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Volumn 48, Issue 3, 1999, Pages 341-347

Evolution of chitin-binding proteins in invertebrates

Author keywords

Chitin binding; Chitinase; Peritrophic matrix

Indexed keywords

BINDING PROTEIN; CHITIN; CHITINASE;

EID: 0033007284     PISSN: 00222844     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00006478     Document Type: Article
Times cited : (139)

References (41)
  • 2
    • 0028086144 scopus 로고
    • The complete DNA sequence of Autographa californica nuclear polyhedrosis virus
    • Ayres MD, Howard SC, Kuzio J, Lopez-Ferber M, Possee RD (1994) The complete DNA sequence of Autographa californica nuclear polyhedrosis virus. Virology 202:586-605
    • (1994) Virology , vol.202 , pp. 586-605
    • Ayres, M.D.1    Howard, S.C.2    Kuzio, J.3    Lopez-Ferber, M.4    Possee, R.D.5
  • 4
  • 5
    • 0025537359 scopus 로고
    • Effect of plant lectins on the larval development of Europena corn borer (Lepidoptera: Pyrailidae) and Southern corn rootworm (Coleoptera:Chrysomelidae)
    • Czapla TH, Lang BA (1991) Effect of plant lectins on the larval development of Europena corn borer (Lepidoptera: Pyrailidae) and Southern corn rootworm (Coleoptera:Chrysomelidae). J Econ Entomol 83:2480-2485
    • (1991) J Econ Entomol , vol.83 , pp. 2480-2485
    • Czapla, T.H.1    Lang, B.A.2
  • 6
    • 0032146495 scopus 로고    scopus 로고
    • Chitinases are a multi-gene family in Aedes, Anopheles, and Drosophila
    • de la Vega H, Specht CA, Liu Y, Robbins PW (1997) Chitinases are a multi-gene family in Aedes, Anopheles, and Drosophila. Insect Mol Biol 7:233-239
    • (1997) Insect Mol Biol , vol.7 , pp. 233-239
    • De La Vega, H.1    Specht, C.A.2    Liu, Y.3    Robbins, P.W.4
  • 7
    • 0029945647 scopus 로고    scopus 로고
    • Characterization of a major peritrophic membrane protein, peritrophin-44, from the larvae of Lucilia cuprina. cDNA and deduced amino acid sequences
    • Elvin CM, Vuocolo T, Pearson RD, East I, Riding GA, Eisemann CH, Tellam RL (1996) Characterization of a major peritrophic membrane protein, peritrophin-44, from the larvae of Lucilia cuprina. cDNA and deduced amino acid sequences. J Biol Chem 271:8925-8935
    • (1996) J Biol Chem , vol.271 , pp. 8925-8935
    • Elvin, C.M.1    Vuocolo, T.2    Pearson, R.D.3    East, I.4    Riding, G.A.5    Eisemann, C.H.6    Tellam, R.L.7
  • 8
    • 0000122573 scopus 로고
    • PHYLIP - Phylogeny inference package (Version 3.2)
    • Felsenstein J (1989) PHYLIP - phylogeny inference package (Version 3.2). Cladistics 5:164-166
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 9
    • 0026565262 scopus 로고
    • Transmission-blocking antibodies recognize microfilarial chitinase in brugian lymphatic filariasis
    • Fuhrman JA, Lane WS, Smith RF, Piessens WF, Perler FB (1992) Transmission-blocking antibodies recognize microfilarial chitinase in brugian lymphatic filariasis. Proc Natl Acad Sci USA 89:1548-1552
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 1548-1552
    • Fuhrman, J.A.1    Lane, W.S.2    Smith, R.F.3    Piessens, W.F.4    Perler, F.B.5
  • 13
    • 0027668880 scopus 로고
    • Sequence of a cDNA and expression of the gene encoding epidermal and gut chitinases of Manduca sexta
    • Kramer KJ, Corpuz L, Choi HK, Muthukrishnan S (1993) Sequence of a cDNA and expression of the gene encoding epidermal and gut chitinases of Manduca sexta. Insect Biochem Mol Biol 23:691-701
    • (1993) Insect Biochem Mol Biol , vol.23 , pp. 691-701
    • Kramer, K.J.1    Corpuz, L.2    Choi, H.K.3    Muthukrishnan, S.4
  • 14
    • 0024962351 scopus 로고
    • Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing
    • Kraulis J, Clore GM, Nilges M, Jones TA, Pettersson G, Knowles J, Gronenborn AM (1989) Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry 28:7241-7257
    • (1989) Biochemistry , vol.28 , pp. 7241-7257
    • Kraulis, J.1    Clore, G.M.2    Nilges, M.3    Jones, T.A.4    Pettersson, G.5    Knowles, J.6    Gronenborn, A.M.7
  • 15
    • 0028017691 scopus 로고
    • Isolation, cloning, and characterization of new chitinase stored in active form in chitin-lined venom reservoir
    • Krishnan A, Nair PN, Jones D (1994) Isolation, cloning, and characterization of new chitinase stored in active form in chitin-lined venom reservoir. J Biol Chem 269:20971-20976
    • (1994) J Biol Chem , vol.269 , pp. 20971-20976
    • Krishnan, A.1    Nair, P.N.2    Jones, D.3
  • 16
    • 0027507719 scopus 로고
    • Sequence variation, differential expression and chromosomal location of rice chitinase genes
    • Nishizawa Y, Kishimoto N, Saito A, Hibi T (1993) Sequence variation, differential expression and chromosomal location of rice chitinase genes. Mol Gen Genet 241:1-10
    • (1993) Mol Gen Genet , vol.241 , pp. 1-10
    • Nishizawa, Y.1    Kishimoto, N.2    Saito, A.3    Hibi, T.4
  • 17
    • 0004174372 scopus 로고
    • Bradshaw SD, Burggren W, Heller HC, Ishii S, Langer H, Neuweiler G, Randall DJ (eds). Springer-Verlag, Berlin
    • Peters W (1992) In: Bradshaw SD, Burggren W, Heller HC, Ishii S, Langer H, Neuweiler G, Randall DJ (eds) Zoophysiology: Peritrophic membranes. Vol 130. Springer-Verlag, Berlin
    • (1992) Zoophysiology: Peritrophic Membranes , vol.130
    • Peters, W.1
  • 18
    • 0028280652 scopus 로고
    • Cloning and characterization of a potentially protective chitinase-like recombinant antigen from Wuchereria bancrofti
    • Raghavan N, Freedman DO, Fitzgerald PC, Unnasch TR, Ottesen EA, Nutman TB (1994) Cloning and characterization of a potentially protective chitinase-like recombinant antigen from Wuchereria bancrofti. Infect Immun 62:1901-1908
    • (1994) Infect Immun , vol.62 , pp. 1901-1908
    • Raghavan, N.1    Freedman, D.O.2    Fitzgerald, P.C.3    Unnasch, T.R.4    Ottesen, E.A.5    Nutman, T.B.6
  • 21
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schlumbaum A, Mauch F, Vogeli U, Boller T (1986) Plant chitinases are potent inhibitors of fungal growth. Nature 324:365-367
    • (1986) Nature , vol.324 , pp. 365-367
    • Schlumbaum, A.1    Mauch, F.2    Vogeli, U.3    Boller, T.4
  • 22
    • 0030665155 scopus 로고    scopus 로고
    • Characterization of a novel gut-specific chitinase gene from the human malaria vector Anopheles gambiae
    • Shen Z, Jacobs-Lorena M (1997) Characterization of a novel gut-specific chitinase gene from the human malaria vector Anopheles gambiae. J Biol Chem 272:28895-28900
    • (1997) J Biol Chem , vol.272 , pp. 28895-28900
    • Shen, Z.1    Jacobs-Lorena, M.2
  • 23
    • 0032504233 scopus 로고    scopus 로고
    • A type I peritrophic matrix protein from the malaria vector Anopheles gambiae binds to chitin
    • Shen Z, Jacobs-Lorena M (1998) A type I peritrophic matrix protein from the malaria vector Anopheles gambiae binds to chitin. J Biol Chem 273:17665-17670
    • (1998) J Biol Chem , vol.273 , pp. 17665-17670
    • Shen, Z.1    Jacobs-Lorena, M.2
  • 24
    • 0028122878 scopus 로고
    • Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum
    • Sim BKL, Chitnis CE, Wasniowska K, Hadley TJ, Miller LH (1994) Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum. Science 264:1941-1944
    • (1994) Science , vol.264 , pp. 1941-1944
    • Sim, B.K.L.1    Chitnis, C.E.2    Wasniowska, K.3    Hadley, T.J.4    Miller, L.H.5
  • 25
    • 0024770872 scopus 로고
    • Nucleotide sequences of cDNA clones encoding wheat germ agglutinin isolectins A and D
    • Smith JJ, Raikhel NV (1989) Nucleotide sequences of cDNA clones encoding wheat germ agglutinin isolectins A and D. Plant Mol Biol 13:601-603
    • (1989) Plant Mol Biol , vol.13 , pp. 601-603
    • Smith, J.J.1    Raikhel, N.V.2
  • 27
    • 0027968068 scopus 로고
    • Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalites and weight matrix choice
    • Thompson JD, Higgins DG, Gibson RJ (1994) Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalites 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, R.J.3
  • 28
    • 0029955959 scopus 로고    scopus 로고
    • Crystal structure of a bacterial family-III cellulose-binding domain: A general mechanism for attachment to cellulose
    • Tormo J, Lamed R, Chirino AJ, Morag E, Bayer EA, Shoham Y, Steitz TA (1996) Crystal structure of a bacterial family-III cellulose-binding domain: A general mechanism for attachment to cellulose. EMBO J 15:5739-5751
    • (1996) EMBO J , vol.15 , pp. 5739-5751
    • Tormo, J.1    Lamed, R.2    Chirino, A.J.3    Morag, E.4    Bayer, E.A.5    Shoham, Y.6    Steitz, T.A.7
  • 29
    • 0026507396 scopus 로고
    • The structure and regulation of homeologous tobacco endochitinase genes of Nicotiana sylvestris and N. Tomentosiformis origin
    • van Buuren M, Neuhaus JM, Shinshi H, Ryals J, Meins, F Jr (1992) The structure and regulation of homeologous tobacco endochitinase genes of Nicotiana sylvestris and N. tomentosiformis origin. Mol Gen Genet 232:460-469
    • (1992) Mol Gen Genet , vol.232 , pp. 460-469
    • Van Buuren, M.1    Neuhaus, J.M.2    Shinshi, H.3    Ryals, J.4    Meins F., Jr.5
  • 30
    • 0030985902 scopus 로고    scopus 로고
    • Molecular cloning and sequencing of a novel invertebrate intestinal mucin
    • Wang P, Granados RR (1997) Molecular cloning and sequencing of a novel invertebrate intestinal mucin. J Biol Chem 272:16663-16669
    • (1997) J Biol Chem , vol.272 , pp. 16663-16669
    • Wang, P.1    Granados, R.R.2
  • 31
    • 0031080395 scopus 로고    scopus 로고
    • Isolation of a cDNA encoding a chitinase family protein from cuticular tissues of the kuruma prawn Penaeus japonicus
    • Watanabe T, Kono M (1997) Isolation of a cDNA encoding a chitinase family protein from cuticular tissues of the kuruma prawn Penaeus japonicus. J Zool Sci 14:65-68
    • (1997) J Zool Sci , vol.14 , pp. 65-68
    • Watanabe, T.1    Kono, M.2
  • 32
    • 0030432812 scopus 로고    scopus 로고
    • Isolation of cDNA encoding a putative chitinase precursor in the kuruma prawn Penaeus japonicus
    • Watanabe T, Kono M, Aida K, Nagasawa H (1996) Isolation of cDNA encoding a putative chitinase precursor in the kuruma prawn Penaeus japonicus. Mol Mari Biol Biotech 5:299-303
    • (1996) Mol Mari Biol Biotech , vol.5 , pp. 299-303
    • Watanabe, T.1    Kono, M.2    Aida, K.3    Nagasawa, H.4
  • 33
    • 4243454567 scopus 로고    scopus 로고
    • Purification and molecular cloning of a chitinase expressed in the hepatopancreas of the penaeid prawn Penaeus japonicus
    • in press
    • Watanabe T, Kono M, Aida K, Nagasawa H (1997) Purification and molecular cloning of a chitinase expressed in the hepatopancreas of the penaeid prawn Penaeus japonicus. Biochim Biophys Acta (in press)
    • (1997) Biochim Biophys Acta
    • Watanabe, T.1    Kono, M.2    Aida, K.3    Nagasawa, H.4
  • 34
    • 0028295681 scopus 로고
    • 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans
    • Wilson R, et al. (1994) 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans. Nature 368:32-38
    • (1994) Nature , vol.368 , pp. 32-38
    • Wilson, R.1
  • 35
    • 0017336920 scopus 로고
    • The crystal structure of wheat germ agglutinin at 2.2A resolution
    • Wright CS (1977) The crystal structure of wheat germ agglutinin at 2.2A resolution. J Mol Biol 111:439-457
    • (1977) J Mol Biol , vol.111 , pp. 439-457
    • Wright, C.S.1
  • 36
    • 0021742330 scopus 로고
    • Evolution of the multidomain protein wheat germ agglutinin
    • Wright HT, Brooks DM, Wright CS (1985) Evolution of the multidomain protein wheat germ agglutinin. J Mol Evol 21:133-138
    • (1985) J Mol Evol , vol.21 , pp. 133-138
    • Wright, H.T.1    Brooks, D.M.2    Wright, C.S.3
  • 37
    • 0025721792 scopus 로고
    • Evolution of a family of N-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat germ agglutinin
    • Wright HT, Sandrasegaram G, Wright CS (1991) Evolution of a family of N-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat germ agglutinin. J Mol Evol 33:283-294
    • (1991) J Mol Evol , vol.33 , pp. 283-294
    • Wright, H.T.1    Sandrasegaram, G.2    Wright, C.S.3
  • 38
    • 0028484871 scopus 로고
    • Molecular analysis of two cDNA clones encoding acidic class I chitinase in maize
    • Wu S, Kriz AL, Widholm JM (1994) Molecular analysis of two cDNA clones encoding acidic class I chitinase in maize. Plant Physiol 105:1097-1105
    • (1994) Plant Physiol , vol.105 , pp. 1097-1105
    • Wu, S.1    Kriz, A.L.2    Widholm, J.M.3
  • 39
    • 0029981630 scopus 로고    scopus 로고
    • Chitinase genes expressed by infective larvae of the filarial nematodes, Acanthocheilonema viteae and Onchocerca volvulus
    • Wu Y, Adam R, Williams SA, Bianco AE (1996) Chitinase genes expressed by infective larvae of the filarial nematodes, Acanthocheilonema viteae and Onchocerca volvulus. Mol Biochem Parasitol 75:207-219
    • (1996) Mol Biochem Parasitol , vol.75 , pp. 207-219
    • Wu, Y.1    Adam, R.2    Williams, S.A.3    Bianco, A.E.4
  • 41
    • 0030200167 scopus 로고    scopus 로고
    • Limited proteolysis and reduction-carboxymethylation of rye seed chitinase-a: Role of the chitin-binding domain in its chitinase action
    • Yamagami T, Funatsu G (1996) Limited proteolysis and reduction-carboxymethylation of rye seed chitinase-a: Role of the chitin-binding domain in its chitinase action. Biosci Biotech Biochem 60:1081-1086
    • (1996) Biosci Biotech Biochem , vol.60 , pp. 1081-1086
    • Yamagami, T.1    Funatsu, G.2


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