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Volumn 391, Issue , 1996, Pages 379-386

Structure and experimental uses of arthropod venom proteins

Author keywords

[No Author keywords available]

Indexed keywords

ARTHROPOD VENOM; KININ; SCORPION VENOM; TETRODOTOXIN;

EID: 0029890053     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4613-0361-9_32     Document Type: Article
Times cited : (4)

References (45)
  • 2
    • 0027207297 scopus 로고
    • 3H] noradrenaline release from rat cerebral cortex
    • 3H] noradrenaline release from rat cerebral cortex. Eur. J. Pharmacol. 248:85-88.
    • (1993) Eur. J. Pharmacol. , vol.248 , pp. 85-88
    • Ennis, C.1    Minchin, M.C.2
  • 3
    • 0026707748 scopus 로고
    • Characteristics of pancreatic exocrine secretion produced by venom from the Brazilian scorpion, Tityus serrulatus
    • Fletchner, P.L., Fletcher, M.D., Possani, L.D., 1992. Characteristics of pancreatic exocrine secretion produced by venom from the Brazilian scorpion, Tityus serrulatus. Eur. J. Cell Biol. 58:259-270.
    • (1992) Eur. J. Cell Biol. , vol.58 , pp. 259-270
    • Fletchner, P.L.1    Fletcher, M.D.2    Possani, L.D.3
  • 4
    • 0016208931 scopus 로고
    • Control of moulting and metamorphosis in the tobacco hornworm, Manduca sexta (L.): Cessation of juvenile hormone secretion as a trigger for pupation
    • Nijhout, H.F. and Williams, C.M., 1974. Control of moulting and metamorphosis in the tobacco hornworm, Manduca sexta (L.): Cessation of juvenile hormone secretion as a trigger for pupation. J. Exp. Biol. 61:493-501.
    • (1974) J. Exp. Biol. , vol.61 , pp. 493-501
    • Nijhout, H.F.1    Williams, C.M.2
  • 5
    • 0016023673 scopus 로고
    • The use of inhibitors in studies on protein synthesis
    • Pestka, S., 1974. The use of inhibitors in studies on protein synthesis. Meth. Enzymol. 30:261-182.
    • (1974) Meth. Enzymol. , vol.30 , pp. 261-1182
    • Pestka, S.1
  • 6
    • 0025597965 scopus 로고
    • Involvement of translation and transcription in insect steroidogenesis
    • Keightley, D.A., Lou, K.J., and Smith, W.A., 1990. Involvement of translation and transcription in insect steroidogenesis. Mol. Cell. Endocrinol. 74:229-237.
    • (1990) Mol. Cell. Endocrinol. , vol.74 , pp. 229-237
    • Keightley, D.A.1    Lou, K.J.2    Smith, W.A.3
  • 7
    • 0025257193 scopus 로고
    • Role of protein synthesis in the accumulation of ferratin mRNA during exposure of cells to iron
    • Mattia, E., den Blaauwen, J., van Renswoude, J., 1990. Role of protein synthesis in the accumulation of ferratin mRNA during exposure of cells to iron. Biochem. J. 267:553-555.
    • (1990) Biochem. J. , vol.267 , pp. 553-555
    • Mattia, E.1    Den Blaauwen, J.2    Van Renswoude, J.3
  • 8
    • 0027409425 scopus 로고
    • Physiologic concentrations of glucose regulate fatty acid synthase activity in Hep G2 cells by mediating fatty acid synthase mRNA stability
    • Semenkovich, C.F., Coleman, T., Goforth, R., 1993. Physiologic concentrations of glucose regulate fatty acid synthase activity in Hep G2 cells by mediating fatty acid synthase mRNA stability. J. Biol. Chem. 265:6961-6970.
    • (1993) J. Biol. Chem. , vol.265 , pp. 6961-6970
    • Semenkovich, C.F.1    Coleman, T.2    Goforth, R.3
  • 9
    • 0028171296 scopus 로고
    • Alpha 9: An acetylcholine receptor with novel pharmacological properties expressed in rat cochlear hair cells
    • Elgoyhen, A.B., Johnson, D.S., Boulter, J., Vetter, D.E., Heineman, S., 1994. Alpha 9: an acetylcholine receptor with novel pharmacological properties expressed in rat cochlear hair cells. Cell 79:705-715.
    • (1994) Cell , vol.79 , pp. 705-715
    • Elgoyhen, A.B.1    Johnson, D.S.2    Boulter, J.3    Vetter, D.E.4    Heineman, S.5
  • 10
    • 0027314274 scopus 로고
    • Nicotinic acetylcholine receptors in isolated type I cells of the neonatal rat carotid body
    • Wyatt, C.N., Peers, C. 1994. Nicotinic acetylcholine receptors in isolated type I cells of the neonatal rat carotid body. Neuroscience 54:275-281.
    • (1994) Neuroscience , vol.54 , pp. 275-281
    • Wyatt, C.N.1    Peers, C.2
  • 13
    • 0024299178 scopus 로고
    • Photoaffinity labelling of scorpion toxin receptors associated with insect synaptosomal Na+ channels
    • de Lima, M.E., Couraud, F., Lapied, B., Pelhate, M., Diniz, C.D. and Rochat, H., 1988. Photoaffinity labelling of scorpion toxin receptors associated with insect synaptosomal Na+ channels. Biochem. Biophys. Res. Comm. 151:187-192.
    • (1988) Biochem. Biophys. Res. Comm. , vol.151 , pp. 187-192
    • De Lima, M.E.1    Couraud, F.2    Lapied, B.3    Pelhate, M.4    Diniz, C.D.5    Rochat, H.6
  • 14
    • 0027332134 scopus 로고
    • Structure and properties of omega-agatoxin IVB, a new antagonist of P-type calcium channels
    • Adams, M.E., Mintz, I.M., Reily, M.D., Thanabal, V., Bean, B.P., 1993. Structure and properties of omega-agatoxin IVB, a new antagonist of P-type calcium channels. Mol. Pharmacol. 44:681-688.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 681-688
    • Adams, M.E.1    Mintz, I.M.2    Reily, M.D.3    Thanabal, V.4    Bean, B.P.5
  • 15
    • 0001812257 scopus 로고
    • Chemistry and phramacology of honey-bee venom
    • T. Pick, ed.
    • Banks, B.E.C. and Shipolini, R.A., 1986. Chemistry and phramacology of honey-bee venom. IN: "Venoms of the Hymenoptera" (T. Pick, ed.), pp. 330-416
    • (1986) Venoms of the Hymenoptera , pp. 330-416
    • Banks, B.E.C.1    Shipolini, R.A.2
  • 16
    • 0023969412 scopus 로고
    • Isolation of nuclei from melittin destabilized cells
    • Smith, R.J., Friede, M.H., Scott, B.J. and von Holt, C., 1988. Isolation of nuclei from melittin destabilized cells. Anal. Biochem. 169:390-394.
    • (1988) Anal. Biochem. , vol.169 , pp. 390-394
    • Smith, R.J.1    Friede, M.H.2    Scott, B.J.3    Von Holt, C.4
  • 17
    • 0025104319 scopus 로고
    • Neurotoxins from venoms of the Hymenoptera - Twenty five years of research in Amsterdam
    • Pick, T., 1990. Neurotoxins from venoms of the Hymenoptera - twenty five years of research in Amsterdam. Comp. Biochem. Physiol. C 96:223-233.
    • (1990) Comp. Biochem. Physiol. C , vol.96 , pp. 223-233
    • Pick, T.1
  • 18
    • 84990465263 scopus 로고
    • Host regulation by insect parasitoids
    • Vinson, S.B. and Iwantsch, G.F., 1980. Host regulation by insect parasitoids. Quart. Rev. Biol, 55: 143-165.
    • (1980) Quart. Rev. Biol , vol.55 , pp. 143-165
    • Vinson, S.B.1    Iwantsch, G.F.2
  • 19
    • 0028859094 scopus 로고
    • The salivary gland-specific apyrase of the mosquito Aedes aegypti is a member of the 5′-nucleotide family
    • Champagne, D.E., Smartt, C.T., Ribeiro, J.M., James, A.A., 1995. The salivary gland-specific apyrase of the mosquito Aedes aegypti is a member of the 5′-nucleotide family. Proc. Natl. Acad. Sci. U.S.A. 92:694-698.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 694-698
    • Champagne, D.E.1    Smartt, C.T.2    Ribeiro, J.M.3    James, A.A.4
  • 20
    • 0027752188 scopus 로고
    • The salivary glands of the vector mosquito, Aedes aegypti, express a novel member of the amylase gene family
    • Grossman, G.L., James, A.A. 1993. The salivary glands of the vector mosquito, Aedes aegypti, express a novel member of the amylase gene family. Insect Mol. Biol. 1:223-232.
    • (1993) Insect Mol. Biol. , vol.1 , pp. 223-232
    • Grossman, G.L.1    James, A.A.2
  • 21
    • 0028036186 scopus 로고
    • Sialokinin I and II: Vasodialtory tachykinins from the yellow fever mosquito Aedes aegypti
    • Champagne, D.E., Ribeiro, J.M., 1994. Sialokinin I and II: vasodialtory tachykinins from the yellow fever mosquito Aedes aegypti. Proc. Natl. Acad. Sci. 91:138-142.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 138-142
    • Champagne, D.E.1    Ribeiro, J.M.2
  • 22
    • 0026502768 scopus 로고
    • Maxadilan. Cloning and functional expression of the gene encoding this potent vasodialator
    • Lerner, E.A. and Shoemaker, C.B., 1992. Maxadilan. Cloning and functional expression of the gene encoding this potent vasodialator. J. Biol. Chem. 267:1062-1066.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1062-1066
    • Lerner, E.A.1    Shoemaker, C.B.2
  • 23
    • 0027213409 scopus 로고
    • Reversible binding of nitric oxide by a salivary heme protein from a bloodsucking insect
    • Ribeiro, J.M., Hazzard, J.M., Nussenzverg, R.H., Champagne, D.E., Walker, F.A., 1993. Reversible binding of nitric oxide by a salivary heme protein from a bloodsucking insect. Science 260:539-541.
    • (1993) Science , vol.260 , pp. 539-541
    • Ribeiro, J.M.1    Hazzard, J.M.2    Nussenzverg, R.H.3    Champagne, D.E.4    Walker, F.A.5
  • 24
    • 0026724927 scopus 로고
    • Sequence, structure and expression of a wasp venom protein with a negatively charged signal peptide and a novel repeating internal structure
    • Jones, D., Sawicki, G. and Wozniak, M., 1992. Sequence, structure and expression of a wasp venom protein with a negatively charged signal peptide and a novel repeating internal structure. J. Biol. Chem 267:14871-14878.
    • (1992) J. Biol. Chem , vol.267 , pp. 14871-14878
    • Jones, D.1    Sawicki, G.2    Wozniak, M.3
  • 25
    • 0000646965 scopus 로고
    • Venom promotes uncoating in vitro and persistence in vivo of DNA from a braconid polydnavirus
    • Stoltz, D.B., Belland, E.R., Lucarotti, C.J., and Mackinnon, E.A., 1988. Venom promotes uncoating in vitro and persistence in vivo of DNA from a braconid polydnavirus. J. Gen. Virol. 69:903-907.
    • (1988) J. Gen. Virol. , vol.69 , pp. 903-907
    • Stoltz, D.B.1    Belland, E.R.2    Lucarotti, C.J.3    Mackinnon, E.A.4
  • 26
    • 0025345454 scopus 로고
    • Isolation and characterization of the 32.5 kDa protein from venom of an endoparasitic wasp
    • Taylor, T. and Jones, D., 1989. Isolation and characterization of the 32.5 kDa protein from venom of an endoparasitic wasp. Biochim. Biophys. Acta 1035:37-43.
    • (1989) Biochim. Biophys. Acta , vol.1035 , pp. 37-43
    • Taylor, T.1    Jones, D.2
  • 27
    • 0002638054 scopus 로고
    • Host-regulating factors associated with parasitic Hymenoptera
    • Coudron, T.A., 1991. Host-regulating factors associated with parasitic Hymenoptera. ACS Symp. Ser. 449:41-65.
    • (1991) ACS Symp. Ser. , vol.449 , pp. 41-65
    • Coudron, T.A.1
  • 28
    • 0028037172 scopus 로고
    • Apparent functional role for a cysteine-rich polydnavirus protein in suppression of the insect cellular immune response
    • Li, X. and Webb, B.A., 1994. Apparent functional role for a cysteine-rich polydnavirus protein in suppression of the insect cellular immune response. J. Virol. 68:7482-7489.
    • (1994) J. Virol. , vol.68 , pp. 7482-7489
    • Li, X.1    Webb, B.A.2
  • 29
    • 0028883228 scopus 로고
    • Microplitis demolitor polydnavirus induces apoptosis of a specific haemocyte morphotype in Pseudoplusia includens
    • Strand, M.R. and Pech, L.L., 1995. Microplitis demolitor polydnavirus induces apoptosis of a specific haemocyte morphotype in Pseudoplusia includens. J. Gen. Virol. 76:283-291.
    • (1995) J. Gen. Virol. , vol.76 , pp. 283-291
    • Strand, M.R.1    Pech, L.L.2
  • 30
    • 0028017691 scopus 로고
    • Isolation, cloning, and characterization of a new chitinase stored in active form in chitin-lined venom reservoir
    • Krishnan, A., Nair, P.N. and Jones, D., 1994. Isolation, cloning, and characterization of a new chitinase stored in active form in chitin-lined venom reservoir. J. Biol. Chem. 269:20971-20976.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20971-20976
    • Krishnan, A.1    Nair, P.N.2    Jones, D.3
  • 31
    • 0018784022 scopus 로고
    • The structure of melittin in lipid bilayer membranes
    • Drake, A.F. and Hider, R.C., 1979. The structure of melittin in lipid bilayer membranes. Biochim. Biophys. Acta 555:371-373.
    • (1979) Biochim. Biophys. Acta , vol.555 , pp. 371-373
    • Drake, A.F.1    Hider, R.C.2
  • 32
    • 0026589880 scopus 로고
    • Stabilities of disulphide bond intermediates in the folding of apamin
    • Huyghues-Despointes, B.M. and Nelson, J.W. 1992. Stabilities of disulphide bond intermediates in the folding of apamin. Biochemistry 31: 1476-1483.
    • (1992) Biochemistry , vol.31 , pp. 1476-1483
    • Huyghues-Despointes, B.M.1    Nelson, J.W.2
  • 33
    • 0027520896 scopus 로고
    • Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm
    • Gmachl, M. and Kreil, G., 1993. Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm. Proc. Natl. Acad. Sci. U.S.A. 90:3569-3573.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 3569-3573
    • Gmachl, M.1    Kreil, G.2
  • 34
    • 0026002418 scopus 로고
    • Chitinase is required for cell separation during the growth of Saccaromyces cerevisiae
    • Kuranda, M.J. and Robbins, P.W. (1991) Chitinase is required for cell separation during the growth of Saccaromyces cerevisiae. J. Biol. Chem. 266:19758-19767.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19758-19767
    • Kuranda, M.J.1    Robbins, P.W.2
  • 35
    • 0027668880 scopus 로고
    • Sequence of a cDNA and expression of the gene encoding epidermal and gut chitinases of Manduca sexta
    • Kramer, K.J., Corpuz, L., Choi, H.K., Muthukrishnan, S., 1993. Sequence of a cDNA and expression of the gene encoding epidermal and gut chitinases of Manduca sexta. Insect Biochem. Molec. Biol. 23: 691-701.
    • (1993) Insect Biochem. Molec. Biol. , vol.23 , pp. 691-701
    • Kramer, K.J.1    Corpuz, L.2    Choi, H.K.3    Muthukrishnan, S.4
  • 36
    • 0001911946 scopus 로고
    • Chelonus sp. near curvimaculatus venom proteins: Analysis of their potential role and processing during development of host Trichoplusia ni
    • Leluk, J. and Jones, D., 1989. Chelonus sp. near curvimaculatus venom proteins: Analysis of their potential role and processing during development of host Trichoplusia ni. Arch. Insect Biochem. Physiol. 10:1-12.
    • (1989) Arch. Insect Biochem. Physiol. , vol.10 , pp. 1-12
    • Leluk, J.1    Jones, D.2
  • 38
    • 84940931140 scopus 로고
    • Venoms of parasitic Hymenoptera as investigatory tools
    • (Beckage, N.E., Thompson, S.N. and Federici, B.A., eds.), Acad. Press
    • Jones, D. and Coudron, T., 1993. Venoms of parasitic Hymenoptera as investigatory tools. IN: Parasites and Pathogens of Insects (Beckage, N.E., Thompson, S.N. and Federici, B.A., eds.), Acad. Press, pp. 227-244.
    • (1993) Parasites and Pathogens of Insects , pp. 227-244
    • Jones, D.1    Coudron, T.2
  • 39
    • 0025172078 scopus 로고
    • Molecular cloning and characterization of the immunologically protective surface glycoprotein of GP46/M-2 of Leishmania amazonensis
    • Lohman, K.L., Langer, P.J. and McMahon-Pratt, D. 1990. Molecular cloning and characterization of the immunologically protective surface glycoprotein of GP46/M-2 of Leishmania amazonensis. Proc. Natl. Acad. Sci. U.S.A. 87:8393-8397.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 8393-8397
    • Lohman, K.L.1    Langer, P.J.2    McMahon-Pratt, D.3
  • 40
    • 0027451594 scopus 로고
    • Kinetics of appearance and disappearance of classes of bacterial ice nuclei support an aggregation model for ice nucleus assembly
    • Ruggles, J.A., Nemecek-Marshall, M. and Fall, R., 1993. Kinetics of appearance and disappearance of classes of bacterial ice nuclei support an aggregation model for ice nucleus assembly. J. Bacter. 175:7216-7221.
    • (1993) J. Bacter. , vol.175 , pp. 7216-7221
    • Ruggles, J.A.1    Nemecek-Marshall, M.2    Fall, R.3
  • 42
    • 0027394764 scopus 로고
    • Cloning and structural analysis of alpha-latroinsectotoxin cDNA. Abundance of ankyrin-like repeats
    • Kiyatkin, N., Dulbova, I., Grishin, E., 1993. Cloning and structural analysis of alpha-latroinsectotoxin cDNA. Abundance of ankyrin-like repeats. Eur. J. Biochem. 213:121-127.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 121-127
    • Kiyatkin, N.1    Dulbova, I.2    Grishin, E.3
  • 43
    • 0028963208 scopus 로고
    • Polydnavirus-facilitated endoparasite protection against host immune defenses
    • Summers, M.D. and Dib-Hajj, S.D., 1995. Polydnavirus-facilitated endoparasite protection against host immune defenses. Proc. Natl. Acad. Sci. U.S.A. 92:29-36.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 29-36
    • Summers, M.D.1    Dib-Hajj, S.D.2
  • 44
    • 0025049915 scopus 로고
    • Biochemical and immunological studies of proteins from polydnavirus from Chelonus sp. near curvimaculatus
    • Chelliah, J. and Jones, D., 1990. Biochemical and immunological studies of proteins from polydnavirus from Chelonus sp. near curvimaculatus. J. Gen. Virol. 71: 2353-2359.
    • (1990) J. Gen. Virol. , vol.71 , pp. 2353-2359
    • Chelliah, J.1    Jones, D.2
  • 45
    • 0024249494 scopus 로고
    • Idenfication and comparision of Campoletis sonorensis virus transcriptions expressed from four genomic segments in the host insects Campoletis sonorensis and Heliothis virescens
    • Theilmann, D.A. and Summers, M.D. 1988. Idenfication and comparision of Campoletis sonorensis virus transcriptions expressed from four genomic segments in the host insects Campoletis sonorensis and Heliothis virescens. Virol. 167:329-341.
    • (1988) Virol. , vol.167 , pp. 329-341
    • Theilmann, D.A.1    Summers, M.D.2


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