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Volumn 32, Issue 10, 2008, Pages 1177-1191

Novel rhamnose-binding lectins from the colonial ascidian Botryllus schlosseri

Author keywords

Ascidians; Botryllus schlosseri; Rhamnose binding lectins; Sequence analysis

Indexed keywords

CYSTEINE; LECTIN; PROTEINASE; RHAMNOSE BINDING LECTIN; SIGNAL PEPTIDE;

EID: 46549085553     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2008.03.006     Document Type: Article
Times cited : (42)

References (73)
  • 1
    • 0031029256 scopus 로고    scopus 로고
    • Animal lectins
    • Gabius H.J. Animal lectins. Eur J Biochem 243 (1997) 543-576
    • (1997) Eur J Biochem , vol.243 , pp. 543-576
    • Gabius, H.J.1
  • 2
    • 0037136419 scopus 로고    scopus 로고
    • Animal lectins: a historical introduction and overview
    • Kilpatrick C.D. Animal lectins: a historical introduction and overview. Bioch Biophys Acta 1572 (2002) 187-197
    • (2002) Bioch Biophys Acta , vol.1572 , pp. 187-197
    • Kilpatrick, C.D.1
  • 3
    • 0037136417 scopus 로고    scopus 로고
    • Principles of structures of animal and plant lectins
    • Loris R. Principles of structures of animal and plant lectins. Biochim Biophys Acta 1572 (2002) 198-208
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 198-208
    • Loris, R.1
  • 4
    • 4744359093 scopus 로고    scopus 로고
    • Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates
    • Vasta G.R., Ahmed H., and Odom E.W. Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates. Curr Opin Struct Biol 14 (2004) 617-630
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 617-630
    • Vasta, G.R.1    Ahmed, H.2    Odom, E.W.3
  • 5
    • 0031784245 scopus 로고    scopus 로고
    • Animal lectins as cell adhesion molecules
    • Kaltner H., and Stierstorfer B. Animal lectins as cell adhesion molecules. Acta Anat 161 (1998) 162-179
    • (1998) Acta Anat , vol.161 , pp. 162-179
    • Kaltner, H.1    Stierstorfer, B.2
  • 7
    • 0030147252 scopus 로고    scopus 로고
    • Lectins as defence molecules in vertebrates and invertebrates
    • Arason G.J. Lectins as defence molecules in vertebrates and invertebrates. Fish Shellfish Immunol 6 (1996) 277-289
    • (1996) Fish Shellfish Immunol , vol.6 , pp. 277-289
    • Arason, G.J.1
  • 8
    • 34147128643 scopus 로고    scopus 로고
    • Purification, cloning and characterization of egg lectins from the teleost Tribolodon brandti
    • Jimbo M., Usui R., Sakai R., Muramoto K., and Kamiya H. Purification, cloning and characterization of egg lectins from the teleost Tribolodon brandti. Comp Biochem Physiol 147B (2007) 164-171
    • (2007) Comp Biochem Physiol , vol.147 B , pp. 164-171
    • Jimbo, M.1    Usui, R.2    Sakai, R.3    Muramoto, K.4    Kamiya, H.5
  • 9
    • 33847125251 scopus 로고    scopus 로고
    • Structural characterization of a rhamnose-binding glycoprotein (lectin) from Spanish mackerel (Scomberomorous niphonius) eggs
    • Terada T., Watanabe Y., Tateno H., Naganuma T., Ogawa T., Muramoto K., et al. Structural characterization of a rhamnose-binding glycoprotein (lectin) from Spanish mackerel (Scomberomorous niphonius) eggs. Biochim Biophys Acta 1770 (2007) 617-629
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 617-629
    • Terada, T.1    Watanabe, Y.2    Tateno, H.3    Naganuma, T.4    Ogawa, T.5    Muramoto, K.6
  • 11
    • 0005282607 scopus 로고
    • Humoral and cellular lectins of ascidians
    • Parrinello N. Humoral and cellular lectins of ascidians. J Mar Biotechnol 3 (1995) 29-34
    • (1995) J Mar Biotechnol , vol.3 , pp. 29-34
    • Parrinello, N.1
  • 12
    • 0020493888 scopus 로고
    • Galactose-specific lectin in the hemolymph of the solitary ascidian Halocynthia roretzi: isolation and characterization
    • Yokosawa H., Sawada H., Abe Y., Numakunai T., and Ishii S. Galactose-specific lectin in the hemolymph of the solitary ascidian Halocynthia roretzi: isolation and characterization. Biochem Biophys Res Commun (1982)
    • (1982) Biochem Biophys Res Commun
    • Yokosawa, H.1    Sawada, H.2    Abe, Y.3    Numakunai, T.4    Ishii, S.5
  • 13
    • 0010104217 scopus 로고
    • Ascidian haemagglutinins: incidence in various species, binding specificities and preliminary characterisation of selected agglutinins
    • Coombe D.R., Ey P.L., and Jenkin C.R. Ascidian haemagglutinins: incidence in various species, binding specificities and preliminary characterisation of selected agglutinins. Comp Biochem Physiol 77B (1984) 811-819
    • (1984) Comp Biochem Physiol , vol.77 B , pp. 811-819
    • Coombe, D.R.1    Ey, P.L.2    Jenkin, C.R.3
  • 14
    • 0023022641 scopus 로고
    • Binding and mitogenic properties of a galactosyl-specific lectin from the tunicate Didemnum candidum for murine thymocytes and splenocytes
    • Vasta G.R., Marchalonis J.J., and Decker J.M. Binding and mitogenic properties of a galactosyl-specific lectin from the tunicate Didemnum candidum for murine thymocytes and splenocytes. J Immunol 137 (1986) 3216-3233
    • (1986) J Immunol , vol.137 , pp. 3216-3233
    • Vasta, G.R.1    Marchalonis, J.J.2    Decker, J.M.3
  • 15
    • 0023729931 scopus 로고
    • D-galactose binding lectins from the tunicate Ascidia malaca: subunit characterization and hemocyte surface distribution
    • Parrinello N., and Arizza V. D-galactose binding lectins from the tunicate Ascidia malaca: subunit characterization and hemocyte surface distribution. Dev Comp Immunol 12 (1988) 495-507
    • (1988) Dev Comp Immunol , vol.12 , pp. 495-507
    • Parrinello, N.1    Arizza, V.2
  • 16
    • 0024624698 scopus 로고
    • Sugar specific cellular lectins of Phallusia mamillata hemocytes: purification, characterization and evidence for cell surface localization
    • Parrinello N., and Arizza V. Sugar specific cellular lectins of Phallusia mamillata hemocytes: purification, characterization and evidence for cell surface localization. Dev Comp Immunol 13 (1989) 113-121
    • (1989) Dev Comp Immunol , vol.13 , pp. 113-121
    • Parrinello, N.1    Arizza, V.2
  • 17
    • 0010166573 scopus 로고
    • Purification of three lectins from the haemolymph of the ascidian Botrylloides leachii
    • Schluter S.F., and Ey P.L. Purification of three lectins from the haemolymph of the ascidian Botrylloides leachii. Comp Biochem Physiol 93B (1989) 145-155
    • (1989) Comp Biochem Physiol , vol.93 B , pp. 145-155
    • Schluter, S.F.1    Ey, P.L.2
  • 18
    • 0025058737 scopus 로고
    • Calcium-dependent, galactose-binding lectin from the tunicate, Polyandrocarpa misakiensis
    • Suzuki T., Takagi T., Furokuohri T., Kawamura K., and Nakauchi M.A. Calcium-dependent, galactose-binding lectin from the tunicate, Polyandrocarpa misakiensis. J Biol Chem 265 (1990) 1274-1281
    • (1990) J Biol Chem , vol.265 , pp. 1274-1281
    • Suzuki, T.1    Takagi, T.2    Furokuohri, T.3    Kawamura, K.4    Nakauchi, M.A.5
  • 21
    • 51249185456 scopus 로고
    • Particle recognition by haemocytes from the colonial ascidian Botrylloides leachi: evidence that the B. leachi HA-2 is opsonic
    • Coombe D.R., Ey P.L., and Jenkin C.R. Particle recognition by haemocytes from the colonial ascidian Botrylloides leachi: evidence that the B. leachi HA-2 is opsonic. J Comp Physiol 154 (1984) 509-521
    • (1984) J Comp Physiol , vol.154 , pp. 509-521
    • Coombe, D.R.1    Ey, P.L.2    Jenkin, C.R.3
  • 22
    • 0026457236 scopus 로고
    • Purification and characterization of a humoral opsonin from the solitary urochordate Styela clava
    • Kelly K.L., Cooper E.L., and Raftos D.S. Purification and characterization of a humoral opsonin from the solitary urochordate Styela clava. Comp Biochem Physiol 103B (1992) 749-753
    • (1992) Comp Biochem Physiol , vol.103 B , pp. 749-753
    • Kelly, K.L.1    Cooper, E.L.2    Raftos, D.S.3
  • 24
    • 0032989492 scopus 로고    scopus 로고
    • Opsonic complement system of the solitary ascidian, Halocynthia roretzi
    • Nonaka M., and Azumi K. Opsonic complement system of the solitary ascidian, Halocynthia roretzi. Dev Comp Immunol 23 (1999) 421-428
    • (1999) Dev Comp Immunol , vol.23 , pp. 421-428
    • Nonaka, M.1    Azumi, K.2
  • 26
    • 0035827589 scopus 로고    scopus 로고
    • Cloning and characterization of novel ficolins from the solitary ascidian, Halocynthhia roretzi
    • Kenjo A., Takahashi M., Matsushita M., Endo Y., Nakata M., Mizuoki T., et al. Cloning and characterization of novel ficolins from the solitary ascidian, Halocynthhia roretzi. J Biol Chem 276 (2001) 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    Mizuoki, T.6
  • 27
    • 0035887616 scopus 로고    scopus 로고
    • An ancient lectin-dependent complement system in an ascidian: novel lectin isolated from the plasma of the solitary ascidian, Halocynthia roretzi
    • Sekine H., Kenjo A., Azumi K., Ohi G., Takahashi M., Kasukawa R., et al. An ancient lectin-dependent complement system in an ascidian: novel lectin isolated from the plasma of the solitary ascidian, Halocynthia roretzi. J Immunol 167 (2001) 4504-4510
    • (2001) J Immunol , vol.167 , pp. 4504-4510
    • Sekine, H.1    Kenjo, A.2    Azumi, K.3    Ohi, G.4    Takahashi, M.5    Kasukawa, R.6
  • 28
    • 0036120959 scopus 로고    scopus 로고
    • A complement component C3-like protein from the tunicate, Styela plicata
    • Raftos D.A., Nair S.V., Robbins J., Newton R.A., and Peters R. A complement component C3-like protein from the tunicate, Styela plicata. Dev Comp Immunol 26 (2002) 307-312
    • (2002) Dev Comp Immunol , vol.26 , pp. 307-312
    • Raftos, D.A.1    Nair, S.V.2    Robbins, J.3    Newton, R.A.4    Peters, R.5
  • 29
    • 0036205799 scopus 로고    scopus 로고
    • Complement in urochordates: cloning and characterization of two C3-like genes in the ascidian Ciona intestinalis
    • Marino R., Kimura Y., De Santis R., Lambris J.D., and Pinto M.R. Complement in urochordates: cloning and characterization of two C3-like genes in the ascidian Ciona intestinalis. Immunogenetics 53 (2002) 1055-1064
    • (2002) Immunogenetics , vol.53 , pp. 1055-1064
    • Marino, R.1    Kimura, Y.2    De Santis, R.3    Lambris, J.D.4    Pinto, M.R.5
  • 30
    • 0242494252 scopus 로고    scopus 로고
    • CiC3-1a-mediated chemotaxis in the deuterostome invertebrate Ciona intestinalis (Urochordata)
    • Pinto M.R., Chinnici C.M., Kimura Y., Melillo D., Marino R., Sdruce L.A., et al. CiC3-1a-mediated chemotaxis in the deuterostome invertebrate Ciona intestinalis (Urochordata). J Immunol 171 (2003) 5521-5528
    • (2003) J Immunol , vol.171 , pp. 5521-5528
    • Pinto, M.R.1    Chinnici, C.M.2    Kimura, Y.3    Melillo, D.4    Marino, R.5    Sdruce, L.A.6
  • 31
    • 33748948442 scopus 로고    scopus 로고
    • Common and divergent pathways in alternative developmental processes of ascidians
    • Manni L., and Burighel P. Common and divergent pathways in alternative developmental processes of ascidians. Bioessays 28 (2006) 902-912
    • (2006) Bioessays , vol.28 , pp. 902-912
    • Manni, L.1    Burighel, P.2
  • 32
    • 33846921832 scopus 로고    scopus 로고
    • Botryllus schlosseri: a model ascidian for the study of asexual reproduction
    • Manni L., Zaniolo G., Cima F., Burighel P., and Ballarin L. Botryllus schlosseri: a model ascidian for the study of asexual reproduction. Dev Dyn 236 (2007) 335-352
    • (2007) Dev Dyn , vol.236 , pp. 335-352
    • Manni, L.1    Zaniolo, G.2    Cima, F.3    Burighel, P.4    Ballarin, L.5
  • 33
    • 0000990465 scopus 로고
    • Le basi genetiche della capacita` di fusione fra colonie in Botryllus schlosseri (Ascidiacea)
    • Sabbadin A. Le basi genetiche della capacita` di fusione fra colonie in Botryllus schlosseri (Ascidiacea). Atti Accad Naz Lincei Rend 32 (1962) 1031-1035
    • (1962) Atti Accad Naz Lincei Rend , vol.32 , pp. 1031-1035
    • Sabbadin, A.1
  • 34
    • 77958404015 scopus 로고
    • Formal genetics of ascidians
    • Sabbadin A. Formal genetics of ascidians. Am Zool 22 (1982) 765-773
    • (1982) Am Zool , vol.22 , pp. 765-773
    • Sabbadin, A.1
  • 35
    • 0024204868 scopus 로고
    • Chimeras and histocompatibility in the colonial ascidian Botryllus schlosseri
    • Sabbadin A., and Astorri C. Chimeras and histocompatibility in the colonial ascidian Botryllus schlosseri. Dev Comp Immunol 12 (1988) 737-748
    • (1988) Dev Comp Immunol , vol.12 , pp. 737-748
    • Sabbadin, A.1    Astorri, C.2
  • 36
    • 21344467415 scopus 로고
    • Morula cells and histocompatibility in the colonial ascidian Botryllus schlosseri
    • Ballarin L., Cima F., and Sabbadin A. Morula cells and histocompatibility in the colonial ascidian Botryllus schlosseri. Zool Sci 12 (1995) 757-764
    • (1995) Zool Sci , vol.12 , pp. 757-764
    • Ballarin, L.1    Cima, F.2    Sabbadin, A.3
  • 37
    • 0036837526 scopus 로고    scopus 로고
    • Oxidative stress induces cytotoxicity during rejection reaction in the compound ascidian Botryllus schlosseri
    • Ballarin L., Cima F., Floreani M., and Sabbadin A. Oxidative stress induces cytotoxicity during rejection reaction in the compound ascidian Botryllus schlosseri. Comp Biochem Physiol 133 (2002) 411-418
    • (2002) Comp Biochem Physiol , vol.133 , pp. 411-418
    • Ballarin, L.1    Cima, F.2    Floreani, M.3    Sabbadin, A.4
  • 38
    • 0031810544 scopus 로고    scopus 로고
    • Contribution of morula cells to allogeneic responses in the colonial urochordate Botryllus schlosseri
    • Rinkevich B., Tartakover S., and Gershon H. Contribution of morula cells to allogeneic responses in the colonial urochordate Botryllus schlosseri. Mar Biol 131 (1998) 227-236
    • (1998) Mar Biol , vol.131 , pp. 227-236
    • Rinkevich, B.1    Tartakover, S.2    Gershon, H.3
  • 39
    • 2942594444 scopus 로고    scopus 로고
    • Cellular aspects of allorecognition in the compound ascidian Botryllus schlosseri
    • Cima F., Sabbadin A., and Ballarin L. Cellular aspects of allorecognition in the compound ascidian Botryllus schlosseri. Dev Comp Immunol 28 (2004) 881-889
    • (2004) Dev Comp Immunol , vol.28 , pp. 881-889
    • Cima, F.1    Sabbadin, A.2    Ballarin, L.3
  • 42
    • 0033930799 scopus 로고    scopus 로고
    • Humoral opsonin from the colonial ascidian Botryllus schlosseri as a member of the galectin family
    • Ballarin L., Tonello C., and Sabbadin A. Humoral opsonin from the colonial ascidian Botryllus schlosseri as a member of the galectin family. Mar Biol 136 (2000) 823-827
    • (2000) Mar Biol , vol.136 , pp. 823-827
    • Ballarin, L.1    Tonello, C.2    Sabbadin, A.3
  • 43
    • 0033011444 scopus 로고    scopus 로고
    • Purification and characterization of a humoral opsonin, with specificity for d-galactose, in the colonial ascidian Botryllus schlosseri
    • Ballarin L., Tonello C., Guidolin L., and Sabbadin A. Purification and characterization of a humoral opsonin, with specificity for d-galactose, in the colonial ascidian Botryllus schlosseri. Comp Biochem Physiol 123B (1999) 115-123
    • (1999) Comp Biochem Physiol , vol.123 B , pp. 115-123
    • Ballarin, L.1    Tonello, C.2    Guidolin, L.3    Sabbadin, A.4
  • 44
    • 0002380845 scopus 로고
    • Ulteriori notizie sull'allevamento e sulla biologia dei Botrilli in condizioni di laboratorio
    • Sabbadin A. Ulteriori notizie sull'allevamento e sulla biologia dei Botrilli in condizioni di laboratorio. Arch Oceanogr Limnol 12 (1960) 97-107
    • (1960) Arch Oceanogr Limnol , vol.12 , pp. 97-107
    • Sabbadin, A.1
  • 45
    • 0020287361 scopus 로고
    • Carbohydrate binding specificity and purification by biospecific affinity chromatography of Ascidia malaca Traust. hemagglutinins
    • Parrinello N., and Canicattì C. Carbohydrate binding specificity and purification by biospecific affinity chromatography of Ascidia malaca Traust. hemagglutinins. Dev Comp Immunol 6 (1982) 53-64
    • (1982) Dev Comp Immunol , vol.6 , pp. 53-64
    • Parrinello, N.1    Canicattì, C.2
  • 46
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 47
    • 0032112719 scopus 로고    scopus 로고
    • Chemotactic responses of tunicate (Urochordata, Ascidiacea) hemocytes in vitro
    • Raftos D.A., Stillman D.L., and Cooper E.L. Chemotactic responses of tunicate (Urochordata, Ascidiacea) hemocytes in vitro. J Invertebr Pathol 72 (1998) 44-49
    • (1998) J Invertebr Pathol , vol.72 , pp. 44-49
    • Raftos, D.A.1    Stillman, D.L.2    Cooper, E.L.3
  • 48
    • 0028618906 scopus 로고
    • Phagocytosis in the colonial ascidian Botryllus schlosseri
    • Ballarin L., Cima F., and Sabbadin A. Phagocytosis in the colonial ascidian Botryllus schlosseri. Dev Comp Immunol 18 (1994) 467-481
    • (1994) Dev Comp Immunol , vol.18 , pp. 467-481
    • Ballarin, L.1    Cima, F.2    Sabbadin, A.3
  • 49
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of the bacteriophage T4
    • Laemmli U.K. Cleavage of structural protein during the assembly of the head of the bacteriophage T4. Nature 277 (1970) 680-685
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 50
    • 0027240517 scopus 로고
    • Detection, isolation and characterization of multiple lectins from the haemolymph of the cockroach Blaberus discoidalis
    • Chen C., Ratcliffe N.A., and Rowley A.F. Detection, isolation and characterization of multiple lectins from the haemolymph of the cockroach Blaberus discoidalis. Biochemistry 294 (1993) 181-190
    • (1993) Biochemistry , vol.294 , pp. 181-190
    • Chen, C.1    Ratcliffe, N.A.2    Rowley, A.F.3
  • 51
    • 28044456518 scopus 로고    scopus 로고
    • Nerve influence on myosin light chain phosphorylation in slow and fast skeletal muscles
    • Bozzo C., Spolaore B., Toniolo L., Stevens L., Bastide B., Cieniewski-Bernard C., et al. Nerve influence on myosin light chain phosphorylation in slow and fast skeletal muscles. FEBS J 272 (2005) 5771-5785
    • (2005) FEBS J , vol.272 , pp. 5771-5785
    • Bozzo, C.1    Spolaore, B.2    Toniolo, L.3    Stevens, L.4    Bastide, B.5    Cieniewski-Bernard, C.6
  • 53
    • 0036924567 scopus 로고    scopus 로고
    • Isolation and characterization of l-rhamnose-binding lectins from chum salmon (Oncorhynchus keta) eggs
    • Shiina N., Tateno H., Ogawa T., Muramoto K., Saneyoshi M., and Kamiya H. Isolation and characterization of l-rhamnose-binding lectins from chum salmon (Oncorhynchus keta) eggs. Fisheries Sci 68 (2002) 1352-1366
    • (2002) Fisheries Sci , vol.68 , pp. 1352-1366
    • Shiina, N.1    Tateno, H.2    Ogawa, T.3    Muramoto, K.4    Saneyoshi, M.5    Kamiya, H.6
  • 54
    • 38649087390 scopus 로고    scopus 로고
    • Isolation and characterization of l-rhamnose-binding lectin, which binds to microsporidian Glugea plecoglossi, from ayu (Plecoglossus altivelis) eggs
    • Watanabe Y., Shiina N., Shinozaki F., Yokoyama H., Kominami J., Nakamura-Tsuruta S., et al. Isolation and characterization of l-rhamnose-binding lectin, which binds to microsporidian Glugea plecoglossi, from ayu (Plecoglossus altivelis) eggs. Dev Comp Immunol 32 (2008) 487-499
    • (2008) Dev Comp Immunol , vol.32 , pp. 487-499
    • Watanabe, Y.1    Shiina, N.2    Shinozaki, F.3    Yokoyama, H.4    Kominami, J.5    Nakamura-Tsuruta, S.6
  • 59
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25 (1997) 4876-4882
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 60
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N., and Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4 (1987) 406-425
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 61
    • 0027099659 scopus 로고
    • Estimating effective population size from samples of sequences: a bootstrap Monte Carlo integration method
    • Felsenstein J. Estimating effective population size from samples of sequences: a bootstrap Monte Carlo integration method. Genet Res 60 (1992) 209-220
    • (1992) Genet Res , vol.60 , pp. 209-220
    • Felsenstein, J.1
  • 62
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Emanuelsson O., Brunak S., von Heijne G., and Nielsen H. Locating proteins in the cell using TargetP, SignalP and related tools. Nat Protoc 2 (2007) 953-971
    • (2007) Nat Protoc , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 63
    • 0025907124 scopus 로고
    • Amino acid sequence and molecular characterization of a d-galactoside-specific lectin purified from sea urchin (Anthocidaris crassispina) eggs
    • Ozeki Y., Matsui T., Suzuki M., and Titani K. Amino acid sequence and molecular characterization of a d-galactoside-specific lectin purified from sea urchin (Anthocidaris crassispina) eggs. Biochemistry 30 (1991) 2391-2394
    • (1991) Biochemistry , vol.30 , pp. 2391-2394
    • Ozeki, Y.1    Matsui, T.2    Suzuki, M.3    Titani, K.4
  • 64
    • 0032729109 scopus 로고    scopus 로고
    • Tandem repeat structure of rhamnose-binding lectin from catfish (Silurus asotus) eggs
    • Hosono M., Ishikawa K., Mineki R., Murayama K., Numata C., Ogawa Y., et al. Tandem repeat structure of rhamnose-binding lectin from catfish (Silurus asotus) eggs. Biochim Biophys Acta 1472 (1999) 668-675
    • (1999) Biochim Biophys Acta , vol.1472 , pp. 668-675
    • Hosono, M.1    Ishikawa, K.2    Mineki, R.3    Murayama, K.4    Numata, C.5    Ogawa, Y.6
  • 65
    • 0032563094 scopus 로고    scopus 로고
    • Isolation an characterization of rhamnose-binding lectins from eggs of steelhead trout (Oncorhynchus mykiss) homologous to low density lipoprotein receptor superfamily
    • Tateno H., Saneyoshi A., Ogawa T., Muramoto K., Kamiya H., and Saneyoshi M. Isolation an characterization of rhamnose-binding lectins from eggs of steelhead trout (Oncorhynchus mykiss) homologous to low density lipoprotein receptor superfamily. J Biol Chem 273 (1998) 19190-19197
    • (1998) J Biol Chem , vol.273 , pp. 19190-19197
    • Tateno, H.1    Saneyoshi, A.2    Ogawa, T.3    Muramoto, K.4    Kamiya, H.5    Saneyoshi, M.6
  • 66
    • 0035376242 scopus 로고    scopus 로고
    • A novel rhamnose-binding lectin family from eggs of steelhead trout (Oncorhynchus mykiss) with different structures and tissue distribution
    • Tateno H., Ogawa T., Muramoto K., Kamiya H., Hirai T., and Saneyoshi M. A novel rhamnose-binding lectin family from eggs of steelhead trout (Oncorhynchus mykiss) with different structures and tissue distribution. Biosci Biotechnol Biochem 65 (2001) 1328-1338
    • (2001) Biosci Biotechnol Biochem , vol.65 , pp. 1328-1338
    • Tateno, H.1    Ogawa, T.2    Muramoto, K.3    Kamiya, H.4    Hirai, T.5    Saneyoshi, M.6
  • 67
    • 0036616919 scopus 로고    scopus 로고
    • Distribution and molecular evolution of rhamnose-binding lectins in Salmonidae: isolation and characterization of two lectins from white-spotted charr (Salvelinus leucomaenis) eggs
    • Tateno H., Ogawa T., Muramoto K., Kamiya H., and Saneyoshi M. Distribution and molecular evolution of rhamnose-binding lectins in Salmonidae: isolation and characterization of two lectins from white-spotted charr (Salvelinus leucomaenis) eggs. Biosci Biotechnol Biochem 66 (2002) 1356-1365
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 1356-1365
    • Tateno, H.1    Ogawa, T.2    Muramoto, K.3    Kamiya, H.4    Saneyoshi, M.5
  • 68
    • 34249938517 scopus 로고    scopus 로고
    • The disulfide bond pattern of salmon egg lectin 24 K from the Chinook salmon Oncorhynchus tshawytscha
    • Yu H., Murata K., Hedrick J.L., Almaraz R.T., Xiang F., and Franz A.H. The disulfide bond pattern of salmon egg lectin 24 K from the Chinook salmon Oncorhynchus tshawytscha. Arch Biochem Biophys 463 (2007) 1-11
    • (2007) Arch Biochem Biophys , vol.463 , pp. 1-11
    • Yu, H.1    Murata, K.2    Hedrick, J.L.3    Almaraz, R.T.4    Xiang, F.5    Franz, A.H.6
  • 69
    • 33845370921 scopus 로고    scopus 로고
    • Isolation, characterization and molecular evolution of a novel shell lectin from a marine bivalve, Pteria penguin
    • Naganuma T., Ogawa T., Hirabayashi J., Kasai K., Kamiya H., and Muramoto K. Isolation, characterization and molecular evolution of a novel shell lectin from a marine bivalve, Pteria penguin. Mol Div 10 (2006) 607-618
    • (2006) Mol Div , vol.10 , pp. 607-618
    • Naganuma, T.1    Ogawa, T.2    Hirabayashi, J.3    Kasai, K.4    Kamiya, H.5    Muramoto, K.6
  • 70
    • 0020582343 scopus 로고
    • Studies on lectins of amago (Oncorhynchus rhodurus) I. Amago ova lectin and its receptor on homologous macrophages
    • Ozaki H., Ohwaki M., and Fukuda T. Studies on lectins of amago (Oncorhynchus rhodurus) I. Amago ova lectin and its receptor on homologous macrophages. Dev Comp Immunol 7 (1983) 77-87
    • (1983) Dev Comp Immunol , vol.7 , pp. 77-87
    • Ozaki, H.1    Ohwaki, M.2    Fukuda, T.3
  • 71
    • 0142029184 scopus 로고    scopus 로고
    • The immunostimulatory activity and stability of grass carp (Ctenopharyngodon idellus) roe lectin
    • Ng T.B., Lam Y.W., and Woo N.Y. The immunostimulatory activity and stability of grass carp (Ctenopharyngodon idellus) roe lectin. Vet Immunopathol 94 (2003) 105-112
    • (2003) Vet Immunopathol , vol.94 , pp. 105-112
    • Ng, T.B.1    Lam, Y.W.2    Woo, N.Y.3
  • 72
    • 36448945436 scopus 로고    scopus 로고
    • Pattern of settlement and natural chimerism in the colonial urochordate Botryllus schlosseri
    • Ben-Shlomo R., Motro U., Paz G., and Rinkevich B. Pattern of settlement and natural chimerism in the colonial urochordate Botryllus schlosseri. Genetica 132 (2008) 51-58
    • (2008) Genetica , vol.132 , pp. 51-58
    • Ben-Shlomo, R.1    Motro, U.2    Paz, G.3    Rinkevich, B.4
  • 73
    • 33747190340 scopus 로고    scopus 로고
    • Allorecognition polymorphism versus parasitic stem cells
    • De Tomaso A.W. Allorecognition polymorphism versus parasitic stem cells. Trends Genet 22 (2006) 485-490
    • (2006) Trends Genet , vol.22 , pp. 485-490
    • De Tomaso, A.W.1


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