메뉴 건너뛰기




Volumn 43, Issue 5, 2004, Pages 527-542

The multiple actions of black widow spider toxins and their selective use in neurosecretion studies

Author keywords

Latrophilin; Latrotoxin; Neurexin; Pore formation; Spider venom

Indexed keywords

ALPHA LATROTOXIN; CALCIUM ION; CELL RECEPTOR; G PROTEIN COUPLED RECEPTOR; NEUREXIN; SPIDER VENOM;

EID: 1942438974     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2004.02.008     Document Type: Review
Times cited : (116)

References (102)
  • 5
    • 0030858662 scopus 로고    scopus 로고
    • Heterogeneity of functional synaptic parameters among single release sites
    • Auger C., Marty A. Heterogeneity of functional synaptic parameters among single release sites. Neuron. 19:1997;139-150.
    • (1997) Neuron , vol.19 , pp. 139-150
    • Auger, C.1    Marty, A.2
  • 8
    • 0031034139 scopus 로고    scopus 로고
    • Effects of black widow spider venom and latrocrustatoxin on crustacean nerve cells: Electrophysiological and ultrastructural study
    • Burmistrov Y.M., Shuranova Z.P., Artiukhina N.I. Effects of black widow spider venom and latrocrustatoxin on crustacean nerve cells: electrophysiological and ultrastructural study. Gen. Pharmacol. 28:1997;159-166.
    • (1997) Gen. Pharmacol. , vol.28 , pp. 159-166
    • Burmistrov, Y.M.1    Shuranova, Z.P.2    Artiukhina, N.I.3
  • 9
    • 0029861269 scopus 로고    scopus 로고
    • Calcium-independent actions of α-latrotoxin on spontaneous and evoked synaptic transmission in the hippocampus
    • Capogna M., Gahwiler B.H., Thompson S.M. Calcium-independent actions of α-latrotoxin on spontaneous and evoked synaptic transmission in the hippocampus. J. Neurophysiol. 76:1996;3149-3158.
    • (1996) J. Neurophysiol. , vol.76 , pp. 3149-3158
    • Capogna, M.1    Gahwiler, B.H.2    Thompson, S.M.3
  • 10
    • 0029940351 scopus 로고    scopus 로고
    • Presynaptic inhibition of calcium-dependent and -independent release elicited with ionomycin, gadolinium, and α-latrotoxin in the hippocampus
    • Capogna M., Gahwiler B.H., Thompson S.M. Presynaptic inhibition of calcium-dependent and -independent release elicited with ionomycin, gadolinium, and α-latrotoxin in the hippocampus. J. Neurophysiol. 75:1996;2017-2028.
    • (1996) J. Neurophysiol. , vol.75 , pp. 2017-2028
    • Capogna, M.1    Gahwiler, B.H.2    Thompson, S.M.3
  • 12
    • 0023516714 scopus 로고
    • Characterization and some properties of the venom gland extract of a theridiid spider (Steatoda paykulliana) frequently mistaken for black widow spider (Latrodectus tredecimguttatus)
    • Cavalieri M., D'Urso D., Lassa A., Pierdominici E., Robello M., Grasso A. Characterization and some properties of the venom gland extract of a theridiid spider (Steatoda paykulliana) frequently mistaken for black widow spider (Latrodectus tredecimguttatus). Toxicon. 25:1987;965-974.
    • (1987) Toxicon , vol.25 , pp. 965-974
    • Cavalieri, M.1    D'Urso, D.2    Lassa, A.3    Pierdominici, E.4    Robello, M.5    Grasso, A.6
  • 13
    • 0025232675 scopus 로고
    • Immunocytological localization by monoclonal antibodies of α-latrotoxin in the venom gland of the spider Latrodectus tredecimguttatus
    • Cavalieri M., Corvaja N., Grasso A. Immunocytological localization by monoclonal antibodies of α-latrotoxin in the venom gland of the spider Latrodectus tredecimguttatus. Toxicon. 28:1990;341-346.
    • (1990) Toxicon , vol.28 , pp. 341-346
    • Cavalieri, M.1    Corvaja, N.2    Grasso, A.3
  • 14
    • 0019069857 scopus 로고
    • 2+-dependent recycling of synaptic vesicles at the frog neuromuscular junction
    • 2+-dependent recycling of synaptic vesicles at the frog neuromuscular junction. J. Cell Biol. 87:1980;297-303.
    • (1980) J. Cell Biol. , vol.87 , pp. 297-303
    • Ceccarelli, B.1    Hurlbut, W.P.2
  • 15
    • 0028327455 scopus 로고
    • Correlations between changes in membrane capacitance induced by changes in ionic environment and the conductance of channels incorporated into bilayer lipid membranes
    • Chanturiya A.N., Nikoloshina H.V. Correlations between changes in membrane capacitance induced by changes in ionic environment and the conductance of channels incorporated into bilayer lipid membranes. J. Membr. Biol. 137:1994;71-77.
    • (1994) J. Membr. Biol. , vol.137 , pp. 71-77
    • Chanturiya, A.N.1    Nikoloshina, H.V.2
  • 16
    • 0027489208 scopus 로고
    • Expression cloning of a human corticotropin-releasing-factor receptor
    • Chen R., Lewis K.A., Perrin M.H., Vale W.W. Expression cloning of a human corticotropin-releasing-factor receptor. Proc. Natl Acad. Sci. USA. 90:1993;8967-8971.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8967-8971
    • Chen, R.1    Lewis, K.A.2    Perrin, M.H.3    Vale, W.W.4
  • 17
    • 0034564456 scopus 로고    scopus 로고
    • The chromosomal genes for black widow spider neurotoxins do not contain introns
    • Danilevich V.N., Grishin E.V. The chromosomal genes for black widow spider neurotoxins do not contain introns. Bioorg. Khim. 26:2000;933-939.
    • (2000) Bioorg. Khim. , vol.26 , pp. 933-939
    • Danilevich, V.N.1    Grishin, E.V.2
  • 21
    • 0016717835 scopus 로고
    • Discrete and discontinuous action of brown widow spider venom on the presynaptic nerve terminals of frog muscle
    • del Castillo J., Pumplin D.W. Discrete and discontinuous action of brown widow spider venom on the presynaptic nerve terminals of frog muscle. J. Physiol. (London). 252:1975;491-508.
    • (1975) J. Physiol. (London) , vol.252 , pp. 491-508
    • Del Castillo, J.1    Pumplin, D.W.2
  • 23
    • 0033372353 scopus 로고    scopus 로고
    • α-Latrocrustatoxin increases neurotransmitter release by activating a calcium influx pathway at crayfish neuromuscular junction
    • Elrick D.B., Charlton M.P. α-Latrocrustatoxin increases neurotransmitter release by activating a calcium influx pathway at crayfish neuromuscular junction. J. Neurophysiol. 82:1999;3550-3562.
    • (1999) J. Neurophysiol. , vol.82 , pp. 3550-3562
    • Elrick, D.B.1    Charlton, M.P.2
  • 25
    • 0017093069 scopus 로고
    • Black widow spider venom: Effect of purified toxin on lipid bilayer membranes
    • Finkelstein A., Rubin L.L., Tzeng M.C. Black widow spider venom: effect of purified toxin on lipid bilayer membranes. Science. 193:1976;1009-1011.
    • (1976) Science , vol.193 , pp. 1009-1011
    • Finkelstein, A.1    Rubin, L.L.2    Tzeng, M.C.3
  • 26
    • 0015327294 scopus 로고
    • Effects of black widow spider venom on acetylcholine release from rat cerebral cortex slices in vitro
    • Frontali N., Granata F., Parisi P. Effects of black widow spider venom on acetylcholine release from rat cerebral cortex slices in vitro. Biochem. Pharmacol. 21:1972;969-974.
    • (1972) Biochem. Pharmacol. , vol.21 , pp. 969-974
    • Frontali, N.1    Granata, F.2    Parisi, P.3
  • 27
    • 0017233792 scopus 로고
    • Purification from black widow spider venom of a protein factor causing the depletion of synaptic vesicles at neuromuscular junctions
    • Frontali N., Ceccarelli B., Gorio A., Mauro A., Siekevitz P., Tzeng M.C., Hurlbut W.P. Purification from black widow spider venom of a protein factor causing the depletion of synaptic vesicles at neuromuscular junctions. J. Cell Biol. 68:1976;462-479.
    • (1976) J. Cell Biol. , vol.68 , pp. 462-479
    • Frontali, N.1    Ceccarelli, B.2    Gorio, A.3    Mauro, A.4    Siekevitz, P.5    Tzeng, M.C.6    Hurlbut, W.P.7
  • 28
    • 0028961149 scopus 로고
    • Furin-induced cleavage and activation of shiga toxin
    • Garred O., van Deurs B., Sandvig K. Furin-induced cleavage and activation of shiga toxin. J. Biol. Chem. 270:1995;10817-10821.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10817-10821
    • Garred, O.1    Van Deurs, B.2    Sandvig, K.3
  • 29
    • 23544469937 scopus 로고    scopus 로고
    • Comparison of effects of α-latrotoxin with a partially purified toxin from another theridiid spider,Steatoda paykulliana, on exocytosis at mouse neuromuscular junctions
    • (see also p.40)
    • Gillingwater T.H., Kalikulov D., Ushkaryov Y., Ribchester R.R. Comparison of effects of α-latrotoxin with a partially purified toxin from another theridiid spider,Steatoda paykulliana, on exocytosis at mouse neuromuscular junctions. J. Physiol. (London). 1999;520P. (see also p.40).
    • (1999) J. Physiol. (London)
    • Gillingwater, T.H.1    Kalikulov, D.2    Ushkaryov, Y.3    Ribchester, R.R.4
  • 30
    • 0030802762 scopus 로고    scopus 로고
    • Clostridium septicum α-toxin is proteolytically activated by furin
    • Gordon V.M., Benz R., Fujii K., Leppla S.H., Tweten R.K. Clostridium septicum α-toxin is proteolytically activated by furin. Infect. Immun. 65:1997;4130-4134.
    • (1997) Infect. Immun. , vol.65 , pp. 4130-4134
    • Gordon, V.M.1    Benz, R.2    Fujii, K.3    Leppla, S.H.4    Tweten, R.K.5
  • 31
    • 0015409112 scopus 로고
    • Effects of chromatographic fractions of black widow spider venom on in vitro biological systems
    • Granata F., Paggi P., Frontali N. Effects of chromatographic fractions of black widow spider venom on in vitro biological systems. Toxicon. 10:1972;551-555.
    • (1972) Toxicon , vol.10 , pp. 551-555
    • Granata, F.1    Paggi, P.2    Frontali, N.3
  • 32
    • 0017128633 scopus 로고
    • Preparation and properties of a neurotoxin purified from the venom of black widow spider (Latrodectus mactans tredecimguttatus)
    • Grasso A. Preparation and properties of a neurotoxin purified from the venom of black widow spider (Latrodectus mactans tredecimguttatus). Biochim. Biophys. Acta. 439:1976;406-412.
    • (1976) Biochim. Biophys. Acta , vol.439 , pp. 406-412
    • Grasso, A.1
  • 33
    • 0018840303 scopus 로고
    • Black widow spider toxin-induced calcium fluxes and transmitter release in a neurosecretory cell line
    • Grasso A., Alema S., Rufini S., Senni M.I. Black widow spider toxin-induced calcium fluxes and transmitter release in a neurosecretory cell line. Nature. 283:1980;774-776.
    • (1980) Nature , vol.283 , pp. 774-776
    • Grasso, A.1    Alema, S.2    Rufini, S.3    Senni, M.I.4
  • 34
    • 0036232249 scopus 로고    scopus 로고
    • Clinical and in vitro evidence for the efficacy of Australian red-back spider (Latrodectus hasselti) antivenom in the treatment of envenomation by a Cupboard spider (Steatoda grossa)
    • Graudins A., Gunja N., Broady K.W., Nicholson G.M. Clinical and in vitro evidence for the efficacy of Australian red-back spider (Latrodectus hasselti) antivenom in the treatment of envenomation by a Cupboard spider (Steatoda grossa). Toxicon. 40:2002;767-775.
    • (2002) Toxicon , vol.40 , pp. 767-775
    • Graudins, A.1    Gunja, N.2    Broady, K.W.3    Nicholson, G.M.4
  • 35
    • 0015838427 scopus 로고
    • Action of black widow spider venom at insect neuromuscular junctions
    • Griffiths D.J., Smyth T. Jr. Action of black widow spider venom at insect neuromuscular junctions. Toxicon. 11:1973;369-374.
    • (1973) Toxicon , vol.11 , pp. 369-374
    • Griffiths, D.J.1    Smyth Jr., T.2
  • 36
    • 0034050342 scopus 로고    scopus 로고
    • Calcium-independent receptor for α-latrotoxin and neurexin Iα facilitate toxin-induced channel formation: Evidence that channel formation results from tethering of toxin to membrane
    • Hlubek M.D., Stuenkel E.L., Krasnoperov V.G., Petrenko A.G., Holz R.W. Calcium-independent receptor for α-latrotoxin and neurexin Iα facilitate toxin-induced channel formation: evidence that channel formation results from tethering of toxin to membrane. Mol. Pharmacol. 57:2000;519-528.
    • (2000) Mol. Pharmacol. , vol.57 , pp. 519-528
    • Hlubek, M.D.1    Stuenkel, E.L.2    Krasnoperov, V.G.3    Petrenko, A.G.4    Holz, R.W.5
  • 37
    • 0030624540 scopus 로고    scopus 로고
    • Better prediction of protein cellular localization sites with the k nearest neighbors classifier
    • Horton P., Nakai K. Better prediction of protein cellular localization sites with the k nearest neighbors classifier. Proc. Int. Conf. Intell. Syst. Mol. Biol. 5:1997;147-152.
    • (1997) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.5 , pp. 147-152
    • Horton, P.1    Nakai, K.2
  • 38
    • 0019957999 scopus 로고
    • Hydrolysis of substance P and bradykinin by black widow spider venom gland extract
    • Huidobro-Toro J.P., Chelala C.A., Musacchio J.M. Hydrolysis of substance P and bradykinin by black widow spider venom gland extract. Biochem. Pharmacol. 31:1982;3323-3328.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 3323-3328
    • Huidobro-Toro, J.P.1    Chelala, C.A.2    Musacchio, J.M.3
  • 39
    • 0025369606 scopus 로고
    • Correlation between quantal secretion and vesicle loss at the frog neuromuscular junction
    • Hurlbut W.P., Iezzi N., Fesce R., Ceccarelli B. Correlation between quantal secretion and vesicle loss at the frog neuromuscular junction. J. Physiol. (London). 425:1990;501-526.
    • (1990) J. Physiol. (London) , vol.425 , pp. 501-526
    • Hurlbut, W.P.1    Iezzi, N.2    Fesce, R.3    Ceccarelli, B.4
  • 41
    • 0032476601 scopus 로고    scopus 로고
    • α-Latrotoxin action probed with recombinant toxin: Receptors recruit α-latrotoxin but do not transduce an exocytotic signal
    • Ichtchenko K., Khvotchev M., Kiyatkin N., Simpson L., Sugita S., Sudhof T.C. α-Latrotoxin action probed with recombinant toxin: receptors recruit α-latrotoxin but do not transduce an exocytotic signal. EMBO J. 17:1998;6188-6199.
    • (1998) EMBO J. , vol.17 , pp. 6188-6199
    • Ichtchenko, K.1    Khvotchev, M.2    Kiyatkin, N.3    Simpson, L.4    Sugita, S.5    Sudhof, T.C.6
  • 42
  • 44
    • 0015440397 scopus 로고
    • Effect of black widow spider venom on the lobster neuromuscular junctions
    • Kawai N., Mauro A., Grundfest H. Effect of black widow spider venom on the lobster neuromuscular junctions. J. Gen. Physiol. 60:1972;650-664.
    • (1972) J. Gen. Physiol. , vol.60 , pp. 650-664
    • Kawai, N.1    Mauro, A.2    Grundfest, H.3
  • 45
    • 0343081085 scopus 로고    scopus 로고
    • α-Latrotoxin triggers transmitter release via direct insertion into the presynaptic plasma membrane
    • Khvotchev M., Sudhof T.C. α-Latrotoxin triggers transmitter release via direct insertion into the presynaptic plasma membrane. EMBO J. 19:2000;3250-3262.
    • (2000) EMBO J. , vol.19 , pp. 3250-3262
    • Khvotchev, M.1    Sudhof, T.C.2
  • 46
    • 0025002906 scopus 로고
    • Cloning and structure of cDNA encoding α-latrotoxin from black widow spider venom
    • Kiyatkin N.I., Dulubova I.E., Chekhovskaya I.A., Grishin E.V. Cloning and structure of cDNA encoding α-latrotoxin from black widow spider venom. FEBS Lett. 270:1990;127-131.
    • (1990) FEBS Lett. , vol.270 , pp. 127-131
    • Kiyatkin, N.I.1    Dulubova, I.E.2    Chekhovskaya, I.A.3    Grishin, E.V.4
  • 47
    • 0026696944 scopus 로고
    • Structure of the low molecular weight protein copurified with α-latrotoxin
    • Kiyatkin N., Dulubova I., Chekhovskaya I., Lipkin A., Grishin E. Structure of the low molecular weight protein copurified with α-latrotoxin. Toxicon. 30:1992;771-774.
    • (1992) Toxicon , vol.30 , pp. 771-774
    • Kiyatkin, N.1    Dulubova, I.2    Chekhovskaya, I.3    Lipkin, A.4    Grishin, E.5
  • 48
    • 0027394764 scopus 로고
    • Cloning and structural analysis of α-latroinsectotoxin cDNA Abundance of ankyrin-like repeats
    • Kiyatkin N., Dulubova I., Grishin E. Cloning and structural analysis of α-latroinsectotoxin cDNA Abundance of ankyrin-like repeats. Eur. J. Biochem. 213:1993;121-127.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 121-127
    • Kiyatkin, N.1    Dulubova, I.2    Grishin, E.3
  • 49
    • 0022514574 scopus 로고
    • Black widow spider venom-induced release of neurotransmitters: Mammalian synaptosomes are stimulated by a unique venom component (α-latrotoxin), insect synaptosomes by multiple components
    • Knipper M., Madeddu L., Breer H., Meldolesi J. Black widow spider venom-induced release of neurotransmitters: mammalian synaptosomes are stimulated by a unique venom component (α-latrotoxin), insect synaptosomes by multiple components. Neuroscience. 19:1986;55-62.
    • (1986) Neuroscience , vol.19 , pp. 55-62
    • Knipper, M.1    Madeddu, L.2    Breer, H.3    Meldolesi, J.4
  • 50
    • 0025475326 scopus 로고
    • Identification and isolation of the protein insect toxin (α-latroinsectotoxin) from venom of the spider Latrodectus mactans tredecimguttatus
    • Kovalevskaia G.I., Pashkov V.N., Bulgakov O.V., Fedorova I.M., Magazanik L.G., Grishin E.V. Identification and isolation of the protein insect toxin (α-latroinsectotoxin) from venom of the spider Latrodectus mactans tredecimguttatus. Bioorg. Khim. 16:1990;1013-1018.
    • (1990) Bioorg. Khim. , vol.16 , pp. 1013-1018
    • Kovalevskaia, G.I.1    Pashkov, V.N.2    Bulgakov, O.V.3    Fedorova, I.M.4    Magazanik, L.G.5    Grishin, E.V.6
  • 51
    • 0026471613 scopus 로고
    • Comparative analysis of latrotoxin channels of different conductance in planar lipid bilayers. Evidence for cluster organization
    • Krasilnikov O.V., Sabirov R.Z. Comparative analysis of latrotoxin channels of different conductance in planar lipid bilayers. Evidence for cluster organization. Biochim. Biophys. Acta. 1112:1992;124-128.
    • (1992) Biochim. Biophys. Acta , vol.1112 , pp. 124-128
    • Krasilnikov, O.V.1    Sabirov, R.Z.2
  • 52
    • 16744363417 scopus 로고
    • A crustacean-specific neurotoxin from the venom of the black widow spider Latrodectus mactans tredecimguttatus
    • Krasnoperov V.G., Shamotienko O.G., Grishin E.V. A crustacean-specific neurotoxin from the venom of the black widow spider Latrodectus mactans tredecimguttatus. Bioorg. Khim. 16:1990;1567-1569.
    • (1990) Bioorg. Khim. , vol.16 , pp. 1567-1569
    • Krasnoperov, V.G.1    Shamotienko, O.G.2    Grishin, E.V.3
  • 53
    • 0025466998 scopus 로고
    • Isolation and properties of insect-specific neurotoxins from venoms of the spider Lactodectus mactans tredecimguttatus
    • Krasnoperov V.G., Shamotienko O.G., Grishin E.V. Isolation and properties of insect-specific neurotoxins from venoms of the spider Lactodectus mactans tredecimguttatus. Bioorg. Khim. 16:1990;1138-1140.
    • (1990) Bioorg. Khim. , vol.16 , pp. 1138-1140
    • Krasnoperov, V.G.1    Shamotienko, O.G.2    Grishin, E.V.3
  • 54
  • 57
    • 0033525112 scopus 로고    scopus 로고
    • Structural requirements for α-latrotoxin binding and α-latrotoxin-stimulated secretion. a study with calcium-independent receptor of α-latrotoxin (CIRL) deletion mutants
    • Krasnoperov V., Bittner M.A., Holz R.W., Chepurny O., Petrenko A.G. Structural requirements for α-latrotoxin binding and α-latrotoxin- stimulated secretion. A study with calcium-independent receptor of α-latrotoxin (CIRL) deletion mutants. J. Biol. Chem. 274:1999;3590-3596.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3590-3596
    • Krasnoperov, V.1    Bittner, M.A.2    Holz, R.W.3    Chepurny, O.4    Petrenko, A.G.5
  • 60
    • 0027076516 scopus 로고
    • Pit-1-dependent expression of the receptor for growth hormone releasing factor mediates pituitary cell growth
    • Lin C., Lin S.C., Chang C.P., Rosenfeld M.G. Pit-1-dependent expression of the receptor for growth hormone releasing factor mediates pituitary cell growth. Nature. 360:1992;765-768.
    • (1992) Nature , vol.360 , pp. 765-768
    • Lin, C.1    Lin, S.C.2    Chang, C.P.3    Rosenfeld, M.G.4
  • 61
    • 0014957263 scopus 로고
    • Effects of black widow spider venom on the frog neuromuscular junction. Effects on end-plate potential, miniature end-plate potential and nerve terminal spike
    • Longenecker H.E., Hurlbut W.P., Mauro A., Clark A.W. Effects of black widow spider venom on the frog neuromuscular junction. Effects on end-plate potential, miniature end-plate potential and nerve terminal spike. Nature. 225:1970;701-703.
    • (1970) Nature , vol.225 , pp. 701-703
    • Longenecker, H.E.1    Hurlbut, W.P.2    Mauro, A.3    Clark, A.W.4
  • 64
    • 0033037979 scopus 로고    scopus 로고
    • The latrophilin family: Multiply spliced G protein-coupled receptors with differential tissue distribution
    • Matsushita H., Lelianova V.G., Ushkaryov Y.A. The latrophilin family: multiply spliced G protein-coupled receptors with differential tissue distribution. FEBS Lett. 443:1999;348-352.
    • (1999) FEBS Lett. , vol.443 , pp. 348-352
    • Matsushita, H.1    Lelianova, V.G.2    Ushkaryov, Y.A.3
  • 65
    • 0023742989 scopus 로고
    • Differential effect of α-latrotoxin on exocytosis from small synaptic vesicles and from large dense-core vesicles containing calcitonin gene-related peptide at the frog neuromuscular junction
    • Matteoli M., Haimann C., Torri-Tarelli F., Polak J.M., Ceccarelli B., De Camilli P. Differential effect of α-latrotoxin on exocytosis from small synaptic vesicles and from large dense-core vesicles containing calcitonin gene-related peptide at the frog neuromuscular junction. Proc. Natl Acad. Sci. USA. 85:1988;7366-7370.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 7366-7370
    • Matteoli, M.1    Haimann, C.2    Torri-Tarelli, F.3    Polak, J.M.4    Ceccarelli, B.5    De Camilli, P.6
  • 66
    • 0025605696 scopus 로고
    • α-Latrotoxin releases both vesicular and cytoplasmic glutamate from isolated nerve terminals
    • McMahon H.T., Rosenthal L., Meldolesi J., Nicholls D.G. α-Latrotoxin releases both vesicular and cytoplasmic glutamate from isolated nerve terminals. J. Neurochem. 55:1990;2039-2047.
    • (1990) J. Neurochem. , vol.55 , pp. 2039-2047
    • McMahon, H.T.1    Rosenthal, L.2    Meldolesi, J.3    Nicholls, D.G.4
  • 67
    • 0020327573 scopus 로고
    • Studies on α-latrotoxin receptors in rat brain synaptosomes: Correlation between toxin binding and stimulation of transmitter release
    • Meldolesi J. Studies on α-latrotoxin receptors in rat brain synaptosomes: correlation between toxin binding and stimulation of transmitter release. J. Neurochem. 38:1982;1559-1569.
    • (1982) J. Neurochem. , vol.38 , pp. 1559-1569
    • Meldolesi, J.1
  • 68
    • 0022998064 scopus 로고
    • Channels produced by spider venoms in bilayer lipid membrane: Mechanisms of ion transport and toxic action
    • Mironov S.L., Sokolov Y.V., Chanturiya A.N., Lishko V.K. Channels produced by spider venoms in bilayer lipid membrane: mechanisms of ion transport and toxic action. Biochim. Biophys. Acta. 862:1986;185-198.
    • (1986) Biochim. Biophys. Acta , vol.862 , pp. 185-198
    • Mironov, S.L.1    Sokolov, Y.V.2    Chanturiya, A.N.3    Lishko, V.K.4
  • 69
    • 0023639423 scopus 로고
    • Dependence on multivalent cations of quantal release of transmitter induced by black widow spider venom
    • Misler S., Falke L.C. Dependence on multivalent cations of quantal release of transmitter induced by black widow spider venom. Am. J. Physiol. 253:1987;C469-C476.
    • (1987) Am. J. Physiol. , vol.253 , pp. 469-C476
    • Misler, S.1    Falke, L.C.2
  • 70
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai K., Horton P. PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem. Sci. 24:1999;34-36.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 71
    • 0030725756 scopus 로고    scopus 로고
    • Furin: A mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins
    • Nakayama K. Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem. J. 327:1997;625-635.
    • (1997) Biochem. J. , vol.327 , pp. 625-635
    • Nakayama, K.1
  • 73
    • 0029032454 scopus 로고
    • The cloning of a cDNA encoding a protein (latrodectin) which co-purifies with the (-latrotoxin from the black widow spider Latrodectus tredecimguttatus (Theridiidae)
    • Pescatori M., Bradbury A., Bouet F., Gargano N., Mastrogiacomo A., Grasso A. The cloning of a cDNA encoding a protein (latrodectin) which co-purifies with the (-latrotoxin from the black widow spider Latrodectus tredecimguttatus (Theridiidae). Eur. J. Biochem. 230:1995;322-328.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 322-328
    • Pescatori, M.1    Bradbury, A.2    Bouet, F.3    Gargano, N.4    Mastrogiacomo, A.5    Grasso, A.6
  • 77
    • 0023151578 scopus 로고
    • Permeation of divalent cations through α-latrotoxin channels in lipid bilayers: Steady-state current-voltage relationships
    • Robello M., Fresia M., Maga L., Grasso A., Ciani S. Permeation of divalent cations through α-latrotoxin channels in lipid bilayers: steady-state current-voltage relationships. J. Membr. Biol. 95:1987;55-62.
    • (1987) J. Membr. Biol. , vol.95 , pp. 55-62
    • Robello, M.1    Fresia, M.2    Maga, L.3    Grasso, A.4    Ciani, S.5
  • 78
  • 81
    • 0024560686 scopus 로고
    • Interactions between α-latrotoxin and trivalent cations in rat striatal synaptosomal preparations
    • Scheer H.W. Interactions between α-latrotoxin and trivalent cations in rat striatal synaptosomal preparations. J. Neurochem. 52:1989;1590-1597.
    • (1989) J. Neurochem. , vol.52 , pp. 1590-1597
    • Scheer, H.W.1
  • 82
    • 0032792551 scopus 로고    scopus 로고
    • The ankyrin repeat: A diversity of interactions on a common structural framework
    • Sedgwick S.G., Smerdon S.J. The ankyrin repeat: a diversity of interactions on a common structural framework. Trends Biochem. Sci. 24:1999;311-316.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 311-316
    • Sedgwick, S.G.1    Smerdon, S.J.2
  • 83
    • 0028985373 scopus 로고
    • Interaction of α-latroinsectotoxin from Latrodectus mactans venom with bilayer lipid membranes
    • Shatursky O.Y., Pashkov V.N., Bulgacov O.V., Grishin E.V. Interaction of α-latroinsectotoxin from Latrodectus mactans venom with bilayer lipid membranes. Biochim. Biophys. Acta. 1233:1995;14-20.
    • (1995) Biochim. Biophys. Acta , vol.1233 , pp. 14-20
    • Shatursky, O.Y.1    Pashkov, V.N.2    Bulgacov, O.V.3    Grishin, E.V.4
  • 84
    • 0002159609 scopus 로고
    • Structure of the venom gland of the black widow spider Latrodectus mactans. a preliminary light and electron microscopic study
    • F.E. Russel, & P.R. Saunders. Oxford: Pergamon
    • Smith D.S., Russell F.E. Structure of the venom gland of the black widow spider Latrodectus mactans. A preliminary light and electron microscopic study. Russel F.E., Saunders P.R. Animal Toxins. 1966;1-15 Pergamon, Oxford.
    • (1966) Animal Toxins , pp. 1-15
    • Smith, D.S.1    Russell, F.E.2
  • 85
    • 0032556697 scopus 로고    scopus 로고
    • Redback spider antivenom used to treat envenomation by a juvenile Steatoda spider
    • South M., Wirth P., Winkel K.D. Redback spider antivenom used to treat envenomation by a juvenile Steatoda spider. Med. J. Aust. 169:1998;642.
    • (1998) Med. J. Aust. , vol.169 , pp. 642
    • South, M.1    Wirth, P.2    Winkel, K.D.3
  • 86
    • 0032484023 scopus 로고    scopus 로고
    • α-Latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an unusual family of ubiquitous G-protein-linked receptors. G-protein coupling not required for triggering exocytosis
    • Sugita S., Ichtchenko K., Khvotchev M., Südhof T.C. α-Latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an unusual family of ubiquitous G-protein-linked receptors. G-protein coupling not required for triggering exocytosis. J. Biol. Chem. 273:1998;32715-32724.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32715-32724
    • Sugita, S.1    Ichtchenko, K.2    Khvotchev, M.3    Südhof, T.C.4
  • 87
    • 0033103549 scopus 로고    scopus 로고
    • Neurexins are functional α-latrotoxin receptors
    • Sugita S., Khvochtev M., Südhof T.C. Neurexins are functional α-latrotoxin receptors. Neuron. 22:1999;489-496.
    • (1999) Neuron , vol.22 , pp. 489-496
    • Sugita, S.1    Khvochtev, M.2    Südhof, T.C.3
  • 88
    • 0037155203 scopus 로고    scopus 로고
    • Genetic analysis of α-latrotoxin receptors reveals functional interdependence of CIRL/Latrophilin 1 and neurexin Iα
    • Tobaben S., Sudhof T.C., Stahl B. Genetic analysis of α-latrotoxin receptors reveals functional interdependence of CIRL/Latrophilin 1 and neurexin Iα J. Biol. Chem. 277:2002;6359-6365.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6359-6365
    • Tobaben, S.1    Sudhof, T.C.2    Stahl, B.3
  • 89
    • 0034551770 scopus 로고    scopus 로고
    • α-Latrotoxin releases calcium in frog motor nerve terminals
    • Tsang C.W., Elrick D.B., Charlton M.P. α-Latrotoxin releases calcium in frog motor nerve terminals. J. Neurosci. 20:2000;8685-8692.
    • (2000) J. Neurosci. , vol.20 , pp. 8685-8692
    • Tsang, C.W.1    Elrick, D.B.2    Charlton, M.P.3
  • 92
    • 0022614013 scopus 로고
    • Neurotoxin of the black widow spider and its interaction with receptors from the rat brain
    • Ushkarev I.A., Grishin E.V. Neurotoxin of the black widow spider and its interaction with receptors from the rat brain. Bioorg. Khim. 12:1986;71-80.
    • (1986) Bioorg. Khim. , vol.12 , pp. 71-80
    • Ushkarev, I.A.1    Grishin, E.V.2
  • 93
    • 0026769035 scopus 로고
    • Neurexins: Synaptic cell surface proteins related to the α-latrotoxin receptor and laminin
    • Ushkaryov Y.A., Petrenko A.G., Geppert M., Sudhof T.C. Neurexins: synaptic cell surface proteins related to the α-latrotoxin receptor and laminin. Science. 257:1992;50-56.
    • (1992) Science , vol.257 , pp. 50-56
    • Ushkaryov, Y.A.1    Petrenko, A.G.2    Geppert, M.3    Sudhof, T.C.4
  • 95
    • 0026144738 scopus 로고
    • Structure of tryptic fragments of a neurotoxin from black widow spider venom
    • Volkova T.M., Galkina T.G., Kudelin A.B., Grishin E.V. Structure of tryptic fragments of a neurotoxin from black widow spider venom. Bioorg. Khim. 17:1991;437-441.
    • (1991) Bioorg. Khim. , vol.17 , pp. 437-441
    • Volkova, T.M.1    Galkina, T.G.2    Kudelin, A.B.3    Grishin, E.V.4
  • 96
    • 0029029647 scopus 로고
    • Low molecular weight components from black widow spider venom
    • Volkova T.M., Pluzhnikov K.A., Woll P.G., Grishin E.V. Low molecular weight components from black widow spider venom. Toxicon. 33:1995;483-489.
    • (1995) Toxicon , vol.33 , pp. 483-489
    • Volkova, T.M.1    Pluzhnikov, K.A.2    Woll, P.G.3    Grishin, E.V.4
  • 101
    • 0022646329 scopus 로고
    • α Latrotoxin of the black widow spider venom opens a small, non-closing cation channel
    • Wanke E., Ferroni A., Gattanini P., Meldolesi J. α Latrotoxin of the black widow spider venom opens a small, non-closing cation channel. Biochem. Biophys. Res. Commun. 134:1986;320-325.
    • (1986) Biochem. Biophys. Res. Commun. , vol.134 , pp. 320-325
    • Wanke, E.1    Ferroni, A.2    Gattanini, P.3    Meldolesi, J.4
  • 102
    • 0025937989 scopus 로고
    • Neurotoxic envenoming by an immigrant spider (Steatoda nobilis) in southern England
    • Warrell D.A., Shaheen J., Hillyard P.D., Jones D. Neurotoxic envenoming by an immigrant spider (Steatoda nobilis) in southern England. Toxicon. 29:1991;1263-1265.
    • (1991) Toxicon , vol.29 , pp. 1263-1265
    • Warrell, D.A.1    Shaheen, J.2    Hillyard, P.D.3    Jones, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.