메뉴 건너뛰기




Volumn 189, Issue 1-2, 2011, Pages 9-16

Quercetin as an inhibitor of snake venom secretory phospholipase A2

Author keywords

Crotalus durissus terrificus; Molecular docking; Pharmacological sites; Quercetin; sPLA

Indexed keywords

QUERCETIN; SECRETORY PHOSPHOLIPASE A2; SNAKE VENOM;

EID: 79251624606     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2010.10.016     Document Type: Article
Times cited : (66)

References (34)
  • 1
    • 1042275605 scopus 로고    scopus 로고
    • Excitement ahead: Structure, function and mechanism of snake venom phospholipase A2 enzymes
    • R. Kini Excitement ahead: structure, function and mechanism of snake venom phospholipase A2 enzymes Toxicon 42 8 2003 827 840
    • (2003) Toxicon , vol.42 , Issue.8 , pp. 827-840
    • Kini, R.1
  • 2
    • 39049170605 scopus 로고    scopus 로고
    • Antibacterial actions of secreted phospholipases A2. Review
    • T. Nevalainen, G. Graham, and K. Scott Antibacterial actions of secreted phospholipases A2. Review Biochim. Biophys. Acta 1781 1-2 2008 1 9
    • (2008) Biochim. Biophys. Acta , vol.1781 , Issue.12 , pp. 1-9
    • Nevalainen, T.1    Graham, G.2    Scott, K.3
  • 3
    • 58549086523 scopus 로고    scopus 로고
    • Phospholipase A2 biochemistry
    • J. Burke, and E. Dennis Phospholipase A2 biochemistry Cardiovasc. Drugs Ther. 23 1 2009 49 59
    • (2009) Cardiovasc. Drugs Ther. , vol.23 , Issue.1 , pp. 49-59
    • Burke, J.1    Dennis, E.2
  • 5
    • 1042287118 scopus 로고    scopus 로고
    • Chemical modifications of phospholipases A2 from snake venoms: Effects on catalytic and pharmacological properties
    • A. Soares, and J. Giglio Chemical modifications of phospholipases A2 from snake venoms: effects on catalytic and pharmacological properties Toxicon 42 8 2003 855 868
    • (2003) Toxicon , vol.42 , Issue.8 , pp. 855-868
    • Soares, A.1    Giglio, J.2
  • 6
    • 0032953625 scopus 로고    scopus 로고
    • Accelerated evolution and molecular surface of venom phospholipase A2 enzymes
    • R. Kini, and Y. Chan Accelerated evolution and molecular surface of venom phospholipase A2 enzymes J. Mol. Evol. 48 2 1999 125 132
    • (1999) J. Mol. Evol. , vol.48 , Issue.2 , pp. 125-132
    • Kini, R.1    Chan, Y.2
  • 7
    • 0038399752 scopus 로고    scopus 로고
    • Phospholipase A(2) isoforms: A perspective
    • S. Chakraborti Phospholipase A(2) isoforms: a perspective Cell Signal. 15 7 2003 637 665
    • (2003) Cell Signal. , vol.15 , Issue.7 , pp. 637-665
    • Chakraborti, S.1
  • 9
    • 0004580398 scopus 로고    scopus 로고
    • Flavonoids: Old and new aspects of a class of natural therapeutic drugs
    • G. Di Carlo, N. Mascolo, A. Izzo, and F. Capasso Flavonoids: old and new aspects of a class of natural therapeutic drugs Life Sci. 65 4 1999 337 353
    • (1999) Life Sci. , vol.65 , Issue.4 , pp. 337-353
    • Di Carlo, G.1    Mascolo, N.2    Izzo, A.3    Capasso, F.4
  • 10
    • 0030888257 scopus 로고    scopus 로고
    • Morelloflavone, a novel biflavonoid inhibitor of human secretory phospholipase A(2) with anti-inflammatory activity
    • B. Gil, M. Sanz, M. Terencio, R. Gunasegaran, M. Paya, and M. Alcaraz Morelloflavone, a novel biflavonoid inhibitor of human secretory phospholipase A(2) with anti-inflammatory activity Biochem. Pharmacol. 53 1997 733
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 733
    • Gil, B.1    Sanz, M.2    Terencio, M.3    Gunasegaran, R.4    Paya, M.5    Alcaraz, M.6
  • 11
    • 0030612780 scopus 로고    scopus 로고
    • Flavonoids as phospholipase A2 inhibitors: Importance of their structure for selective inhibition of group II phospholipase A2
    • M. Lindahl, and C. Tagesson Flavonoids as phospholipase A2 inhibitors: importance of their structure for selective inhibition of group II phospholipase A2 Inflammation 21 3 1997 347 356
    • (1997) Inflammation , vol.21 , Issue.3 , pp. 347-356
    • Lindahl, M.1    Tagesson, C.2
  • 13
    • 0027208761 scopus 로고
    • Selective inhibition of group II phospholipase A2 by quercetin
    • M. Lindahl, and C. Tagesson Selective inhibition of group II phospholipase A2 by quercetin Inflammation 17 5 1993 573 582
    • (1993) Inflammation , vol.17 , Issue.5 , pp. 573-582
    • Lindahl, M.1    Tagesson, C.2
  • 14
    • 0142119464 scopus 로고    scopus 로고
    • 2 isoform from Crotalus durissus terrificus venom
    • DOI 10.1016/S0041-0101(03)00085-0
    • M. Toyama, D. de Oliveira, L. Beriam, J. Novello, L. Rodrigues-Simioni, and S. Marangoni Structural, enzymatic and biological properties of new PLA(2) isoform from Crotalus durissus terrificus venom Toxicon 41 8 2003 1033 1038 (Pubitemid 37548369)
    • (2003) Toxicon , vol.41 , Issue.8 , pp. 1033-1038
    • Toyama, M.H.1    De Oliveira, D.G.2    Beriam, L.O.S.3    Novello, J.C.4    Rodrigues-Simioni, L.5    Marangoni, S.6
  • 15
    • 0031858925 scopus 로고    scopus 로고
    • Structure of a snake venom phospholipase A2 modified by p-bromo-phenacyl-bromide
    • H Zhao, L. Tang, X. Wang, Y. Zhou, and Z. Lin Structure of a snake venom phospholipase A2 modified by p-bromo-phenacyl-bromide Toxicon 36 6 1998 875 886
    • (1998) Toxicon , vol.36 , Issue.6 , pp. 875-886
    • Zhao, H.1    Tang, L.2    Wang, X.3    Zhou, Y.4    Lin, Z.5
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 5259 1970 680 685
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.1
  • 20
    • 0343312812 scopus 로고
    • The isolated chick biventer cervicis nerve-muscle preparation
    • B. Ginsborg, and J. Warriner The isolated chick biventer cervicis nerve-muscle preparation Br. J. Pharmacol. Chemother. 15 1960 410 411
    • (1960) Br. J. Pharmacol. Chemother. , vol.15 , pp. 410-411
    • Ginsborg, B.1    Warriner, J.2
  • 21
    • 0842341771 scopus 로고
    • Development and use of quantum mechanical molecular models. 76. AM1: A new general purpose quantum mechanical molecular model
    • M.J.S. Dewar, E.G. Zoebisch, E.F. Healy, and J.J.P. Stewart Development and use of quantum mechanical molecular models. 76. AM1: a new general purpose quantum mechanical molecular model J. Am. Chem. Soc. 107 13 1985 8
    • (1985) J. Am. Chem. Soc. , vol.107 , Issue.13 , pp. 8
    • Dewar, M.J.S.1    Zoebisch, E.G.2    Healy, E.F.3    Stewart, J.J.P.4
  • 22
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • G. Jones, P. Willett, R. Glen, A. Leach, and R. Taylor Development and validation of a genetic algorithm for flexible docking J. Mol. Biol. 267 3 1997 727 748
    • (1997) J. Mol. Biol. , vol.267 , Issue.3 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.3    Leach, A.4    Taylor, R.5
  • 23
    • 0019328522 scopus 로고
    • Methylation of histidine-48 in pancreatic phospholipase A2. Role of histidine and calcium ion in the catalytic mechanism
    • H. Verheij, J. Volwerk, E. Jansen, W. Puyk, B. Dijkstra, J. Drenth, and G. de Haas Methylation of histidine-48 in pancreatic phospholipase A2. Role of histidine and calcium ion in the catalytic mechanism Biochemistry 19 4 1980 743 750
    • (1980) Biochemistry , vol.19 , Issue.4 , pp. 743-750
    • Verheij, H.1    Volwerk, J.2    Jansen, E.3    Puyk, W.4    Dijkstra, B.5    Drenth, J.6    De Haas, G.7
  • 24
    • 0028358009 scopus 로고
    • Structure and catalytic mechanism of secretory phospholipases A2
    • D. Scott, and P. Sigler Structure and catalytic mechanism of secretory phospholipases A2 Adv. Protein Chem. 45 1994 53 88
    • (1994) Adv. Protein Chem. , vol.45 , pp. 53-88
    • Scott, D.1    Sigler, P.2
  • 25
    • 0005604706 scopus 로고
    • Effects of flavonoids on Naja naja and human recombinant synovial phospholipases A2 and inflammatory responses in mice
    • B. Gil, M. Sanz, M. Terencio, M. Ferrándiz, G. Bustos, M. Payá, R. Gunasegaran, and M. Alcaraz Effects of flavonoids on Naja naja and human recombinant synovial phospholipases A2 and inflammatory responses in mice Life Sci. 54 20 1994 PL333 338
    • (1994) Life Sci. , vol.54 , Issue.20 , pp. 333-338
    • Gil, B.1    Sanz, M.2    Terencio, M.3    Ferrándiz, M.4    Bustos, G.5    Payá, M.6    Gunasegaran, R.7    Alcaraz, M.8
  • 26
  • 27
    • 0034918136 scopus 로고    scopus 로고
    • Effects of chemical modifications of crotoxin B, the phospholipase A(2) subunit of crotoxin from Crotalus durissus terrificus snake venom, on its enzymatic and pharmacological activities
    • A. Soares, A. Mancin, A. Cecchini, E. Arantes, S. Frana, J. Gutiérrez, and J. Giglio Effects of chemical modifications of crotoxin B, the phospholipase A(2) subunit of crotoxin from Crotalus durissus terrificus snake venom, on its enzymatic and pharmacological activities Int. J. Biochem. Cell Biol. 33 9 2001 877 888
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , Issue.9 , pp. 877-888
    • Soares, A.1    Mancin, A.2    Cecchini, A.3    Arantes, E.4    Frana, S.5    Gutiérrez, J.6    Giglio, J.7
  • 29
    • 0034739437 scopus 로고    scopus 로고
    • The antibacterial properties of secreted phospholipases A(2)
    • A. Buckland, and D. Wilton The antibacterial properties of secreted phospholipases A(2) Biochim. Biophys. Acta 1488 1-2 2000 71 82
    • (2000) Biochim. Biophys. Acta , vol.1488 , Issue.12 , pp. 71-82
    • Buckland, A.1    Wilton, D.2
  • 30
    • 0035724930 scopus 로고    scopus 로고
    • Flavonoids differentially inhibit guinea pig epidermal cytosolic phospholipase A2
    • H. Kim, H. Pham, and V. Ziboh Flavonoids differentially inhibit guinea pig epidermal cytosolic phospholipase A2 Prostaglandins Leukot. Essent. Fatty Acids 65 5-6 2001 281 286
    • (2001) Prostaglandins Leukot. Essent. Fatty Acids , vol.65 , Issue.56 , pp. 281-286
    • Kim, H.1    Pham, H.2    Ziboh, V.3
  • 31
    • 60749114975 scopus 로고    scopus 로고
    • Effect of umbelliferone (7-hydroxycoumarin, 7-HOC) on the enzymatic, edematogenic and necrotic activities of secretory phospholipase A2 (sPLA2) isolated from Crotalus durissus collilineatus venom
    • D. Toyama, S. Marangoni, E. Diz-Filho, S. Oliveira, and M. Toyama Effect of umbelliferone (7-hydroxycoumarin, 7-HOC) on the enzymatic, edematogenic and necrotic activities of secretory phospholipase A2 (sPLA2) isolated from Crotalus durissus collilineatus venom Toxicon 53 4 2009 417 426
    • (2009) Toxicon , vol.53 , Issue.4 , pp. 417-426
    • Toyama, D.1    Marangoni, S.2    Diz-Filho, E.3    Oliveira, S.4    Toyama, M.5
  • 32
    • 1042298845 scopus 로고    scopus 로고
    • Molecular evolution of myotoxic phospholipases A2 from snake venom
    • M. Ohno, T. Chijiwa, N. Oda-Ueda, T. Ogawa, and S. Hattori Molecular evolution of myotoxic phospholipases A2 from snake venom Toxicon 42 8 2003 841 854
    • (2003) Toxicon , vol.42 , Issue.8 , pp. 841-854
    • Ohno, M.1    Chijiwa, T.2    Oda-Ueda, N.3    Ogawa, T.4    Hattori, S.5
  • 33
    • 0034739474 scopus 로고    scopus 로고
    • Increasing molecular diversity of secreted phospholipases A(2) and their receptors and binding proteins
    • E. Valentin, and G. Lambeau Increasing molecular diversity of secreted phospholipases A(2) and their receptors and binding proteins Biochim. Biophys. Acta 1488 1-2 2000 59 70
    • (2000) Biochim. Biophys. Acta , vol.1488 , Issue.12 , pp. 59-70
    • Valentin, E.1    Lambeau, G.2
  • 34
    • 0036606483 scopus 로고    scopus 로고
    • Principles of docking: An overview of search algorithms and a guide to scoring functions
    • I. Halperin, B. Ma, H. Wolfson, and R. Nussinov Principles of docking: an overview of search algorithms and a guide to scoring functions Proteins 47 4 2002 409 443
    • (2002) Proteins , vol.47 , Issue.4 , pp. 409-443
    • Halperin, I.1    Ma, B.2    Wolfson, H.3    Nussinov, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.