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Volumn 1844, Issue 2, 2014, Pages 374-383

Secreted major Venus flytrap chitinase enables digestion of Arthropod prey

Author keywords

Carnivorous plants; Chitin; Chitinases; Digestive enzymes; Plant biology

Indexed keywords

CHITINASE; CHITINASE I; UNCLASSIFIED DRUG;

EID: 84890282706     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.11.009     Document Type: Article
Times cited : (37)

References (73)
  • 3
    • 0242503945 scopus 로고
    • Leaf closure in the venus flytrap: An acid growth response
    • S.E. Williams, and A.B. Bennett Leaf closure in the venus flytrap: an acid growth response Science 218 1982 1120 1122
    • (1982) Science , vol.218 , pp. 1120-1122
    • Williams, S.E.1    Bennett, A.B.2
  • 4
    • 37049192479 scopus 로고
    • Victims of the Venus flytrap
    • R.F. Griggs Victims of the Venus flytrap Science 81 1935 7 8
    • (1935) Science , vol.81 , pp. 7-8
    • Griggs, R.F.1
  • 5
    • 3242809091 scopus 로고    scopus 로고
    • Design and mechanical properties of insect cuticle
    • J.F.V. Vincent, and U.G.K. Wegst Design and mechanical properties of insect cuticle Arthropod. Struct. Dev. 33 2004 187 199
    • (2004) Arthropod. Struct. Dev. , vol.33 , pp. 187-199
    • Vincent, J.F.V.1    Wegst, U.G.K.2
  • 6
    • 28844463100 scopus 로고    scopus 로고
    • Insect chitin synthases: A review
    • H. Merzendorfer Insect chitin synthases: a review J. Comp. Physiol. B. 176 2006 1 15
    • (2006) J. Comp. Physiol. B. , vol.176 , pp. 1-15
    • Merzendorfer, H.1
  • 9
    • 0036161444 scopus 로고    scopus 로고
    • Chemoselective protection of the amino groups of chitosan by controlled phthaloylation: Facile preparation of a precursor useful for chemical modifications
    • K. Kurita, H. Ikeda, Y. Yoshida, M. Shimojoh, and M. Harata Chemoselective protection of the amino groups of chitosan by controlled phthaloylation: facile preparation of a precursor useful for chemical modifications Biomacromolecules 3 2002 1 4
    • (2002) Biomacromolecules , vol.3 , pp. 1-4
    • Kurita, K.1    Ikeda, H.2    Yoshida, Y.3    Shimojoh, M.4    Harata, M.5
  • 11
    • 0031866632 scopus 로고    scopus 로고
    • The molecular biology of chitin digestion
    • R. Cohen-Kupiec, and I. Chet The molecular biology of chitin digestion Curr. Opin. Biotechnol. 9 1998 270 277
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 270-277
    • Cohen-Kupiec, R.1    Chet, I.2
  • 12
    • 0141645390 scopus 로고    scopus 로고
    • Plant chitinases - Regulation and function
    • A. Kasprzewska Plant chitinases - regulation and function Cell. Mol. Biol. Lett. 8 2003 809 824
    • (2003) Cell. Mol. Biol. Lett. , vol.8 , pp. 809-824
    • Kasprzewska, A.1
  • 14
    • 0032974640 scopus 로고    scopus 로고
    • Plant pathogenesis-related proteins: Molecular mechanisms of gene expression and protein function
    • S. Kitajima, and F. Sato Plant pathogenesis-related proteins: molecular mechanisms of gene expression and protein function J. Biochem. 125 1999 1 8
    • (1999) J. Biochem. , vol.125 , pp. 1-8
    • Kitajima, S.1    Sato, F.2
  • 15
    • 33748941620 scopus 로고    scopus 로고
    • Significance of inducible defense-related proteins in infected plants
    • L.C. van Loon, M. Rep, and C.M. Pieterse Significance of inducible defense-related proteins in infected plants Annu. Rev. Phytopathol. 44 2006 135 162
    • (2006) Annu. Rev. Phytopathol. , vol.44 , pp. 135-162
    • Van Loon, L.C.1    Rep, M.2    Pieterse, C.M.3
  • 16
    • 0015390755 scopus 로고
    • Digestive enzymes in insectivorous plants. IV. Enzymatic digestion of insects by Nepenthes secretion and Drosera peltata extract: Proteolytic and chitinolytic activities
    • S. Amagase, M. Mori, and S. Nakayama Digestive enzymes in insectivorous plants. IV. Enzymatic digestion of insects by Nepenthes secretion and Drosera peltata extract: proteolytic and chitinolytic activities J. Biochem. 72 1972 765 767
    • (1972) J. Biochem. , vol.72 , pp. 765-767
    • Amagase, S.1    Mori, M.2    Nakayama, S.3
  • 17
    • 33747871549 scopus 로고    scopus 로고
    • Isolation and characterization of chitinase genes from pitchers of the carnivorous plant Nepenthes khasiana
    • H. Eilenberg, S. Pnini-Cohen, S. Schuster, A. Movtchan, and A. Zilberstein Isolation and characterization of chitinase genes from pitchers of the carnivorous plant Nepenthes khasiana J. Exp. Bot. 57 2006 2775 2784
    • (2006) J. Exp. Bot. , vol.57 , pp. 2775-2784
    • Eilenberg, H.1    Pnini-Cohen, S.2    Schuster, S.3    Movtchan, A.4    Zilberstein, A.5
  • 18
    • 39749087658 scopus 로고    scopus 로고
    • Proteome analysis of pitcher fluid of the carnivorous plant Nepenthes alata
    • N. Hatano, and T. Hamada Proteome analysis of pitcher fluid of the carnivorous plant Nepenthes alata J. Proteome Res. 7 2008 809 816
    • (2008) J. Proteome Res. , vol.7 , pp. 809-816
    • Hatano, N.1    Hamada, T.2
  • 19
    • 28244492028 scopus 로고    scopus 로고
    • Tentacles of in vitro-grown round-leaf sundew (Drosera rotundifolia L.) show induction of chitinase activity upon mimicking the presence of prey
    • I. Matusikova, J. Salaj, J. Moravcikova, L. Mlynarova, J.P. Nap, and J. Libantova Tentacles of in vitro-grown round-leaf sundew (Drosera rotundifolia L.) show induction of chitinase activity upon mimicking the presence of prey Planta 222 2005 1020 1027
    • (2005) Planta , vol.222 , pp. 1020-1027
    • Matusikova, I.1    Salaj, J.2    Moravcikova, J.3    Mlynarova, L.4    Nap, J.P.5    Libantova, J.6
  • 20
    • 84866887347 scopus 로고    scopus 로고
    • Molecular and functional evolution of class i chitinases for plant carnivory in the Caryophyllales
    • T. Renner, and C.D. Specht Molecular and functional evolution of class I chitinases for plant carnivory in the Caryophyllales Mol. Biol. Evol. 29 2012 2971 2985
    • (2012) Mol. Biol. Evol. , vol.29 , pp. 2971-2985
    • Renner, T.1    Specht, C.D.2
  • 21
    • 80052911154 scopus 로고    scopus 로고
    • Functional characterization of a class III acid endochitinase from the traps of the carnivorous pitcher plant genus, Nepenthes
    • S. Rottloff, R. Stieber, H. Maischak, F.G. Turini, G. Heubl, and A. Mithofer Functional characterization of a class III acid endochitinase from the traps of the carnivorous pitcher plant genus, Nepenthes J. Exp. Bot. 62 2011 4639 4647
    • (2011) J. Exp. Bot. , vol.62 , pp. 4639-4647
    • Rottloff, S.1    Stieber, R.2    Maischak, H.3    Turini, F.G.4    Heubl, G.5    Mithofer, A.6
  • 22
    • 84864103899 scopus 로고    scopus 로고
    • Proteomic analysis of secreted protein induced by a component of prey in pitcher fluid of the carnivorous plant Nepenthes alata
    • N. Hatano, and T. Hamada Proteomic analysis of secreted protein induced by a component of prey in pitcher fluid of the carnivorous plant Nepenthes alata J. Proteome 75 2012 4844 4852
    • (2012) J. Proteome , vol.75 , pp. 4844-4852
    • Hatano, N.1    Hamada, T.2
  • 24
    • 0019792891 scopus 로고
    • Analysis of protein and peptide mixtures - Evaluation of 3 sodium dodecyl sulfate-polyacrylamide gel-electrophoresis buffer systems
    • A.F. Bury Analysis of protein and peptide mixtures - evaluation of 3 sodium dodecyl sulfate-polyacrylamide gel-electrophoresis buffer systems J. Chromatogr. 213 1981 491 500
    • (1981) J. Chromatogr. , vol.213 , pp. 491-500
    • Bury, A.F.1
  • 25
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • A. Shevchenko, M. Wilm, O. Vorm, and M. Mann Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels Anal. Chem. 68 1996 850 858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 27
    • 0035326344 scopus 로고    scopus 로고
    • Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching
    • A. Shevchenko, S. Sunyaev, A. Loboda, P. Bork, W. Ens, and K.G. Standing Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching Anal. Chem. 73 2001 1917 1926
    • (2001) Anal. Chem. , vol.73 , pp. 1917-1926
    • Shevchenko, A.1    Sunyaev, S.2    Loboda, A.3    Bork, P.4    Ens, W.5    Standing, K.G.6
  • 28
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • L.A. Kelley, and M.J. Sternberg Protein structure prediction on the Web: a case study using the Phyre server Nat. Protoc. 4 2009 363 371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 32
    • 0019517581 scopus 로고
    • Transformation in Escherichia coli: Stages in the process
    • H.E. Bergmans, I.M. van Die, and W.P. Hoekstra Transformation in Escherichia coli: stages in the process J. Bacteriol. 146 1981 564 570
    • (1981) J. Bacteriol. , vol.146 , pp. 564-570
    • Bergmans, H.E.1    Van Die, I.M.2    Hoekstra, W.P.3
  • 33
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • J.R. Wisniewski, A. Zougman, N. Nagaraj, and M. Mann Universal sample preparation method for proteome analysis Nat. Methods 6 2009 359 362
    • (2009) Nat. Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 34
    • 84866147350 scopus 로고    scopus 로고
    • MS data miner: A web-based software tool to analyze, compare and share mass spectrometry protein identifications
    • T.F. Dyrlund, E.T. Poulsen, C. Scavenius, K.W. Sanggaard, and J.J. Enghild MS data miner: a web-based software tool to analyze, compare and share mass spectrometry protein identifications Proteomics 12 2012 2792 2796
    • (2012) Proteomics , vol.12 , pp. 2792-2796
    • Dyrlund, T.F.1    Poulsen, E.T.2    Scavenius, C.3    Sanggaard, K.W.4    Enghild, J.J.5
  • 35
    • 33746449573 scopus 로고    scopus 로고
    • Analysis of the hyperthermophilic chitinase from Pyrococcus furiosus: Activity toward crystalline chitin
    • T. Oku, and K. Ishikawa Analysis of the hyperthermophilic chitinase from Pyrococcus furiosus: activity toward crystalline chitin Biosci. Biotechnol. Biochem. 70 2006 1696 1701
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 1696-1701
    • Oku, T.1    Ishikawa, K.2
  • 36
    • 77049251255 scopus 로고
    • A modified colorimetric method for the estimation of N-acetylamino sugars
    • J.L. Reissig, J.L. Storminger, and L.F. Leloir A modified colorimetric method for the estimation of N-acetylamino sugars J. Biol. Chem. 217 1955 959 966
    • (1955) J. Biol. Chem. , vol.217 , pp. 959-966
    • Reissig, J.L.1    Storminger, J.L.2    Leloir, L.F.3
  • 37
    • 34247124903 scopus 로고
    • The measurement of lysozyme activity and the ultra-violet inactivation of lysozyme
    • D. Shugar The measurement of lysozyme activity and the ultra-violet inactivation of lysozyme Biochim. Biophys. Acta 8 1952 302 309
    • (1952) Biochim. Biophys. Acta , vol.8 , pp. 302-309
    • Shugar, D.1
  • 39
    • 0030464643 scopus 로고    scopus 로고
    • Characterization of seven basic endochitinases isolated from cell cultures of Citrus sinensis (L.)
    • R.T. Mayer, T.G. McCollam, R.P. Niedz, C.J. Hearn, R.E. McDonald, E. Berdis, and H. Doostdar Characterization of seven basic endochitinases isolated from cell cultures of Citrus sinensis (L.) Planta 200 1996 289 295
    • (1996) Planta , vol.200 , pp. 289-295
    • Mayer, R.T.1    McCollam, T.G.2    Niedz, R.P.3    Hearn, C.J.4    McDonald, R.E.5    Berdis, E.6    Doostdar, H.7
  • 40
  • 41
    • 0025840612 scopus 로고
    • A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole
    • J.M. Neuhaus, L. Sticher, F. Meins, and T. Boller A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole Proc. Natl. Acad. Sci. U. S. A. 88 1991 10362 10366
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 10362-10366
    • Neuhaus, J.M.1    Sticher, L.2    Meins, F.3    Boller, T.4
  • 43
    • 84982746189 scopus 로고
    • +-Co-Transport of d-alanine by the digestive glands of Dionaea-Muscipula Ellis
    • +-Co-Transport of d-alanine by the digestive glands of Dionaea-Muscipula Ellis Plant Cell Environ. 7 1984 363 366
    • (1984) Plant Cell Environ. , vol.7 , pp. 363-366
    • Rea, P.A.1
  • 45
    • 80255132110 scopus 로고    scopus 로고
    • Chitin oligosaccharide binding to a family GH19 chitinase from the moss Bryum coronatum
    • T. Ohnuma, M. Sorlie, T. Fukuda, N. Kawamoto, T. Taira, and T. Fukamizo Chitin oligosaccharide binding to a family GH19 chitinase from the moss Bryum coronatum FEBS J. 278 2011 3991 4001
    • (2011) FEBS J. , vol.278 , pp. 3991-4001
    • Ohnuma, T.1    Sorlie, M.2    Fukuda, T.3    Kawamoto, N.4    Taira, T.5    Fukamizo, T.6
  • 47
    • 84866383476 scopus 로고    scopus 로고
    • Crystal structure and chitin oligosaccharide-binding mode of a 'loopful' family GH19 chitinase from rye, Secale cereale, seeds
    • T. Ohnuma, T. Numata, T. Osawa, H. Inanaga, Y. Okazaki, S. Shinya, K. Kondo, T. Fukuda, and T. Fukamizo Crystal structure and chitin oligosaccharide-binding mode of a 'loopful' family GH19 chitinase from rye, Secale cereale, seeds FEBS J. 279 2012 3639 3651
    • (2012) FEBS J. , vol.279 , pp. 3639-3651
    • Ohnuma, T.1    Numata, T.2    Osawa, T.3    Inanaga, H.4    Okazaki, Y.5    Shinya, S.6    Kondo, K.7    Fukuda, T.8    Fukamizo, T.9
  • 48
    • 77955778566 scopus 로고    scopus 로고
    • Structure of full-length class i chitinase from rice revealed by X-ray crystallography and small-angle X-ray scattering
    • Y. Kezuka, M. Kojima, R. Mizuno, K. Suzuki, T. Watanabe, and T. Nonaka Structure of full-length class I chitinase from rice revealed by X-ray crystallography and small-angle X-ray scattering Proteins 78 2010 2295 2305
    • (2010) Proteins , vol.78 , pp. 2295-2305
    • Kezuka, Y.1    Kojima, M.2    Mizuno, R.3    Suzuki, K.4    Watanabe, T.5    Nonaka, T.6
  • 49
    • 34447306024 scopus 로고    scopus 로고
    • Crystal structures of a family 19 chitinase from Brassica juncea show flexibility of binding cleft loops
    • W. Ubhayasekera, C.M. Tang, S.W. Ho, G. Berglund, T. Bergfors, M.L. Chye, and S.L. Mowbray Crystal structures of a family 19 chitinase from Brassica juncea show flexibility of binding cleft loops FEBS J. 274 2007 3695 3703
    • (2007) FEBS J. , vol.274 , pp. 3695-3703
    • Ubhayasekera, W.1    Tang, C.M.2    Ho, S.W.3    Berglund, G.4    Bergfors, T.5    Chye, M.L.6    Mowbray, S.L.7
  • 50
    • 0029071185 scopus 로고
    • The refined crystal structure of an endochitinase from Hordeum vulgare L. Seeds at 1.8 A resolution
    • P.J. Hart, H.D. Pfluger, A.F. Monzingo, T. Hollis, and J.D. Robertus The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 A resolution J. Mol. Biol. 248 1995 402 413
    • (1995) J. Mol. Biol. , vol.248 , pp. 402-413
    • Hart, P.J.1    Pfluger, H.D.2    Monzingo, A.F.3    Hollis, T.4    Robertus, J.D.5
  • 51
    • 49449116267 scopus 로고    scopus 로고
    • X-ray structure of papaya chitinase reveals the substrate binding mode of glycosyl hydrolase family 19 chitinases
    • J. Huet, P. Rucktooa, B. Clantin, M. Azarkan, Y. Looze, V. Villeret, and R. Wintjens X-ray structure of papaya chitinase reveals the substrate binding mode of glycosyl hydrolase family 19 chitinases Biochemistry 47 2008 8283 8291
    • (2008) Biochemistry , vol.47 , pp. 8283-8291
    • Huet, J.1    Rucktooa, P.2    Clantin, B.3    Azarkan, M.4    Looze, Y.5    Villeret, V.6    Wintjens, R.7
  • 52
    • 1442286045 scopus 로고    scopus 로고
    • Proline versus charge concept for protein stabilization against proteolytic attack
    • Y. Markert, J. Koditz, R. Ulbrich-Hofmann, and U. Arnold Proline versus charge concept for protein stabilization against proteolytic attack Protein Eng. 16 2003 1041 1046
    • (2003) Protein Eng. , vol.16 , pp. 1041-1046
    • Markert, Y.1    Koditz, J.2    Ulbrich-Hofmann, R.3    Arnold, U.4
  • 54
    • 0020490907 scopus 로고
    • Carbohydrates selectively protect a specific domain of fibronectin against proteases
    • B.A. Bernard, K.M. Yamada, and K. Olden Carbohydrates selectively protect a specific domain of fibronectin against proteases J. Biol. Chem. 257 1982 8549 8554
    • (1982) J. Biol. Chem. , vol.257 , pp. 8549-8554
    • Bernard, B.A.1    Yamada, K.M.2    Olden, K.3
  • 57
    • 0035078812 scopus 로고    scopus 로고
    • +-ATPases are expressed in pitchers of the carnivorous plant Nepenthes alata Blanco
    • +-ATPases are expressed in pitchers of the carnivorous plant Nepenthes alata Blanco Planta 212 2001 547 555
    • (2001) Planta , vol.212 , pp. 547-555
    • An, C.I.1    Fukusaki, E.2    Kobayashi, A.3
  • 58
    • 78649765368 scopus 로고    scopus 로고
    • Comparative studies on the acid proteinase activities in the digestive fluids of Nepenthes, Cephalotous, Dionaea, and Drosera
    • K. Takahashi, K. Matsumoto, W. Nishi, M. Muramatsu, and K. Kubota Comparative studies on the acid proteinase activities in the digestive fluids of Nepenthes, Cephalotous, Dionaea, and Drosera Carnivorous Plant Newsl. 38 2009 75 82
    • (2009) Carnivorous Plant Newsl. , vol.38 , pp. 75-82
    • Takahashi, K.1    Matsumoto, K.2    Nishi, W.3    Muramatsu, M.4    Kubota, K.5
  • 59
    • 84866671110 scopus 로고    scopus 로고
    • Biochemical characterization of a recombinant plant class III chitinase from the pitcher of the carnivorous plant Nepenthes alata
    • K. Ishisaki, S. Arai, T. Hamada, and Y. Honda Biochemical characterization of a recombinant plant class III chitinase from the pitcher of the carnivorous plant Nepenthes alata Carbohyd. Res. 361 2012 170 174
    • (2012) Carbohyd. Res. , vol.361 , pp. 170-174
    • Ishisaki, K.1    Arai, S.2    Hamada, T.3    Honda, Y.4
  • 60
    • 84856301036 scopus 로고    scopus 로고
    • Heterogonous expression and characterization of a plant class IV chitinase from the pitcher of the carnivorous plant Nepenthes alata
    • K. Ishisaki, Y. Honda, H. Taniguchi, N. Hatano, and T. Hamada Heterogonous expression and characterization of a plant class IV chitinase from the pitcher of the carnivorous plant Nepenthes alata Glycobiology 22 2012 345 351
    • (2012) Glycobiology , vol.22 , pp. 345-351
    • Ishisaki, K.1    Honda, Y.2    Taniguchi, H.3    Hatano, N.4    Hamada, T.5
  • 62
  • 63
    • 0033598751 scopus 로고    scopus 로고
    • The chitinase PfCHT1 from the human malaria parasite Plasmodium falciparum lacks proenzyme and chitin-binding domains and displays unique substrate preferences
    • J.M. Vinetz, S.K. Dave, C.A. Specht, K.A. Brameld, B. Xu, R. Hayward, and D.A. Fidock The chitinase PfCHT1 from the human malaria parasite Plasmodium falciparum lacks proenzyme and chitin-binding domains and displays unique substrate preferences Proc. Natl. Acad. Sci. U. S. A. 96 1999 14061 14066
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 14061-14066
    • Vinetz, J.M.1    Dave, S.K.2    Specht, C.A.3    Brameld, K.A.4    Xu, B.5    Hayward, R.6    Fidock, D.A.7
  • 64
    • 23344446196 scopus 로고    scopus 로고
    • The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation
    • G. Vaaje-Kolstad, S.J. Horn, D.M. van Aalten, B. Synstad, and V.G. Eijsink The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation J. Biol. Chem. 280 2005 28492 28497
    • (2005) J. Biol. Chem. , vol.280 , pp. 28492-28497
    • Vaaje-Kolstad, G.1    Horn, S.J.2    Van Aalten, D.M.3    Synstad, B.4    Eijsink, V.G.5
  • 65
    • 15744367514 scopus 로고    scopus 로고
    • Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21
    • G. Vaaje-Kolstad, D.R. Houston, A.H. Riemen, V.G. Eijsink, and D.M. van Aalten Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21 J. Biol. Chem. 280 2005 11313 11319
    • (2005) J. Biol. Chem. , vol.280 , pp. 11313-11319
    • Vaaje-Kolstad, G.1    Houston, D.R.2    Riemen, A.H.3    Eijsink, V.G.4    Van Aalten, D.M.5
  • 66
    • 11044235197 scopus 로고    scopus 로고
    • Carnivorous pitcher plant uses free radicals in the digestion of prey
    • T.F. Chia, H.H. Aung, A.N. Osipov, N.K. Goh, and L.S. Chia Carnivorous pitcher plant uses free radicals in the digestion of prey Redox Rep. 9 2004 255 261
    • (2004) Redox Rep. , vol.9 , pp. 255-261
    • Chia, T.F.1    Aung, H.H.2    Osipov, A.N.3    Goh, N.K.4    Chia, L.S.5
  • 67
    • 0025613877 scopus 로고
    • Oxidative protein modification as predigestive mechanism of the carnivorous plant Dionaea muscipula: An hypothesis based on in vitro experiments
    • H. Galek, W.F. Osswald, and E.F. Elstner Oxidative protein modification as predigestive mechanism of the carnivorous plant Dionaea muscipula: an hypothesis based on in vitro experiments Free Radic. Biol. Med. 9 1990 427 434
    • (1990) Free Radic. Biol. Med. , vol.9 , pp. 427-434
    • Galek, H.1    Osswald, W.F.2    Elstner, E.F.3
  • 70
  • 71
    • 84863132928 scopus 로고    scopus 로고
    • Chitooligosaccharides as potential nutraceuticals: Production and bioactivities
    • J.Y. Je, and S.K. Kim Chitooligosaccharides as potential nutraceuticals: production and bioactivities Adv. Food Nutr. Res. 65 2012 321 336
    • (2012) Adv. Food Nutr. Res. , vol.65 , pp. 321-336
    • Je, J.Y.1    Kim, S.K.2
  • 72
    • 17144436519 scopus 로고    scopus 로고
    • Antifungal activity of Bacillus thuringiensis chitinase and its potential for the biocontrol of phytopathogenic fungi in soybean seeds
    • A. Reyes-Ramirez, B.I. Escudero-Abarca, G. Aguilar-Uscanga, P.M. Hayward-Jones, and J.E. Barboza-Corona Antifungal activity of Bacillus thuringiensis chitinase and its potential for the biocontrol of phytopathogenic fungi in soybean seeds J. Food Sci. 69 2004 M131 M134
    • (2004) J. Food Sci. , vol.69
    • Reyes-Ramirez, A.1    Escudero-Abarca, B.I.2    Aguilar-Uscanga, G.3    Hayward-Jones, P.M.4    Barboza-Corona, J.E.5
  • 73
    • 77952965887 scopus 로고    scopus 로고
    • Production of chitooligosaccharides and their potential applications in medicine
    • B.B. Aam, E.B. Heggset, A.L. Norberg, M. Sorlie, K.M. Varum, and V.G. Eijsink Production of chitooligosaccharides and their potential applications in medicine Mar Drugs 8 2010 1482 1517
    • (2010) Mar Drugs , vol.8 , pp. 1482-1517
    • Aam, B.B.1    Heggset, E.B.2    Norberg, A.L.3    Sorlie, M.4    Varum, K.M.5    Eijsink, V.G.6


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