334.
    • (1997) Mol. Biol. Evol. , vol.14 , pp. 1326-1334
    • Kruse, M.1    Müller, I.M.2    Müller, W.E.G.3
  • 25
    • 0033853972 scopus 로고    scopus 로고
    • Expression of silicatein and collagen genes in the marine sponge Suberites domuncula is controlled by silicate and myotrophin
    • Krasko, A., Batel, R., Schröder, H.C., Müller, I.M. & Müller, W.E.G. (2000) Expression of silicatein and collagen genes in the marine sponge Suberites domuncula is controlled by silicate and myotrophin. Eur. J. Biochem. 267, 4878-4887.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4878-4887
    • Krasko, A.1    Batel, R.2    Schröder, H.C.3    Müller, I.M.4    Müller, W.E.G.5
  • 26
    • 0029798874 scopus 로고    scopus 로고
    • Preparation of water-soluble and water-insoluble poly(acrylamide- allylamine) derivatives of polysaccharides
    • Novotna, V., Mikes, L., Horak, P., Jonakova, V. & Ticha, M. (1996) Preparation of water-soluble and water-insoluble poly(acrylamide-allylamine) derivatives of polysaccharides. Int. J. Bio-Chromatogr. 2, 37-47.
    • (1996) Int. J. Bio-Chromatogr. , vol.2 , pp. 37-47
    • Novotna, V.1    Mikes, L.2    Horak, P.3    Jonakova, V.4    Ticha, M.5
  • 27
    • 0000123928 scopus 로고    scopus 로고
    • Effect of different β-D-glucans on the respiratory burst of turbot (Psetta maxima) and gilthead seabream (Sparus aurata) phagocytosis
    • Castro, R., Couso, N., Obach, A. & Lamas, J. (1999) Effect of different β-D-glucans on the respiratory burst of turbot (Psetta maxima) and gilthead seabream (Sparus aurata) phagocytosis. Fish Shellfish Immunol. 9, 529-541.
    • (1999) Fish Shellfish Immunol. , vol.9 , pp. 529-541
    • Castro, R.1    Couso, N.2    Obach, A.3    Lamas, J.4
  • 28
    • 0034177252 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase p38 pathway is conserved in metazoans: Cloning and activation of p38 of the SAPK2 subfamily from the sponge Suberites domuncula
    • Böhm, M., Müller, I.M., Müller, W.E.G. & Gamulin, V. (2000) The mitogen-activated protein kinase p38 pathway is conserved in metazoans: cloning and activation of p38 of the SAPK2 subfamily from the sponge Suberites domuncula. Biol. Cell 29, 95-104.
    • (2000) Biol. Cell , vol.29 , pp. 95-104
    • Böhm, M.1    Müller, I.M.2    Müller, W.E.G.3    Gamulin, V.4
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0032493118 scopus 로고    scopus 로고
    • Expression of the chaperones 14-3-3 and HSP70 induced by PCB 118 (2,3′,4,47prime;,5-pentachlorobiphenyl) in the marine sponge Geodia cydonium
    • Wiens, M., Koziol, C., Hassanein, H.M.A., Batel, R. & Müller, W.E.G. (1998) Expression of the chaperones 14-3-3 and HSP70 induced by PCB 118 (2,3′,4,47prime;,5-pentachlorobiphenyl) in the marine sponge Geodia cydonium. Mar. Ecol. Prog. Series 165, 247-257.
    • (1998) Mar. Ecol. Prog. Series , vol.165 , pp. 247-257
    • Wiens, M.1    Koziol, C.2    Hassanein, H.M.A.3    Batel, R.4    Müller, W.E.G.5
  • 33
    • 2442688416 scopus 로고    scopus 로고
    • BLAST (2003) http://www.ncbi.nlm.nih.gov/blast/blast.cgi
    • (2003)
  • 34
    • 2442674579 scopus 로고    scopus 로고
    • FASTA (2003) http://www.ncbi.nlm.nih.gov/BLAST/fasta.html
    • (2003)
  • 35
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. & Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 37
    • 0000228203 scopus 로고
    • A model of evolutionary change in protein
    • Dayhoff, M.O., ed., National Biomedical Research Foundation, Washington, DC
    • Dayhoff, M.O., Schwartz, R.M. & Orcutt, B.C. (1978) A model of evolutionary change in protein. In Atlas of Protein Sequence and Structure (Dayhoff, M.O., ed.), pp. 345-352. National Biomedical Research Foundation, Washington, DC.
    • (1978) Atlas of Protein Sequence and Structure , pp. 345-352
    • Dayhoff, M.O.1    Schwartz, R.M.2    Orcutt, B.C.3
  • 39
    • 0034799201 scopus 로고    scopus 로고
    • Cloning and expression of the putative aggregation factor from the marine sponge Geodia cydonium
    • Schütze, J., Krasko, A., Diehl-Seifert, B. & Müller, W.E.G. (2001) Cloning and expression of the putative aggregation factor from the marine sponge Geodia cydonium. J. Cell Sci. 114, 3189-3198.
    • (2001) J. Cell Sci. , vol.114 , pp. 3189-3198
    • Schütze, J.1    Krasko, A.2    Diehl-Seifert, B.3    Müller, W.E.G.4
  • 40
    • 0036005876 scopus 로고    scopus 로고
    • Induction of (2′-5′) oligoadenylate synthetase in the marine sponges Suberites domuncula and Geodia cydonium by the bacterial endotoxin lipopolysaccharide
    • Grebenjuk, V.A., Kuusksalu, A., Kelve, M., Schütze, J., Schröder, H.C. & Müller, W.E.G. (2002) Induction of (2′-5′) oligoadenylate synthetase in the marine sponges Suberites domuncula and Geodia cydonium by the bacterial endotoxin lipopolysaccharide. Eur. J. Biochem. 269, 1382-1392.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1382-1392
    • Grebenjuk, V.A.1    Kuusksalu, A.2    Kelve, M.3    Schütze, J.4    Schröder, H.C.5    Müller, W.E.G.6
  • 43
    • 0023059178 scopus 로고
    • A conformational preference parameter to predict helices in integral membrane proteins
    • Rao, J. & Argos, P. (1986) A conformational preference parameter to predict helices in integral membrane proteins. Biochem. Biophys. Acta 869, 197-214.
    • (1986) Biochem. Biophys. Acta , vol.869 , pp. 197-214
    • Rao, J.1    Argos, P.2
  • 44
    • 0003764925 scopus 로고
    • Intelligenetics, Inc., Mountain View, CA
    • PC/GENE (1995) Data Banks CD-ROM; Release 14.0. Intelligenetics, Inc., Mountain View, CA.
    • (1995) Data Banks CD-ROM; Release 14.0
  • 45
    • 0021118122 scopus 로고
    • Fibrinogen and fibrin
    • Doolittle, R.F. (1984) Fibrinogen and fibrin. Annu. Rev. Biochem. 53, 195-229.
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 195-229
    • Doolittle, R.F.1
  • 48
    • 0032534784 scopus 로고    scopus 로고
    • Oligomeric structure and tissue distribution of ficolins from mouse, pig and human
    • Ohashi, T. & Erickson, H.P. (1998) Oligomeric structure and tissue distribution of ficolins from mouse, pig and human. Arch. Biochem. Biophys. 360, 223-232.
    • (1998) Arch. Biochem. Biophys. , vol.360 , pp. 223-232
    • Ohashi, T.1    Erickson, H.P.2
  • 49
    • 2442644500 scopus 로고    scopus 로고
    • Isrec-Server (2003) http://hits.isb-sib.ch/cgi-bin/hits_motifscan
    • (2003)
  • 51
    • 0023821842 scopus 로고
    • Structure-function studies of murine epidermal growth factor, expression and site-directed mutagenesis of epidermal growth factor gene
    • Ray, P., Mey, F.J., Montelione, G.T., Liu, J.F., Narang, S.A., Scheraga, H.A. & Wu, R. (1988) Structure-function studies of murine epidermal growth factor, expression and site-directed mutagenesis of epidermal growth factor gene. Biochemistry 27, 7289-7295.
    • (1988) Biochemistry , vol.27 , pp. 7289-7295
    • Ray, P.1    Mey, F.J.2    Montelione, G.T.3    Liu, J.F.4    Narang, S.A.5    Scheraga, H.A.6    Wu, R.7
  • 52
    • 0025184139 scopus 로고
    • Human epidermal growth factor. Distinct role of tyrosine 37 and arginine 41 in receptor binding as determined by site-directed mutagenesis and nuclear magnetic resonance spectroscopy
    • Engler, D.A., Montelione, G.T. & Niyogi, S.K. (1990) Human epidermal growth factor. Distinct role of tyrosine 37 and arginine 41 in receptor binding as determined by site-directed mutagenesis and nuclear magnetic resonance spectroscopy. FEBS Lett. 271, 47-50.
    • (1990) FEBS Lett. , vol.271 , pp. 47-50
    • Engler, D.A.1    Montelione, G.T.2    Niyogi, S.K.3
  • 53
    • 0013021692 scopus 로고    scopus 로고
    • Marine natural products chemistry as an evolutionary narrative
    • McClintock, J.B. & Baker, B.J., eds, CRC Press, Boca Raton
    • Cimino, G. & Ghiselin, M.T. (2001) Marine natural products chemistry as an evolutionary narrative. In Marine Chemical Ecology (McClintock, J.B. & Baker, B.J., eds), pp. 115-154. CRC Press, Boca Raton.
    • (2001) Marine Chemical Ecology , pp. 115-154
    • Cimino, G.1    Ghiselin, M.T.2
  • 55
    • 20244389517 scopus 로고    scopus 로고
    • Antibacterial activity of the sponge Suberites domuncula and its primmorphs: Potential basis for epibacterial chemical defense
    • Thakur, N.L., Hentschel, U., Krasko, A., Pabel, C.T., Anil, A.C. & Müller, W.E.G. (2003) Antibacterial activity of the sponge Suberites domuncula and its primmorphs: potential basis for epibacterial chemical defense. Aquat. Microbiol. Ecol. 31, 77-83.
    • (2003) Aquat. Microbiol. Ecol. , vol.31 , pp. 77-83
    • Thakur, N.L.1    Hentschel, U.2    Krasko, A.3    Pabel, C.T.4    Anil, A.C.5    Müller, W.E.G.6
  • 58
    • 2442677071 scopus 로고    scopus 로고
    • A β1,3-glucan recognition protein from an insect, Manduca sexta, agglutinates microorganisms and activates the phenoloxidase cascade
    • Ma, C. & Kanost, M.R. (2000) A β1,3-glucan recognition protein from an insect, Manduca sexta, agglutinates microorganisms and activates the phenoloxidase cascade. J. Biol. Chem. 277, 36825-36831.
    • (2000) J. Biol. Chem. , vol.277 , pp. 36825-36831
    • Ma, C.1    Kanost, M.R.2
  • 59
    • 0036137985 scopus 로고    scopus 로고
    • The beta-1,3-glucan binding protein from the black tiger shrimp, Penaeus monodon
    • Sritunyalucksana, K., Lee, S.Y. & Söderhäll, K. (2002) The beta-1,3-glucan binding protein from the black tiger shrimp, Penaeus monodon. Dev. Comp. Immunol. 26, 237-245.
    • (2002) Dev. Comp. Immunol. , vol.26 , pp. 237-245
    • Sritunyalucksana, K.1    Lee, S.Y.2    Söderhäll, K.3
  • 60
    • 0028077775 scopus 로고
    • A β-D-glucan binding protein in crustacean blood. Structure and biological activity of a fungal recognition cascade
    • Cerenius, L., Liang, Z., Duvic, B., Keyser, P., Hellman, U., Palva, E.T., Iwanaga, S. & Söderhäll, K. (1994) A β-D-glucan binding protein in crustacean blood. Structure and biological activity of a fungal recognition cascade. J. Biol. Chem. 269, 29462-29467.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29462-29467
    • Cerenius, L.1    Liang, Z.2    Duvic, B.3    Keyser, P.4    Hellman, U.5    Palva, E.T.6    Iwanaga, S.7    Söderhäll, K.8
  • 62
    • 0042704060 scopus 로고    scopus 로고
    • Innate immunity in the horseshoe crab
    • Ezekowitz, R.A.B. & Hoffmann, J.A., eds, Humana Press, Totowa
    • Kawabata, S.I., Osaki, T. & Iwanaga, S. (2003) Innate immunity in the horseshoe crab. In Innate Immunity (Ezekowitz, R.A.B. & Hoffmann, J.A., eds), pp. 109-125. Humana Press, Totowa.
    • (2003) Innate Immunity , pp. 109-125
    • Kawabata, S.I.1    Osaki, T.2    Iwanaga, S.3
  • 63
    • 0035090591 scopus 로고    scopus 로고
    • Isolation and cloning of the C-type lectin from the hexactinellidian sponge Aphrocallistes vastus: A putative aggregation factor
    • Gundacker, D., Leys, S.P., Schröder, H.C., Müller, I.M. & Müller. W.E.G. (2001) Isolation and cloning of the C-type lectin from the hexactinellidian sponge Aphrocallistes vastus: a putative aggregation factor. Glycobiology 11, 21-29.
    • (2001) Glycobiology , vol.11 , pp. 21-29
    • Gundacker, D.1    Leys, S.P.2    Schröder, H.C.3    Müller, I.M.4    Müller, W.E.G.5
  • 65
    • 0025230414 scopus 로고
    • Presence of a vertebrate fibrinogen-like sequence in an echinoderm
    • Xu, X. & Doolittle, R.F. (1990) Presence of a vertebrate fibrinogen-like sequence in an echinoderm. Proc. Natl Acad. Sci. USA 87, 2097-2101.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 2097-2101
    • Xu, X.1    Doolittle, R.F.2
  • 66
    • 18344409247 scopus 로고    scopus 로고
    • Human L-ficolin: Plasma levels, sugar specificity and assignment of its lectin activity to the fbrinogen-like (FBG) domain
    • Le, Y., Lee, S.H., Kon, O.L. & Lu, J. (1998) Human L-ficolin: plasma levels, sugar specificity and assignment of its lectin activity to the fbrinogen-like (FBG) domain. FEBS Lett. 425, 367-370.
    • (1998) FEBS Lett. , vol.425 , pp. 367-370
    • Le, Y.1    Lee, S.H.2    Kon, O.L.3    Lu, J.4
  • 68
    • 0026507982 scopus 로고
    • cDNA sequence of a second fibrinogen α chain in lamprey: An archetypal version alignable with full length β and γ chains
    • Pan, Y. & Doolittle, R.F. (1992) cDNA sequence of a second fibrinogen α chain in lamprey: an archetypal version alignable with full length β and γ chains. Proc. Natl Acad. Sci. USA 89, 2066-2070.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 2066-2070
    • Pan, Y.1    Doolittle, R.F.2
  • 71
    • 0027278514 scopus 로고
    • Molecular cloning and characterization of ficolin, a multimeric protein with fibrinogen- and collagen-like domains
    • Ichijo, H., Hellman, U., Wernstedt, C., Gonez, L.J., Claesson-Welsh, L., Heldin, C.H. & Miyazono, K. (1993) Molecular cloning and characterization of ficolin, a multimeric protein with fibrinogen- and collagen-like domains. J. Biol. Chem. 268, 14505-14513.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14505-14513
    • Ichijo, H.1    Hellman, U.2    Wernstedt, C.3    Gonez, L.J.4    Claesson-Welsh, L.5    Heldin, C.H.6    Miyazono, K.7
  • 73
    • 0034489895 scopus 로고    scopus 로고
    • Sponge proteins are more similar to those of Homo sapiens than to Caenorhabditis elegans
    • Gamulin, V., Müller, I.M. & Müller, W.E.G. (2000) Sponge proteins are more similar to those of Homo sapiens than to Caenorhabditis elegans. Biol. J. Linnean Soc. 71, 821-828.
    • (2000) Biol. J. Linnean Soc. , vol.71 , pp. 821-828
    • Gamulin, V.1    Müller, I.M.2    Müller, W.E.G.3
  • 74
    • 0043205198 scopus 로고    scopus 로고
    • Evolution of the innate and adaptive immune systems: Relationships between potential immune molecules in the lowest metazoan phylum (Porifera) and those in vertebrates
    • Müller, W.E.G., Blumbach, B. & Müller, I.M. (1999) Evolution of the innate and adaptive immune systems: relationships between potential immune molecules in the lowest metazoan phylum (Porifera) and those in vertebrates. Transplantation 68, 1215-1227.
    • (1999) Transplantation , vol.68 , pp. 1215-1227
    • Müller, W.E.G.1    Blumbach, B.2    Müller, I.M.3
  • 75
    • 0032005367 scopus 로고    scopus 로고
    • Role of the prophenoloxidase activating system in invertebrate immunity
    • Söderhäll, K. & Cerenius, L. (1998) Role of the prophenoloxidase activating system in invertebrate immunity. Curr. Opin. Immunol. 10, 23-28.
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 23-28
    • Söderhäll, K.1    Cerenius, L.2
  • 76
    • 0030000090 scopus 로고    scopus 로고
    • Solution structure of a pair of calcium-binding epidermal growth factor-like domain: Implication for the Marfan syndrome and other genetic disorders
    • Downing, A.K., Knott, V., Werner, J.M., Cardy, C.M., Campbell, I.D. & Handford, P.A. (1996) Solution structure of a pair of calcium-binding epidermal growth factor-like domain: implication for the Marfan syndrome and other genetic disorders. Cell 85, 597-605.
    • (1996) Cell , vol.85 , pp. 597-605
    • Downing, A.K.1    Knott, V.2    Werner, J.M.3    Cardy, C.M.4    Campbell, I.D.5    Handford, P.A.6
  • 77
    • 0015523701 scopus 로고
    • Epidermal growth factor: Physical and chemical properties
    • Taylor, J.M., Mitchell, W.M. & Cohen, S. (1972) Epidermal growth factor: physical and chemical properties. J. Biol. Chem. 247, 5928-5934.
    • (1972) J. Biol. Chem. , vol.247 , pp. 5928-5934
    • Taylor, J.M.1    Mitchell, W.M.2    Cohen, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.