메뉴 건너뛰기




Volumn 85, Issue 4, 2011, Pages 305-313

Characterization of toxins from the broad-banded water snake Helicops angulatus (Linnaeus, 1758): Isolation of a cysteine-rich secretory protein, Helicopsin

Author keywords

Broad banded water snake; Colubroidea; CRISP; Dipsadidae salivary excretion; Helicops angulatus; Neurotoxin

Indexed keywords

HELICOPSIN; SECRETORY PROTEIN; SNAKE VENOM; UNCLASSIFIED DRUG;

EID: 79954418536     PISSN: 03405761     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00204-010-0597-6     Document Type: Article
Times cited : (26)

References (44)
  • 1
    • 0003746046 scopus 로고
    • Principles of laboratory animal care
    • Anonymous, Pub. 85 No 23, USA
    • Anonymous (1985) Principles of laboratory animal care. National Institute of Health, Pub. 85 No 23, USA
    • (1985) National Institute of Health
  • 2
    • 0004202155 scopus 로고
    • AOAC INTERNATIONAL. In: Cunniff P (ed), Arlington, VA, sec. 991.31
    • AOAC INTERNATIONAL (1995) Official methods of analysis. In: Cunniff P (ed), Arlington, VA, sec. 991.31
    • (1995) Official Methods of Analysis
  • 3
    • 67049132403 scopus 로고    scopus 로고
    • Exploring the venom proteome of the Western diamondback rattlesnake, Crotalus atrox, via snake venomics and combinatorial peptide ligand library approaches
    • 19371136 10.1021/pr900249q 1:CAS:528:DC%2BD1MXlsF2hsro%3D
    • JJ Calvete E Fasoli L Sanz E Boschetti PG Righetti 2009 Exploring the venom proteome of the Western diamondback rattlesnake, Crotalus atrox, via snake venomics and combinatorial peptide ligand library approaches J Proteome Res 8 3055 3067 19371136 10.1021/pr900249q 1:CAS:528:DC%2BD1MXlsF2hsro%3D
    • (2009) J Proteome Res , vol.8 , pp. 3055-3067
    • Calvete, J.J.1    Fasoli, E.2    Sanz, L.3    Boschetti, E.4    Righetti, P.G.5
  • 4
    • 0017067054 scopus 로고
    • Androgen-controlled specific proteins in rat epididymis
    • 10.1677/joe.0.0690047
    • MS Cameo JA Blaquier 1976 Androgen-controlled specific proteins in rat epididymis J Endocrinol 69 317 324 10.1677/joe.0.0690047
    • (1976) J Endocrinol , vol.69 , pp. 317-324
    • Cameo, M.S.1    Blaquier, J.A.2
  • 7
    • 33748061640 scopus 로고    scopus 로고
    • Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family
    • DOI 10.1016/j.ydbio.2006.05.013, PII S0012160606008013
    • DA Ellerman DJ Cohen VG Da Ros MM Morgenfeld D Busso PS Cuasnicú 2006 Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family Dev Biol 297 228 237 16872593 10.1016/j.ydbio.2006.05.013 1:CAS:528:DC%2BD28XptFSqtrw%3D (Pubitemid 44301105)
    • (2006) Developmental Biology , vol.297 , Issue.1 , pp. 228-237
    • Ellerman, D.A.1    Cohen, D.J.2    Da Ros, V.G.3    Morgenfeld, M.M.4    Busso, D.5    Cuasnicu, P.S.6
  • 8
    • 66149091950 scopus 로고    scopus 로고
    • Improved electrospray ionization efficiency compensates for diminished chromatographic resolution and enables proteomics analysis of tyrosine signaling in embryonic stem cells
    • 19331382 10.1021/ac802720e 1:CAS:528:DC%2BD1MXkvVartrw%3D
    • SB Ficarro Y Zhang Y Lu AR Moghimi M Askenazi E Hyatt ED Smith L Boyer TM Schlaeger CJ Luckey JA Marto 2009 Improved electrospray ionization efficiency compensates for diminished chromatographic resolution and enables proteomics analysis of tyrosine signaling in embryonic stem cells Anal Chem 81 3440 3447 19331382 10.1021/ac802720e 1:CAS:528:DC%2BD1MXkvVartrw%3D
    • (2009) Anal Chem , vol.81 , pp. 3440-3447
    • Ficarro, S.B.1    Zhang, Y.2    Lu, Y.3    Moghimi, A.R.4    Askenazi, M.5    Hyatt, E.6    Smith, E.D.7    Boyer, L.8    Schlaeger, T.M.9    Luckey, C.J.10    Marto, J.A.11
  • 9
    • 31344440692 scopus 로고    scopus 로고
    • Notes on the ecology of the South American water snake Helicops angulatus (Squamata: Colubridae) in Nariva Swamp, Trinidad
    • NB Ford DF Ford 2002 Notes on the ecology of the South American water snake Helicops angulatus (Squamata: Colubridae) in Nariva Swamp, Trinidad Carib J Sci 38 129 131
    • (2002) Carib J Sci , vol.38 , pp. 129-131
    • Ford, N.B.1    Ford, D.F.2
  • 10
    • 0028270942 scopus 로고
    • Detection of type A, B, and E botulism neurotoxin genes in Clostridium botulinum and other Clostridium species by PCR: Evidence of unexpressed type B toxin genes in type A toxigenic organisms
    • G Franciosa JL Ferreira CL Hatheway 1994 Detection of type A, B, and E botulism neurotoxin genes in Clostridium botulinum and other Clostridial species by PCR: evidence of unexpressed type B toxin genes in type A toxigenic organisms J Clin Microbiol 32 1911 1917 7989542 1:CAS:528:DyaK2MXkvVCkug%3D%3D (Pubitemid 24222270)
    • (1994) Journal of Clinical Microbiology , vol.32 , Issue.8 , pp. 1911-1917
    • Franciosa, G.1    Ferreira, J.L.2    Hatheway, C.L.3
  • 11
    • 1942533494 scopus 로고    scopus 로고
    • Assembling an Arsenal: Origin and Evolution of the Snake Venom Proteome Inferred from Phylogenetic Analysis of Toxin Sequences
    • DOI 10.1093/molbev/msh091
    • BG Fry W Wüster 2004 Assembling an arsenal: origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences Mol Biol Evol 21 870 883 15014162 10.1093/molbev/msh091 1:CAS:528: DC%2BD2cXjsFyqsrY%3D (Pubitemid 38529729)
    • (2004) Molecular Biology and Evolution , vol.21 , Issue.5 , pp. 870-883
    • Fry, B.G.1    Wuster, W.2
  • 15
    • 38449098244 scopus 로고    scopus 로고
    • Cysteine rich secretory proteins in reproduction and venom
    • 17644967 1:CAS:528:DC%2BD1cXpvVyrt7c%3D
    • GM Gibbs MK O'Bryan 2007 Cysteine rich secretory proteins in reproduction and venom Soc Reprod Fertil Suppl 65 261 267 17644967 1:CAS:528: DC%2BD1cXpvVyrt7c%3D
    • (2007) Soc Reprod Fertil Suppl , vol.65 , pp. 261-267
    • Gibbs, G.M.1    O'Bryan, M.K.2
  • 16
    • 57349149450 scopus 로고    scopus 로고
    • The CAP superfamily: Cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins-roles in reproduction, cancer and immune defense
    • 10.1210/er.2008-0032 1:CAS:528:DC%2BD1MXmt1yjtA%3D%3D
    • GM Gibbs K Roelants MK O'Bryan 2008 The CAP superfamily: cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins-roles in reproduction, cancer and immune defense Endocrine Rev 29 865 897 10.1210/er.2008-0032 1:CAS:528:DC%2BD1MXmt1yjtA%3D%3D
    • (2008) Endocrine Rev , vol.29 , pp. 865-897
    • Gibbs, G.M.1    Roelants, K.2    O'Bryan, M.K.3
  • 17
    • 16844376656 scopus 로고    scopus 로고
    • Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K+ channel inhibitor-like fold
    • 15596436 10.1074/jbc.M413566200 1:CAS:528:DC%2BD2MXislyhtLk%3D
    • M Guo M Teng L Niu Q Liu Q Huang Q Hao 2005 Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K+ channel inhibitor-like fold J Biol Chem 280 12405 12412 15596436 10.1074/jbc.M413566200 1:CAS:528:DC%2BD2MXislyhtLk%3D
    • (2005) J Biol Chem , vol.280 , pp. 12405-12412
    • Guo, M.1    Teng, M.2    Niu, L.3    Liu, Q.4    Huang, Q.5    Hao, Q.6
  • 18
    • 0022354215 scopus 로고
    • Neutralization of proteolytic and hemorrhagic activities of Costa Rican snake venoms by a polyvalent antivenom
    • DOI 10.1016/0041-0101(85)90380-0
    • JM Gutiérrez JA Gené G Rojas L Cerdas 1985 Neutralization of proteolytic and hemorrhagic activities of Costa Rican snake venoms by a polyvalent antivenom Toxicon 23 887 893 3913055 10.1016/0041-0101(85)90380-0 (Pubitemid 16207989)
    • (1985) Toxicon , vol.23 , Issue.6 , pp. 887-893
    • Gutierrez, J.M.1    Gene, J.A.2    Rojas, G.3    Cerdas, L.4
  • 19
    • 0017729725 scopus 로고
    • The mode of action at the mouse neuromuscular junction of the phospholipase A-crotapotin complex isolated from venom of the South American rattlesnake
    • BJ Hawgood JW Smith 1977 The mode of action at the mouse neuromuscular junction of the phospholipase A-crotapotin complex isolated from venom of the South American rattlesnake Br J Pharmacol 61 597 606 202359 1:CAS:528: DyaE1cXhtFKjurk%3D (Pubitemid 8233442)
    • (1977) British Journal of Pharmacology , vol.61 , Issue.4 , pp. 597-606
    • Hawgood, B.J.1    Smith, J.W.2
  • 20
    • 0036628335 scopus 로고    scopus 로고
    • Conus peptides and neuroprotection
    • CE Heading 2002 Conus peptides and neuroprotection Curr Opin Investig Drugs 3 915 920 12137413 1:CAS:528:DC%2BD38XlvVWgu78%3D (Pubitemid 36266811)
    • (2002) Current Opinion in Investigational Drugs , vol.3 , Issue.6 , pp. 915-920
    • Heading, C.E.1
  • 21
    • 80052828618 scopus 로고    scopus 로고
    • Cysteine-rich proteins in reptile secretory venoms
    • S.P. Mackessy (eds). CRC Press, Taylor and Francis Group USA
    • Heyborne WH, Mackessy SP (2009) Cysteine-rich proteins in reptile secretory venoms. In: Mackessy SP (ed) Handbook of venoms and toxins of reptiles. CRC Press, Taylor and Francis Group, USA
    • (2009) Handbook of Venoms and Toxins of Reptiles
    • Heyborne, W.H.1    MacKessy, S.P.2
  • 22
    • 0034594348 scopus 로고    scopus 로고
    • Characterization of venom (Duvernoy's secretion) from twelve species of colubrid snakes and partial sequence of four venom proteins
    • DOI 10.1016/S0041-0101(00)00091-X, PII S004101010000091X
    • RE Hill SP Mackessy 2000 Characterization of venom (Duvernoy's secretion) from twelve species of colubrid snakes and partial sequence of four venom proteins Toxicon 38 1663 1687 10858509 10.1016/S0041-0101(00)00091-X 1:CAS:528:DC%2BD3cXlslyqt70%3D (Pubitemid 30349121)
    • (2000) Toxicon , vol.38 , Issue.12 , pp. 1663-1687
    • Hill, R.E.1    Mackessy, S.P.2
  • 23
    • 0019167491 scopus 로고
    • Comparative study on hemorrhagic and proteolytic activities of snake venoms
    • DOI 10.1016/0041-0101(80)90049-5
    • SY Huang JC Perez 1980 Comparative study on hemorrhagic and proteolytic activities of snake venoms Toxicon 18 421 426 7010684 10.1016/0041-0101(80) 90049-5 1:CAS:528:DyaL3MXpslGmsA%3D%3D (Pubitemid 11207065)
    • (1980) Toxicon , vol.18 , Issue.4 , pp. 421-426
    • Huang, S.Y.1    Perez, J.C.2
  • 24
    • 0019547287 scopus 로고
    • Isolation, culture, and immunocytochemical characterization of epididymal epithelial cells from pubertal and adult rats
    • 7015341 10.1073/pnas.78.3.1675 1:CAS:528:DyaL3MXhslajsbg%3D
    • AL Kierszenbaum O Lea P Petrusz FS French LL Tres 1981 Isolation, culture, and immunocytochemical characterization of epididymal epithelial cells from pubertal and adult rats Proc Natl Acad Sci USA 78 1675 1679 7015341 10.1073/pnas.78.3.1675 1:CAS:528:DyaL3MXhslajsbg%3D
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 1675-1679
    • Kierszenbaum, A.L.1    Lea, O.2    Petrusz, P.3    French, F.S.4    Tres, L.L.5
  • 25
    • 21944450300 scopus 로고    scopus 로고
    • Phylogenetic relationships of colubroid snakes based on mitochondrial DNA sequences
    • DOI 10.1006/zjls.1997.0097
    • F Kraus WM Brown 1998 Phylogenetic relationships of colubroid snakes based on mitochondrial DNA sequences Zool J Linn Soc 122 455 487 10.1111/j.1096-3642.1998.tb02159.x (Pubitemid 128052060)
    • (1998) Zoological Journal of the Linnean Society , vol.122 , Issue.3 , pp. 455-487
    • Kraus, F.1    Brown, W.M.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 5432063 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • UK Laemmli 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 680 685 5432063 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 2442423893 scopus 로고    scopus 로고
    • Haemorrhagic, proteolytic and neurotoxic activities produced by Duvernoy's gland secretion from the false coral snake (Erythrolamprus bizona Jan 1863) (Serpentes:Colubridae)
    • K Lemoine A Rodríguez-Acosta 2003 Hemorrhagic, proteolytic and neurotoxic activities produced by the false coral snake (Erythrolamprus Bizona Jan 1863) (Serpentes: Colubridae) Duvernoy's gland secretion Rev Cient FCV-LUZ 13 371 377 (Pubitemid 38650714)
    • (2003) Revista Cientifica de la Facultad de Ciencias Veterinarias de la Universidad del Zulia , vol.13 , Issue.5 , pp. 371-377
    • Lemoine, K.1    Rodriguez-Acosta, A.2
  • 28
    • 0345742546 scopus 로고    scopus 로고
    • Neurotoxic, haemorrhagic and proteolytic activities caused by Thamnodynastes strigilis (Serpentes: Colubridae) Duvernoy's gland secretion
    • 14748408 1:STN:280:DC%2BD2c%2FkslGjtw%3D%3D
    • K Lemoine LM Salgueiro A Rodríguez-Acosta. 2004 Neurotoxic, haemorrhagic and proteolytic activities caused by Thamnodynastes strigilis (Serpentes: Colubridae) Duvernoy's gland secretion Vet Hum Toxicol 46 10 14 14748408 1:STN:280:DC%2BD2c%2FkslGjtw%3D%3D
    • (2004) Vet Hum Toxicol , vol.46 , pp. 10-14
    • Lemoine, K.1    Salgueiro, L.M.2    Rodríguez-Acosta, A.3
  • 29
    • 2942621857 scopus 로고    scopus 로고
    • Proteolytic, hemorrhagic, and neurotoxic activities caused by Leptodeira annulata ashmeadii (Serpentes: Colubridae) Duvernoy's gland secretion
    • K Lemoine ME Girón I Aguilar LF Navarrete A Rodríguez- Acosta 2004 Proteolytic, haemorrhagic and neurotoxic activities caused by Leptodeira annulata ashmeadii (Serpentes: Colubridae) Duvernoy's gland secretion J Wild Env Med 15 82 89 10.1580/1080-6032(2004)015[0082:PHANAC]2.0.CO;2 (Pubitemid 38758560)
    • (2004) Wilderness and Environmental Medicine , vol.15 , Issue.2 , pp. 82-89
    • Lemoine, K.1    Giron, M.E.2    Aguilar, I.3    Navarrete, L.F.4    Rodriguez-Acosta, A.5
  • 30
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • 14907713 1:CAS:528:DyaG38XhsVyrsw%3D%3D
    • OH Lowry NJ Rosebrough AL Farr RJ Randall 1951 Protein measurement with the Folin phenol reagent J Biol Chem 193 265 275 14907713 1:CAS:528: DyaG38XhsVyrsw%3D%3D
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3    Randall, R.J.4
  • 31
    • 0036298002 scopus 로고    scopus 로고
    • Biochemistry and pharmacology of colubrid snake venoms
    • 1:CAS:528:DC%2BD38XlslCksL8%3D
    • SP Mackessy 2002 Biochemistry and pharmacology of colubrid snake venoms J Toxicol Toxin Rev 21 43 83 1:CAS:528:DC%2BD38XlslCksL8%3D
    • (2002) J Toxicol Toxin Rev , vol.21 , pp. 43-83
    • MacKessy, S.P.1
  • 32
    • 33645969259 scopus 로고    scopus 로고
    • Venom of the Brown Treesnake, Boiga irregularis: Ontogenetic shifts and taxa-specific toxicity
    • 16545413 10.1016/j.toxicon.2006.01.007 1:CAS:528:DC%2BD28XjsFaqt7o%3D
    • SP Mackessy NM Sixberry WH Heyborne T Fritts 2006 Venom of the Brown Treesnake, Boiga irregularis: ontogenetic shifts and taxa-specific toxicity Toxicon 47 537 548 16545413 10.1016/j.toxicon.2006.01.007 1:CAS:528: DC%2BD28XjsFaqt7o%3D
    • (2006) Toxicon , vol.47 , pp. 537-548
    • MacKessy, S.P.1    Sixberry, N.M.2    Heyborne, W.H.3    Fritts, T.4
  • 33
    • 0025259449 scopus 로고
    • Isolation and characterization of helothermine, a novel toxin from Heloderma horridum horridum (mexican beaded lizard) venom
    • DOI 10.1016/0041-0101(90)90065-F
    • J Mochca-Morales BM Martin LD Possani 1990 Isolation and characterization of helothermine, a novel toxin from Heloderma horridum horridum (Mexican beaded lizard) venom Toxicon 28 299 309 1693019 10.1016/0041-0101(90)90065-F 1:CAS:528:DyaK3cXktF2hs7k%3D (Pubitemid 20156685)
    • (1990) Toxicon , vol.28 , Issue.3 , pp. 299-309
    • Morales-Mochca, J.1    Martin, B.M.2    Possani, L.D.3
  • 36
    • 34447639424 scopus 로고    scopus 로고
    • Proteins, lethality and in vivo effects of Iurus dufoureius asiaticus scorpion venom
    • DOI 10.1016/j.toxicon.2007.04.010, PII S0041010107001511
    • O Ozkan G Ciftci GZ Pekmezci S Kar H Uysal KZ Karaer 2007 Proteins, lethality and in vivo effects of Iurus dufoureius asiaticus scorpion venom Toxicon 50 394 399 17532357 10.1016/j.toxicon.2007.04.010 1:CAS:528: DC%2BD2sXot1Cns7c%3D (Pubitemid 47094882)
    • (2007) Toxicon , vol.50 , Issue.3 , pp. 394-399
    • Ozkan, O.1    Ciftci, G.2    Pekmezci, G.Z.3    Kar, S.4    Uysal, H.5    Karaer, K.Z.6
  • 38
    • 39349112321 scopus 로고    scopus 로고
    • Presynaptic neurotoxins with enzymatic activities
    • 18064414 10.1007/978-3-540-74805-2-6 1:CAS:528:DC%2BD1cXitlWrtbs%3D
    • O Rossetto C Montecucco 2008 Presynaptic neurotoxins with enzymatic activities Handb Exp Pharmacol 184 129 170 18064414 10.1007/978-3-540-74805-2-6 1:CAS:528:DC%2BD1cXitlWrtbs%3D
    • (2008) Handb Exp Pharmacol , vol.184 , pp. 129-170
    • Rossetto, O.1    Montecucco, C.2
  • 39
    • 2542484781 scopus 로고
    • Alternative methods of analysis for quantal responses, 2nd ed
    • D. Finney (eds). Charles Griffin London
    • Spearman-Karber R (1964) Alternative methods of analysis for quantal responses, 2nd ed. In: Finney D (ed) Statistical method in biological assay. Charles Griffin, London
    • (1964) Statistical Method in Biological Assay
    • Spearman-Karber, R.1
  • 40
    • 0029878263 scopus 로고    scopus 로고
    • Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone
    • DOI 10.1038/nsb0496-317
    • JE Tudor PK Pallaghy MW Pennington RS Norton 1996 Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone Nat Struct Biol 3 317 320 8599755 10.1038/nsb0496-317 1:CAS:528:DyaK28XitFantbs%3D (Pubitemid 26112627)
    • (1996) Nature Structural Biology , vol.3 , Issue.4 , pp. 317-320
    • Tudor, J.E.1    Pallaghy, P.K.2    Pennington, M.W.3    Norton, R.S.4
  • 41
    • 4043092774 scopus 로고    scopus 로고
    • Structure and function of snake venom cysteine-rich secretory proteins
    • DOI 10.1016/j.toxicon.2004.05.023, PII S0041010104002090
    • Y Yamazaki T Morita 2004 Structure and biology of snake venom cysteine-rich secretory proteins Toxicon 44 227 231 15302528 10.1016/j.toxicon.2004.05.023 1:CAS:528:DC%2BD2cXmtlOksr4%3D (Pubitemid 39078338)
    • (2004) Toxicon , vol.44 , Issue.3 , pp. 227-231
    • Yamazaki, Y.1    Morita, T.2
  • 42
    • 38449104703 scopus 로고    scopus 로고
    • Snake venom components affecting blood coagulation and the vascular system: Structural similarities and marked diversity
    • DOI 10.2174/138161207782023775
    • Y Yamazaki T Morita 2007 Snake venom components affecting blood coagulation and the vascular system: structural similarities and marked diversity Curr Pharm Des 13 2872 2886 17979732 10.2174/138161207782023775 1:CAS:528:DC%2BD2sXhtFGmt7rP (Pubitemid 351545890)
    • (2007) Current Pharmaceutical Design , vol.13 , Issue.28 , pp. 2872-2886
    • Yamazaki, Y.1    Morita, T.2
  • 43
    • 0037167616 scopus 로고    scopus 로고
    • Purification and cloning of toxins from elapid venoms that target cyclic nucleotide-gated ion channels
    • 12234174 10.1021/bi026132h 1:CAS:528:DC%2BD38XmsVOjur0%3D
    • Y Yamazaki RL Brown T Morita 2002 Purification and cloning of toxins from elapid venoms that target cyclic nucleotide-gated ion channels Biochemistry 41 11331 11337 12234174 10.1021/bi026132h 1:CAS:528:DC%2BD38XmsVOjur0%3D
    • (2002) Biochemistry , vol.41 , pp. 11331-11337
    • Yamazaki, Y.1    Brown, R.L.2    Morita, T.3
  • 44
    • 65349176393 scopus 로고    scopus 로고
    • Molecular phylogeny of advanced snakes (Serpentes-Caenophidia) with an emphasis on South American Xenodontines: A revised classification and descriptions of new taxa
    • H Zaher F Gobbi-Grazziotin JE Cadle RW Murphy JC de Moura-Leite SL Bonatto 2009 Molecular phylogeny of advanced snakes (Serpentes-Caenophidia) with an emphasis on South American Xenodontines: a revised classification and descriptions of new taxa Pap Avulsos Zool 49 115 153
    • (2009) Pap Avulsos Zool , vol.49 , pp. 115-153
    • Zaher, H.1    Gobbi-Grazziotin, F.2    Cadle, J.E.3    Murphy, R.W.4    De Moura-Leite, J.C.5    Bonatto, S.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.