메뉴 건너뛰기




Volumn 8, Issue 6, 2009, Pages 3055-3067

Exploring the venom proteome of the western diamondback rattlesnake, Crotalus atrox, via snake venomics and combinatorial peptide ligand library approaches

Author keywords

Combinatorial peptide ligand library; Crotalus atrox; Glutaminyl cyclase; Low abundance proteins; Mass spectrometry; N terminal sequencing; Peroxiredoxin; Snake venomics; Venom proteome; Viperid toxins; Western diamond rattlesnake

Indexed keywords

GLUTAMINYL CYCLASE; METALLOPROTEINASE; METALLOPROTEINASE INHIBITOR; PEPTIDE LIBRARY; PEROXIREDOXIN; PHOSPHOLIPASE A2; SERINE PROTEINASE; SNAKE VENOM; UNCLASSIFIED DRUG; VASOACTIVE AGENT;

EID: 67049132403     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr900249q     Document Type: Article
Times cited : (135)

References (83)
  • 1
    • 0000651593 scopus 로고
    • Physiology of an infrared receptor: The facial pit of pit vipers
    • Bullock, T. H.; Cowles, R. B. Physiology of an infrared receptor: the facial pit of pit vipers. Science 1952, 115, 541-543.
    • (1952) Science , vol.115 , pp. 541-543
    • Bullock, T.H.1    Cowles, R.B.2
  • 2
    • 34548623413 scopus 로고    scopus 로고
    • The imaging properties and sensitivity of the facial pits of pitvipers as determined by optical and heat-transfer analysis
    • DOI 10.1242/jeb.006965
    • Bakken, G. S.; Krochmal, A. R. The imaging properties and sensitivity of the facial pit of pitvipers as determined by optical and heat-transfer analysis. J. Exp. Biol. 2007, 210, 2801-2810. (Pubitemid 47401647)
    • (2007) Journal of Experimental Biology , vol.210 , Issue.16 , pp. 2801-2810
    • Bakken, G.S.1    Krochmal, A.R.2
  • 4
    • 33645007877 scopus 로고    scopus 로고
    • Bayesian mixed models and the phylogeny of pitvipers (Viperidae: Serpentes)
    • Castoe, T. A.; Parkinson, C. L. Bayesian mixed models and the phylogeny of pitvipers (Viperidae: Serpentes). Mol. Phylogenet. Evol. 2006, 39, 91-110.
    • (2006) Mol. Phylogenet. Evol. , vol.39 , pp. 91-110
    • Castoe, T.A.1    Parkinson, C.L.2
  • 7
    • 0005207945 scopus 로고
    • Food habits of the western diamond rattlesnake, Crotalus atrox, in Texas (Viperidae)
    • Beavers, R. A. Food habits of the western diamond rattlesnake, Crotalus atrox, in Texas (Viperidae). Southwest. Nat. 1976, 20, 503-515.
    • (1976) Southwest. Nat. , vol.20 , pp. 503-515
    • Beavers, R.A.1
  • 8
    • 1942533494 scopus 로고    scopus 로고
    • Assembling an Arsenal: Origin and Evolution of the Snake Venom Proteome Inferred from Phylogenetic Analysis of Toxin Sequences
    • DOI 10.1093/molbev/msh091
    • Fry, B. G.; Wüster, W. Assembling an arsenal: origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences. Mol. Biol. Evol. 2004, 21, 870-883. (Pubitemid 38529729)
    • (2004) Molecular Biology and Evolution , vol.21 , Issue.5 , pp. 870-883
    • Fry, B.G.1    Wuster, W.2
  • 9
    • 15544369378 scopus 로고    scopus 로고
    • From genome to "venome": Molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins
    • DOI 10.1101/gr.3228405
    • Fry, B. G. From genome to "venome": molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins. Genome Res. 2005, 15, 403-420. (Pubitemid 40467782)
    • (2005) Genome Research , vol.15 , Issue.3 , pp. 403-420
    • Fry, B.G.1
  • 11
    • 0002832583 scopus 로고
    • The rattlesnakes and their venomyield and lethal toxicity
    • Tu, A. T., Ed.; Marcel Dekker: New York
    • Glenn, J. L.; Straight, R. The rattlesnakes and their venomyield and lethal toxicity. In Rattlesnake Venoms; Tu, A. T., Ed.; Marcel Dekker: New York, 1982; pp 3-119.
    • (1982) Rattlesnake Venoms , pp. 3-119
    • Glenn, J.L.1    Straight, R.2
  • 13
    • 0022655860 scopus 로고
    • Geographic and ontogenic variation in venom of the western diamondback rattlesnake (Crotalus atrox)
    • DOI 10.1016/0041-0101(86)90167-4
    • Minton, S. A.; Weinstein, S. A. Geographic and Ontogenetic variation in venom of the western diamondback rattlesnake (Crotalus atrox). Toxicon 1986, 24, 71-80. (Pubitemid 16211689)
    • (1986) Toxicon , vol.24 , Issue.1 , pp. 71-80
    • Minton, S.A.1    Weinstein, S.A.2
  • 14
    • 0025931518 scopus 로고
    • Snake venom variability: Methods of study, results ad interpretation
    • Chippaux, J. P.; Williams, V.; White, J. Snake venom variability: methods of study, results ad interpretation. Toxicon 1991, 29, 1279-1303.
    • (1991) Toxicon , vol.29 , pp. 1279-1303
    • Chippaux, J.P.1    Williams, V.2    White, J.3
  • 15
    • 85063475698 scopus 로고
    • Clinical toxicology of snakebite in North America
    • Meier, J.; White, J., Eds.; CRC Press: Boca Raton, FL
    • Gomez, H. F.; Dart, R. C. Clinical toxicology of snakebite in North America. In Handbook of Clinical Toxicology of Animal Venoms and Poisons; Meier, J.; White, J., Eds.; CRC Press: Boca Raton, FL, 1995; pp 619-644.
    • (1995) Handbook of Clinical Toxicology of Animal Venoms and Poisons , pp. 619-644
    • Gomez, H.F.1    Dart, R.C.2
  • 16
    • 60149098025 scopus 로고    scopus 로고
    • Snake venomics and antivenomics: Proteomic tools in the design and control of antivenoms for the treatment of snakebite envenoming
    • Gutiérrez, J. M.; Lomonte, B.; León, G.; Alape-Girón, A.; Flores-Díaz, M.; Sanz, L.; Angulo, Y.; Calvete, J. J. Snake venomics and antivenomics: proteomic tools in the design and control of antivenoms for the treatment of snakebite envenoming. J. Proteomics 2009, 72, 165-182.
    • (2009) J. Proteomics , vol.72 , pp. 165-182
    • Gutiérrez, J.M.1    Lomonte, B.2    León, G.3    Alape-Girón, A.4    Flores-Díaz, M.5    Sanz, L.6    Angulo, Y.7    Calvete, J.J.8
  • 18
    • 33846105870 scopus 로고    scopus 로고
    • Snake venom components and their applications in biomedicine
    • DOI 10.1007/s00018-006-6315-0
    • Koh, D. C. I.; Armugam, A.; Jeyaseelan, K. Snake venom components and their applications in biomedicine. Cell. Mol. Life Sci. 2006, 63, 3030-3041. (Pubitemid 46072306)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.24 , pp. 3030-3041
    • Koh, D.C.I.1    Armugam, A.2    Jeyaseelan, K.3
  • 19
    • 60249100679 scopus 로고    scopus 로고
    • Digging into the evolution of venomous systems and learning to twist nature to fight pathology
    • Calvete, J. J. Venomics: Digging into the evolution of venomous systems and learning to twist nature to fight pathology. J. Proteomics 2009, 72, 121-126.
    • (2009) J. Proteomics , vol.72 , pp. 121-126
    • Venomics, C.J.J.1
  • 20
    • 36148976495 scopus 로고    scopus 로고
    • Snake venomics. Strategy and applications
    • DOI 10.1002/jms.1242
    • Calvete, J. J.; Juárez, P.; Sanz, L. Snake venomics. Strategy and applications. J. Mass Spectrom. 2007, 42, 1405-1414. (Pubitemid 350113458)
    • (2007) Journal of Mass Spectrometry , vol.42 , Issue.11 , pp. 1405-1414
    • Calvete, J.J.1    Juarez, P.2    Sanz, L.3
  • 22
    • 33750112796 scopus 로고    scopus 로고
    • Protein Equalizer technology: The quest for a "democratic proteome"
    • Righetti, P. G.; Boschetti, E.; Lomas, L.; Citterio, A. Protein Equalizer technology: the quest for a "democratic proteome". Proteomics 2006, 6, 3980-3992.
    • (2006) Proteomics , vol.6 , pp. 3980-3992
    • Righetti, P.G.1    Boschetti, E.2    Lomas, L.3    Citterio, A.4
  • 23
    • 33846844892 scopus 로고    scopus 로고
    • Sherlock Holmes and the proteome - A detective story
    • Righetti, P. G.; Boschetti, E. Sherlock Holmes and the proteome - a detective story. FEBS J. 2007, 274, 897-905.
    • (2007) FEBS J. , vol.274 , pp. 897-905
    • Righetti, P.G.1    Boschetti, E.2
  • 24
    • 33846782845 scopus 로고    scopus 로고
    • Romancing the "hidden proteome", Anno Domini two zero zero seven
    • Boschetti, E.; Lomas, L.; Citterio, A.; Righetti, P. G. Romancing the "hidden proteome", Anno Domini two zero zero seven. J. Chromatogr., A 2007, 1153, 277-290.
    • (2007) J. Chromatogr., A , vol.1153 , pp. 277-290
    • Boschetti, E.1    Lomas, L.2    Citterio, A.3    Righetti, P.G.4
  • 25
    • 48849086000 scopus 로고    scopus 로고
    • The ProteoMiner and the FortyNiners: Searching for gold nuggets in the proteomic arena
    • Righetti, P. G.; Boschetti, E. The ProteoMiner and the FortyNiners: Searching for gold nuggets in the proteomic arena. Mass Spectrom. Rev. 2008, 27, 596-608.
    • (2008) Mass Spectrom. Rev. , vol.27 , pp. 596-608
    • Righetti, P.G.1    Boschetti, E.2
  • 26
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • DOI 10.1093/nar/25.17.3389
    • Altschul, S. F.; Madden, T. L.; Schaffer, A. A.; Zhang, J.; Zhang, Z.; Miller, W.; Lipman, D. J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 1997, 25, 3389-3402. (Pubitemid 27359211)
    • (1997) Nucleic Acids Research , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 27
    • 0037709383 scopus 로고    scopus 로고
    • Unique scanning capabilities of a new hybrid linear ion trap mass spectrometer (Q TRAP) used for high sensitivity proteomics applications
    • DOI 10.1002/pmic.200300415
    • Le Blanc, J. C.; Hager, J. W.; Ilisiu, A. M.; Hunter, C.; Zhong, F.; Chu, I. Unique scanning capabilities of a new hybrid linear ion trap mass spectrometer (Q TRAP) used for high sensitivity proteomics applications. Proteomics 2003, 3, 859-869. (Pubitemid 36801672)
    • (2003) Proteomics , vol.3 , Issue.6 , pp. 859-869
    • Le Blanc, J.C.Y.1    Hager, J.W.2    Ilisiu, A.M.P.3    Hunter, C.4    Zhong, F.5    Chu, I.6
  • 29
    • 1042287114 scopus 로고    scopus 로고
    • 2: Insights into the mechanisms of local and systemic myotoxicity
    • 2: insights into the mechanisms of local and systemic myotoxicity. Toxicon 2003, 42, 915-931.
    • (2003) Toxicon , vol.42 , pp. 915-931
    • Gutierrez, J.M.1    Ownby, C.L.2
  • 30
    • 1042264060 scopus 로고    scopus 로고
    • 2 myotoxins from crotalid snake venoms and their structural determinants of myotoxic action
    • 2 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    Calderón, L.3
  • 31
    • 19544381172 scopus 로고    scopus 로고
    • Hemorrhage induced by snake venom metalloproteinases: Biochemical and biophysical mechanisms involved in microvessel damage
    • DOI 10.1016/j.toxicon.2005.02.029, PII S0041010105000668, Snake Toxins and Hemostasis
    • Gutiérrez, J. M.; Rucavado, A.; Escalante, T.; Díaz, C. Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage. Toxicon 2005, 45, 997-1011. (Pubitemid 40732576)
    • (2005) Toxicon , vol.45 , Issue.8 , pp. 997-1011
    • Gutierrez, J.M.1    Rucavado, A.2    Escalante, T.3    Diaz, C.4
  • 32
    • 19544382337 scopus 로고    scopus 로고
    • Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases
    • DOI 10.1016/j.toxicon.2005.02.012, PII S0041010105000644, Snake Toxins and Hemostasis
    • Fox, J. W.; Serrano, S. M. T. Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases. Toxicon 2005, 45, 969-985. (Pubitemid 40732574)
    • (2005) Toxicon , vol.45 , Issue.8 , pp. 969-985
    • Fox, J.W.1    Serrano, S.M.T.2
  • 33
    • 60149105208 scopus 로고    scopus 로고
    • Timeline of key events in snake venom metalloproteinase research
    • Fox, J. W.; Serrano, S. M. T. Timeline of key events in snake venom metalloproteinase research. J. Proteomics 2009, 72, 200-209.
    • (2009) J. Proteomics , vol.72 , pp. 200-209
    • Fox, J.W.1    Serrano, S.M.T.2
  • 34
    • 33646780927 scopus 로고    scopus 로고
    • Serine proteases affecting blood coagulation and fibrinolysis from snake venoms
    • Kini, M. R. Serine proteases affecting blood coagulation and fibrinolysis from snake venoms. Pathophysiol. Haemostasis Thromb. 2005, 34, 200-204.
    • (2005) Pathophysiol. Haemostasis Thromb. , vol.34 , pp. 200-204
    • Kini, M.R.1
  • 36
    • 0019914881 scopus 로고
    • A new type of toxin in the venom of snakes of the genus Atractaspis (Atractaspidinae)
    • Kochva, E.; Viljoen, C. C.; Botes, D. P. A new type of toxin in the venom of snakes of the genus Atractaspis (Atractaspidinae). Toxicon 1982, 20, 581-592.
    • (1982) Toxicon , vol.20 , pp. 581-592
    • Kochva, E.1    Viljoen, C.C.2    Botes, D.P.3
  • 38
    • 0031195282 scopus 로고    scopus 로고
    • Sequence and biological activity of catrocollastatin-C: A disintegrin- Like/cysteine-rich two-domain protein from Crotalus atrox venom
    • DOI 10.1006/abbi.1997.0133
    • Shimokawa, K.; Shannon, J. D.; Jia, L. G.; Fox, J. W. Sequence and biological activity of catrocollastatin-C: a disintegrin-like/cysteinerich two-domain protein from Crotalus atrox venom. Arch. Biochem. Biophys. 1997, 343, 35-43. (Pubitemid 27274340)
    • (1997) Archives of Biochemistry and Biophysics , vol.343 , Issue.1 , pp. 35-43
    • Shimokawa, K.-I.1    Shannon, J.D.2    Jia, L.-G.3    Fox, J.W.4
  • 39
    • 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
    • DOI 10.1111/j.1742-4658.2008.06466.x
    • Fox, J. W.; Serrano, S. M. T. Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity. FEBS J. 2008, 275, 3016-3030. (Pubitemid 351743588)
    • (2008) FEBS Journal , vol.275 , Issue.12 , pp. 3016-3030
    • Fox, J.W.1    Serrano, S.M.T.2
  • 40
    • 19544381539 scopus 로고    scopus 로고
    • Snake venom disintegrins: Evolution of structure and function
    • DOI 10.1016/j.toxicon.2005.02.024, PII S0041010105000711, Snake Toxins and Hemostasis
    • Calvete, J. J.; Marcinkiewicz, C.; Monleón, D.; Esteve, V.; Celda, B.; Juárez, P.; Sanz, L. Snake venom disintegrins: evolution of structure and function. Toxicon 2005, 45, 1063-1074. (Pubitemid 40732581)
    • (2005) Toxicon , vol.45 , Issue.8 , pp. 1063-1074
    • Calvete, J.J.1    Marcinkiewicz, C.2    Monleon, D.3    Esteve, V.4    Celda, B.5    Juarez, P.6    Sanz, L.7
  • 41
    • 14744294145 scopus 로고    scopus 로고
    • Structure-function correlations of snake venom disintegrins
    • DOI 10.2174/1381612053381783
    • Calvete, J. J. Structure-function correlations of snake venom disintegrins. Curr. Pharm. Des. 2005, 11, 829-835. (Pubitemid 40340103)
    • (2005) Current Pharmaceutical Design , vol.11 , Issue.7 , pp. 829-835
    • Calvete, J.J.1
  • 42
    • 33745731954 scopus 로고    scopus 로고
    • Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold
    • DOI 10.1038/sj.emboj.7601131, PII 7601131
    • Takeda, S.; Igarashi, T.; Mori, H.; Araki, S. Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold. EMBO J. 2006, 25, 2388-2396. (Pubitemid 44012222)
    • (2006) EMBO Journal , vol.25 , Issue.11 , pp. 2388-2396
    • Takeda, S.1    Igarashi, T.2    Mori, H.3    Araki, S.4
  • 43
    • 34248594754 scopus 로고    scopus 로고
    • Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins
    • DOI 10.1016/j.febslet.2007.04.057, PII S0014579307004498
    • Igarashi, T.; Araki, S.; Mori, H.; Takeda, S. Crystal structures of catrocollastatin/ VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins. FEBS Lett. 2007, 581, 2416-2422. (Pubitemid 46764699)
    • (2007) FEBS Letters , vol.581 , Issue.13 , pp. 2416-2422
    • Igarashi, T.1    Araki, S.2    Mori, H.3    Takeda, S.4
  • 44
    • 0033854970 scopus 로고    scopus 로고
    • The disulfide bond pattern of catrocollastatin C, a disintegrin- Like/cysteine-rich protein isolated from Crotalus atrox venom
    • Calvete, J. J.; Moreno-Murciano, M. P.; Sanz, L.; Juürgens, M.; Schrader, M.; Raida, M.; Benjamin, D. C.; Fox, J. W. The disulfide bond pattern of catrocollastatin C, a disintegrin-like/cysteine-rich protein isolated from Crotalus atrox venom. Protein Sci. 2000, 9, 1365-1373. (Pubitemid 30602290)
    • (2000) Protein Science , vol.9 , Issue.7 , pp. 1365-1373
    • Calvete, J.J.1    Moreno-Murciano, M.P.2    Sanz, L.3    Jurgens, M.4    Schrader, M.5    Raida, M.6    Benjamin, D.C.7    Fox, J.W.8
  • 45
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: History, character, and diagnostic prospects
    • Anderson, N. L.; Anderson, N. G. The human plasma proteome: history, character, and diagnostic prospects. Mol. Cell. Proteomics 2002, 1, 845-867.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 46
    • 13844276803 scopus 로고    scopus 로고
    • Prefractionation techniques in proteome analysis: The mining tools of the third millennium
    • DOI 10.1002/elps.200406189
    • Righetti, P. G.; Castagna, A.; Antonioli, P.; Boschetti, E. Prefractionation techniques in proteome analysis: the mining tools of the third millennium. Electrophoresis 2005, 26, 297-319. (Pubitemid 40253785)
    • (2005) Electrophoresis , vol.26 , Issue.2 , pp. 297-319
    • Righetti, P.G.1    Castagna, A.2    Antonioli, P.3    Boschetti, E.4
  • 47
    • 40549120285 scopus 로고    scopus 로고
    • Technologies and methods for sample pretreatment in efficient proteome and peptidome analysis
    • DOI 10.1002/pmic.200700617
    • Jiang, X.; Ye, M.; Zou, H. Technologies and methods for sample pretreatment in efficient proteome and peptidome analysis. Proteomics 2008, 8, 686-705. (Pubitemid 351362930)
    • (2008) Proteomics , vol.8 , Issue.4 , pp. 686-705
    • Jiang, X.1    Ye, M.2    Zou, H.3
  • 48
    • 20544478148 scopus 로고    scopus 로고
    • Reduction of the concentration difference of proteins in biological liquids using a library of combinatorial ligands
    • DOI 10.1002/elps.200500147
    • Thulasiraman, V.; Lin, S.; Gheorghiu, L.; Lathrop, J.; Lomas, L.; Hammond, D.; Boschetti, E. Reduction of the concentration difference of proteins in biological liquids using a library of combinatorial ligands. Electrophoresis 2005, 26, 3561-3571. (Pubitemid 41410379)
    • (2005) Electrophoresis , vol.26 , Issue.18 , pp. 3561-3571
    • Thulasiraman, V.1    Lin, S.2    Gheorghiu, L.3    Lathrop, J.4    Lomas, L.5    Hammond, D.6    Boschetti, E.7
  • 55
    • 58849127707 scopus 로고    scopus 로고
    • Combinatorial peptide ligand libraries and plant proteomics: A winning strategy at a price
    • Boschetti, E.; Bindschedler, L. V.; Tang, C.; Fasoli, E.; Righetti, P. G. Combinatorial peptide ligand libraries and plant proteomics: A winning strategy at a price. J. Chromatogr., A 2009, 1216, 1215-1222.
    • (2009) J. Chromatogr., A , vol.1216 , pp. 1215-1222
    • Boschetti, E.1    Bindschedler, L.V.2    Tang, C.3    Fasoli, E.4    Righetti, P.G.5
  • 57
    • 34249651243 scopus 로고    scopus 로고
    • Capturing and amplifying impurities from purified recombinant monoclonal antibodies via peptide library beads: A proteomic study
    • DOI 10.1002/pmic.200600778
    • Antonioli, P.; Fortis, F.; Guerrier, L.; Rinalducci, S.; Zolla, L.; Righetti, P. G.; Boschetti, E. 2007. Capturing and amplifying impurities from purified recombinant monoclonal antibodies via peptide library beads: A proteomic study. Proteomics 2007, 7, 1624-1633. (Pubitemid 46841824)
    • (2007) Proteomics , vol.7 , Issue.10 , pp. 1624-1633
    • Antonioli, P.1    Fortis, F.2    Guerrier, L.3    Rinalducci, S.4    Zolla, L.5    Righetti, P.G.6    Boschetti, E.7
  • 58
    • 55249123169 scopus 로고    scopus 로고
    • Evaluation of the combination of bead technology with SELDITOF-MS and 2D DIGE for detection of plasma proteins
    • Sihlbom, C.; Kanmert, I.; von Bahr, H.; Davidsson, P. Evaluation of the combination of bead technology with SELDITOF-MS and 2D DIGE for detection of plasma proteins. J. Proteome Res. 2008, 7, 4191-4198.
    • (2008) J. Proteome Res. , vol.7 , pp. 4191-4198
    • Sihlbom, C.1    Kanmert, I.2    Von Bahr, H.3    Davidsson, P.4
  • 59
    • 63049100764 scopus 로고    scopus 로고
    • The art of observing rare protein species in proteomes with peptide ligand libraries
    • Boschetti, E.; Righetti, P. G. The art of observing rare protein species in proteomes with peptide ligand libraries. Proteomics 2009, 9 (6), 1492-1510.
    • (2009) Proteomics , vol.9 , Issue.6 , pp. 1492-1510
    • Boschetti, E.1    Righetti, P.G.2
  • 60
    • 0037222255 scopus 로고    scopus 로고
    • Structure, mechanism and regulation of peroxiredoxins
    • DOI 10.1016/S0968-0004(02)00003-8, PII S0968000402000038
    • Wood, Z.; Schröder, E.; Robin Harris, J.; Poole, L. Structure, mechanism and regulation of peroxiredoxins. Trends Biochem. Sci. 2003, 28, 32-40. (Pubitemid 36051004)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.1 , pp. 32-40
    • Wood, Z.A.1    Schroder, E.2    Harris, J.R.3    Poole, L.B.4
  • 61
    • 0035104132 scopus 로고    scopus 로고
    • Disulfide bond effects on protein stability: Designed variants of Cucurbita maxima trypsin inhibitor-V
    • DOI 10.1110/ps.26801
    • Zavodszky, M.; Chen, C.-W.; Huang, J.-K.; Zolkiewski, M.; Wen, L.; Krishnamoorthi, R. Disulfide bond effects on protein stability: Designed variants of Cucurbita maxima trypsin inhibitor-V. Protein Sci. 2001, 10, 149-160. (Pubitemid 32221173)
    • (2001) Protein Science , vol.10 , Issue.1 , pp. 149-160
    • Zavodszky, M.1    Chen, C.-W.2    Huang, J.-K.3    Zolkiewski, M.4    Wen, L.5    Krishnamoorthi, R.6
  • 62
    • 0037591683 scopus 로고    scopus 로고
    • Snake venom disintegrins: Novel dimeric disintegrins and structural diversification by disulphide bond engineering
    • DOI 10.1042/BJ20021739
    • Calvete, J. J.; Moreno-Murciano, M. P.; Theakston, R. D. G.; Kisiel, D. G.; Marcinkiewicz, C. Snake venom disintegrins: novel dimeric disintegrins and structural diversification by disulphide bond engineering. Biochem. J. 2003, 372, 725-734. (Pubitemid 36760386)
    • (2003) Biochemical Journal , vol.372 , Issue.3 , pp. 725-734
    • Calvete, J.J.1    Moreno-Murciano, M.P.2    Theakston, R.D.G.3    Kisiel, D.G.4    Marcinkiewicz, C.5
  • 63
    • 54149086758 scopus 로고    scopus 로고
    • Evolution of snake venom disintegrins by positive Darwinian selection
    • Juárez, P.; Comas, I.; González-Candelas, F.; Calvete, J. J. Evolution of snake venom disintegrins by positive Darwinian selection. Mol. Biol. Evol. 2008, 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
  • 64
    • 58249139780 scopus 로고    scopus 로고
    • Combined snake venomics and venom gland transcriptomic analysis of the ocellated carpet viper, Echis ocellatus
    • Wagstaff, S. C.; Sanz, L.; Juárez, P.; Harrison, R. A.; Calvete, J. J. Combined snake venomics and venom gland transcriptomic analysis of the ocellated carpet viper, Echis ocellatus. J. Proteomics 2009, 71, 609-623.
    • (2009) J. Proteomics , vol.71 , pp. 609-623
    • Wagstaff, S.C.1    Sanz, L.2    Juárez, P.3    Harrison, R.A.4    Calvete, J.J.5
  • 65
    • 9744281932 scopus 로고    scopus 로고
    • Molecular diversity and accelerated evolution of C-type lectin-like proteins from snake venom
    • DOI 10.1016/j.toxicon.2004.07.028, PII S0041010104003411
    • 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. (Pubitemid 39586562)
    • (2005) Toxicon , vol.45 , Issue.1 , pp. 1-14
    • Ogawa, T.1    Chijiwa, T.2    Oda-Ueda, N.3    Ohno, M.4
  • 66
    • 19544368798 scopus 로고    scopus 로고
    • Snake venom C-type lectins interacting with platelet receptors. Structure-function relationships and effects on haemostasis
    • DOI 10.1016/j.toxicon.2005.02.022, PII S0041010105000735, Snake Toxins and Hemostasis
    • Lu, Q.; Navdaev, A.; Clemetson, J. M.; Clemetson, K. J. Snake venom C-type lectins interacting with platelet receptors. Structure-function relationships and effects on haemostasis. Toxicon 2005, 45, 1089-1098. (Pubitemid 40732583)
    • (2005) Toxicon , vol.45 , Issue.8 , pp. 1089-1098
    • Lu, Q.1    Navdaev, A.2    Clemetson, J.M.3    Clemetson, K.J.4
  • 67
    • 1842591876 scopus 로고    scopus 로고
    • X-ray Crystal Structure of a Galactose-Specific C-Type Lectin Possessing a Novel Decameric Quaternary Structure
    • DOI 10.1021/bi035871a
    • Walker, J. R.; Nagar, B.; Young, N. M.; Hirama, Y.; Rini, J. M. X-ray crystal structure of a galactose-specific C-type lectin possessing a novel decameric quaternary structure. Biochemistry 2004, 43, 3783-3792. (Pubitemid 38437045)
    • (2004) Biochemistry , vol.43 , Issue.13 , pp. 3783-3792
    • Walker, J.R.1    Nagar, B.2    Young, N.M.3    Hirama, T.4    Rini, J.M.5
  • 68
    • 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
    • DOI 10.1021/pr060494k
    • 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, 326-336. (Pubitemid 46173684)
    • (2007) Journal of Proteome Research , vol.6 , Issue.1 , pp. 326-336
    • Calvete, J.J.1    Marcinkiewicz, C.2    Sanz, L.3
  • 70
    • 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. T. 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.T.5
  • 73
    • 15944366565 scopus 로고    scopus 로고
    • Presence of peptide inhibitors in rattlesnake venoms and their effects on endogenous metalloproteases
    • DOI 10.1016/j.toxicon.2004.10.009
    • Munekiyo, S. M.; Mackessy, S. P. Presence of peptide inhibitors in rattlesnake venoms and their effects on endogenous metalloproteases. Toxicon 2005, 45, 255-263. (Pubitemid 40439199)
    • (2005) Toxicon , vol.45 , Issue.3 , pp. 255-263
    • Munekiyo, S.M.1    Mackessy, S.P.2
  • 75
    • 0036310675 scopus 로고    scopus 로고
    • Determinants of the inhibition of a Taiwan habu venom metalloproteinase by its endogenous inhibitors revealed by X-ray crystallography and synthetic inhibitor analogues
    • DOI 10.1046/j.1432-1033.2002.02982.x
    • Huang, K.-F.; Chiou, S.-H.; Ko, T.-P.; Wang, A.H.-J. Determinants of the inhibition of a Taiwan habu venom metalloprotease by its endogenous inhibitors revealed by X-ray crystallography and synthetic inhibitor analogues. Eur. J. Biochem. 2002, 269, 3047-3056. (Pubitemid 34754035)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.12 , pp. 3047-3056
    • Huang, K.-F.1    Chiou, S.-H.2    Ko, T.-P.3    Wang, A.H.-J.4
  • 76
    • 20444438029 scopus 로고    scopus 로고
    • Identification of novel bradykinin-potentiating peptides and C-type natriuretic peptide from Lachesis muta venom
    • DOI 10.1016/j.toxicon.2005.03.006, PII S0041010105001121
    • Soares, M. R.; Oliveira-Carvalho, A. L.; Wermelinger, L. S.; Zingali, R. B.; Ho, P. L.; Junqueira-de-Azevedo, I. L. M.; Diniz, R. M. V. Identification of novel bradykinin-potentiating peptides and Ctype natriuretic peptide from Lachesis muta venom. Toxicon 2005, 46, 31-38. (Pubitemid 40825066)
    • (2005) Toxicon , vol.46 , Issue.1 , pp. 31-38
    • Soares, M.R.1    Oliveira-Carvalho, A.L.2    Wermelinger, L.S.3    Zingali, R.B.4    Ho, P.L.5    Junqueira-De-Azevedo, I.D.L.M.6    Diniz, M.R.V.7
  • 77
    • 43649100299 scopus 로고    scopus 로고
    • High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry
    • Menin, L.; Perchuć, A.; Favreau, P.; Perret, F.; Michalet, S.; Schöni, R.; Wilmer, M.; Stöcklin, R. High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry. Toxicon 2008, 51, 1288-1302.
    • (2008) Toxicon , vol.51 , pp. 1288-1302
    • Menin, L.1    Perchuć, A.2    Favreau, P.3    Perret, F.4    Michalet, S.5    Schöni, R.6    Wilmer, M.7    Stöcklin, R.8
  • 78
    • 34248560785 scopus 로고    scopus 로고
    • Earliest fossil record of a Pigmy Rattlesnake (Viperidae: Sistrurus Garman)
    • DOI 10.1670/0022-1511(2007)41[141:EFROAP]2.0.CO;2
    • Parmley, D.; Holman, J. A. Earliest fossil record of a pigmy rattlesnake (Viperidae: Sistrurus Garman). J. Herpetol. 2007, 41, 141-144. (Pubitemid 46761214)
    • (2007) Journal of Herpetology , vol.41 , Issue.1 , pp. 141-144
    • Parmley, D.1    Holman, J.A.2
  • 79
    • 33748286744 scopus 로고    scopus 로고
    • Venom proteomes of closely related Sistrurus rattlesnakes with divergent diets
    • DOI 10.1021/pr0602500
    • Sanz, L.; Gibbs, H. L.; Mackessy, S. P.; Calvete, J. J. Venom proteomes of closely-related Sistrurus rattlesnakes with divergent diets. J. Proteome Res. 2006, 5, 2098-2112. (Pubitemid 44330802)
    • (2006) Journal of Proteome Research , vol.5 , Issue.9 , pp. 2098-2112
    • Sanz, L.1    Lisle Gibbs, H.2    Mackessy, S.P.3    Calvete, J.J.4
  • 81
    • 33644541469 scopus 로고    scopus 로고
    • 'Venomics' or: The venomous systems genome project
    • DOI 10.1016/j.toxicon.2005.12.010, PII S0041010105004277
    • Ménez, A.; Stöcklin, R.; Mebs, D. "Venomics" or: The venomous systems genome project. Toxicon 2006, 47, 255-259. (Pubitemid 43294452)
    • (2006) Toxicon , vol.47 , Issue.3 , pp. 255-259
    • Menez, A.1    Stocklin, R.2    Mebs, D.3
  • 82
    • 13844310831 scopus 로고    scopus 로고
    • A multifaceted analysis of viperid snake venoms by two-dimensional gel electrophoresis: An approach to understanding venom proteomics
    • DOI 10.1002/pmic.200400931
    • Serrano, S. M. T.; Shannon, J. D.; Wang, D.; Camargo, A. C. M.; Jox, J. W. A multifaceted analysis of viperid snake venoms by two-dimensional gel electrophoresis: an approach to understanding venom proteomics. Proteomics 2005, 501-510. (Pubitemid 40262067)
    • (2005) Proteomics , vol.5 , Issue.2 , pp. 501-510
    • Serrano, S.M.T.1    Shannon, J.D.2    Wang, D.3    Camargo, A.C.M.4    Fox, J.W.5
  • 83
    • 40549090210 scopus 로고    scopus 로고
    • Exploring snake venom proteomes: Multifaceted analyses for complex toxin mixtures
    • DOI 10.1002/pmic.200700777
    • Fox, J. W.; Serrano, S. M. T. Exploring snake venom proteomes: multifaceted analyses for complex toxin mixtures. Proteomics 2008, 909-920. (Pubitemid 351362943)
    • (2008) Proteomics , vol.8 , Issue.4 , pp. 909-920
    • Fox, J.W.1    Serrano, S.M.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.