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Volumn 487, Issue 2, 2011, Pages 118-128

The cDNA sequence of three hemocyanin subunits from the garden snail Helix lucorum

Author keywords

Evolution; Mass spectrometry; Mollusks

Indexed keywords

COMPLEMENTARY DNA; HEMOCYANIN;

EID: 80052869946     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2011.07.030     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 0034997129 scopus 로고    scopus 로고
    • Rhogocytes (pore cells) as the site of hemocyanin biosynthesis in the marine gastropod Haliotis tuberculata
    • Albrecht U., Keller H., Gebauer W., Markl J. Rhogocytes (pore cells) as the site of hemocyanin biosynthesis in the marine gastropod Haliotis tuberculata. Cell Tissue Res. 2001, 304:455-462.
    • (2001) Cell Tissue Res. , vol.304 , pp. 455-462
    • Albrecht, U.1    Keller, H.2    Gebauer, W.3    Markl, J.4
  • 2
    • 0037073432 scopus 로고    scopus 로고
    • Gene structure and hemocyanin isoform HtH2 from the mollusc Haliotis tuberculata indicate early and late intron hot spots
    • Altenhein B., Markl J., Lieb B. Gene structure and hemocyanin isoform HtH2 from the mollusc Haliotis tuberculata indicate early and late intron hot spots. Gene 2002, 301:53-60.
    • (2002) Gene , vol.301 , pp. 53-60
    • Altenhein, B.1    Markl, J.2    Lieb, B.3
  • 3
    • 80052877944 scopus 로고
    • Chapman and Hall, London, M.J. Benton (Ed.)
    • The Fossil Record 2 1993, 125-270. Chapman and Hall, London. M.J. Benton (Ed.).
    • (1993) The Fossil Record 2 , pp. 125-270
  • 4
    • 33644927549 scopus 로고    scopus 로고
    • The hemocyanin from a living fossil, the cephalopod Nautilus pompilius: protein structure, gene organization, and evolution
    • Bergmann S., Lieb B., Ruth P., Markl J. The hemocyanin from a living fossil, the cephalopod Nautilus pompilius: protein structure, gene organization, and evolution. J. Mol. Evol. 2006, 62:362-374.
    • (2006) J. Mol. Evol. , vol.62 , pp. 362-374
    • Bergmann, S.1    Lieb, B.2    Ruth, P.3    Markl, J.4
  • 5
    • 34248195015 scopus 로고    scopus 로고
    • The first complete cDNA sequence of the hemocyanin of a bivalve, the protobranch Nucula nucleus
    • Bergmann S., Markl J., Lieb B. The first complete cDNA sequence of the hemocyanin of a bivalve, the protobranch Nucula nucleus. J. Mol. Evol. 2007, 64:500-510.
    • (2007) J. Mol. Evol. , vol.64 , pp. 500-510
    • Bergmann, S.1    Markl, J.2    Lieb, B.3
  • 6
    • 0035140529 scopus 로고    scopus 로고
    • Molecular evolution of the arthropod hemocyanin superfamily
    • Burmester T. Molecular evolution of the arthropod hemocyanin superfamily. Mol. Biol. Evol. 2001, 18:184-195.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 184-195
    • Burmester, T.1
  • 7
    • 2942735216 scopus 로고    scopus 로고
    • Hemocyanin of the molluscan Concholepas concholepas exhibits an unusual heterodecameric array of subunits
    • De Ioannes P., Moltedo B., Oliva H., Pacheco R., Faunes F., De Ioannes A.E., et al. Hemocyanin of the molluscan Concholepas concholepas exhibits an unusual heterodecameric array of subunits. J. Biol. Chem. 2004, 279:26134-26142.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26134-26142
    • De Ioannes, P.1    Moltedo, B.2    Oliva, H.3    Pacheco, R.4    Faunes, F.5    De Ioannes, A.E.6
  • 8
    • 0034255667 scopus 로고    scopus 로고
    • Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism
    • Decker H., Tuczek F. Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism. Trends Biochem. Sci. 2000, 25:392-397.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 392-397
    • Decker, H.1    Tuczek, F.2
  • 9
    • 78650960236 scopus 로고    scopus 로고
    • Antitumor activity of glycosylated molluscan hemocyanins via guerin ascites tumor
    • Dolashka P., Velkova L., Iliev I., Beck A., Dolashki A., Yossifova L., et al. Antitumor activity of glycosylated molluscan hemocyanins via guerin ascites tumor. Immunol. Invest. 2011, 40:130-149.
    • (2011) Immunol. Invest. , vol.40 , pp. 130-149
    • Dolashka, P.1    Velkova, L.2    Iliev, I.3    Beck, A.4    Dolashki, A.5    Yossifova, L.6
  • 13
    • 67650658076 scopus 로고    scopus 로고
    • Identification of glycosylated sites in Rapana hemocyanin by mass spectrometry and gene sequence, and their antiviral effect
    • Dolashka-Angelova P., Lieb B., Velkova L., Heilen N., Sandra K., Nikolaeva-Glomb L., et al. Identification of glycosylated sites in Rapana hemocyanin by mass spectrometry and gene sequence, and their antiviral effect. Bioconjug. Chem. 2009, 20(7):1315-1322.
    • (2009) Bioconjug. Chem. , vol.20 , Issue.7 , pp. 1315-1322
    • Dolashka-Angelova, P.1    Lieb, B.2    Velkova, L.3    Heilen, N.4    Sandra, K.5    Nikolaeva-Glomb, L.6
  • 14
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP, and related tools
    • Emanuelsson O., Brunak S., von Heijne G., Nielsen H. Locating proteins in the cell using TargetP, SignalP, and related tools. Nat. Protoc. 2007, 2:953-971.
    • (2007) Nat. Protoc. , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 15
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng J.K., McCormack A.L., Yates J.R. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 1994, 5:976-989.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 16
    • 58149107143 scopus 로고    scopus 로고
    • Keyhole limpet hemocyanin: 9-Å CryoEM structure and molecular model of the KLH1 didecamer reveal the interfaces and intricate topology of the 160 functional units
    • Gatsogiannis Ch., Markl J. Keyhole limpet hemocyanin: 9-Å CryoEM structure and molecular model of the KLH1 didecamer reveal the interfaces and intricate topology of the 160 functional units. J. Mol. Biol. 2009, 385:963-983.
    • (2009) J. Mol. Biol. , vol.385 , pp. 963-983
    • Gatsogiannis, C.1    Markl, J.2
  • 17
    • 0033485264 scopus 로고    scopus 로고
    • Keyhole limpet hemocyanin (KLH): a biomedical review
    • Harris J.R., Markl J. Keyhole limpet hemocyanin (KLH): a biomedical review. Micron 1999, 30:597-623.
    • (1999) Micron , vol.30 , pp. 597-623
    • Harris, J.R.1    Markl, J.2
  • 18
    • 0034064793 scopus 로고    scopus 로고
    • Keyhole limpet hemocyanin: molecular structure of a potent marine immunoactivator
    • Harris J.R., Markl J. Keyhole limpet hemocyanin: molecular structure of a potent marine immunoactivator. J. Eur. Urol. 2000, 37:24-33.
    • (2000) J. Eur. Urol. , vol.37 , pp. 24-33
    • Harris, J.R.1    Markl, J.2
  • 19
    • 1242277839 scopus 로고    scopus 로고
    • 3D reconstruction of the hemocyanin subunit dimer from the chiton Acanthochiton fascicularis
    • Harris J.R., Meissner U., Gebauer W., Markl J. 3D reconstruction of the hemocyanin subunit dimer from the chiton Acanthochiton fascicularis. Micron 2004, 35:23-26.
    • (2004) Micron , vol.35 , pp. 23-26
    • Harris, J.R.1    Meissner, U.2    Gebauer, W.3    Markl, J.4
  • 20
    • 41549119369 scopus 로고    scopus 로고
    • Haemocyanins from Rapana venosa and Helix lucorum display an antitumour activity via specific activation of spleen lymphocytes
    • Iliev I., Toshkova R., Dolashka-Angelova P., Yossifova L., Hristova R., Yaneva J., et al. Haemocyanins from Rapana venosa and Helix lucorum display an antitumour activity via specific activation of spleen lymphocytes. C. R. Acad. Bulg. Sci. 2008, 61:203-210.
    • (2008) C. R. Acad. Bulg. Sci. , vol.61 , pp. 203-210
    • Iliev, I.1    Toshkova, R.2    Dolashka-Angelova, P.3    Yossifova, L.4    Hristova, R.5    Yaneva, J.6
  • 21
    • 0031760504 scopus 로고    scopus 로고
    • Crystal structure of a plant catechol oxidase containing a dicopper center
    • Klabunde T., Eicken C., Sacchettini J.C., Krebs B. Crystal structure of a plant catechol oxidase containing a dicopper center. Nat. Struct. Biol. 1998, 5:1084-1090.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1084-1090
    • Klabunde, T.1    Eicken, C.2    Sacchettini, J.C.3    Krebs, B.4
  • 22
    • 0028990445 scopus 로고
    • Three-dimensional reconstruction of the alpha D and beta C-hemocyanins of Helix pomatia from frozen-hydrated specimens
    • Lambert O., Boisset N., Taveau J.C., Préaux G., Lamy J.N. Three-dimensional reconstruction of the alpha D and beta C-hemocyanins of Helix pomatia from frozen-hydrated specimens. J. Mol. Biol. 1995, 248:431-448.
    • (1995) J. Mol. Biol. , vol.248 , pp. 431-448
    • Lambert, O.1    Boisset, N.2    Taveau, J.C.3    Préaux, G.4    Lamy, J.N.5
  • 23
    • 0034007385 scopus 로고    scopus 로고
    • The sequence of a gastropod hemocyanin (HtH1 from Haliotis tuberculata)
    • Lieb B., Altenhein B., Markl J. The sequence of a gastropod hemocyanin (HtH1 from Haliotis tuberculata). J. Biol. Chem. 2000, 275:5675-5681.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5675-5681
    • Lieb, B.1    Altenhein, B.2    Markl, J.3
  • 25
    • 4644316521 scopus 로고    scopus 로고
    • CDNA sequence, protein structure, and evolution of the single hemocyanin from Aplysia californica, an opisthobranch gastropod
    • Lieb B., Boisguérin V., Gebauer W., Markl J. cDNA sequence, protein structure, and evolution of the single hemocyanin from Aplysia californica, an opisthobranch gastropod. J. Mol. Evol. 2004, 59:536-545.
    • (2004) J. Mol. Evol. , vol.59 , pp. 536-545
    • Lieb, B.1    Boisguérin, V.2    Gebauer, W.3    Markl, J.4
  • 26
    • 0030860309 scopus 로고    scopus 로고
    • Primary structure of 21 novel monoantennary and diantennary N-linked carbohydrate chains from alphaD-hemocyanin of Helix pomatia
    • Lommerse J.P., Thomas-Oates J.E., Gielens C., Préaux G., Kamerling J.P., Vliegenthart J.F. Primary structure of 21 novel monoantennary and diantennary N-linked carbohydrate chains from alphaD-hemocyanin of Helix pomatia. Eur. J. Biochem. 1997, 249:195-222.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 195-222
    • Lommerse, J.P.1    Thomas-Oates, J.E.2    Gielens, C.3    Préaux, G.4    Kamerling, J.P.5    Vliegenthart, J.F.6
  • 27
    • 0003546217 scopus 로고
    • Components, functional units, and active sites of Helix pomatia hemocyanin
    • Lontie R. Components, functional units, and active sites of Helix pomatia hemocyanin. Life Chem. Rep. 1983, S1:109-120.
    • (1983) Life Chem. Rep. , vol.S1 , pp. 109-120
    • Lontie, R.1
  • 28
    • 33846638741 scopus 로고    scopus 로고
    • Limulus polyphemus hemocyanin: 10Å structure, sequence analysis, molecular modelling and rigid-body fitting reveal the interfaces between the eight hexamers
    • Martin A., Depoix F., Stohr M., Meissner U., Hagner-Holler S., Hammouti K., et al. Limulus polyphemus hemocyanin: 10Å structure, sequence analysis, molecular modelling and rigid-body fitting reveal the interfaces between the eight hexamers. J. Mol. Biol. 2007, 366:1332-1350.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1332-1350
    • Martin, A.1    Depoix, F.2    Stohr, M.3    Meissner, U.4    Hagner-Holler, S.5    Hammouti, K.6
  • 29
    • 41549089987 scopus 로고    scopus 로고
    • An easy-to-use Decoy Database Builder software tool, implementing different decoy strategies for false discovery rate calculation in automated MS/MS protein identifications
    • Reidegeld K.A., Eisenacher M., Kohl M., Chamrad D., Körting G., Blüggel M., et al. An easy-to-use Decoy Database Builder software tool, implementing different decoy strategies for false discovery rate calculation in automated MS/MS protein identifications. Proteomics 2008, 8:1129-1137.
    • (2008) Proteomics , vol.8 , pp. 1129-1137
    • Reidegeld, K.A.1    Eisenacher, M.2    Kohl, M.3    Chamrad, D.4    Körting, G.5    Blüggel, M.6
  • 30
    • 0017724250 scopus 로고
    • Haemocyanin synthesis in pore cells of the terrestrial snail Helix aspersa
    • Sminia T., Vlugh-vanDallen J.E. Haemocyanin synthesis in pore cells of the terrestrial snail Helix aspersa. Cell Tissue Res. 1977, 183:299-301.
    • (1977) Cell Tissue Res. , vol.183 , pp. 299-301
    • Sminia, T.1    Vlugh-vanDallen, J.E.2
  • 31
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: molecular evolutionary. Genetics analysis (MEGA) software version 4.0
    • Tamura K., Dudley J., Nei M., Kumar S. MEGA4: molecular evolutionary. Genetics analysis (MEGA) software version 4.0. Mol. Biol. Evol. 2007, 24:1596-1599.
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 32
    • 0033568502 scopus 로고    scopus 로고
    • Disulfide bond reduction: a powerful, chemical probe for the study of structure-function relationships in the hemocyanins
    • Topham R., Tesh S., Westcott A., Cole G., Mercatante D., Kaufman G., et al. Disulfide bond reduction: a powerful, chemical probe for the study of structure-function relationships in the hemocyanins. Arch. Biochem. Biophys. 1999, 369:261-266.
    • (1999) Arch. Biochem. Biophys. , vol.369 , pp. 261-266
    • Topham, R.1    Tesh, S.2    Westcott, A.3    Cole, G.4    Mercatante, D.5    Kaufman, G.6
  • 34
    • 0031213675 scopus 로고    scopus 로고
    • Sequence and structural features of plant and fungal tyrosinases
    • Van Gelder C.W., Flurkey W.H., Wichers H.J. Sequence and structural features of plant and fungal tyrosinases. Phytochemistry 1997, 45:1309-1323.
    • (1997) Phytochemistry , vol.45 , pp. 1309-1323
    • Van Gelder, C.W.1    Flurkey, W.H.2    Wichers, H.J.3
  • 35
    • 0035844294 scopus 로고    scopus 로고
    • Hemocyanins and invertebrate evolution
    • Van Holde K., Miller K., Decker H. Hemocyanins and invertebrate evolution. J. Biol. Chem. 2001, 276:15563-15566.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15563-15566
    • Van Holde, K.1    Miller, K.2    Decker, H.3
  • 37
    • 79951579818 scopus 로고    scopus 로고
    • Assessing divergence time of Spirulida and Sepiida (Cephalopoda) based on hemocyanin sequences
    • Warnke K.M., Meyer A., Ebner B., Lieb B. Assessing divergence time of Spirulida and Sepiida (Cephalopoda) based on hemocyanin sequences. Mol. Phylogenet. Evol. 2011, 58:390-394.
    • (2011) Mol. Phylogenet. Evol. , vol.58 , pp. 390-394
    • Warnke, K.M.1    Meyer, A.2    Ebner, B.3    Lieb, B.4
  • 38
    • 0000282006 scopus 로고
    • Relative molecular mass of the polypeptide chain of bc-haemocyanin of Helix pomatia and carbohydrate composition of the functional units
    • Wood E., Chaplin M., Gielens C., De Saedeleer J., Préaux G., Lontie R. Relative molecular mass of the polypeptide chain of bc-haemocyanin of Helix pomatia and carbohydrate composition of the functional units. Comp. Biochem. Physiol. B 1985, 82:179-186.
    • (1985) Comp. Biochem. Physiol. B , vol.82 , pp. 179-186
    • Wood, E.1    Chaplin, M.2    Gielens, C.3    De Saedeleer, J.4    Préaux, G.5    Lontie, R.6
  • 39
    • 0033736753 scopus 로고    scopus 로고
    • A fucose-containing epitope is shared by keyhole limpet haemocyanin and Schistosoma mansoni glycosphingolipids
    • Wuhrer M., Dennis R.D., Doenhoff M.J., Geyer R. A fucose-containing epitope is shared by keyhole limpet haemocyanin and Schistosoma mansoni glycosphingolipids. Mol. Biochem. Parasitol. 2000, 110:237-246.
    • (2000) Mol. Biochem. Parasitol. , vol.110 , pp. 237-246
    • Wuhrer, M.1    Dennis, R.D.2    Doenhoff, M.J.3    Geyer, R.4
  • 40
    • 1642383648 scopus 로고    scopus 로고
    • A novel Gal(b1-4)Gal(b1-4)Fuc(a1-6)-core modification attached to the proximal N-acetylglucosamine of keyhole limpet haemocyanin (KLH) N-glycans
    • Wuhrer M., Robijn M.L.M., Koeleman C.A.M., Balog C.I.A., Geyer R., Deelder A.M., et al. A novel Gal(b1-4)Gal(b1-4)Fuc(a1-6)-core modification attached to the proximal N-acetylglucosamine of keyhole limpet haemocyanin (KLH) N-glycans. Biochem. J. 2004, 378:625-632.
    • (2004) Biochem. J. , vol.378 , pp. 625-632
    • Wuhrer, M.1    Robijn, M.L.M.2    Koeleman, C.A.M.3    Balog, C.I.A.4    Geyer, R.5    Deelder, A.M.6
  • 41
    • 84988003044 scopus 로고    scopus 로고
    • Immunological research on the protective properties of a conjugate of total larval antigen with hemocyanin derived from Helix lucorum against infection with Trichinella spiralis
    • Yossifova L., Petkova S., Dolashka-Angelova P., Mihov L., Zacharieva S. Immunological research on the protective properties of a conjugate of total larval antigen with hemocyanin derived from Helix lucorum against infection with Trichinella spiralis. Biotech. Equip. 2009, 23:597-600.
    • (2009) Biotech. Equip. , vol.23 , pp. 597-600
    • Yossifova, L.1    Petkova, S.2    Dolashka-Angelova, P.3    Mihov, L.4    Zacharieva, S.5


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