메뉴 건너뛰기




Volumn 79, Issue 1, 2011, Pages 61-78

Structural, functional, and bioinformatics studies reveal a new snake venom homologue phospholipase A 2 class

Author keywords

Calcium imaging; Myotoxin; Myotube cell culture; Phospholipase A 2; Phylogenetic analysis; X ray crystallography

Indexed keywords

ASPARTIC ACID 49 PHOSPHOLIPASE A2; PHOSPHOLIPASE A2; SNAKE VENOM; UNCLASSIFIED DRUG;

EID: 78649775567     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22858     Document Type: Article
Times cited : (44)

References (108)
  • 1
    • 4243499480 scopus 로고
    • Hydrolysis of synthetic mixed-acid phosphatides by phospholipase A from human pancreas
    • van Deenen LLM, de Haas GH, Heemskerk CHT. Hydrolysis of synthetic mixed-acid phosphatides by phospholipase A from human pancreas. Biochim Biophys Acta 1963; 67: 295-304.
    • (1963) Biochim Biophys Acta , vol.67 , pp. 295-304
    • van Deenen, L.L.M.1    de Haas, G.H.2    Heemskerk, C.H.T.3
  • 2
    • 0032952704 scopus 로고    scopus 로고
    • Mechanisms of cellular uptake of long chain free fatty acids
    • Berk PD, Stump DD. Mechanisms of cellular uptake of long chain free fatty acids. Mol Cell Biochem 1999; 192: 17-31.
    • (1999) Mol Cell Biochem , vol.192 , pp. 17-31
    • Berk, P.D.1    Stump, D.D.2
  • 3
    • 0033023923 scopus 로고    scopus 로고
    • Regulation of arachidonic acid release and cytosolic phospholipase A2 activation
    • Gijon MA, Leslie CC. Regulation of arachidonic acid release and cytosolic phospholipase A2 activation. J Leukoc Biol 1999; 65: 330-336.
    • (1999) J Leukoc Biol , vol.65 , pp. 330-336
    • Gijon, M.A.1    Leslie, C.C.2
  • 4
    • 0032708511 scopus 로고    scopus 로고
    • Insight into prostaglandin, leukotriene, and other eicosanoid functions using mice with targeted gene disruptions
    • Austin SC, Funk CD. Insight into prostaglandin, leukotriene, and other eicosanoid functions using mice with targeted gene disruptions. Prostaglandins Other Lipid Mediat 1999; 58: 231-252.
    • (1999) Prostaglandins Other Lipid Mediat , vol.58 , pp. 231-252
    • Austin, S.C.1    Funk, C.D.2
  • 5
    • 0033219838 scopus 로고    scopus 로고
    • Phospholipase A2 enzymes in eicosanoid generation
    • Bingham CO, III, Austen KF. Phospholipase A2 enzymes in eicosanoid generation. Proc Assoc Am Physicians 1999; 111: 516-524.
    • (1999) Proc Assoc Am Physicians , vol.111 , pp. 516-524
    • Bingham III, C.O.1    Austen, K.F.2
  • 6
    • 0034698035 scopus 로고    scopus 로고
    • Identification of a third pathway for arachidonic acid mobilization and prostaglandin production in activated P388D1 macrophage-like cells
    • Balsinde J, Balboa MA, Dennis EA. Identification of a third pathway for arachidonic acid mobilization and prostaglandin production in activated P388D1 macrophage-like cells. J Biol Chem 2000; 275: 22544-22549.
    • (2000) J Biol Chem , vol.275 , pp. 22544-22549
    • Balsinde, J.1    Balboa, M.A.2    Dennis, E.A.3
  • 8
    • 0030201175 scopus 로고    scopus 로고
    • Phospholipase A2-a structural review
    • Arni RK, Ward RJ. Phospholipase A2-a structural review. Toxicon 1996; 34: 827-841.
    • (1996) Toxicon , vol.34 , pp. 827-841
    • Arni, R.K.1    Ward, R.J.2
  • 9
    • 0023914394 scopus 로고
    • Crystal-structure of bovine pancreatic phospholipase-A2 covalently inhibited by para-bromo-phenacyl-bromide
    • Renetseder R, Dijkstra BW, Huizinga K, Kalk KH, Drenth J. Crystal-structure of bovine pancreatic phospholipase-A2 covalently inhibited by para-bromo-phenacyl-bromide. J Mol Biol 1988; 200: 181-188.
    • (1988) J Mol Biol , vol.200 , pp. 181-188
    • Renetseder, R.1    Dijkstra, B.W.2    Huizinga, K.3    Kalk, K.H.4    Drenth, J.5
  • 10
    • 0027248903 scopus 로고
    • The divalent cation is obligatory for the binding of ligands to the catalytic site of secreted phospholipase A2
    • Yu BZ, Berg OG, Jain MK. The divalent cation is obligatory for the binding of ligands to the catalytic site of secreted phospholipase A2. Biochemistry 1993; 32: 6485-6492.
    • (1993) Biochemistry , vol.32 , pp. 6485-6492
    • Yu, B.Z.1    Berg, O.G.2    Jain, M.K.3
  • 11
    • 0034739463 scopus 로고    scopus 로고
    • The expanding superfamily of phospholipase A(2) enzymes: classification and characterization
    • Six DA, Dennis EA. The expanding superfamily of phospholipase A(2) enzymes: classification and characterization. Biochim Biophys Acta 2000; 1488: 1-19.
    • (2000) Biochim Biophys Acta , vol.1488 , pp. 1-19
    • Six, D.A.1    Dennis, E.A.2
  • 13
    • 0025608353 scopus 로고
    • Crystal structure of cobra-venom phospholipase A2 in a complex with a transition-state analogue
    • White SP, Scott DL, Otwinowski Z, Gelb MH, Sigler PB. Crystal structure of cobra-venom phospholipase A2 in a complex with a transition-state analogue. Science 1990; 250: 1560-1563.
    • (1990) Science , vol.250 , pp. 1560-1563
    • White, S.P.1    Scott, D.L.2    Otwinowski, Z.3    Gelb, M.H.4    Sigler, P.B.5
  • 15
    • 33751028489 scopus 로고    scopus 로고
    • The phospholipase A2 superfamily and its group numbering system
    • Schaloske RH, Dennis EA. The phospholipase A2 superfamily and its group numbering system. Biochim Biophys Acta 2006; 1761: 1246-1259.
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 1246-1259
    • Schaloske, R.H.1    Dennis, E.A.2
  • 16
    • 0017376906 scopus 로고
    • Amino acid sequence of phospholipase A2-alpha from the venom of Crotalus adamanteus. A new classification of phospholipases A2 based upon structural determinants
    • Heinrikson RL, Krueger ET, Keim PS. Amino acid sequence of phospholipase A2-alpha from the venom of Crotalus adamanteus. A new classification of phospholipases A2 based upon structural determinants. J Biol Chem 1977; 252: 4913-4921.
    • (1977) J Biol Chem , vol.252 , pp. 4913-4921
    • Heinrikson, R.L.1    Krueger, E.T.2    Keim, P.S.3
  • 17
    • 36148976495 scopus 로고    scopus 로고
    • Snake venomics. Strategy and applications
    • Calvete JJ, Juarez P, Sanz L. Snake venomics. Strategy and applications. J Mass Spectrom 2007; 42: 1405-1414.
    • (2007) J Mass Spectrom , vol.42 , pp. 1405-1414
    • Calvete, J.J.1    Juarez, P.2    Sanz, L.3
  • 18
    • 0037103457 scopus 로고    scopus 로고
    • Structural and functional characterization of an acidic platelet aggregation inhibitor and hypotensive phospholipase A(2) from Bothrops jararacussu snake venom
    • Andriao-Escarso SH, Soares AM, Fontes MR, Fuly AL, Correa FM, Rosa JC, Greene LJ, Giglio JR. Structural and functional characterization of an acidic platelet aggregation inhibitor and hypotensive phospholipase A(2) from Bothrops jararacussu snake venom. Biochem Pharmacol 2002; 64: 723-732.
    • (2002) Biochem Pharmacol , vol.64 , pp. 723-732
    • Andriao-Escarso, S.H.1    Soares, A.M.2    Fontes, M.R.3    Fuly, A.L.4    Correa, F.M.5    Rosa, J.C.6    Greene, L.J.7    Giglio, J.R.8
  • 19
    • 0037127316 scopus 로고    scopus 로고
    • The antibacterial properties of secreted phospholipases A2: a major physiological role for the group IIA enzyme that depends on the very high pI of the enzyme to allow penetration of the bacterial cell wall
    • Beers SA, Buckland AG, Koduri RS, Cho W, Gelb MH, Wilton DC. The antibacterial properties of secreted phospholipases A2: a major physiological role for the group IIA enzyme that depends on the very high pI of the enzyme to allow penetration of the bacterial cell wall. J Biol Chem 2002; 277: 1788-1793.
    • (2002) J Biol Chem , vol.277 , pp. 1788-1793
    • Beers, S.A.1    Buckland, A.G.2    Koduri, R.S.3    Cho, W.4    Gelb, M.H.5    Wilton, D.C.6
  • 21
    • 0017355161 scopus 로고
    • Short communications the presynaptic neuromuscular blocking action of taipoxin. A comparison with beta-bungarotoxin and crotoxin
    • Chang CC, Lee JD, Eaker D, Fohlman J. Short communications the presynaptic neuromuscular blocking action of taipoxin. A comparison with beta-bungarotoxin and crotoxin. Toxicon 1977; 15: 571-576.
    • (1977) Toxicon , vol.15 , pp. 571-576
    • Chang, C.C.1    Lee, J.D.2    Eaker, D.3    Fohlman, J.4
  • 22
    • 0027665462 scopus 로고
    • Increased phosphatidic acid and decreased lysophosphatidic acid in response to thrombin is associated with inhibition of platelet aggregation
    • Gerrard JM, Robinson P, Narvey M, McNicol A. Increased phosphatidic acid and decreased lysophosphatidic acid in response to thrombin is associated with inhibition of platelet aggregation. Biochem Cell Biol 1993; 71: 432-439.
    • (1993) Biochem Cell Biol , vol.71 , pp. 432-439
    • Gerrard, J.M.1    Robinson, P.2    Narvey, M.3    McNicol, A.4
  • 23
    • 0019412190 scopus 로고
    • Lack of correlation between anticoagulant activity and phospholipid hydrolysis by snake venom phospholipases A2
    • Condrea E, Yang CC, Rosenberg P. Lack of correlation between anticoagulant activity and phospholipid hydrolysis by snake venom phospholipases A2. Thromb Haemost 1981; 45: 82-85.
    • (1981) Thromb Haemost , vol.45 , pp. 82-85
    • Condrea, E.1    Yang, C.C.2    Rosenberg, P.3
  • 24
    • 0004129553 scopus 로고    scopus 로고
    • Phospholipases A2 Enzymes: Structure, Function, and Mechanism
    • In, Kini RM, editor., Chichester, Wiley;, p
    • Gutiérrez JM, Lomonte B. Phospholipase A2 miotoxins from Bothrops snake venoms. In: Kini RM, editor. Phospholipases A2 Enzymes: Structure, Function, and Mechanism. Chichester: Wiley; 1997. p 321-352.
    • (1997) Phospholipase A2 miotoxins from Bothrops snake venoms , pp. 321-352
    • Gutiérrez, J.M.1    Lomonte, B.2
  • 25
    • 0027248052 scopus 로고
    • Oedema formation and degranulation of mast cells by phospholipase A2 purified from porcine pancreas and snake venoms
    • Lloret S, Moreno JJ. Oedema formation and degranulation of mast cells by phospholipase A2 purified from porcine pancreas and snake venoms. Toxicon 1993; 31: 949-956.
    • (1993) Toxicon , vol.31 , pp. 949-956
    • Lloret, S.1    Moreno, J.J.2
  • 26
    • 0032522765 scopus 로고    scopus 로고
    • Bactericidal activity of Lys49 and Asp49 myotoxic phospholipases A2 from Bothrops asper snake venom--synthetic Lys49 myotoxin II-(115-129)-peptide identifies its bactericidal region
    • Paramo L, Lomonte B, Pizarro-Cerda J, Bengoechea JA, Gorvel JP, Moreno E. Bactericidal activity of Lys49 and Asp49 myotoxic phospholipases A2 from Bothrops asper snake venom--synthetic Lys49 myotoxin II-(115-129)-peptide identifies its bactericidal region. Eur J Biochem 1998; 253: 452-461.
    • (1998) Eur J Biochem , vol.253 , pp. 452-461
    • Paramo, L.1    Lomonte, B.2    Pizarro-Cerda, J.3    Bengoechea, J.A.4    Gorvel, J.P.5    Moreno, E.6
  • 27
    • 0002351813 scopus 로고
    • Handbook of toxinology
    • In, Shyer WT, Mebs D, editors., New York, Dekker;, p
    • Rosenberg P. Phospholipases. In: Shyer WT, Mebs D, editors. Handbook of toxinology. New York: Dekker; 1990. p 67-277.
    • (1990) Phospholipases , pp. 67-277
    • Rosenberg, P.1
  • 28
    • 19544373621 scopus 로고    scopus 로고
    • Structure-function relationships and mechanism of anticoagulant phospholipase A2 enzymes from snake venoms
    • Kini RM. Structure-function relationships and mechanism of anticoagulant phospholipase A2 enzymes from snake venoms. Toxicon 2005; 45: 1147-1161.
    • (2005) Toxicon , vol.45 , pp. 1147-1161
    • Kini, R.M.1
  • 30
    • 0025959248 scopus 로고
    • Myotoxin II from Bothrops asper (Terciopelo) venom is a lysine-49 phospholipase A2
    • Francis B, Gutierrez JM, Lomonte B, Kaiser, II. Myotoxin II from Bothrops asper (Terciopelo) venom is a lysine-49 phospholipase A2. Arch Biochem Biophys 1991; 284: 352-359.
    • (1991) Arch Biochem Biophys , vol.284 , pp. 352-359
    • Francis, B.1    Gutierrez, J.M.2    Lomonte, B.3    Kaiser, I.I.4
  • 31
    • 0033486343 scopus 로고    scopus 로고
    • Characterization of a basic phospholipase A2-homologue myotoxin isolated from the venom of the snake Bothrops neuwiedii (yarara chica) from Argentina
    • Geoghegan P, Angulo Y, Cangelosi A, Diaz M, Lomonte B. Characterization of a basic phospholipase A2-homologue myotoxin isolated from the venom of the snake Bothrops neuwiedii (yarara chica) from Argentina. Toxicon 1999; 37: 1735-1746.
    • (1999) Toxicon , vol.37 , pp. 1735-1746
    • Geoghegan, P.1    Angulo, Y.2    Cangelosi, A.3    Diaz, M.4    Lomonte, B.5
  • 32
    • 0024377772 scopus 로고
    • Myonecrosis induced in mice by a basic myotoxin isolated from the venom of the snake Bothrops nummifer (jumping viper) from Costa Rica
    • Gutierrez JM, Chaves F, Gene JA, Lomonte B, Camacho Z, Schosinsky K. Myonecrosis induced in mice by a basic myotoxin isolated from the venom of the snake Bothrops nummifer (jumping viper) from Costa Rica. Toxicon 1989; 27: 735-745.
    • (1989) Toxicon , vol.27 , pp. 735-745
    • Gutierrez, J.M.1    Chaves, F.2    Gene, J.A.3    Lomonte, B.4    Camacho, Z.5    Schosinsky, K.6
  • 33
    • 0028972997 scopus 로고
    • Phospholipase A2 myotoxins from Bothrops snake venoms
    • Gutierrez JM, Lomonte B. Phospholipase A2 myotoxins from Bothrops snake venoms. Toxicon 1995; 33: 1405-1424.
    • (1995) Toxicon , vol.33 , pp. 1405-1424
    • Gutierrez, J.M.1    Lomonte, B.2
  • 34
    • 1042264060 scopus 로고    scopus 로고
    • An overview of lysine-49 phospholipase A2 myotoxins from crotalid snake venoms and their structural determinants of myotoxic action
    • Lomonte B, Angulo Y, Calderon L. An overview of lysine-49 phospholipase A2 myotoxins from crotalid snake venoms and their structural determinants of myotoxic action. Toxicon 2003; 42: 885-901.
    • (2003) Toxicon , vol.42 , pp. 885-901
    • Lomonte, B.1    Angulo, Y.2    Calderon, L.3
  • 35
    • 33746795959 scopus 로고    scopus 로고
    • Biochemical and biological activities of the venom of the Chinese pitviper Zhaoermia mangshanensis, with the complete amino acid sequence and phylogenetic analysis of a novel Arg49 phospholipase A(2) myotoxin
    • Mebs D, Kuch U, Coronas FIV, Batista CVF, Gumprecht A, Possani LD. Biochemical and biological activities of the venom of the Chinese pitviper Zhaoermia mangshanensis, with the complete amino acid sequence and phylogenetic analysis of a novel Arg49 phospholipase A(2) myotoxin. Toxicon 2006; 47: 797-811.
    • (2006) Toxicon , vol.47 , pp. 797-811
    • Mebs, D.1    Kuch, U.2    Coronas, F.I.V.3    Batista, C.V.F.4    Gumprecht, A.5    Possani, L.D.6
  • 37
    • 0023002506 scopus 로고
    • Isolation and partial characterization of a myotoxin from the venom of the snake Bothrops nummifer
    • Gutierrez JM, Lomonte B, Cerdas L. Isolation and partial characterization of a myotoxin from the venom of the snake Bothrops nummifer. Toxicon 1986; 24: 885-894.
    • (1986) Toxicon , vol.24 , pp. 885-894
    • Gutierrez, J.M.1    Lomonte, B.2    Cerdas, L.3
  • 38
    • 0027102350 scopus 로고
    • A clinical and epidemiologic study of 292 cases of lance-headed viper bite in a Brazilian teaching hospital
    • Nishioka Sde A, Silveira PV. A clinical and epidemiologic study of 292 cases of lance-headed viper bite in a Brazilian teaching hospital. Am J Trop Med Hyg 1992; 47: 805-810.
    • (1992) Am J Trop Med Hyg , vol.47 , pp. 805-810
    • Nishioka Sde, A.1    Silveira, P.V.2
  • 40
    • 33745617121 scopus 로고    scopus 로고
    • Confronting the neglected problem of snake bite envenoming: the need for a global partnership
    • Gutierrez JM, Theakston RD, Warrell DA. Confronting the neglected problem of snake bite envenoming: the need for a global partnership. PLoS Med 2006; 3: e150.
    • (2006) PLoS Med , vol.3
    • Gutierrez, J.M.1    Theakston, R.D.2    Warrell, D.A.3
  • 43
    • 70249088378 scopus 로고    scopus 로고
    • Neutralization of Bothrops asper venom by antibodies, natural products and synthetic drugs: contributions to understanding snakebite envenomings and their treatment
    • Lomonte B, Leon G, Angulo Y, Rucavado A, Nunez V. Neutralization of Bothrops asper venom by antibodies, natural products and synthetic drugs: contributions to understanding snakebite envenomings and their treatment. Toxicon 2009; 54: 1012-1028.
    • (2009) Toxicon , vol.54 , pp. 1012-1028
    • Lomonte, B.1    Leon, G.2    Angulo, Y.3    Rucavado, A.4    Nunez, V.5
  • 44
    • 0037084001 scopus 로고    scopus 로고
    • Active-site mutagenesis of a Lys49-phospholipase A2: biological and membrane-disrupting activities in the absence of catalysis
    • Ward RJ, Chioato L, de Oliveira AH, Ruller R, Sa JM. Active-site mutagenesis of a Lys49-phospholipase A2: biological and membrane-disrupting activities in the absence of catalysis. Biochem J 2002; 362(Part 1): 89-96.
    • (2002) Biochem J , vol.362 , Issue.PART 1 , pp. 89-96
    • Ward, R.J.1    Chioato, L.2    de Oliveira, A.H.3    Ruller, R.4    Sa, J.M.5
  • 45
    • 0021723288 scopus 로고
    • A new class of phospholipases A2 with lysine in place of aspartate 49. Functional consequences for calcium and substrate binding
    • Maraganore JM, Merutka G, Cho W, Welches W, Kezdy FJ, Heinrikson RL. A new class of phospholipases A2 with lysine in place of aspartate 49. Functional consequences for calcium and substrate binding. J Biol Chem 1984; 259: 13839-13843.
    • (1984) J Biol Chem , vol.259 , pp. 13839-13843
    • Maraganore, J.M.1    Merutka, G.2    Cho, W.3    Welches, W.4    Kezdy, F.J.5    Heinrikson, R.L.6
  • 46
    • 68849085882 scopus 로고    scopus 로고
    • The intriguing phospholipases A2 homologues: relevant structural features on myotoxicity and catalytic inactivity
    • dos Santos JI, Fernandes CA, Magro AJ, Fontes MR. The intriguing phospholipases A2 homologues: relevant structural features on myotoxicity and catalytic inactivity. Protein Pept Lett 2009; 16: 887-893.
    • (2009) Protein Pept Lett , vol.16 , pp. 887-893
    • dos Santos, J.I.1    Fernandes, C.A.2    Magro, A.J.3    Fontes, M.R.4
  • 47
    • 0037106330 scopus 로고    scopus 로고
    • Distinct sites for myotoxic and membrane-damaging activities in the C-terminal region of a Lys(49)-phospholipase A(2)
    • Chioato L, de Oliveira AHC, Ruller R, Sa JM, Ward RJ. Distinct sites for myotoxic and membrane-damaging activities in the C-terminal region of a Lys(49)-phospholipase A(2). Biochem J 2002; 366: 971-976.
    • (2002) Biochem J , vol.366 , pp. 971-976
    • Chioato, L.1    de Oliveira, A.H.C.2    Ruller, R.3    Sa, J.M.4    Ward, R.J.5
  • 48
    • 34047264804 scopus 로고    scopus 로고
    • Mapping of the structural determinants of artificial and biological membrane damaging activities of a Lys49 phospholipase A(2) by scanning alanine mutagenesis
    • Chioato L, Aragao EA, Ferreira TL, de Medeiros AI, Faccioli LH, Ward RJ. Mapping of the structural determinants of artificial and biological membrane damaging activities of a Lys49 phospholipase A(2) by scanning alanine mutagenesis. Biochim Et Biophys Acta-Biomemb 2007; 1768: 1247-1257.
    • (2007) Biochim Et Biophys Acta-Biomemb , vol.1768 , pp. 1247-1257
    • Chioato, L.1    Aragao, E.A.2    Ferreira, T.L.3    de Medeiros, A.I.4    Faccioli, L.H.5    Ward, R.J.6
  • 49
    • 0034899916 scopus 로고    scopus 로고
    • Identification of the myotoxic site of the Lys49 phospholipase A(2) from Agkistrodon piscivorus piscivorus snake venom: synthetic C-terminal peptides from Lys49, but not from Asp49 myotoxins, exert membrane-damaging activities
    • Nunez CE, Angulo Y, Lomonte B. Identification of the myotoxic site of the Lys49 phospholipase A(2) from Agkistrodon piscivorus piscivorus snake venom: synthetic C-terminal peptides from Lys49, but not from Asp49 myotoxins, exert membrane-damaging activities. Toxicon 2001; 39: 1587-1594.
    • (2001) Toxicon , vol.39 , pp. 1587-1594
    • Nunez, C.E.1    Angulo, Y.2    Lomonte, B.3
  • 50
    • 0031745866 scopus 로고    scopus 로고
    • A SequenceSpace analysis of Lys49 phopholipases A2: clues towards identification of residues involved in a novel mechanism of membrane damage and in myotoxicity
    • Ward RJ, Alves AR, Ruggiero Neto J, Arni RK, Casari G. A SequenceSpace analysis of Lys49 phopholipases A2: clues towards identification of residues involved in a novel mechanism of membrane damage and in myotoxicity. Protein Eng 1998; 11: 285-294.
    • (1998) Protein Eng , vol.11 , pp. 285-294
    • Ward, R.J.1    Alves, A.R.2    Ruggiero Neto, J.3    Arni, R.K.4    Casari, G.5
  • 52
    • 0032532383 scopus 로고    scopus 로고
    • Immunochemical characterization and role in toxic activities of region 115-129 of myotoxin II, a Lys49 phospholipase A2 from Bothrops asper snake venom
    • Calderon L, Lomonte B. Immunochemical characterization and role in toxic activities of region 115-129 of myotoxin II, a Lys49 phospholipase A2 from Bothrops asper snake venom. Arch Biochem Biophys 1998; 358: 343-350.
    • (1998) Arch Biochem Biophys , vol.358 , pp. 343-350
    • Calderon, L.1    Lomonte, B.2
  • 53
    • 0032969823 scopus 로고    scopus 로고
    • Inhibition of the myotoxic activity of Bothrops asper myotoxin II in mice by immunization with its synthetic 13-mer peptide 115-129
    • Calderon L, Lomonte B. Inhibition of the myotoxic activity of Bothrops asper myotoxin II in mice by immunization with its synthetic 13-mer peptide 115-129. Toxicon 1999; 37: 683-687.
    • (1999) Toxicon , vol.37 , pp. 683-687
    • Calderon, L.1    Lomonte, B.2
  • 54
    • 0033370390 scopus 로고    scopus 로고
    • Tyr-->Trp-substituted peptide 115-129 of a Lys49 phospholipase A(2) expresses enhanced membrane-damaging activities and reproduces its in vivo myotoxic effect
    • Lomonte B, Pizarro-Cerda J, Angulo Y, Gorvel JP, Moreno E. Tyr-->Trp-substituted peptide 115-129 of a Lys49 phospholipase A(2) expresses enhanced membrane-damaging activities and reproduces its in vivo myotoxic effect. Biochim Biophys Acta 1999; 1461: 19-26.
    • (1999) Biochim Biophys Acta , vol.1461 , pp. 19-26
    • Lomonte, B.1    Pizarro-Cerda, J.2    Angulo, Y.3    Gorvel, J.P.4    Moreno, E.5
  • 55
    • 0242286033 scopus 로고    scopus 로고
    • Comparative study of synthetic peptides corresponding to region 115-129 in Lys49 myotoxic phospholipases A2 from snake venoms
    • Lomonte B, Angulo Y, Santamaria C. Comparative study of synthetic peptides corresponding to region 115-129 in Lys49 myotoxic phospholipases A2 from snake venoms. Toxicon 2003; 42: 307-312.
    • (2003) Toxicon , vol.42 , pp. 307-312
    • Lomonte, B.1    Angulo, Y.2    Santamaria, C.3
  • 56
    • 67650001629 scopus 로고    scopus 로고
    • Comparative structural studies on Lys49-phospholipases A(2) from Bothrops genus reveal their myotoxic site
    • dos Santos JI, Soares AM, Fontes MR. Comparative structural studies on Lys49-phospholipases A(2) from Bothrops genus reveal their myotoxic site. J Struct Biol 2009; 167: 106-116.
    • (2009) J Struct Biol , vol.167 , pp. 106-116
    • dos Santos, J.I.1    Soares, A.M.2    Fontes, M.R.3
  • 57
    • 0023878851 scopus 로고
    • Fractionation of Bothrops jararacussu snake venom: partial chemical characterization and biological activity of bothropstoxin
    • Homsi-Brandeburgo MI, Queiroz LS, Santo-Neto H, Rodrigues-Simioni L, Giglio JR. Fractionation of Bothrops jararacussu snake venom: partial chemical characterization and biological activity of bothropstoxin. Toxicon 1988; 26: 615-627.
    • (1988) Toxicon , vol.26 , pp. 615-627
    • Homsi-Brandeburgo, M.I.1    Queiroz, L.S.2    Santo-Neto, H.3    Rodrigues-Simioni, L.4    Giglio, J.R.5
  • 58
    • 0026337883 scopus 로고
    • Skeletal muscle degeneration and regeneration after injection of bothropstoxin-II, a phospholipase A2 isolated from the venom of the snake Bothrops jararacussu
    • Gutierrez JM, Nunez J, Diaz C, Cintra AC, Homsi-Brandeburgo MI, Giglio JR. Skeletal muscle degeneration and regeneration after injection of bothropstoxin-II, a phospholipase A2 isolated from the venom of the snake Bothrops jararacussu. Exp Mol Pathol 1991; 55: 217-229.
    • (1991) Exp Mol Pathol , vol.55 , pp. 217-229
    • Gutierrez, J.M.1    Nunez, J.2    Diaz, C.3    Cintra, A.C.4    Homsi-Brandeburgo, M.I.5    Giglio, J.R.6
  • 59
    • 0031800426 scopus 로고    scopus 로고
    • The amino acid sequence of bothropstoxin-II, an Asp-49 myotoxin from Bothrops jararacussu (Jararacucu) venom with low phospholipase A2 activity
    • Pereira MF, Novello JC, Cintra AC, Giglio JR, Landucci ET, Oliveira B, Marangoni S. The amino acid sequence of bothropstoxin-II, an Asp-49 myotoxin from Bothrops jararacussu (Jararacucu) venom with low phospholipase A2 activity. J Protein Chem 1998; 17: 381-386.
    • (1998) J Protein Chem , vol.17 , pp. 381-386
    • Pereira, M.F.1    Novello, J.C.2    Cintra, A.C.3    Giglio, J.R.4    Landucci, E.T.5    Oliveira, B.6    Marangoni, S.7
  • 60
    • 0033013266 scopus 로고    scopus 로고
    • Purification and amino acid sequence of MP-III 4R D49 phospholipase A2 from Bothrops pirajai snake venom, a toxin with moderate PLA2 and anticoagulant activities and high myotoxic activity
    • Toyama MH, Costa PD, Novello JC, de Oliveira B, Giglio JR, da Cruz-Hofling MA, Marangoni S. Purification and amino acid sequence of MP-III 4R D49 phospholipase A2 from Bothrops pirajai snake venom, a toxin with moderate PLA2 and anticoagulant activities and high myotoxic activity. J Protein Chem 1999; 18: 371-378.
    • (1999) J Protein Chem , vol.18 , pp. 371-378
    • Toyama, M.H.1    Costa, P.D.2    Novello, J.C.3    de Oliveira, B.4    Giglio, J.R.5    da Cruz-Hofling, M.A.6    Marangoni, S.7
  • 61
    • 40849111743 scopus 로고    scopus 로고
    • Crystal structure of a myotoxic Asp49-phospholipase A2 with low catalytic activity: insights into Ca2+-independent catalytic mechanism
    • Correa LC, Marchi-Salvador DP, Cintra AC, Sampaio SV, Soares AM, Fontes MR. Crystal structure of a myotoxic Asp49-phospholipase A2 with low catalytic activity: insights into Ca2+-independent catalytic mechanism. Biochim Biophys Acta 2008; 1784: 591-599.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 591-599
    • Correa, L.C.1    Marchi-Salvador, D.P.2    Cintra, A.C.3    Sampaio, S.V.4    Soares, A.M.5    Fontes, M.R.6
  • 62
    • 0037319939 scopus 로고    scopus 로고
    • The structure of the D49 phospholipase A2 piratoxin III from Bothrops pirajai reveals unprecedented structural displacement of the calcium-binding loop: possible relationship to cooperative substrate binding
    • Rigden DJ, Hwa LW, Marangoni S, Toyama MH, Polikarpov I. The structure of the D49 phospholipase A2 piratoxin III from Bothrops pirajai reveals unprecedented structural displacement of the calcium-binding loop: possible relationship to cooperative substrate binding. Acta Crystallogr D Biol Crystallogr 2003; 59(Part 2): 255-262.
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , Issue.PART 2 , pp. 255-262
    • Rigden, D.J.1    Hwa, L.W.2    Marangoni, S.3    Toyama, M.H.4    Polikarpov, I.5
  • 64
    • 8844274085 scopus 로고    scopus 로고
    • Signal transduction pathways involved in the platelet aggregation induced by a D-49 phospholipase A2 isolated from Bothrops jararacussu snake venom
    • Fuly AL, Soares AM, Marcussi S, Giglio JR, Guimaraes JA. Signal transduction pathways involved in the platelet aggregation induced by a D-49 phospholipase A2 isolated from Bothrops jararacussu snake venom. Biochimie 2004; 86: 731-739.
    • (2004) Biochimie , vol.86 , pp. 731-739
    • Fuly, A.L.1    Soares, A.M.2    Marcussi, S.3    Giglio, J.R.4    Guimaraes, J.A.5
  • 65
    • 28944455143 scopus 로고    scopus 로고
    • Introduction to macromolecular crystallography
    • Hoboken, Wiley-Liss;
    • McPherson A. Introduction to macromolecular crystallography. Hoboken: Wiley-Liss; 2003. 237 p.
    • (2003)
    • McPherson, A.1
  • 66
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Macromol Crystallogr A 1997; 276: 307-326.
    • (1997) Macromol Crystallogr A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 67
    • 0026597444 scopus 로고
    • Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger AT. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 1992; 355: 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 68
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 1997; 53(Part 3): 240-255.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , Issue.PART 3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 69
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 2004; 60(Part 12, Part 1): 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PPART 12 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 71
    • 0035094475 scopus 로고    scopus 로고
    • Geometry of metal-ligand interactions in proteins
    • Harding MM. Geometry of metal-ligand interactions in proteins. Acta Crystallogr D Biol Crystallogr 2001; 57 (Part 3): 401-411.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , Issue.PART 3 , pp. 401-411
    • Harding, M.M.1
  • 72
    • 0033937430 scopus 로고    scopus 로고
    • The geometry of metal-ligand interactions relevant to proteins. II. Angles at the metal atom, additional weak metal-donor interactions
    • Harding MM. The geometry of metal-ligand interactions relevant to proteins. II. Angles at the metal atom, additional weak metal-donor interactions. Acta Crystallogr D Biol Crystallogr 2000; 56(Part 7): 857-867.
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , Issue.PART 7 , pp. 857-867
    • Harding, M.M.1
  • 73
    • 84856368815 scopus 로고
    • The Biological Chemistry of the Elements-The Inorganic Chemistry of Life
    • Oxford University Press, Oxford;
    • Fraústo da Silva JJR, Willians RJP. The Biological Chemistry of the Elements-The Inorganic Chemistry of Life. Oxford University Press: Oxford; 1991. 561 p.
    • (1991) , pp. 561
    • Fraústo da Silva, J.J.R.1    Willians, R.J.P.2
  • 75
    • 0000078168 scopus 로고
    • Crystallographic and Modeling Methods in Molecular Design
    • In, Bugg C, Ealick SE, editors., New York, Springer-Verlag;
    • Jones TA, Bergdoll M, Kjeldgaard M. O: a macromolecule modeling environment. In: Bugg C, Ealick SE, editors. Crystallographic and Modeling Methods in Molecular Design. New York: Springer-Verlag; 1990. p 189-195.
    • (1990) O: a macromolecule modeling environment , pp. 189-195
    • Jones, T.A.1    Bergdoll, M.2    Kjeldgaard, M.3
  • 76
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K. Inference of macromolecular assemblies from crystalline state. J Mol Biol 2007; 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 77
    • 0003845223 scopus 로고    scopus 로고
    • The PyMOL molecular graphics system
    • San Carlos, CA, DeLano Scientific LLC;
    • DeLano WL. The PyMOL molecular graphics system. San Carlos, CA: DeLano Scientific LLC; 2002.
    • (2002)
    • DeLano, W.L.1
  • 78
    • 33846659941 scopus 로고    scopus 로고
    • Multiple alignment by sequence annealing
    • Schwartz AS, Pachter L. Multiple alignment by sequence annealing. Bioinformatics 2007; 23: e24-e29.
    • (2007) Bioinformatics , vol.23
    • Schwartz, A.S.1    Pachter, L.2
  • 79
    • 0034849408 scopus 로고    scopus 로고
    • MRBAYES: Bayesian inference of phylogenetic trees
    • Huelsenbeck JP, Ronquist F. MRBAYES: Bayesian inference of phylogenetic trees. Bioinformatics 2001; 17: 754-755.
    • (2001) Bioinformatics , vol.17 , pp. 754-755
    • Huelsenbeck, J.P.1    Ronquist, F.2
  • 80
    • 78649769751 scopus 로고    scopus 로고
    • Mesquite: a modular system for evolutionary analysis. Version 2.72., Available at.
    • Maddison WP, Maddison DR. Mesquite: a modular system for evolutionary analysis. Version 2.72. 2009. Available at:
    • (2009)
    • Maddison, W.P.1    Maddison, D.R.2
  • 82
    • 0024412266 scopus 로고
    • A new muscle damaging toxin, myotoxin II, from the venom of the snake Bothrops asper (terciopelo)
    • Lomonte B, Gutierrez JM. A new muscle damaging toxin, myotoxin II, from the venom of the snake Bothrops asper (terciopelo). Toxicon 1989; 27: 725-733.
    • (1989) Toxicon , vol.27 , pp. 725-733
    • Lomonte, B.1    Gutierrez, J.M.2
  • 84
    • 0029124677 scopus 로고
    • Structure of a calcium-independent phospholipase-like myotoxic protein from Bothrops asper venom
    • Arni RK, Ward RJ, Gutierrez JM, Tulinsky A. Structure of a calcium-independent phospholipase-like myotoxic protein from Bothrops asper venom. Acta Crystallogr D Biol Crystallogr 1995; 51(Part 3): 311-317.
    • (1995) Acta Crystallogr D Biol Crystallogr , vol.51 , Issue.PART 3 , pp. 311-317
    • Arni, R.K.1    Ward, R.J.2    Gutierrez, J.M.3    Tulinsky, A.4
  • 85
    • 17344384790 scopus 로고    scopus 로고
    • A rapid procedure for the isolation of the Lys-49 myotoxin II from Bothrops moojeni (caissaca) venom: biochemical characterization, crystallization, myotoxic and edematogenic activity
    • Soares AM, Rodrigues VM, Homsi-Brandeburgo MI, Toyama MH, Lombardi FR, Arni RK, Giglio JR. A rapid procedure for the isolation of the Lys-49 myotoxin II from Bothrops moojeni (caissaca) venom: biochemical characterization, crystallization, myotoxic and edematogenic activity. Toxicon 1998; 36: 503-514.
    • (1998) Toxicon , vol.36 , pp. 503-514
    • Soares, A.M.1    Rodrigues, V.M.2    Homsi-Brandeburgo, M.I.3    Toyama, M.H.4    Lombardi, F.R.5    Arni, R.K.6    Giglio, J.R.7
  • 86
    • 14844304297 scopus 로고    scopus 로고
    • Structural insights for fatty acid binding in a Lys49-phospholipase A(2): crystal structure of myotoxin II from Bothrops molojeni complexed with stearic acid
    • Watanabe L, Soares AM, Ward RJ, Fontes MRM, Arni RK. Structural insights for fatty acid binding in a Lys49-phospholipase A(2): crystal structure of myotoxin II from Bothrops molojeni complexed with stearic acid. Biochimie 2005; 87: 161-167.
    • (2005) Biochimie , vol.87 , pp. 161-167
    • Watanabe, L.1    Soares, A.M.2    Ward, R.J.3    Fontes, M.R.M.4    Arni, R.K.5
  • 87
    • 22744455994 scopus 로고    scopus 로고
    • Myotoxic and cytolytic activities of dimeric Lys49 phospholipase A(2) homologues are reduced, but not abolished, by a pH-induced dissociation
    • Angulo Y, Gutierrez JM, Soares AM, Cho W, Lomonte B. Myotoxic and cytolytic activities of dimeric Lys49 phospholipase A(2) homologues are reduced, but not abolished, by a pH-induced dissociation. Toxicon 2005; 46: 291-296.
    • (2005) Toxicon , vol.46 , pp. 291-296
    • Angulo, Y.1    Gutierrez, J.M.2    Soares, A.M.3    Cho, W.4    Lomonte, B.5
  • 88
    • 33846638198 scopus 로고    scopus 로고
    • Interfacial surface charge and free accessibility to the PLA(2)-active site-like region are essential requirements for the activity of Lys49 PLA(2) homologues
    • Murakami MT, Vicoti MM, Abrego JRB, Lourenzoni MR, Cintra ACO, Arruda EZ, Tomaz MA, Melo PA, Arni RK. Interfacial surface charge and free accessibility to the PLA(2)-active site-like region are essential requirements for the activity of Lys49 PLA(2) homologues. Toxicon 2007; 49: 378-387.
    • (2007) Toxicon , vol.49 , pp. 378-387
    • Murakami, M.T.1    Vicoti, M.M.2    Abrego, J.R.B.3    Lourenzoni, M.R.4    Cintra, A.C.O.5    Arruda, E.Z.6    Tomaz, M.A.7    Melo, P.A.8    Arni, R.K.9
  • 90
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. Solvent content of protein crystals. J Mol Biol 1968; 33: 491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 92
    • 0030003699 scopus 로고    scopus 로고
    • Crystal structure of an acidic phospholipase A2 from the venom of Agkistrodon halys pallas at 2.0 A resolution
    • Wang XQ, Yang J, Gui LL, Lin ZJ, Chen YC, Zhou YC. Crystal structure of an acidic phospholipase A2 from the venom of Agkistrodon halys pallas at 2.0 A resolution. J Mol Biol 1996; 255: 669-676.
    • (1996) J Mol Biol , vol.255 , pp. 669-676
    • Wang, X.Q.1    Yang, J.2    Gui, L.L.3    Lin, Z.J.4    Chen, Y.C.5    Zhou, Y.C.6
  • 93
    • 0036006762 scopus 로고    scopus 로고
    • Structure of an acidic phospholipase A2 from the venom of Deinagkistrodon acutus
    • Gu L, Zhang H, Song S, Zhou Y, Lin Z. Structure of an acidic phospholipase A2 from the venom of Deinagkistrodon acutus. Acta Crystallogr D Biol Crystallogr 2002; 58(Part 1): 104-110.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , Issue.PART 1 , pp. 104-110
    • Gu, L.1    Zhang, H.2    Song, S.3    Zhou, Y.4    Lin, Z.5
  • 94
    • 0035207975 scopus 로고    scopus 로고
    • Regulation of catalytic function by molecular association: structure of phospholipase A2 from Daboia russelli pulchella (DPLA2) at 1.9 A resolution
    • Chandra V, Kaur P, Jasti J, Betzel C, Singh TP. Regulation of catalytic function by molecular association: structure of phospholipase A2 from Daboia russelli pulchella (DPLA2) at 1.9 A resolution. Acta Crystallogr D Biol Crystallogr 2001; 57(Part 12): 1793-1798.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , Issue.PART 12 , pp. 1793-1798
    • Chandra, V.1    Kaur, P.2    Jasti, J.3    Betzel, C.4    Singh, T.P.5
  • 95
    • 0025668794 scopus 로고
    • Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue
    • Scott DL, Otwinowski Z, Gelb MH, Sigler PB. Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue. Science 1990; 250: 1563-1566.
    • (1990) Science , vol.250 , pp. 1563-1566
    • Scott, D.L.1    Otwinowski, Z.2    Gelb, M.H.3    Sigler, P.B.4
  • 97
    • 0033563920 scopus 로고    scopus 로고
    • Crystal structure of myotoxin II, a monomeric Lys49-phospholipase A2 homologue isolated from the venom of Cerrophidion (Bothrops) godmani
    • Arni RK, Fontes MR, Barberato C, Gutierrez JM, Diaz C, Ward RJ. Crystal structure of myotoxin II, a monomeric Lys49-phospholipase A2 homologue isolated from the venom of Cerrophidion (Bothrops) godmani. Arch Biochem Biophys 1999; 366: 177-182.
    • (1999) Arch Biochem Biophys , vol.366 , pp. 177-182
    • Arni, R.K.1    Fontes, M.R.2    Barberato, C.3    Gutierrez, J.M.4    Diaz, C.5    Ward, R.J.6
  • 98
    • 4444265324 scopus 로고    scopus 로고
    • Crystal structure of an acidic platelet aggregation inhibitor and hypotensive phospholipase A2 in the monomeric and dimeric states: insights into its oligomeric state
    • Magro AJ, Murakami MT, Marcussi S, Soares AM, Arni RK, Fontes MR. Crystal structure of an acidic platelet aggregation inhibitor and hypotensive phospholipase A2 in the monomeric and dimeric states: insights into its oligomeric state. Biochem Biophys Res Commun 2004; 323: 24-31.
    • (2004) Biochem Biophys Res Commun , vol.323 , pp. 24-31
    • Magro, A.J.1    Murakami, M.T.2    Marcussi, S.3    Soares, A.M.4    Arni, R.K.5    Fontes, M.R.6
  • 99
    • 0242409823 scopus 로고    scopus 로고
    • Crystal structures of BnSP-7 and BnSP-6, two Lys49-phospholipases A(2): quaternary structure and inhibition mechanism insights
    • Magro AJ, Soares AM, Giglio JR, Fontes MR. Crystal structures of BnSP-7 and BnSP-6, two Lys49-phospholipases A(2): quaternary structure and inhibition mechanism insights. Biochem Biophys Res Commun 2003; 311: 713-720.
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 713-720
    • Magro, A.J.1    Soares, A.M.2    Giglio, J.R.3    Fontes, M.R.4
  • 100
    • 47349114449 scopus 로고    scopus 로고
    • Insights into the role of oligomeric state on the biological activities of crotoxin: crystal structure of a tetrameric phospholipase A2 formed by two isoforms of crotoxin B from Crotalus durissus terrificus venom
    • Marchi-Salvador DP, Correa LC, Magro AJ, Oliveira CZ, Soares AM, Fontes MR. Insights into the role of oligomeric state on the biological activities of crotoxin: crystal structure of a tetrameric phospholipase A2 formed by two isoforms of crotoxin B from Crotalus durissus terrificus venom. Proteins 2008; 72: 883-891.
    • (2008) Proteins , vol.72 , pp. 883-891
    • Marchi-Salvador, D.P.1    Correa, L.C.2    Magro, A.J.3    Oliveira, C.Z.4    Soares, A.M.5    Fontes, M.R.6
  • 102
    • 33744975713 scopus 로고    scopus 로고
    • Insights into metal ion binding in phospholipases A(2): ultra high-resolution crystal structures of an acidic phospholipase A(2) in the Ca2+ free and bound states
    • Murakami MT, Gabdoulkhakov A, Genov N, Cintra ACO, Betzel C, Arni RK. Insights into metal ion binding in phospholipases A(2): ultra high-resolution crystal structures of an acidic phospholipase A(2) in the Ca2+ free and bound states. Biochimie 2006; 88: 543-549.
    • (2006) Biochimie , vol.88 , pp. 543-549
    • Murakami, M.T.1    Gabdoulkhakov, A.2    Genov, N.3    Cintra, A.C.O.4    Betzel, C.5    Arni, R.K.6
  • 103
    • 70349169826 scopus 로고    scopus 로고
    • Crystal structure of a phospholipase A(2) homologue complexed with p-bromophenacyl bromide reveals important structural changes associated with the inhibition of myotoxic activity
    • Marchi-Salvador DP, Fernandes CA, Silveira LB, Soares AM, Fontes MR. Crystal structure of a phospholipase A(2) homologue complexed with p-bromophenacyl bromide reveals important structural changes associated with the inhibition of myotoxic activity. Biochim Biophys Acta 2009; 1794: 1583-1590.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 1583-1590
    • Marchi-Salvador, D.P.1    Fernandes, C.A.2    Silveira, L.B.3    Soares, A.M.4    Fontes, M.R.5
  • 104
    • 68849086384 scopus 로고    scopus 로고
    • Influence of quaternary conformation on the biological activities of the Asp49-phospholipases A2s from snake venoms
    • Magro AJ, Fernandes CA, dos Santos JI, Fontes MR. Influence of quaternary conformation on the biological activities of the Asp49-phospholipases A2s from snake venoms. Protein Pept Lett 2009; 16: 852-859.
    • (2009) Protein Pept Lett , vol.16 , pp. 852-859
    • Magro, A.J.1    Fernandes, C.A.2    dos Santos, J.I.3    Fontes, M.R.4
  • 105
    • 1042298845 scopus 로고    scopus 로고
    • Molecular evolution of myotoxic phospholipases A2 from snake venom
    • Ohno M, Chijiwa T, Oda-Ueda N, Ogawa T, Hattori S. Molecular evolution of myotoxic phospholipases A2 from snake venom. Toxicon 2003; 42: 841-854.
    • (2003) Toxicon , vol.42 , pp. 841-854
    • Ohno, M.1    Chijiwa, T.2    Oda-Ueda, N.3    Ogawa, T.4    Hattori, S.5
  • 106
    • 34547861651 scopus 로고    scopus 로고
    • Neurotoxic activity of Gln49 phospholipase A(2) from Gloydius ussuriensis snake venom
    • Chang Y, Li Y, Bao Y, An L. Neurotoxic activity of Gln49 phospholipase A(2) from Gloydius ussuriensis snake venom. J Appl Toxicol 2007; 27: 447-452.
    • (2007) J Appl Toxicol , vol.27 , pp. 447-452
    • Chang, Y.1    Li, Y.2    Bao, Y.3    An, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.