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Volumn 8, Issue 5, 2009, Pages 2351-2360

Crotalid snake venom subproteomes unraveled by the antiophidic protein DM43

Author keywords

Inhibitor; Mass spectrometry; Metalloproteinase; Proteomics; Snake; Toxin; Venom

Indexed keywords

AMINO ACID OXIDASE; BATROXOBIN; DECTIN 2; METALLOPROTEINASE; NERVE GROWTH FACTOR; PLASMA PROTEIN; PROTEIN DM43; PROTEOME; SERINE PROTEINASE; SNAKE VENOM; UNCLASSIFIED DRUG;

EID: 66749172929     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr800977s     Document Type: Article
Times cited : (19)

References (51)
  • 1
    • 33745617121 scopus 로고    scopus 로고
    • Confronting the neglected problem of snake bite envenoming: The need for a global partnership
    • Gutierrez, J. M.; Theakston, R. D.; Warrell, D. A. 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
  • 2
    • 0032428679 scopus 로고    scopus 로고
    • Snake-bites: Appraisal of the global situation
    • Chippaux, J. P. Snake-bites: appraisal of the global situation. Bull. WHO 1998, 76 , 515-524.
    • (1998) Bull. WHO , vol.76 , pp. 515-524
    • Chippaux, J.P.1
  • 3
    • 33845383046 scopus 로고    scopus 로고
    • Strengthening antivenom production in Central and South American public laboratories: Report of a workshop
    • Gutierrez, J. M.; Gondo Higashi, H.; Hui Wen, F.; Burnouf, T. Strengthening antivenom production in Central and South American public laboratories: Report of a workshop. Toxicon 2007, 49 , 30-35.
    • (2007) Toxicon , vol.49 , pp. 30-35
    • Gutierrez, J.M.1    Gondo Higashi, H.2    Hui Wen, F.3    Burnouf, T.4
  • 4
    • 33846105870 scopus 로고    scopus 로고
    • Snake venom components and their applications in biomedicine
    • Koh, D. C.; Armugam, A.; Jeyaseelan, K. Snake venom components and their applications in biomedicine. Cell. Mol. Life Sci . 2006, 63 , 3030-3041.
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 3030-3041
    • Koh, D.C.1    Armugam, A.2    Jeyaseelan, K.3
  • 5
    • 38449110166 scopus 로고    scopus 로고
    • Approaching the golden age of natural product pharmaceuticals from venom libraries: An overview of toxins and toxin-derivatives currently involved in therapeutic or diagnostic applications
    • Fox, J. W.; Serrano, S. M. Approaching the golden age of natural product pharmaceuticals from venom libraries: an overview of toxins and toxin-derivatives currently involved in therapeutic or diagnostic applications. Curr. Pharm. Des . 2007, 13 , 2927-2934.
    • (2007) Curr. Pharm. Des , vol.13 , pp. 2927-2934
    • Fox, J.W.1    Serrano, S.M.2
  • 6
    • 0010301159 scopus 로고    scopus 로고
    • Overview of snake venom chemistry
    • Singh, B. R, Tu, A. T, Eds, Plenum Press: New York
    • Tu, A. T. Overview of snake venom chemistry. In Natural Toxins II , Singh, B. R.; Tu, A. T., Eds.; Plenum Press: New York, 1996.
    • (1996) Natural Toxins II
    • Tu, A.T.1
  • 8
    • 40549090210 scopus 로고    scopus 로고
    • Exploring snake venom proteomes: Multifaceted analyses for complex toxin mixtures
    • Fox, J. W.; Serrano, S. M. Exploring snake venom proteomes: multifaceted analyses for complex toxin mixtures. Proteomics 2008, 8 , 909-920.
    • (2008) Proteomics , vol.8 , pp. 909-920
    • Fox, J.W.1    Serrano, S.M.2
  • 9
    • 33646152321 scopus 로고    scopus 로고
    • Comparison of indirect and direct approaches using ion-trap and Fourier transform ion cyclotron resonance mass spectrometry for exploring viperid venom proteomes
    • Fox, J. W.; Ma, L.; Nelson, K.; Sherman, N. E.; Serrano, S. M. Comparison of indirect and direct approaches using ion-trap and Fourier transform ion cyclotron resonance mass spectrometry for exploring viperid venom proteomes. Toxicon 2006, 47 , 700-714.
    • (2006) Toxicon , vol.47 , pp. 700-714
    • Fox, J.W.1    Ma, L.2    Nelson, K.3    Sherman, N.E.4    Serrano, S.M.5
  • 10
    • 4444279812 scopus 로고    scopus 로고
    • Analysis of lectin-bound glycoproteins in snake venom from the Elapidae and Viperidae families
    • Nawarak, J.; Phutrakul, S.; Chen, S. T. Analysis of lectin-bound glycoproteins in snake venom from the Elapidae and Viperidae families. J. Proteome Res . 2004, 3 , 383-392.
    • (2004) J. Proteome Res , vol.3 , pp. 383-392
    • Nawarak, J.1    Phutrakul, S.2    Chen, S.T.3
  • 11
    • 20644445645 scopus 로고    scopus 로고
    • Fast analysis of low molecular mass compounds present in snake venom: Identification of ten new pyroglutamate-containing peptides
    • Wermelinger, L. S.; Dutra, D. L.; Oliveira-Carvalho, A. L.; Soares, M. R.; Bloch, C., Jr.; Zingali, R. B. Fast analysis of low molecular mass compounds present in snake venom: identification of ten new pyroglutamate-containing peptides. Rapid Commun. Mass Spectrom . 2005, 19 , 1703-1708.
    • (2005) Rapid Commun. Mass Spectrom , vol.19 , pp. 1703-1708
    • Wermelinger, L.S.1    Dutra, D.L.2    Oliveira-Carvalho, A.L.3    Soares, M.R.4    Bloch Jr., C.5    Zingali, R.B.6
  • 12
    • 13844310831 scopus 로고    scopus 로고
    • A multifaceted analysis of viperid snake venoms by two-dimensional gel electrophoresis: An approach to understanding venom proteomics
    • Serrano, S. M.; Shannon, J. D.; Wang, D.; Camargo, A. C.; Fox, J. W. A multifaceted analysis of viperid snake venoms by two-dimensional gel electrophoresis: an approach to understanding venom proteomics. Proteomics 2005, 5 , 501-510.
    • (2005) Proteomics , vol.5 , pp. 501-510
    • Serrano, S.M.1    Shannon, J.D.2    Wang, D.3    Camargo, A.C.4    Fox, J.W.5
  • 14
    • 0037066708 scopus 로고    scopus 로고
    • Structural and functional analyses of DM43, a snake venom metalloproteinase inhibitor from Didelphis marsupialis serum
    • Neves-Ferreira, A. G. C.; Perales, J.; Fox, J. W.; Shannon, J. D.; Makino, D. L.; Garratt, R. C.; Domont, G. B. Structural and functional analyses of DM43, a snake venom metalloproteinase inhibitor from Didelphis marsupialis serum. J. Biol. Chem . 2002, 277 , 13129-13137.
    • (2002) J. Biol. Chem , vol.277 , pp. 13129-13137
    • Neves-Ferreira, A.G.C.1    Perales, J.2    Fox, J.W.3    Shannon, J.D.4    Makino, D.L.5    Garratt, R.C.6    Domont, G.B.7
  • 15
    • 0034478574 scopus 로고    scopus 로고
    • Morphometric differentiation between Neotropical black-eared opossums Didelphis marsupialis and D. aurita (Didelphimorphia, Didelphidae)
    • Cerqueira, R.; Lemos, B. Morphometric differentiation between Neotropical black-eared opossums Didelphis marsupialis and D. aurita (Didelphimorphia, Didelphidae). Mammalia 2000, 64 , 319-327.
    • (2000) Mammalia , vol.64 , pp. 319-327
    • Cerqueira, R.1    Lemos, B.2
  • 16
    • 0034193970 scopus 로고    scopus 로고
    • Isolation and characterization of DM40 and DM43, two snake venom metalloproteinase inhibitors from Didelphis marsupialis serum
    • Neves-Ferreira, A. G. C.; Cardinale, N.; Rocha, S. L. G.; Perales, J.; Domont, G. B. Isolation and characterization of DM40 and DM43, two snake venom metalloproteinase inhibitors from Didelphis marsupialis serum. Biochim. Biophys. Acta 2000, 1474 , 309-320.
    • (2000) Biochim. Biophys. Acta , vol.1474 , pp. 309-320
    • Neves-Ferreira, A.G.C.1    Cardinale, N.2    Rocha, S.L.G.3    Perales, J.4    Domont, G.B.5
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 1970, 227 , 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Gorg, A.; Weiss, W.; Dunn, M. J. Current two-dimensional electrophoresis technology for proteomics. Proteomics 2004, 4 , 3665-3685.
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Gorg, A.1    Weiss, W.2    Dunn, M.J.3
  • 22
    • 33748795376 scopus 로고    scopus 로고
    • Cidade, D. A.; Simao, T. A.; Davila, A. M.; Wagner, G.; L., J.-d.-A I.; Ho, P. L.; Bon, C.; Zingali, R. B.; Albano, R. M. Bothrops jararaca venom gland transcriptome: analysis of the gene expression pattern. Toxicon 2006, 48 , 437-461.
    • Cidade, D. A.; Simao, T. A.; Davila, A. M.; Wagner, G.; L., J.-d.-A I.; Ho, P. L.; Bon, C.; Zingali, R. B.; Albano, R. M. Bothrops jararaca venom gland transcriptome: analysis of the gene expression pattern. Toxicon 2006, 48 , 437-461.
  • 23
    • 30144443840 scopus 로고    scopus 로고
    • Peptide sequence analysis
    • Medzihradszky, K. F. Peptide sequence analysis. Methods Enzymol . 2005, 402 , 209-244.
    • (2005) Methods Enzymol , vol.402 , pp. 209-244
    • Medzihradszky, K.F.1
  • 24
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet, F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res . 1988, 16 , 10881-10890.
    • (1988) Nucleic Acids Res , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 28
    • 0029030882 scopus 로고
    • J. B. Atrolysins: Metalloproteinases from Crotalus atrox venom
    • Fox, J. W.; B arnason, J. B. Atrolysins: metalloproteinases from Crotalus atrox venom. Methods Enzymol . 1995, 248 , 368-387.
    • (1995) Methods Enzymol , vol.248 , pp. 368-387
    • Fox, J.W.1    arnason, B.2
  • 31
    • 19544381172 scopus 로고    scopus 로고
    • Hemorrhage induced by snake venom metalloproteinases: Biochemical and biophysical mechanisms involved in microvessel damage
    • Gutierrez, J. M.; Rucavado, A.; Escalante, T.; Diaz, C. Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage. Toxicon 2005, 45 , 997-1011.
    • (2005) Toxicon , vol.45 , pp. 997-1011
    • Gutierrez, J.M.1    Rucavado, A.2    Escalante, T.3    Diaz, C.4
  • 32
    • 0037121083 scopus 로고    scopus 로고
    • A survey of gene expression and diversity in the venom glands of the pitviper snake Bothrops insularis through the generation of expressed sequence tags (ESTs)
    • Junqueira-de-Azevedo, I. L.; Ho, P. L. A survey of gene expression and diversity in the venom glands of the pitviper snake Bothrops insularis through the generation of expressed sequence tags (ESTs). Gene 2002, 299 , 279-291.
    • (2002) Gene , vol.299 , pp. 279-291
    • Junqueira-de-Azevedo, I.L.1    Ho, P.L.2
  • 33
    • 33846625097 scopus 로고    scopus 로고
    • Snake venomics of Bitis gabonica gabonica . Protein family composition, subunit organization of venom toxins, and characterization of dimeric disintegrins bitisgabonin-1 and bitisgabonin-2
    • Calvete, J. J.; Marcinkiewicz, C.; Sanz, L. Snake venomics of Bitis gabonica gabonica . Protein family composition, subunit organization of venom toxins, and characterization of dimeric disintegrins bitisgabonin-1 and bitisgabonin-2. J. Proteome Res . 2007, 6 , 326-236.
    • (2007) J. Proteome Res , vol.6 , pp. 326-236
    • Calvete, J.J.1    Marcinkiewicz, C.2    Sanz, L.3
  • 34
    • 13844299232 scopus 로고    scopus 로고
    • Integrating gene and protein expression data: Pattern analysis and profile mining
    • Cox, B.; Kislinger, T.; Emili, A. Integrating gene and protein expression data: pattern analysis and profile mining. Methods 2005, 35 , 303-314.
    • (2005) Methods , vol.35 , pp. 303-314
    • Cox, B.1    Kislinger, T.2    Emili, A.3
  • 35
    • 0025931518 scopus 로고
    • Snake venom variability: Methods of study, results and interpretation
    • Chippaux, J. P.; Williams, V.; White, J. Snake venom variability: methods of study, results and interpretation. Toxicon 1991, 29 , 1279-1303.
    • (1991) Toxicon , vol.29 , pp. 1279-1303
    • Chippaux, J.P.1    Williams, V.2    White, J.3
  • 36
    • 44349151718 scopus 로고    scopus 로고
    • Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulde bond formation and their contribution to venom complexity
    • Fox, J. W.; Serrano, S. M. Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulde bond formation and their contribution to venom complexity. FEBS J. 2008, 275 , 3016-3030
    • (2008) FEBS J , vol.275 , pp. 3016-3030
    • Fox, J.W.1    Serrano, S.M.2
  • 37
    • 0028176523 scopus 로고
    • Refined 2.0 A X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin
    • Gomis-Ruth, F. X.; Kress, L. F.; Kellermann, J.; Mayr, I.; Lee, X.; Huber, R.; Bode, W. Refined 2.0 A X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin. J. Mol. Biol . 1994, 239 , 513-544.
    • (1994) J. Mol. Biol , vol.239 , pp. 513-544
    • Gomis-Ruth, F.X.1    Kress, L.F.2    Kellermann, J.3    Mayr, I.4    Lee, X.5    Huber, R.6    Bode, W.7
  • 38
    • 0033850683 scopus 로고    scopus 로고
    • Primary structure and autoproteolysis of brevilysin H6 from the venom of Gloydius halys brevicaudus
    • Fujimura, S.; Oshikawa, K.; Terada, S.; Kimoto, E. Primary structure and autoproteolysis of brevilysin H6 from the venom of Gloydius halys brevicaudus. J. Biochem. (Tokyo) 2000, 128 , 167-173.
    • (2000) J. Biochem. (Tokyo) , vol.128 , pp. 167-173
    • Fujimura, S.1    Oshikawa, K.2    Terada, S.3    Kimoto, E.4
  • 40
    • 19544382337 scopus 로고    scopus 로고
    • Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases
    • Fox, J. W.; Serrano, S. M. Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases. Toxicon 2005, 45 , 969-985.
    • (2005) Toxicon , vol.45 , pp. 969-985
    • Fox, J.W.1    Serrano, S.M.2
  • 41
    • 0028233804 scopus 로고    scopus 로고
    • Usami, Y.; Fujimura, Y.; Miura, S.; Shima, H.; Yoshida, E.; Yoshioka, A.; Hirano, K.; Suzuki, M.; Titani, K. A 28 kDa-protein with disintegrin-like structure (jararhagin-C) purified from Bothrops jararaca venom inhibits collagen- and ADP-induced platelet aggregation. Biochem. Biophys. Res. Commun . 1994, 201 , 331-339.
    • Usami, Y.; Fujimura, Y.; Miura, S.; Shima, H.; Yoshida, E.; Yoshioka, A.; Hirano, K.; Suzuki, M.; Titani, K. A 28 kDa-protein with disintegrin-like structure (jararhagin-C) purified from Bothrops jararaca venom inhibits collagen- and ADP-induced platelet aggregation. Biochem. Biophys. Res. Commun . 1994, 201 , 331-339.
  • 43
    • 0029814973 scopus 로고    scopus 로고
    • Evolution of disintegrin cysteine-rich and mammalian matrix-degrading metalloproteinases: Gene duplication and divergence of a common ancestor rather than convergent evolution
    • Moura-da-Silva, A. M.; Theakston, R. D.; Crampton, J. M. Evolution of disintegrin cysteine-rich and mammalian matrix-degrading metalloproteinases: gene duplication and divergence of a common ancestor rather than convergent evolution. J. Mol. Evol . 1996, 43 , 263-269.
    • (1996) J. Mol. Evol , vol.43 , pp. 263-269
    • Moura-da-Silva, A.M.1    Theakston, R.D.2    Crampton, J.M.3
  • 45
    • 9744281932 scopus 로고    scopus 로고
    • Molecular diversity and accelerated evolution of C-type lectin-like proteins from snake venom
    • Ogawa, T.; Chijiwa, T.; Oda-Ueda, N.; Ohno, M. Molecular diversity and accelerated evolution of C-type lectin-like proteins from snake venom. Toxicon 2005, 45 , 1-14.
    • (2005) Toxicon , vol.45 , pp. 1-14
    • Ogawa, T.1    Chijiwa, T.2    Oda-Ueda, N.3    Ohno, M.4
  • 47
    • 19544386458 scopus 로고    scopus 로고
    • Snake venom probes of platelet adhesion receptors and their ligands
    • Wijeyewickrema, L. C.; Berndt, M. C.; Andrews, R. K. Snake venom probes of platelet adhesion receptors and their ligands. Toxicon 2005, 45 , 1051-1061.
    • (2005) Toxicon , vol.45 , pp. 1051-1061
    • Wijeyewickrema, L.C.1    Berndt, M.C.2    Andrews, R.K.3
  • 48
    • 0031172514 scopus 로고    scopus 로고
    • Inhibitory properties of the antibothropic complex from the South American opossum (Didelphis marsupialis) serum
    • Neves-Ferreira, A. G. C.; Perales, J.; Ovadia, M.; Moussatche, H.; Domont, G. B. Inhibitory properties of the antibothropic complex from the South American opossum (Didelphis marsupialis) serum. Toxicon 1997, 35 , 849-863.
    • (1997) Toxicon , vol.35 , pp. 849-863
    • Neves-Ferreira, A.G.C.1    Perales, J.2    Ovadia, M.3    Moussatche, H.4    Domont, G.B.5
  • 49
    • 0025879175 scopus 로고
    • Complete primary structure of a galactose-specific lectin from the venom of the rattlesnake Crotalus atrox . Homologies with Ca2(+)-dependent-type lectins
    • Hirabayashi, J.; Kusunoki, T.; Kasai, K. Complete primary structure of a galactose-specific lectin from the venom of the rattlesnake Crotalus atrox . Homologies with Ca2(+)-dependent-type lectins. J. Biol. Chem . 1991, 266 , 2320-2326.
    • (1991) J. Biol. Chem , vol.266 , pp. 2320-2326
    • Hirabayashi, J.1    Kusunoki, T.2    Kasai, K.3
  • 50
    • 4043092774 scopus 로고    scopus 로고
    • Structure and function of snake venom cysteine-rich secretory proteins
    • Yamazaki, Y.; Morita, T. Structure and function of snake venom cysteine-rich secretory proteins. Toxicon 2004, 44 , 227-231.
    • (2004) Toxicon , vol.44 , pp. 227-231
    • Yamazaki, Y.1    Morita, T.2
  • 51
    • 38449100299 scopus 로고    scopus 로고
    • Trends in snakebite envenomation therapy: Scientific, technological and public health considerations
    • Gutierrez, J. M.; Lomonte, B.; Leon, G.; Rucavado, A.; Chaves, F.; Angulo, Y. Trends in snakebite envenomation therapy: scientific, technological and public health considerations. Curr. Pharm. Des . 2007, 13 , 2935-2950.
    • (2007) Curr. Pharm. Des , vol.13 , pp. 2935-2950
    • Gutierrez, J.M.1    Lomonte, B.2    Leon, G.3    Rucavado, A.4    Chaves, F.5    Angulo, Y.6


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