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Volumn , Issue , 2011, Pages 285-300

Brief history and molecular determinants of snake venom disintegrin evolution

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EID: 79960075940     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-90-481-9295-3_18     Document Type: Chapter
Times cited : (24)

References (52)
  • 1
    • 33846434837 scopus 로고    scopus 로고
    • Loss of introns along the evolutionary diversification pathway of snake venom disintegrins evidenced by sequence analysis of genomic DNA from Macrovipera lebetina transmediterranea and Echis ocellatus
    • Bazaa, A., Juárez, P., Marrakchi, N., Lasfer, Z.B., El Ayeb, M., Harrison, R.A., Calvete, J.J., Sanz, L., 2007. Loss of introns along the evolutionary diversification pathway of snake venom disintegrins evidenced by sequence analysis of genomic DNA from Macrovipera lebetina transmediterranea and Echis ocellatus. J. Mol. Evol. 64, 261-271.
    • (2007) J. Mol. Evol. , vol.64 , pp. 261-271
    • Bazaa, A.1    Juárez, P.2    Marrakchi, N.3    Lasfer, Z.B.4    El Ayeb, M.5    Harrison, R.A.6    Calvete, J.J.7    Sanz, L.8
  • 2
    • 4344607978 scopus 로고    scopus 로고
    • Crystal structure of schistatin, a disintegrin homodimer from saw-scaled viper (Echis carinatus) at 2.5 Å resolution
    • Bilgrami, S., Tomar, S., Yadav, S., Kaur, P., Kumar, J., Jabeen, T., Sharma, S., Singh, T.P., 2004. Crystal structure of schistatin, a disintegrin homodimer from saw-scaled viper (Echis carinatus) at 2.5 Å resolution. J. Mol. Biol. 341, 829-837.
    • (2004) J. Mol. Biol. , vol.341 , pp. 829-837
    • Bilgrami, S.1    Tomar, S.2    Yadav, S.3    Kaur, P.4    Kumar, J.5    Jabeen, T.6    Sharma, S.7    Singh, T.P.8
  • 3
    • 23944518374 scopus 로고    scopus 로고
    • Crystal structure of the disintegrin heterodimer from saw-scaled viper (Echis carinatus) at 1.9 Å resolution
    • Bilgrami, S., Yadav, S., Sharma, S., Perbandt, M., Betzel, C., Singh, T.P., 2005. Crystal structure of the disintegrin heterodimer from saw-scaled viper (Echis carinatus) at 1.9 Å resolution. Biochemistry 44, 11058-11066.
    • (2005) Biochemistry , vol.44 , pp. 11058-11066
    • Bilgrami, S.1    Yadav, S.2    Sharma, S.3    Perbandt, M.4    Betzel, C.5    Singh, T.P.6
  • 4
    • 0030786687 scopus 로고    scopus 로고
    • The disulphide bond pattern of bitistatin, a disintegrin isolated from the venom of the viper Bitis arietans
    • Calvete, J.J., Schrader, M., Raida, M., McLane, M.A., Romero, A., Niewiarowski, S., 1997. The disulphide bond pattern of bitistatin, a disintegrin isolated from the venom of the viper Bitis arietans. FEBS Lett. 416, 197-202.
    • (1997) FEBS Lett , vol.416 , pp. 197-202
    • Calvete, J.J.1    Schrader, M.2    Raida, M.3    McLane, M.A.4    Romero, A.5    Niewiarowski, S.6
  • 5
    • 0038385565 scopus 로고    scopus 로고
    • Disulfide bond pattern and molecular modelling of the dimeric disintegrin EMF-10, a potent and selective integrin α5β1 antagonist from Eristocophis macmahoni venom
    • Calvete, J.J., Jürgens, M., Marcinkiewicz, C., Romero, A., Schrader, M., Niewiarowski, S., 2000. Disulfide bond pattern and molecular modelling of the dimeric disintegrin EMF-10, a potent and selective integrin α5β1 antagonist from Eristocophis macmahoni venom. Biochem. J. 345, 573-581.
    • (2000) Biochem. J. , vol.345 , pp. 573-581
    • Calvete, J.J.1    Jürgens, M.2    Marcinkiewicz, C.3    Romero, A.4    Schrader, M.5    Niewiarowski, S.6
  • 6
    • 0037065736 scopus 로고    scopus 로고
    • The presence of theWGD motif in CC8 heterodimeric disintegrin increases its inhibitory effect on αIIbβ3, αvβ3, and α5β1 integrins
    • Calvete, J.J., Fox, J.W., Agelan, A., Niewiarowski, S., Marcinkiewicz, C., 2002. The presence of theWGD motif in CC8 heterodimeric disintegrin increases its inhibitory effect on αIIbβ3, αvβ3, and α5β1 integrins. Biochemistry 41, 2014-2021.
    • (2002) Biochemistry , vol.41 , pp. 2014-2021
    • Calvete, J.J.1    Fox, J.W.2    Agelan, A.3    Niewiarowski, S.4    Marcinkiewicz, C.5
  • 7
    • 0037591683 scopus 로고    scopus 로고
    • Snake venom disintegrins: Novel dimeric disintegrins and structural diversification by disulfide bond engineering
    • Calvete, J.J., Moreno-Murciano, M.P., Theakston, R.D.G., Kisiel, D.G., Marcinkiewicz, C., 2003. Snake venom disintegrins: novel dimeric disintegrins and structural diversification by disulfide bond engineering. Biochem. J. 372, 725-734.
    • (2003) Biochem. J. , vol.372 , pp. 725-734
    • Calvete, J.J.1    Moreno-Murciano, M.P.2    Theakston, R.D.G.3    Kisiel, D.G.4    Marcinkiewicz, C.5
  • 8
    • 14744294145 scopus 로고    scopus 로고
    • Structure-function correlations of snake venom disintegrins
    • Calvete, J.J., 2005. Structure-function correlations of snake venom disintegrins. Curr. Pharm. Des. 11, 829-835.
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 829-835
    • Calvete, J.J.1
  • 10
    • 38449112500 scopus 로고    scopus 로고
    • KTS- And RTS-disintegrins: Anti-angiogenic viper venom peptides specifically targeting the α1β1 integrin
    • Calvete, J.J., Marcinkiewicz, C., Sanz, L., 2007. KTS- And RTS-disintegrins: Anti-angiogenic viper venom peptides specifically targeting the α1β1 integrin. Curr. Pharm. Des. 13, 2853-2859.
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 2853-2859
    • Calvete, J.J.1    Marcinkiewicz, C.2    Sanz, L.3
  • 11
    • 84863778982 scopus 로고    scopus 로고
    • Snake venomics and disintegrins, Portrait and evolution of a family of snake venom integrin antagonists
    • Mackessy, S.P. (Ed.), CRC Press, Taylor & Francis, Boca Raton
    • Calvete, J.J., Juárez, P., Sanz, L., 2009. Snake venomics and disintegrins. Portrait and evolution of a family of snake venom integrin antagonists, in: Mackessy, S.P. (Ed.), Handbook of Venoms and Toxins of Reptiles. CRC Press, Taylor & Francis, Boca Raton, 337-357.
    • (2009) Handbook of Venoms and Toxins of Reptiles , pp. 337-357
    • Calvete, J.J.1    Juárez, P.2    Sanz, L.3
  • 12
    • 79952242815 scopus 로고    scopus 로고
    • Snake venomics, antivenomics, and venom phenotyping: The ménage à trois of proteomic tools aimed at understanding the biodiversity of venoms
    • Kini, R.M. Clemetson, K.J. Markland, F.S. McLane, M.A. Morita, T. (Eds.), Springer, Dordrecht, The Netherlands
    • Calvete, J.J., 2010. Snake venomics, antivenomics, and venom phenotyping: The ménage à trois of proteomic tools aimed at understanding the biodiversity of venoms, in: Kini, R.M., Clemetson, K.J., Markland, F.S., McLane, M.A., Morita, T. (Eds.), Toxins and Hemostasis: From Bench to Bedside. Springer, Dordrecht, The Netherlands.
    • (2010) Toxins and Hemostasis: from Bench to Bedside
    • Calvete, J.J.1
  • 13
    • 73649091449 scopus 로고    scopus 로고
    • Snake venomics of the Central American rattlesnake Crotalus simus and the South American Crotalus durissus complex points to neurotoxicity as an adaptive paedomorphic trend along Crotalus dispersal in South America
    • Calvete, J.J., Sanz, L., Cid, P., De La Torre, P., Flores-Díaz, M., Dos Santos, M.C., Borges, A., Bremo, A., Angulo, Y., Lomonte, B., Alape-Girón, A., Gutiérrez, J.M., 2010. Snake venomics of the Central American rattlesnake Crotalus simus and the South American Crotalus durissus complex points to neurotoxicity as an adaptive paedomorphic trend along Crotalus dispersal in South America. J. Proteome Res. 9(1), 528-544.
    • (2010) J. Proteome Res. , vol.9 , Issue.1 , pp. 528-544
    • Calvete, J.J.1    Sanz, L.2    Cid, P.3    De La Torre, P.4    Flores-Díaz, M.5    Dos Santos, M.C.6    Borges, A.7    Bremo, A.8    Angulo, Y.9    Lomonte, B.10    Alape-Girón, A.11    Gutiérrez, J.M.12
  • 14
    • 33645007877 scopus 로고    scopus 로고
    • Bayesian mixed models and the phylogeny of pitvipers (Viperidae: Serpentes)
    • Castoe, T.A., Parkinson, C.L., 2006. Bayesian mixed models and the phylogeny of pitvipers (Viperidae: Serpentes). Mol. Phylogenet. Evol. 39, 91-110.
    • (2006) Mol. Phylogenet. Evol. , vol.39 , pp. 91-110
    • Castoe, T.A.1    Parkinson, C.L.2
  • 17
    • 19544394601 scopus 로고    scopus 로고
    • Snake toxins and hemostasis
    • Fox, J.W., Serrano, S.M., 2005. Snake toxins and hemostasis. Toxicon 45, 951-1181.
    • (2005) Toxicon , vol.45 , pp. 951-1181
    • Fox, J.W.1    Serrano, S.M.2
  • 18
    • 44349151718 scopus 로고    scopus 로고
    • Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity
    • Fox, J.W., Serrano, S.M.T., 2008. Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity. FEBS J. 275, 3016-3030.
    • (2008) FEBS J , vol.275 , pp. 3016-3030
    • Fox, J.W.1    Serrano, S.M.T.2
  • 19
    • 60149105208 scopus 로고    scopus 로고
    • Timeline of key events in snake venom metalloproteinase research
    • Fox, J.W., Serrano, S.M., 2009. Timeline of key events in snake venom metalloproteinase research. J. Proteomics 72, 200-209.
    • (2009) J. Proteomics , vol.72 , pp. 200-209
    • Fox, J.W.1    Serrano, S.M.2
  • 21
    • 60149097881 scopus 로고    scopus 로고
    • Evolution and diversification of the Toxicofera reptile venom system
    • Fry, B.G., Vidal, N., van derWeerd, L., Kochva, E., Renjifo, C., 2009. Evolution and diversification of the Toxicofera reptile venom system. J. Proteomics 72, 127-136.
    • (2009) J. Proteomics , vol.72 , pp. 127-136
    • Fry, B.G.1    Vidal, N.2    Van DerWeerd, L.3    Kochva, E.4    Renjifo, C.5
  • 22
    • 1942533493 scopus 로고    scopus 로고
    • Positive selection at reproductive ADAM genes with potential intercellular binding activity
    • Glassey, B, Civetta, A., 2004. Positive selection at reproductive ADAM genes with potential intercellular binding activity. Mol. Biol. Evol. 21:851-859.
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 851-859
    • Glassey, B.1    Civetta, A.2
  • 23
    • 0028342845 scopus 로고
    • The evolution of functionally novel proteins after gene duplication
    • Hughes, A.L., 1994. The evolution of functionally novel proteins after gene duplication. Proc. Roy. Soc. London Scr. B. 256, 119-124.
    • (1994) Proc. Roy. Soc. London Scr. B. , vol.256 , pp. 119-124
    • Hughes, A.L.1
  • 25
    • 0030273873 scopus 로고    scopus 로고
    • Snake venom metalloproteinases: Structure, function and relationship to the ADAMs family of proteins
    • Jia, L-G., Shimokawa, K-I., Bjarnason, J.B., Fox, J.W., 1996. Snake venom metalloproteinases: structure, function and relationship to the ADAMs family of proteins. Toxicon 34, 1269-1276.
    • (1996) Toxicon , vol.34 , pp. 1269-1276
    • Jia, L.-G.1    Shimokawa, K.-I.2    Bjarnason, J.B.3    Fox, J.W.4
  • 26
    • 33745600373 scopus 로고    scopus 로고
    • Molecular cloning of disintegrin-like transcript BA-5A from Bitis arietans venom gland cDNA library: A putative intermediate in the evolution of the long chain disintegrin bitistatin
    • Juárez, P., Wagstaff, S.C., Oliver, J., Sanz, L., Harrison, R.A., Calvete, J.J., 2006a. Molecular cloning of disintegrin-like transcript BA-5A from Bitis arietans venom gland cDNA library: A putative intermediate in the evolution of the long chain disintegrin bitistatin. J. Mol. Evol. 63, 142-152.
    • (2006) J. Mol. Evol. , vol.63 , pp. 142-152
    • Juárez, P.1    Wagstaff, S.C.2    Oliver, J.3    Sanz, L.4    Harrison, R.A.5    Calvete, J.J.6
  • 27
    • 33745601887 scopus 로고    scopus 로고
    • Molecular cloning of Echis ocellatus disintegrins reveals non-venom-secreted proteins and a pathway for the evolution of ocellatusin
    • Juárez, P., Wagstaff, S.C., Sanz, L., Harrison, R.A., Calvete, J.J., 2006b. Molecular cloning of Echis ocellatus disintegrins reveals non-venom-secreted proteins and a pathway for the evolution of ocellatusin. J. Mol. Evol. 63, 183-193.
    • (2006) J. Mol. Evol. , vol.63 , pp. 183-193
    • Juárez, P.1    Wagstaff, S.C.2    Sanz, L.3    Harrison, R.A.4    Calvete, J.J.5
  • 28
    • 54149086758 scopus 로고    scopus 로고
    • Evolution of snake venom disintegrins by positive Darwinian selection
    • Juárez, P., Comas, I., González-Candelas, F., Calvete, J.J., 2008. Evolution of snake venom disintegrins by positive Darwinian selection. Mol. Biol. Evol. 25, 2391-2407.
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 2391-2407
    • Juárez, P.1    Comas, I.2    González-Candelas, F.3    Calvete, J.J.4
  • 29
    • 0026506731 scopus 로고
    • Structural domains in venom proteins: Evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor
    • Kini, R.M., Evans, H.J., 1992. Structural domains in venom proteins: evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor. Toxicon 30, 265-293.
    • (1992) Toxicon , vol.30 , pp. 265-293
    • Kini, R.M.1    Evans, H.J.2
  • 30
    • 0034782555 scopus 로고    scopus 로고
    • Evolutionary relationships among the true vipers (Reptilia: Viperidae) inferred from mitochondrial dna sequences
    • Lenk, P., Kalyabina, S., Wink, M., Joger, U., 2001. Evolutionary relationships among the true vipers (Reptilia: Viperidae) inferred from mitochondrial dna sequences. Mol. Phylogenet. Evol. 19, 94-104.
    • (2001) Mol. Phylogenet. Evol. , vol.19 , pp. 94-104
    • Lenk, P.1    Kalyabina, S.2    Wink, M.3    Joger, U.4
  • 35
    • 0034644725 scopus 로고    scopus 로고
    • Inhibitory effects of MLDG-containing heterodimeric disintegrins reveal distinct structural requirements for interaction of the integrin α9β1 with VCAM-1, tenascin-C, and osteopontin
    • Marcinkiewicz, C., Taooka, Y., Yokosaki, Y., Calvete, J.J., Marcinkiewicz, M.M., Lobb, R.R., Niewiarowski, S., Sheppard, D., 2000. Inhibitory effects of MLDG-containing heterodimeric disintegrins reveal distinct structural requirements for interaction of the integrin α9β1 with VCAM-1, tenascin-C, and osteopontin. J. Biol. Chem. 275, 31930-31937.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31930-31937
    • Marcinkiewicz, C.1    Taooka, Y.2    Yokosaki, Y.3    Calvete, J.J.4    Marcinkiewicz, M.M.5    Lobb, R.R.6    Niewiarowski, S.7    Sheppard, D.8
  • 36
    • 14744285652 scopus 로고    scopus 로고
    • Functional characteristics of snake venom disintegrins: Potential therapeutic implications
    • Marcinkiewicz, C., 2005. Functional characteristics of snake venom disintegrins: potential therapeutic implications. Curr. Pharm. Des. 11, 815-827.
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 815-827
    • Marcinkiewicz, C.1
  • 37
    • 0242664789 scopus 로고    scopus 로고
    • Concerted motions of the integrin-binding loop and the C-terminal tail of the non-RGD disintegrin obtustatin
    • Monleón, D., Moreno-Murciano, M.P., Kovacs, H., Marcinkiewicz, C., Calvete, J.J., Celda, B., 2003. Concerted motions of the integrin-binding loop and the C-terminal tail of the non-RGD disintegrin obtustatin. J. Biol. Chem. 278, 45570-45576.
    • (2003) J. Biol. Chem. , vol.278 , pp. 45570-45576
    • Monleón, D.1    Moreno-Murciano, M.P.2    Kovacs, H.3    Marcinkiewicz, C.4    Calvete, J.J.5    Celda, B.6
  • 38
    • 17144392170 scopus 로고    scopus 로고
    • Conformation and concerted dynamics of the integrin-binding site and the C-terminal region of echistatin revealed by homonuclear NMR
    • Monleón, D., Esteve, V., Kovacs, H., Calvete, J.J., Celda, B., 2005. Conformation and concerted dynamics of the integrin-binding site and the C-terminal region of echistatin revealed by homonuclear NMR. Biochem. J. 387, 57-66.
    • (2005) Biochem. J. , vol.387 , pp. 57-66
    • Monleón, D.1    Esteve, V.2    Kovacs, H.3    Calvete, J.J.4    Celda, B.5
  • 40
    • 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.G., Crampton, J.M., 1996. 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. 43, 263-269.
    • (1996) J. Mol. Evol. , vol.43 , pp. 263-269
    • Moura Da Silva, A.M.1    Theakston, R.D.G.2    Crampton, J.M.3
  • 41
    • 0030791307 scopus 로고    scopus 로고
    • Evolution by the birth-and-death process in multigene families of the vertebrate immune system
    • Nei, M., Gu, X., Sitnikova, T., 1997. Evolution by the birth-and-death process in multigene families of the vertebrate immune system. Proc. Natl. Acad. Sci. U.S.A. 94, 7799-7806.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 7799-7806
    • Nei, M.1    Gu, X.2    Sitnikova, T.3
  • 42
    • 0028150753 scopus 로고
    • Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors
    • Niewiarowski, S., McLane, M.A., Kloczewiak, M., Stewart, G.J., 1994. Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors. Semin. Hematol. 31, 289-300.
    • (1994) Semin. Hematol. , vol.31 , pp. 289-300
    • Niewiarowski, S.1    McLane, M.A.2    Kloczewiak, M.3    Stewart, G.J.4
  • 43
    • 0034213348 scopus 로고    scopus 로고
    • Primary structure and functional characterization of bilitoxin-1, a novel dimeric P-II snake venom metalloproteinase from Agkistrodon bilineatus venom
    • Nikai, T., Taniguchi, K., Komori, Y., Masuda, K., Fox, J.W., Sugihara, S., 2000. Primary structure and functional characterization of bilitoxin-1, a novel dimeric P-II snake venom metalloproteinase from Agkistrodon bilineatus venom. Arch. Biochem. Biophys. 378, 6-15.
    • (2000) Arch. Biochem. Biophys. , vol.378 , pp. 6-15
    • Nikai, T.1    Taniguchi, K.2    Komori, Y.3    Masuda, K.4    Fox, J.W.5    Sugihara, S.6
  • 44
    • 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., 2005. Molecular diversity and accelerated evolution of C-type lectin-like proteins from snake venom. Toxicon 45, 1-14.
    • (2005) Toxicon , vol.45 , pp. 1-14
    • Ogawa, T.1    Chijiwa, T.2    Oda-Ueda, N.3    Ohno, M.4
  • 45
    • 0037016015 scopus 로고    scopus 로고
    • A new gene structure of the disintegrin family: A subunit of dimeric disintegrin has a short coding region
    • Okuda, D., Koike, H., Morita, T., 2002. A new gene structure of the disintegrin family: A subunit of dimeric disintegrin has a short coding region. Biochemistry 41, 14248-14254.
    • (2002) Biochemistry , vol.41 , pp. 14248-14254
    • Okuda, D.1    Koike, H.2    Morita, T.3
  • 46
    • 33645789298 scopus 로고    scopus 로고
    • Molecular cloning of disintegrins from Cerastes vipera and Macrovipera lebetina transmediterranea venom gland cDNA libraries, Insight into the evolution of the snake venom's integrin inhibition system
    • Sanz, L., Bazaa, A., Marrakchi, N., Pérez, A., Chenik, M., Bel Lasfer, Z., El Ayeb, M., Calvete, J.J., 2006. Molecular cloning of disintegrins from Cerastes vipera and Macrovipera lebetina transmediterranea venom gland cDNA libraries. Insight into the evolution of the snake venom's integrin inhibition system. Biochem. J. 395, 385-392.
    • (2006) Biochem. J. , vol.395 , pp. 385-392
    • Sanz, L.1    Bazaa, A.2    Marrakchi, N.3    Pérez, A.4    Chenik, M.5    Bel Lasfer, Z.6    El Ayeb, M.7    Calvete, J.J.8
  • 47
    • 33745731954 scopus 로고    scopus 로고
    • Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold
    • Takeda, S., Igarashi, T., Mori, H., Araki, S., 2006. Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold. EMBO J. 25, 2388-2396.
    • (2006) EMBO J , vol.25 , pp. 2388-2396
    • Takeda, S.1    Igarashi, T.2    Mori, H.3    Araki, S.4
  • 48
    • 63649149047 scopus 로고    scopus 로고
    • Three-dimensional domain architecture of the ADAM family proteinases
    • Takeda, S., 2009. Three-dimensional domain architecture of the ADAM family proteinases. Semin. Cell. Dev. Biol., 20, 146-152.
    • (2009) Semin. Cell. Dev. Biol. , vol.20 , pp. 146-152
    • Takeda, S.1
  • 49
    • 0036760668 scopus 로고    scopus 로고
    • Higher-level relationships of snakes inferred from four nuclear and mitochondrial genes
    • Vidal, N., Hedges, S.B., 2002. Higher-level relationships of snakes inferred from four nuclear and mitochondrial genes. C. R. Biol. 325, 977-985.
    • (2002) C. R. Biol. , vol.325 , pp. 977-985
    • Vidal, N.1    Hedges, S.B.2
  • 50
    • 0035423930 scopus 로고    scopus 로고
    • Purification, molecular cloning and mechanism of action of graminelysin I, a snake-venom-derived metalloproteinase that induces apoptosis of human endothelial cells
    • Wu, W.B., Chang, S.C., Liau, M.Y., Huang, T.F., 2001. Purification, molecular cloning and mechanism of action of graminelysin I, a snake-venom-derived metalloproteinase that induces apoptosis of human endothelial cells. Biochem. J. 357, 719-728.
    • (2001) Biochem. J. , vol.357 , pp. 719-728
    • Wu, W.B.1    Chang, S.C.2    Liau, M.Y.3    Huang, T.F.4
  • 51
    • 55049125206 scopus 로고    scopus 로고
    • A nesting of vipers: Phylogeny and historical biogeography of the Viperidae (Squamata: Serpentes)
    • Wüster, W., Peppin, L., Pook, C.E., Walker, D.E., 2008. A nesting of vipers: phylogeny and historical biogeography of the Viperidae (Squamata: Serpentes). Mol. Phylogenet. Evol. 49, 445-459.
    • (2008) Mol. Phylogenet. Evol. , vol.49 , pp. 445-459
    • Wüster, W.1    Peppin, L.2    Pook, C.E.3    Walker, D.E.4
  • 52
    • 0037023363 scopus 로고    scopus 로고
    • The crystal structure of the extracellular segment of integrin αvβ3 in complex with an Arg-Gly-Asp ligand
    • Xiong, J-P., Stehle, T., Zhang, R., Joachimiak, A., Frech, M., Goodman, S.L., Arnaout, M.A., 2002. The crystal structure of the extracellular segment of integrin αvβ3 in complex with an Arg-Gly-Asp ligand. Science 296, 151-155.
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.-P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.L.6    Arnaout, M.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.