메뉴 건너뛰기




Volumn 31, Issue 8, 2014, Pages 2124-2148

Clawing through evolution: Toxin diversification and convergence in the ancient lineage chilopoda (Centipedes)

Author keywords

centipede; convergence; evolution; toxin; venom

Indexed keywords

ARTHROPOD VENOM;

EID: 84904989275     PISSN: 07374038     EISSN: 15371719     Source Type: Journal    
DOI: 10.1093/molbev/msu162     Document Type: Article
Times cited : (85)

References (101)
  • 2
    • 0036135117 scopus 로고    scopus 로고
    • Ophidian envenomation strategies and the role of purines
    • Aird SD. 2002. Ophidian envenomation strategies and the role of purines. Toxicon 40:335-393
    • (2002) Toxicon , vol.40 , pp. 335-393
    • Aird, S.D.1
  • 4
    • 0141993544 scopus 로고    scopus 로고
    • A serine proteinase homolog venom protein from an endoparasitoid wasp inhibits melanization of the host hemolymph
    • Asgari S, Zhang G, Zareie R, Schmidt O. 2003. A serine proteinase homolog venom protein from an endoparasitoid wasp inhibits melanization of the host hemolymph. Insect Biochem Mol Biol. 33: 1017-1024
    • (2003) Insect Biochem Mol Biol , vol.33 , pp. 1017-1024
    • Asgari, S.1    Zhang, G.2    Zareie, R.3    Schmidt, O.4
  • 5
    • 0014200117 scopus 로고
    • Studies on glucose dehydrogenase of Aspergillus oryzae II. Purification and physical and chemical properties
    • Bak TG. 1967. Studies on glucose dehydrogenase of Aspergillus oryzae. II. Purification and physical and chemical properties. Biochim Biophys Acta. 139:277-293
    • (1967) Biochim Biophys Acta , vol.139 , pp. 277-293
    • Bak, T.G.1
  • 10
    • 0029016839 scopus 로고
    • The astacin family of metalloendopeptidases
    • Bond JS, Beynon RJ. 1995. The astacin family of metalloendopeptidases. Protein Sci. 4:1247-1261
    • (1995) Protein Sci , vol.4 , pp. 1247-1261
    • Bond, J.S.1    Beynon, R.J.2
  • 11
    • 0027190974 scopus 로고
    • The CUB domain: A widespread module in developmentally regulated proteins
    • Bork P, Beckmann G. 1993. The CUB domain: A widespread module in developmentally regulated proteins. J Mol Biol. 231:539-545
    • (1993) J Mol Biol , vol.231 , pp. 539-545
    • Bork, P.1    Beckmann, G.2
  • 14
    • 54349118795 scopus 로고    scopus 로고
    • Transcriptome analysis revealed novel possible venom components and cellular processes of the tarantula Chilobrachys jingzhao venom gland
    • Chen J, Zhao L, Jiang L, Meng E, Zhang Y, Xiong X, Liang S. 2008. Transcriptome analysis revealed novel possible venom components and cellular processes of the tarantula Chilobrachys jingzhao venom gland. Toxicon 52:794-806
    • (2008) Toxicon , vol.52 , pp. 794-806
    • Chen, J.1    Zhao, L.2    Jiang, L.3    Meng, E.4    Zhang, Y.5    Xiong, X.6    Liang, S.7
  • 15
    • 79952439531 scopus 로고    scopus 로고
    • Identification and functional characterization of Dicer2 and five single VWC domain proteins of Litopenaeus vannamei
    • Chen Y-H, Jia X-T, Zhao L, Li C-Z, Zhang S, Chen Y-G, Weng S-P, He J-G. 2011. Identification and functional characterization of Dicer2 and five single VWC domain proteins of Litopenaeus vannamei. Dev Comp Immunol. 35:661-671
    • (2011) Dev Comp Immunol , vol.35 , pp. 661-671
    • Chen, Y.-H.1    Jia, X.-T.2    Zhao, L.3    Li, C.-Z.4    Zhang, S.5    Chen, Y.-G.6    Weng, S.-P.7    He, J.-G.8
  • 16
    • 0023814379 scopus 로고
    • Cloning the human lysozyme cDNA: Inverted Alu repeat in the mRNA and in situ hybridization for macrophages and Paneth cells
    • Chung LP, Keshav S, Gordon S. 1988. Cloning the human lysozyme cDNA: Inverted Alu repeat in the mRNA and in situ hybridization for macrophages and Paneth cells. Proc Natl Acad Sci U S A. 85: 6227-6231
    • (1988) Proc Natl Acad Sci U S A. , vol.85 , pp. 6227-6231
    • Chung, L.P.1    Keshav, S.2    Gordon, S.3
  • 17
    • 24644503098 scopus 로고    scopus 로고
    • Blast2GO: A universal tool for annotation, visualization and analysis in functional genomics research
    • Conesa A, Götz S, García-Gómez JM, Terol J, Talón M, Robles M. 2005. Blast2GO: A universal tool for annotation, visualization and analysis in functional genomics research. Bioinformatics 21:3674-3676
    • (2005) Bioinformatics , vol.21 , pp. 3674-3676
    • Conesa, A.1    Götz, S.2    García-Gómez, J.M.3    Terol, J.4    Talón, M.5    Robles, M.6
  • 19
  • 20
    • 0029020912 scopus 로고
    • Three-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptor
    • Daly NL, Scanlon MJ, Djordjevic JT, Kroon PA, Smith R. 1995. Three-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptor. Proc Natl Acad Sci U S A. 92: 6334-6338
    • (1995) Proc Natl Acad Sci U S A. , vol.92 , pp. 6334-6338
    • Daly, N.L.1    Scanlon, M.J.2    Djordjevic, J.T.3    Kroon, P.A.4    Smith, R.5
  • 21
    • 74549203358 scopus 로고    scopus 로고
    • Insights into the venom composition of the ectoparasitoid wasp Nasonia vitripennis from bioinformatic and proteomic studies
    • De Graaf DC, Aerts M, Brunain M, Desjardins CA, Jacobs FJ, Werren JH, Devreese B. 2010. Insights into the venom composition of the ectoparasitoid wasp Nasonia vitripennis from bioinformatic and proteomic studies. Insect Mol Biol. 19:11-26
    • (2010) Insect Mol Biol , vol.19 , pp. 11-26
    • De Graaf, D.C.1    Aerts, M.2    Brunain, M.3    Desjardins, C.A.4    Jacobs, F.J.5    Werren, J.H.6    Devreese, B.7
  • 22
    • 77953569982 scopus 로고    scopus 로고
    • The pharmacological role of nucleotidases in snake venoms
    • Dhananjaya BL, D'Souza CJM. 2010. The pharmacological role of nucleotidases in snake venoms. Cell Biochem Funct. 28:171-177
    • (2010) Cell Biochem Funct , vol.28 , pp. 171-177
    • Dhananjaya, B.L.1    D'Souza, C.J.M.2
  • 23
    • 84860570751 scopus 로고    scopus 로고
    • Comparative studies on the structure and development of the venom-delivery system of centipedes, and a hypothesis on the origin of this evolutionary novelty
    • Dugon MM, Arthur W. 2012. Comparative studies on the structure and development of the venom-delivery system of centipedes, and a hypothesis on the origin of this evolutionary novelty. Evol Dev. 14: 128-137
    • (2012) Evol Dev , vol.14 , pp. 128-137
    • Dugon, M.M.1    Arthur, W.2
  • 24
    • 84860560885 scopus 로고    scopus 로고
    • Variation and specialisation of the forcipular apparatus of centipedes (Arthropoda: Chilopoda): A comparative morphometric and microscopic investigation of an evolutionary novelty
    • Dugon MM, Black A, Arthur W. 2012. Variation and specialisation of the forcipular apparatus of centipedes (Arthropoda: Chilopoda): A comparative morphometric and microscopic investigation of an evolutionary novelty. Arthropod Struct Dev. 41:231-243
    • (2012) Arthropod Struct Dev , vol.41 , pp. 231-243
    • Dugon, M.M.1    Black, A.2    Arthur, W.3
  • 25
    • 33646133193 scopus 로고    scopus 로고
    • Venom landscapes: Mining the complexity of spider venoms via a combined cDNA and mass spectrometric approach
    • Escoubas P, Sollod B, King GF. 2006. Venom landscapes: Mining the complexity of spider venoms via a combined cDNA and mass spectrometric approach. Toxicon 47:650-663
    • (2006) Toxicon , vol.47 , pp. 650-663
    • Escoubas, P.1    Sollod, B.2    King, G.F.3
  • 28
    • 0037904919 scopus 로고    scopus 로고
    • Cloning of a salivary gland metalloprotease and characterization of gelatinase and fibrin( ogen)lytic activities in the saliva of the Lyme disease tick vector Ixodes scapularis
    • Francischetti IM, Mather TN, Ribeiro JM. 2003. Cloning of a salivary gland metalloprotease and characterization of gelatinase and fibrin( ogen)lytic activities in the saliva of the Lyme disease tick vector Ixodes scapularis. Biochem Biophys Res Commun. 305: 869-875
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 869-875
    • Francischetti, I.M.1    Mather, T.N.2    Ribeiro, J.M.3
  • 29
    • 15544369378 scopus 로고    scopus 로고
    • From genome to venome" molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins
    • Fry BG. 2005. From genome to "venome": Molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins. Genome Res. 15: 403-420
    • (2005) Genome Res , vol.15 , pp. 403-420
    • Fry, B.G.1
  • 31
    • 64949131873 scopus 로고    scopus 로고
    • Tentacles of venom: Toxic protein convergence in the kingdom Animalia
    • Fry BG, Roelants K, Norman J. 2009. Tentacles of venom: Toxic protein convergence in the kingdom Animalia. J Mol Evol. 68:311-321
    • (2009) J Mol Evol , vol.68 , pp. 311-321
    • Fry, B.G.1    Roelants, K.2    Norman, J.3
  • 33
    • 2342462926 scopus 로고    scopus 로고
    • Isolation and characterization of hyaluronidase a spreading factor" from Indian cobra (Naja naja) venom
    • Girish KS, Shashidharamurthy R, Nagaraju S, GowDa TV, Kemparaju K. 2004. Isolation and characterization of hyaluronidase a "spreading factor" from Indian cobra (Naja naja) venom. Biochimie 86: 193-202
    • (2004) Biochimie , vol.86 , pp. 193-202
    • Girish, K.S.1    Shashidharamurthy, R.2    Nagaraju, S.3    GowDa, T.V.4    Kemparaju, K.5
  • 34
    • 0020960765 scopus 로고
    • Isolation, purification and pharmacodynamics of a toxin from the venom of the centipede Scolopendra subspinipes dehaani Brandt
    • Gomes A, Datta A, Sarangi B, Kar PK, Lahiri SC. 1983. Isolation, purification and pharmacodynamics of a toxin from the venom of the centipede Scolopendra subspinipes dehaani Brandt. Indian J Exp Biol. 21:203-207
    • (1983) Indian J Exp Biol , vol.21 , pp. 203-207
    • Gomes, A.1    Datta, A.2    Sarangi, B.3    Kar, P.K.4    Lahiri, S.C.5
  • 35
    • 67349220716 scopus 로고    scopus 로고
    • Venom from the centipede Scolopendra viridis Say: Purification, gene cloning and phylogenetic analysis of a phospholipase A2
    • González-Morales L, Diego-GarcÌa E, Segovia L, Gutiérrez MdC, Possani LD. 2009. Venom from the centipede Scolopendra viridis Say: Purification, gene cloning and phylogenetic analysis of a phospholipase A2. Toxicon 54:8-15
    • (2009) Toxicon , vol.54 , pp. 8-15
    • González-Morales, L.1    Diego-GarcÌa, E.2    Segovia, L.3    Gutiérrez, M.D.C.4    Possani, L.D.5
  • 38
    • 0033731921 scopus 로고    scopus 로고
    • Snake venom metalloproteinases: Their role in the pathogenesis of local tissue damage
    • Gutiérrez JM, Rucavado A. 2000. Snake venom metalloproteinases: Their role in the pathogenesis of local tissue damage. Biochimie 82: 841-850
    • (2000) Biochimie , vol.82 , pp. 841-850
    • Gutiérrez, J.M.1    Rucavado, A.2
  • 39
    • 4444313548 scopus 로고    scopus 로고
    • A simplified procedure for the reduction and alkylation of cysteine residues in proteins prior to proteolytic digestion and mass spectral analysis
    • Hale JE, Butler JP, Gelfanova V, You JS, Knierman MD. 2004. A simplified procedure for the reduction and alkylation of cysteine residues in proteins prior to proteolytic digestion and mass spectral analysis. Anal Biochem. 333:174-181
    • (2004) Anal Biochem , vol.333 , pp. 174-181
    • Hale, J.E.1    Butler, J.P.2    Gelfanova, V.3    You, J.S.4    Knierman, M.D.5
  • 40
    • 0016371973 scopus 로고
    • Characteristics of an alkaline phosphatase activity in brown recluse venom
    • Heitz JR, Norment BR. 1974. Characteristics of an alkaline phosphatase activity in brown recluse venom. Toxicon 12:181-187
    • (1974) Toxicon , vol.12 , pp. 181-187
    • Heitz, J.R.1    Norment, B.R.2
  • 41
    • 17844365300 scopus 로고    scopus 로고
    • Ultrastructure of the epidermal maxilla II-gland of Scutigera coleoptrata (Chilopoda, Notostigmophora) and the ground pattern of epidermal gland organs in Myriapoda
    • Hilken G, Rosenberg J, Brockmann C. 2005. Ultrastructure of the epidermal maxilla II-gland of Scutigera coleoptrata (Chilopoda, Notostigmophora) and the ground pattern of epidermal gland organs in Myriapoda. J Morphol. 264:53-61
    • (2005) J Morphol , vol.264 , pp. 53-61
    • Hilken, G.1    Rosenberg, J.2    Brockmann, C.3
  • 42
    • 33646896936 scopus 로고    scopus 로고
    • Hymenoptera venom allergens
    • Hoffman D. 2006. Hymenoptera venom allergens. Clin Rev Allergy Immunol. 30:109-128
    • (2006) Clin Rev Allergy Immunol , vol.30 , pp. 109-128
    • Hoffman, D.1
  • 43
    • 79959658965 scopus 로고    scopus 로고
    • Cretaceous-Tertiary diversification among select Scolopendrid centipedes of South India
    • Joshi J, Karanth KP. 2011. Cretaceous-Tertiary diversification among select Scolopendrid centipedes of South India. Mol Phylogenet Evol. 60:287-294
    • (2011) Mol Phylogenet Evol , vol.60 , pp. 287-294
    • Joshi, J.1    Karanth, K.P.2
  • 45
    • 80053645532 scopus 로고    scopus 로고
    • Venoms as a platform for human drugs: Translating toxins into therapeutics
    • King GF. 2011. Venoms as a platform for human drugs: Translating toxins into therapeutics. Expert Opin Biol Ther. 11:1469-1484
    • (2011) Expert Opin Biol Ther , vol.11 , pp. 1469-1484
    • King, G.F.1
  • 46
    • 49449116956 scopus 로고    scopus 로고
    • A rational nomenclature for naming peptide toxins from spiders and other venomous animals
    • King GF, Gentz MC, Escoubas P, Nicholson GM. 2008. A rational nomenclature for naming peptide toxins from spiders and other venomous animals. Toxicon 52:264-276
    • (2008) Toxicon , vol.52 , pp. 264-276
    • King, G.F.1    Gentz, M.C.2    Escoubas, P.3    Nicholson, G.M.4
  • 47
    • 84872130087 scopus 로고    scopus 로고
    • Spider-venom peptides: Structure, pharmacology, and potential for control of insect pests
    • King GF, Hardy MC. 2013. Spider-venom peptides: Structure, pharmacology, and potential for control of insect pests. Annu Rev Entomol. 58:475-496
    • (2013) Annu Rev Entomol , vol.58 , pp. 475-496
    • King, G.F.1    Hardy, M.C.2
  • 48
    • 0036447597 scopus 로고    scopus 로고
    • Structure and function of insecticidal neurotoxins from Australian funnel-web spiders
    • King GF, Tedford HW, Maggio F. 2002. Structure and function of insecticidal neurotoxins from Australian funnel-web spiders. J Toxicol Toxin Rev. 21:359-389
    • (2002) J Toxicol Toxin Rev , vol.21 , pp. 359-389
    • King, G.F.1    Tedford, H.W.2    Maggio, F.3
  • 49
    • 79961087000 scopus 로고    scopus 로고
    • The aerolysin-like toxin family of cytolytic, pore-forming toxins
    • Knapp O, Stiles B, Popoff MR. 2010. The aerolysin-like toxin family of cytolytic, pore-forming toxins. Open Toxinol J. 3:53-68
    • (2010) Open Toxinol J. , vol.3 , pp. 53-68
    • Knapp, O.1    Stiles, B.2    Popoff, M.R.3
  • 50
    • 84970546336 scopus 로고
    • Revision of the Australian centipedes of the genus Cormocephalus Newport (Chilopoda: Scolopendridae: Scolopendrinae
    • Koch L. 1983a. Revision of the Australian centipedes of the genus Cormocephalus Newport (Chilopoda: Scolopendridae: Scolopendrinae). Aust J Zool. 31:799-833
    • (1983) Aust J Zool , vol.31 , pp. 799-833
    • Koch, L.1
  • 51
    • 84970549227 scopus 로고
    • A taxonomic study of the centipede genus Ethmostigmus Pocock (Chilopoda: Scolopendridae: Otostigminae) in Australia
    • Koch L. 1983b. A taxonomic study of the centipede genus Ethmostigmus Pocock (Chilopoda: Scolopendridae: Otostigminae) in Australia. Aust J Zool. 31:835-849
    • (1983) Aust J Zool , vol.31 , pp. 835-849
    • Koch, L.1
  • 52
    • 84971060150 scopus 로고
    • Morphological characters of Australian scolopendrid centipedes, and the taxonomy and distribution of Scolopendra morsitans L. (Chilopoda: Scolopendridae: Scolopendrinae
    • Koch LE. 1983c. Morphological characters of Australian scolopendrid centipedes, and the taxonomy and distribution of Scolopendra morsitans L. (Chilopoda: Scolopendridae: Scolopendrinae). Aust J Zool. 31:79-91
    • (1983) Aust J Zool , vol.31 , pp. 79-91
    • Koch, L.E.1
  • 53
    • 0344110241 scopus 로고    scopus 로고
    • Insect chitinases: Molecular biology and potential use as biopesticides
    • Kramer KJ, Muthukrishnan S. 1998. Insect chitinases: Molecular biology and potential use as biopesticides. Insect Biochem Mol Biol. 27: 887-900
    • (1998) Insect Biochem Mol Biol , vol.27 , pp. 887-900
    • Kramer, K.J.1    Muthukrishnan, S.2
  • 54
    • 1942534998 scopus 로고    scopus 로고
    • Biochemistry, toxicology and ecology of the venom of the spider Cupiennius salei (Ctenidae
    • Kuhn-Nentwig L, Schaller J, Nentwig W. 2004. Biochemistry, toxicology and ecology of the venom of the spider Cupiennius salei (Ctenidae). Toxicon 43:543-553
    • (2004) Toxicon , vol.43 , pp. 543-553
    • Kuhn-Nentwig, L.1    Schaller, J.2    Nentwig, W.3
  • 57
    • 0027972221 scopus 로고
    • Characteristics of hyaluronidase and hemolytic activity in fishing tentacle nematocyst venom of Chrysaora quinquecirrha
    • Long-Rowe KO, Burnett JW. 1994. Characteristics of hyaluronidase and hemolytic activity in fishing tentacle nematocyst venom of Chrysaora quinquecirrha. Toxicon 32:165-174
    • (1994) Toxicon , vol.32 , pp. 165-174
    • Long-Rowe, K.O.1    Burnett, J.W.2
  • 59
    • 84856322933 scopus 로고    scopus 로고
    • Extreme diversity of scorpion venom peptides and proteins revealed by transcriptomic analysis: Implication for proteome evolution of scorpion venom arsenal
    • Ma Y, He Y, Zhao R, Wu Y, Li W, Cao Z. 2012. Extreme diversity of scorpion venom peptides and proteins revealed by transcriptomic analysis: Implication for proteome evolution of scorpion venom arsenal. J Proteomics. 75:1563-1576
    • (2012) J Proteomics , vol.75 , pp. 1563-1576
    • Ma, Y.1    He, Y.2    Zhao, R.3    Wu, Y.4    Li, W.5    Cao, Z.6
  • 62
    • 1842552157 scopus 로고
    • Centipedes and centipede bites
    • McKeown KC. 1930. Centipedes and centipede bites. Aust Mus Mag. 4: 59-60
    • (1930) Aust Mus Mag , vol.4 , pp. 59-60
    • McKeown, K.C.1
  • 63
    • 0020965501 scopus 로고
    • Proteins, lipids, lipoproteins and some enzyme characterizations of the venom extract from the centipede Scolopendra morsitans
    • Mohamed AH, Abu-Sinna G, El-Shabaka HA, Abd El-Aal A. 1983. Proteins, lipids, lipoproteins and some enzyme characterizations of the venom extract from the centipede Scolopendra morsitans. Toxicon 21:371-377
    • (1983) Toxicon , vol.21 , pp. 371-377
    • Mohamed, A.H.1    Abu-Sinna, G.2    El-Shabaka, H.A.3    Abd El-Aal, A.4
  • 64
    • 84876164436 scopus 로고    scopus 로고
    • Analysis of soluble protein contents from the nematocysts of a model sea anemone sheds light on venom evolution
    • Moran Y, Praher D, Schlesinger A, Ayalon A, Tal Y, Technau U. 2013. Analysis of soluble protein contents from the nematocysts of a model sea anemone sheds light on venom evolution. Mar Biotechnol. 15:329-339
    • (2013) Mar Biotechnol , vol.15 , pp. 329-339
    • Moran, Y.1    Praher, D.2    Schlesinger, A.3    Ayalon, A.4    Tal, Y.5    Technau, U.6
  • 65
    • 84872144447 scopus 로고    scopus 로고
    • The venom optimization hypothesis revisited
    • Morgenstern D, King GF. 2013. The venom optimization hypothesis revisited. Toxicon 63:120-128
    • (2013) Toxicon , vol.63 , pp. 120-128
    • Morgenstern, D.1    King, G.F.2
  • 66
    • 77956230468 scopus 로고    scopus 로고
    • Including secondary structure, fossils and molecular dating in the centipede tree of life
    • Murienne J, Edgecombe GD, Giribet G. 2010. Including secondary structure, fossils and molecular dating in the centipede tree of life. Mol Phylogenet Evol. 57:301-313
    • (2010) Mol Phylogenet Evol , vol.57 , pp. 301-313
    • Murienne, J.1    Edgecombe, G.D.2    Giribet, G.3
  • 68
    • 84863780530 scopus 로고    scopus 로고
    • Development of a rational nomenclature for naming peptide and protein toxins from sea anemones
    • Oliveira JS, Fuentes-Silva D, King GF. 2012. Development of a rational nomenclature for naming peptide and protein toxins from sea anemones. Toxicon 60:539-550
    • (2012) Toxicon , vol.60 , pp. 539-550
    • Oliveira, J.S.1    Fuentes-Silva, D.2    King, G.F.3
  • 69
    • 0028090517 scopus 로고
    • A common structural motif incorporating a cystine knot and a triple-stranded b-sheet in toxic and inhibitory polypeptides
    • Pallaghy PK, Nielsen KJ, Craik DJ, Norton RS. 1994. A common structural motif incorporating a cystine knot and a triple-stranded b-sheet in toxic and inhibitory polypeptides. Protein Sci. 3: 1833-1839
    • (1994) Protein Sci , vol.3 , pp. 1833-1839
    • Pallaghy, P.K.1    Nielsen, K.J.2    Craik, D.J.3    Norton, R.S.4
  • 71
    • 72749107259 scopus 로고    scopus 로고
    • Two novel antimicrobial peptides from centipede venoms
    • Peng K, Kong Y, Zhai L, Wu X, Jia P, Liu J, Yu H. 2009. Two novel antimicrobial peptides from centipede venoms. Toxicon 55: 274-279
    • (2009) Toxicon , vol.55 , pp. 274-279
    • Peng, K.1    Kong, Y.2    Zhai, L.3    Wu, X.4    Jia, P.5    Liu, J.6    Yu, H.7
  • 73
    • 0002156649 scopus 로고
    • Insecticidal activity of spider (Araneae), centipede (Chilopoda), scorpion (Scorpionidae), and snake (Serpentes) venoms
    • Quistad GB, Dennis PA, Skinner WS. 1992. Insecticidal activity of spider (Araneae), centipede (Chilopoda), scorpion (Scorpionidae), and snake (Serpentes) venoms. J Econ Entomol. 85:33-39
    • (1992) J Econ Entomol , vol.85 , pp. 33-39
    • Quistad, G.B.1    Dennis, P.A.2    Skinner, W.S.3
  • 75
    • 34247200488 scopus 로고    scopus 로고
    • Venomic analyses of Scolopendra viridicornis nigra and Scolopendra angulata (Centipede, Scolopendromorpha): Shedding light on venoms from a neglected group
    • Rates B, Bemquerer MP, Richardson M, Borges MH, Morales RAV, De Lima ME, Pimenta A. 2007. Venomic analyses of Scolopendra viridicornis nigra and Scolopendra angulata (Centipede, Scolopendromorpha): Shedding light on venoms from a neglected group. Toxicon 49:810-826
    • (2007) Toxicon , vol.49 , pp. 810-826
    • Rates, B.1    Bemquerer, M.P.2    Richardson, M.3    Borges, M.H.4    Morales, R.A.V.5    De Lima, M.E.6    Pimenta, A.7
  • 76
    • 33745024525 scopus 로고    scopus 로고
    • Acid and alkaline phosphatase activities of a fraction isolated from Parawixia bistriata spider venom
    • Rodrigues MCA, Guimarães LHS, Liberato JL, Polizeli MdLTdM, dos Santos WF. 2006. Acid and alkaline phosphatase activities of a fraction isolated from Parawixia bistriata spider venom. Toxicon 47: 854-858
    • (2006) Toxicon , vol.47 , pp. 854-858
    • Rodrigues, M.C.A.1    Guimarães, L.H.S.2    Liberato, J.L.3    Polizeli, M.4    Dos Santos, W.F.5
  • 78
    • 64749096772 scopus 로고    scopus 로고
    • Fine structural organization of the poison gland of Lithobius forficatus (Chilopoda, Lithobiomorpha
    • Rosenberg J, Hilken G. 2006. Fine structural organization of the poison gland of Lithobius forficatus (Chilopoda, Lithobiomorpha). Nor J Entomol. 53:119-127
    • (2006) Nor J Entomol , vol.53 , pp. 119-127
    • Rosenberg, J.1    Hilken, G.2
  • 80
    • 0029240453 scopus 로고
    • Isolation, cloning and deduced amino acid sequence of a novel glycoprotein from the haemolymph of the hawkmoth Manduca sexta
    • Samaraweera P, Law JH. 1995. Isolation, cloning and deduced amino acid sequence of a novel glycoprotein from the haemolymph of the hawkmoth Manduca sexta. Insect Mol Biol. 4:7-13
    • (1995) Insect Mol Biol , vol.4 , pp. 7-13
    • Samaraweera, P.1    Law, J.H.2
  • 83
    • 0035424604 scopus 로고    scopus 로고
    • A novel superfamily of enzymes that catalyze the modification of guanidino groups
    • Shirai H, Blundell TL, Mizuguchi K. 2001. A novel superfamily of enzymes that catalyze the modification of guanidino groups. Trends Biochem Sci. 26:465-468
    • (2001) Trends Biochem Sci , vol.26 , pp. 465-468
    • Shirai, H.1    Blundell, T.L.2    Mizuguchi, K.3
  • 84
    • 0030896832 scopus 로고    scopus 로고
    • Subtilases: The superfamily of subtilisinlike serine proteases
    • Siezen RJ, Leunissen JAM. 1997. Subtilases: The superfamily of subtilisinlike serine proteases. Protein Sci. 6:501-523
    • (1997) Protein Sci , vol.6 , pp. 501-523
    • Siezen, R.J.1    Leunissen, J.A.M.2
  • 85
    • 67649414216 scopus 로고    scopus 로고
    • Cloning and characterization of cDNA sequences encoding for new venom peptides of the Brazilian scorpion Opisthacanthus cayaporum
    • Silva ÉCN, Camargos TS, Maranhão AQ, Silva-Pereira I, Silva LP, Possani LD, Schwartz EF. 2009. Cloning and characterization of cDNA sequences encoding for new venom peptides of the Brazilian scorpion Opisthacanthus cayaporum. Toxicon 54:252-261
    • (2009) Toxicon , vol.54 , pp. 252-261
    • Silvaé, C.N.1    Camargos, T.S.2    Maranhão, A.Q.3    Silva-Pereira, I.4    Silva, L.P.5    Possani, L.D.6    Schwartz, E.F.7
  • 87
    • 0033020821 scopus 로고    scopus 로고
    • Effects of a centipede venom fraction on insect nervous system, a native Xenopus oocyte receptor and on an expressed Drosophila muscarinic receptor
    • Stankiewicz M, Hamon A, Benkhalifa R, Kadziela W, Hue B, Lucas S, Mebs D, Pelhate M. 1999. Effects of a centipede venom fraction on insect nervous system, a native Xenopus oocyte receptor and on an expressed Drosophila muscarinic receptor. Toxicon 37: 1431-1445
    • (1999) Toxicon , vol.37 , pp. 1431-1445
    • Stankiewicz, M.1    Hamon, A.2    Benkhalifa, R.3    Kadziela, W.4    Hue, B.5    Lucas, S.6    Mebs, D.7    Pelhate, M.8
  • 88
    • 73649209802 scopus 로고
    • A specific and nonspecific alkalinemonophosphatase in the venom of Bothrops atrox and their occurrence in the purified venom phosphodiesterase
    • Sulkowski E, Björk W, Laskowski M. 1963. A specific and nonspecific alkalinemonophosphatase in the venom of Bothrops atrox and their occurrence in the purified venom phosphodiesterase. J Biol Chem. 238:2477-2486
    • (1963) J Biol Chem , vol.238 , pp. 2477-2486
    • Sulkowski, E.1    Björk, W.2    Laskowski, M.3
  • 90
    • 0013866250 scopus 로고
    • Acid and alkaline phosphomonoesterase activities in snake venoms
    • Tu AT, Chua A. 1966. Acid and alkaline phosphomonoesterase activities in snake venoms. Comp Biochem Physiol. 17:297-307
    • (1966) Comp Biochem Physiol , vol.17 , pp. 297-307
    • Tu, A.T.1    Chua, A.2
  • 92
    • 79952363866 scopus 로고    scopus 로고
    • On the venom system of centipedes (Chilopoda), a neglected group of venomous animals
    • Undheim EAB, King GF. 2011. On the venom system of centipedes (Chilopoda), a neglected group of venomous animals. Toxicon 57: 512-524
    • (2011) Toxicon , vol.57 , pp. 512-524
    • Undheim, E.A.B.1    King, G.F.2
  • 99
    • 0025342986 scopus 로고
    • Constant and hypervariable regions in conotoxin propeptides
    • Woodward SR, Cruz LJ, Olivera BM, Hillyard DR. 1990. Constant and hypervariable regions in conotoxin propeptides. EMBO J. 9: 1015-1020
    • (1990) EMBO J. , vol.9 , pp. 1015-1020
    • Woodward, S.R.1    Cruz, L.J.2    Olivera, B.M.3    Hillyard, D.R.4
  • 101
    • 0034800374 scopus 로고    scopus 로고
    • InterProScan-An integration platform for the signature-recognition methods in InterPro
    • Zdobnov EM, Apweiler R. 2001. InterProScan-An integration platform for the signature-recognition methods in InterPro. Bioinformatics 17: 847-848.
    • (2001) Bioinformatics , vol.17 , pp. 847-848
    • Zdobnov, E.M.1    Apweiler, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.