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Volumn 111, Issue 2, 2009, Pages 275-290

Penelope's web: Using α-latrotoxin to untangle the mysteries of exocytosis

Author keywords

latrotoxin; Exocytosis; Latrophilin; Neurexin; Protein tyrosine phosphatase; Synapse

Indexed keywords

ALPHA LATROTOXIN; CALCIUM; LATROPHILIN 1; LATROPHILIN 2; LATROPHILIN 3; NERVE PROTEIN; NEUREXIN; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE DELTA; UNCLASSIFIED DRUG;

EID: 70349335828     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2009.06329.x     Document Type: Review
Times cited : (29)

References (138)
  • 2
    • 0030803696 scopus 로고    scopus 로고
    • Regulated secretion is impaired in AtT-20 endocrine cells stably transfected with botulinum neurotoxin type A light chain
    • Aguado F., Gombau L., Majo G., Marsal J., Blanco J. Blasi J. (1997) Regulated secretion is impaired in AtT-20 endocrine cells stably transfected with botulinum neurotoxin type A light chain. J. Biol. Chem. 272, 26005 26008.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26005-26008
    • Aguado, F.1    Gombau, L.2    Majo, G.3    Marsal, J.4    Blanco, J.5    Blasi, J.6
  • 3
    • 0032577994 scopus 로고    scopus 로고
    • Incorporation of synaptotagmin II to the axolemma of botulinum type-A poisoned mouse motor endings during enhanced quantal acetylcholine release
    • Angaut-Petit D., Molgo J., Faille L., Juzans P. Takahashi M. (1998) Incorporation of synaptotagmin II to the axolemma of botulinum type-A poisoned mouse motor endings during enhanced quantal acetylcholine release. Brain Res. 797, 357 360.
    • (1998) Brain Res. , vol.797 , pp. 357-360
    • Angaut-Petit, D.1    Molgo, J.2    Faille, L.3    Juzans, P.4    Takahashi, M.5
  • 4
    • 27744547034 scopus 로고    scopus 로고
    • Properties of synaptic vesicle pools in mature central nerve terminals
    • Ashton A. C. Ushkaryov Y. A. (2005) Properties of synaptic vesicle pools in mature central nerve terminals. J. Biol. Chem. 280, 37278 37288.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37278-37288
    • Ashton, A.C.1    Ushkaryov, Y.A.2
  • 7
    • 0030858662 scopus 로고    scopus 로고
    • Heterogeneity of functional synaptic parameters among single release sites
    • Auger C. Marty A. (1997) Heterogeneity of functional synaptic parameters among single release sites. Neuron 19, 139 150.
    • (1997) Neuron , vol.19 , pp. 139-150
    • Auger, C.1    Marty, A.2
  • 9
    • 0034704089 scopus 로고    scopus 로고
    • Mints as adaptors. Direct binding to neurexins and recruitment of munc18
    • Biederer T. Sudhof T. C. (2000) Mints as adaptors. Direct binding to neurexins and recruitment of munc18. J. Biol. Chem. 275, 39803 39806.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39803-39806
    • Biederer, T.1    Sudhof, T.C.2
  • 10
    • 70349351529 scopus 로고
    • Poisoning poisonous spiders: An experimental investigation in the control of the black widow spider (Latrodectus mactans)
    • Bogen E. Loomis R. (1936) Poisoning poisonous spiders: an experimental investigation in the control of the black widow spider (Latrodectus mactans). Cal. West Med. 45, 31 38.
    • (1936) Cal. West Med. , vol.45 , pp. 31-38
    • Bogen, E.1    Loomis, R.2
  • 11
    • 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. (1996) Calcium-independent actions of α-latrotoxin on spontaneous and evoked synaptic transmission in the hippocampus. J. Neurophysiol. 76, 3149 3158.
    • (1996) J. Neurophysiol. , vol.76 , pp. 3149-3158
    • Capogna, M.1    Gahwiler, B.H.2    Thompson, S.M.3
  • 12
    • 0030612655 scopus 로고    scopus 로고
    • 2+partially rescues synaptic transmission in hippocampal cultures treated with botulinum toxin A and C, but not tetanus toxin
    • 2+partially rescues synaptic transmission in hippocampal cultures treated with botulinum toxin A and C, but not tetanus toxin. J. Neurosci. 17, 7190 7202.
    • (1997) J. Neurosci. , vol.17 , pp. 7190-7202
    • Capogna, M.1    McKinney, R.A.2    O'Connor, V.3    Gahwiler, B.H.4    Thompson, S.M.5
  • 14
    • 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. (1975) Discrete and discontinuous action of brown widow spider venom on the presynaptic nerve terminals of frog muscle. J. Physiol. (Lond.) 252, 491 508.
    • (1975) J. Physiol. (Lond.) , vol.252 , pp. 491-508
    • Del Castillo, J.1    Pumplin, D.W.2
  • 15
    • 0022476713 scopus 로고
    • A functional domain on the α-latrotoxin molecule, distinct from the binding site, involved in catecholamine secretion from PC12 cells: Identification with monoclonal antibodies
    • Cattaneo A. Grasso A. (1986) A functional domain on the α-latrotoxin molecule, distinct from the binding site, involved in catecholamine secretion from PC12 cells: identification with monoclonal antibodies. Biochemistry 25, 2730 2736.
    • (1986) Biochemistry , vol.25 , pp. 2730-2736
    • Cattaneo, A.1    Grasso, A.2
  • 16
    • 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. (1990) Immunocytological localization by monoclonal antibodies of α-latrotoxin in the venom gland of the spider Latrodectus tredecimguttatus. Toxicon 28, 341 346.
    • (1990) Toxicon , vol.28 , pp. 341-346
    • Cavalieri, M.1    Corvaja, N.2    Grasso, A.3
  • 17
    • 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, 297 303.
    • (1980) J. Cell Biol. , vol.87 , pp. 297-303
    • Ceccarelli, B.1    Hurlbut, W.P.2
  • 18
    • 0015618402 scopus 로고
    • Turnover of transmitter and synaptic vesicles at the frog neuromuscular junction
    • Ceccarelli B., Hurlbut W. P. Mauro A. (1973) Turnover of transmitter and synaptic vesicles at the frog neuromuscular junction. J. Cell Biol. 57, 499 524.
    • (1973) J. Cell Biol. , vol.57 , pp. 499-524
    • Ceccarelli, B.1    Hurlbut, W.P.2    Mauro, A.3
  • 20
    • 0030273232 scopus 로고    scopus 로고
    • Probing the structure-function relationship of α-latrotoxin-formed channels with antibodies and pronase
    • Chanturiya A. N., Nikolaenko A. N., Shatursky O. Y. Lishko V. K. (1996) Probing the structure-function relationship of α-latrotoxin-formed channels with antibodies and pronase. Toxicon 34, 1157 1164.
    • (1996) Toxicon , vol.34 , pp. 1157-1164
    • Chanturiya, A.N.1    Nikolaenko, A.N.2    Shatursky, O.Y.3    Lishko, V.K.4
  • 21
    • 34250211762 scopus 로고    scopus 로고
    • Activity-dependent validation of excitatory versus inhibitory synapses by neuroligin-1 versus neuroligin-2
    • Chubykin A. A., Atasoy D., Etherton M. R., Brose N., Kavalali E. T., Gibson J. R. Sudhof T. C. (2007) Activity-dependent validation of excitatory versus inhibitory synapses by neuroligin-1 versus neuroligin-2. Neuron 54, 919 931.
    • (2007) Neuron , vol.54 , pp. 919-931
    • Chubykin, A.A.1    Atasoy, D.2    Etherton, M.R.3    Brose, N.4    Kavalali, E.T.5    Gibson, J.R.6    Sudhof, T.C.7
  • 22
    • 0014957128 scopus 로고
    • Effects of black widow spider venom on the frog neuromuscular junction. Effects on the fine structure of the frog neuromuscular junction
    • Clark A. W., Mauro A., Longenecker H. E. Jr. Hurlbut W. P. (1970) Effects of black widow spider venom on the frog neuromuscular junction. Effects on the fine structure of the frog neuromuscular junction. Nature 225, 703 705.
    • (1970) Nature , vol.225 , pp. 703-705
    • Clark, A.W.1    Mauro, A.2    Longenecker, Jr.H.E.3    Hurlbut, W.P.4
  • 23
    • 0017157878 scopus 로고
    • Effects of botulinum toxin on neuromuscular transmission in the rat
    • Cull-Candy S. G., Lundh H. Thesleff S. (1976) Effects of botulinum toxin on neuromuscular transmission in the rat. J. Physiol. (Lond.) 260, 177 203.
    • (1976) J. Physiol. (Lond.) , vol.260 , pp. 177-203
    • Cull-Candy, S.G.1    Lundh, H.2    Thesleff, S.3
  • 29
    • 0027305999 scopus 로고
    • +-binding benzofuran isophthalate: The effect of veratridine, ouabain, and α-latrotoxin
    • +-binding benzofuran isophthalate: the effect of veratridine, ouabain, and α-latrotoxin. J. Neurochem. 61, 818 825.
    • (1993) J. Neurochem. , vol.61 , pp. 818-825
    • Deri, Z.1    Adam-Vizi, V.2
  • 30
    • 0023101807 scopus 로고
    • Differential effects of various secretagogues on quantal transmitter release from mouse motor nerve terminals treated with botulinum A and tetanus toxin
    • Dreyer F., Rosenberg F., Becker C., Bigalke H. Penner R. (1987) Differential effects of various secretagogues on quantal transmitter release from mouse motor nerve terminals treated with botulinum A and tetanus toxin. Naunyn Schmiedebergs Arch. Pharmacol. 335, 1 7.
    • (1987) Naunyn Schmiedebergs Arch. Pharmacol. , vol.335 , pp. 1-7
    • Dreyer, F.1    Rosenberg, F.2    Becker, C.3    Bigalke, H.4    Penner, R.5
  • 31
    • 33845202625 scopus 로고    scopus 로고
    • Extraction and protein component analysis of venom from the dissected venom glands of Latrodectus tredecimguttatus
    • Duan Z. G. et al. (2006) Extraction and protein component analysis of venom from the dissected venom glands of Latrodectus tredecimguttatus. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 145, 350 357.
    • (2006) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.145 , pp. 350-357
    • Duan, Z.G.1
  • 33
    • 0028177276 scopus 로고
    • Mechanism of α-latrotoxin action as revealed by patch-clamp experiments on Xenopus oocytes injected with rat brain messenger RNA
    • Filippov A. K., Tertishnikova S. M., Alekseev A. E., Tsurupa G. P., Pashkov V. N. Grishin E. V. (1994) Mechanism of α-latrotoxin action as revealed by patch-clamp experiments on Xenopus oocytes injected with rat brain messenger RNA. Neuroscience 61, 179 189.
    • (1994) Neuroscience , vol.61 , pp. 179-189
    • Filippov, A.K.1    Tertishnikova, S.M.2    Alekseev, A.E.3    Tsurupa, G.P.4    Pashkov, V.N.5    Grishin, E.V.6
  • 34
    • 0017093069 scopus 로고
    • Black widow spider venom: Effect of purified toxin on lipid bilayer membranes
    • Finkelstein A., Rubin L. L. Tzeng M.-C. (1976) Black widow spider venom: effect of purified toxin on lipid bilayer membranes. Science 193, 1009 1011.
    • (1976) Science , vol.193 , pp. 1009-1011
    • Finkelstein, A.1    Rubin, L.L.2    Tzeng, M.-C.3
  • 35
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • Fredriksson R., Lagerstrom M. C., Lundin L. G. Schioth H. B. (2003) The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol. Pharmacol. 63, 1256 1272.
    • (2003) Mol. Pharmacol. , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerstrom, M.C.2    Lundin, L.G.3    Schioth, H.B.4
  • 36
    • 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. (1972) Effects of black widow spider venom on acetylcholine release from rat cerebral cortex slices in vitro. Biochem. Pharmacol. 21, 969 974.
    • (1972) Biochem. Pharmacol. , vol.21 , pp. 969-974
    • Frontali, N.1    Granata, F.2    Parisi, P.3
  • 37
    • 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. (1976) Purification from black widow spider venom of a protein factor causing the depletion of synaptic vesicles at neuromuscular junctions. J. Cell Biol. 68, 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
  • 39
    • 67349182343 scopus 로고    scopus 로고
    • Autism genome-wide copy number variation reveals ubiquitin and neuronal genes
    • Glessner J. T. et al. (2009) Autism genome-wide copy number variation reveals ubiquitin and neuronal genes. Nature 459, 569 573.
    • (2009) Nature , vol.459 , pp. 569-573
    • Glessner, J.T.1
  • 40
    • 0018171739 scopus 로고
    • Acetylcholine compartments in mouse diaphragm. Comparison of the effects of black widow spider venom, electrical stimulation, and high concentrations of potassium
    • Gorio A., Hurlbut W. P. Ceccarelli B. (1978a) Acetylcholine compartments in mouse diaphragm. Comparison of the effects of black widow spider venom, electrical stimulation, and high concentrations of potassium. J. Cell Biol. 78, 716 733.
    • (1978) J. Cell Biol. , vol.78 , pp. 716-733
    • Gorio, A.1    Hurlbut, W.P.2    Ceccarelli, B.3
  • 41
    • 0017849571 scopus 로고
    • Double mode of action of black widow spider venom on frog neuromuscular junction
    • Gorio A., Rubin L. L. Mauro A. (1978b) Double mode of action of black widow spider venom on frog neuromuscular junction. J. Neurocytol. 7, 193 202.
    • (1978) J. Neurocytol. , vol.7 , pp. 193-202
    • Gorio, A.1    Rubin, L.L.2    Mauro, A.3
  • 42
    • 0017128633 scopus 로고
    • Preparation and properties of a neurotoxin purified from the venom of black widow spider (Latrodectus mactans tredecimguttatus)
    • Grasso A. (1976) Preparation and properties of a neurotoxin purified from the venom of black widow spider (Latrodectus mactans tredecimguttatus). Biochim. Biophys. Acta 439, 406 412.
    • (1976) Biochim. Biophys. Acta , vol.439 , pp. 406-412
    • Grasso, A.1
  • 43
    • 0027180657 scopus 로고
    • The secretion of amino acid transmitters from cerebellar primary cultures probed by α-latrotoxin
    • Grasso A. Mercanti-Ciotti M. T. (1993) The secretion of amino acid transmitters from cerebellar primary cultures probed by α-latrotoxin. Neuroscience 54, 595 604.
    • (1993) Neuroscience , vol.54 , pp. 595-604
    • Grasso, A.1    Mercanti-Ciotti, M.T.2
  • 44
    • 0017801549 scopus 로고
    • Concanavalin A blocks black widow spider toxin stimulation of transmitter release from synaptosomes
    • Grasso A., Rufini S. Senni I. (1978) Concanavalin A blocks black widow spider toxin stimulation of transmitter release from synaptosomes. FEBS Lett. 85, 241 244.
    • (1978) FEBS Lett. , vol.85 , pp. 241-244
    • Grasso, A.1    Rufini, S.2    Senni, I.3
  • 45
    • 0020073947 scopus 로고
    • Characterization of α-latrotoxin interaction with rat brain synaptosomes and PC12 cells
    • Grasso A., Pelliccia M. Alema S. (1982) Characterization of α-latrotoxin interaction with rat brain synaptosomes and PC12 cells. Toxicon 20, 149 156.
    • (1982) Toxicon , vol.20 , pp. 149-156
    • Grasso, A.1    Pelliccia, M.2    Alema, S.3
  • 46
    • 0031740473 scopus 로고    scopus 로고
    • Black widow spider toxins: The present and the future
    • Grishin E. V. (1998) Black widow spider toxins: the present and the future. Toxicon 36, 1693 1701.
    • (1998) Toxicon , vol.36 , pp. 1693-1701
    • Grishin, E.V.1
  • 47
    • 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. (2000) 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, 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
  • 48
    • 0242321672 scopus 로고    scopus 로고
    • Mechanism of α-latrotoxin action at nerve endings of neurohypophysis
    • Hlubek M., Tian D. Stuenkel E. L. (2003) Mechanism of α-latrotoxin action at nerve endings of neurohypophysis. Brain Res. 992, 30 42.
    • (2003) Brain Res. , vol.992 , pp. 30-42
    • Hlubek, M.1    Tian, D.2    Stuenkel, E.L.3
  • 49
    • 0025369606 scopus 로고
    • Correlation between quantal secretion and vesicle loss at the frog neuromuscular junction
    • Hurlbut W. P., Iezzi N., Fesce R. Ceccarelli B. (1990) Correlation between quantal secretion and vesicle loss at the frog neuromuscular junction. J. Physiol. (Lond.) 425, 501 526.
    • (1990) J. Physiol. (Lond.) , vol.425 , pp. 501-526
    • Hurlbut, W.P.1    Iezzi, N.2    Fesce, R.3    Ceccarelli, B.4
  • 51
    • 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. (1998) α-Latrotoxin action probed with recombinant toxin: receptors recruit α-latrotoxin but do not transduce an exocytotic signal. EMBO J. 17, 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
  • 52
    • 0033605390 scopus 로고    scopus 로고
    • A novel ubiquitously expressed α-latrotoxin receptor is a member of the CIRL family of G-protein-coupled receptors
    • Ichtchenko K., Bittner M. A., Krasnoperov V., Little A. R., Chepurny O., Holz R. W. Petrenko A. G. (1999) A novel ubiquitously expressed α-latrotoxin receptor is a member of the CIRL family of G-protein-coupled receptors. J. Biol. Chem. 274, 5491 5498.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5491-5498
    • Ichtchenko, K.1    Bittner, M.A.2    Krasnoperov, V.3    Little, A.R.4    Chepurny, O.5    Holz, R.W.6    Petrenko, A.G.7
  • 53
    • 0020592243 scopus 로고
    • Tetanus and botulinum toxins inhibit, and black widow spider venom stimulates the release of methionine-enkephalin-like material in vitro
    • Janicki P. K. Habermann E. (1983) Tetanus and botulinum toxins inhibit, and black widow spider venom stimulates the release of methionine-enkephalin- like material in vitro. J. Neurochem. 41, 395 402.
    • (1983) J. Neurochem. , vol.41 , pp. 395-402
    • Janicki, P.K.1    Habermann, E.2
  • 54
    • 0034669216 scopus 로고    scopus 로고
    • Role of calcium in neurotransmitter release evoked by α-latrotoxin or hypertonic sucrose
    • Khvotchev M., Lonart G. Sudhof T. C. (2000) Role of calcium in neurotransmitter release evoked by α-latrotoxin or hypertonic sucrose. Neuroscience 101, 793 802.
    • (2000) Neuroscience , vol.101 , pp. 793-802
    • Khvotchev, M.1    Lonart, G.2    Sudhof, T.C.3
  • 55
    • 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. (1990) Cloning and structure of cDNA encoding α-latrotoxin from black widow spider venom. FEBS Lett. 270, 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
  • 56
    • 0029016079 scopus 로고
    • Functional characterization of black widow spider neurotoxins synthesised in insect cells
    • Kiyatkin N. I., Kulikovskaya I. M., Grishin E. V., Beadle D. J. King L. A. (1995) Functional characterization of black widow spider neurotoxins synthesised in insect cells. Eur. J. Biochem. 230, 854 859.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 854-859
    • Kiyatkin, N.I.1    Kulikovskaya, I.M.2    Grishin, E.V.3    Beadle, D.J.4    King, L.A.5
  • 57
    • 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. (1992) Comparative analysis of latrotoxin channels of different conductance in planar lipid bilayers. Evidence for cluster organization. Biochim. Biophys. Acta 1112, 124 128.
    • (1992) Biochim. Biophys. Acta , vol.1112 , pp. 124-128
    • Krasilnikov, O.V.1    Sabirov, R.Z.2
  • 58
    • 0025466998 scopus 로고
    • Isolation and properties of insect-specific neurotoxins from venoms of the spider Lactodectus mactans tredecimguttatus
    • letter
    • Krasnoperov V. G., Shamotienko O. G. Grishin E. V. (1990) Isolation and properties of insect-specific neurotoxins from venoms of the spider Lactodectus mactans tredecimguttatus letter Bioorg. Khim. 16, 1138 1140.
    • (1990) Bioorg. Khim. , vol.16 , pp. 1138-1140
    • Krasnoperov, V.G.1    Shamotienko, O.G.2    Grishin, E.V.3
  • 60
    • 0031006123 scopus 로고    scopus 로고
    • α-Latrotoxin stimulates exocytosis by the interaction with a neuronal G-protein-coupled receptor
    • Krasnoperov V. G. et al. (1997) α-Latrotoxin stimulates exocytosis by the interaction with a neuronal G-protein-coupled receptor. Neuron 18, 925 937.
    • (1997) Neuron , vol.18 , pp. 925-937
    • Krasnoperov, V.G.1
  • 61
    • 0037195853 scopus 로고    scopus 로고
    • Post-translational proteolytic processing of the calcium-independent receptor of α-latrotoxin (CIRL), a natural chimera of the cell adhesion protein and the G protein-coupled receptor. Role of the G protein-coupled receptor proteolysis site (GPS) motif
    • Krasnoperov V., Lu Y., Buryanovsky L., Neubert T. A., Ichtchenko K. Petrenko A. G. (2002a) Post-translational proteolytic processing of the calcium-independent receptor of α-latrotoxin (CIRL), a natural chimera of the cell adhesion protein and the G protein-coupled receptor. Role of the G protein-coupled receptor proteolysis site (GPS) motif. J. Biol. Chem. 277, 46518 46526.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46518-46526
    • Krasnoperov, V.1    Lu, Y.2    Buryanovsky, L.3    Neubert, T.A.4    Ichtchenko, K.5    Petrenko, A.G.6
  • 63
    • 0034693141 scopus 로고    scopus 로고
    • The calcium-independent receptor for α-latrotoxin from human and rodent brains interacts with members of the ProSAP/SSTRIP/Shank family of multidomain proteins
    • Kreienkamp H. J., Zitzer H., Gundelfinger E. D., Richter D. Bockers T. M. (2000) The calcium-independent receptor for α-latrotoxin from human and rodent brains interacts with members of the ProSAP/SSTRIP/Shank family of multidomain proteins. J. Biol. Chem. 275, 32387 32390.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32387-32390
    • Kreienkamp, H.J.1    Zitzer, H.2    Gundelfinger, E.D.3    Richter, D.4    Bockers, T.M.5
  • 64
    • 33746552163 scopus 로고    scopus 로고
    • Splice variant 3, but not 2 of receptor protein-tyrosine phosphatase σ can mediate stimulation of insulin-secretion by α-latrotoxin
    • Lajus S. Lang J. (2006) Splice variant 3, but not 2 of receptor protein-tyrosine phosphatase σ can mediate stimulation of insulin-secretion by α-latrotoxin. J. Cell. Biochem. 98, 1552 1559.
    • (2006) J. Cell. Biochem. , vol.98 , pp. 1552-1559
    • Lajus, S.1    Lang, J.2
  • 65
    • 0032472437 scopus 로고    scopus 로고
    • 2+-independent insulin exocytosis induced by α-latrotoxin requires latrophilin, a G protein-coupled receptor
    • 2+-independent insulin exocytosis induced by α-latrotoxin requires latrophilin, a G protein-coupled receptor. EMBO J. 17, 648 657.
    • (1998) EMBO J. , vol.17 , pp. 648-657
    • Lang, J.1    Ushkaryov, Y.2    Grasso, A.3    Wollheim, C.B.4
  • 67
    • 70449651526 scopus 로고    scopus 로고
    • Activation of α-latrotoxin receptors at neuromuscular nerve terminals leads to a prolonged burst-like release of acetylcholine
    • In press).
    • Lelianova V., Thomson D., Ribchester R. R., Tonevitsky A. G. Ushkaryov Y. A. (2009) Activation of α-latrotoxin receptors at neuromuscular nerve terminals leads to a prolonged burst-like release of acetylcholine. Bull. Exp. Biol. Med. 147 (In press).
    • (2009) Bull. Exp. Biol. Med. , vol.147
    • Lelianova, V.1    Thomson, D.2    Ribchester, R.R.3    Tonevitsky, A.G.4    Ushkaryov, Y.A.5
  • 69
    • 33845934490 scopus 로고    scopus 로고
    • Ankyrin repeat: A unique motif mediating protein-protein interactions
    • Li J., Mahajan A. Tsai M. D. (2006) Ankyrin repeat: a unique motif mediating protein-protein interactions. Biochemistry 45, 15168 15178.
    • (2006) Biochemistry , vol.45 , pp. 15168-15178
    • Li, J.1    Mahajan, A.2    Tsai, M.D.3
  • 70
    • 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. (1970) 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, 701 703.
    • (1970) Nature , vol.225 , pp. 701-703
    • Longenecker, H.E.1    Hurlbut, W.P.2    Mauro, A.3    Clark, A.W.4
  • 71
    • 0026200206 scopus 로고
    • [Electron microscopy of α-latrotoxin from the venom of the black widow spider Latrodectus mactans tredecimguttatus]
    • Lunev A. V., Demin V. V., Zaitsev O. I., Spadir S. I. Grishin E. V. (1991) [Electron microscopy of α-latrotoxin from the venom of the black widow spider Latrodectus mactans tredecimguttatus]. Bioorg. Khim. 17, 1021 1026.
    • (1991) Bioorg. Khim. , vol.17 , pp. 1021-1026
    • Lunev, A.V.1    Demin, V.V.2    Zaitsev, O.I.3    Spadir, S.I.4    Grishin, E.V.5
  • 72
    • 77956431855 scopus 로고    scopus 로고
    • High-density SNP association study and copy number variation analysis of the AUTS1 and AUTS5 loci implicate IMMP2L-DOCK4 gene region in autism susceptibility
    • (in press).
    • Maestrini E. et al. (2009) High-density SNP association study and copy number variation analysis of the AUTS1 and AUTS5 loci implicate IMMP2L-DOCK4 gene region in autism susceptibility. Mol. Psychiatry 1 15 (in press).
    • (2009) Mol. Psychiatry , pp. 1-15
    • Maestrini, E.1
  • 73
    • 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. (1999) The latrophilin family: multiply spliced G protein-coupled receptors with differential tissue distribution. FEBS Lett. 443, 348 352.
    • (1999) FEBS Lett. , vol.443 , pp. 348-352
    • Matsushita, H.1    Lelianova, V.G.2    Ushkaryov, Y.A.3
  • 74
    • 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. (1988) 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, 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
  • 75
    • 0036663073 scopus 로고    scopus 로고
    • Enhanced rate of nerve regeneration and directional errors after sciatic nerve injury in receptor protein tyrosine phosphatase σ knock-out mice
    • McLean J., Batt J., Doering L. C., Rotin D. Bain J. R. (2002) Enhanced rate of nerve regeneration and directional errors after sciatic nerve injury in receptor protein tyrosine phosphatase σ knock-out mice. J. Neurosci. 22, 5481 5491.
    • (2002) J. Neurosci. , vol.22 , pp. 5481-5491
    • McLean, J.1    Batt, J.2    Doering, L.C.3    Rotin, D.4    Bain, J.R.5
  • 76
    • 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. (1990) α-Latrotoxin releases both vesicular and cytoplasmic glutamate from isolated nerve terminals. J. Neurochem. 55, 2039 2047.
    • (1990) J. Neurochem. , vol.55 , pp. 2039-2047
    • McMahon, H.T.1    Rosenthal, L.2    Meldolesi, J.3    Nicholls, D.G.4
  • 77
    • 0022998064 scopus 로고
    • Channels produced by spider venoms in bilayer lipid membrane: Mechanisms of ion transport and toxic action
    • Mironov S. L., Sokolov Y., Chanturiya A. N. Lishko V. K. (1986) Channels produced by spider venoms in bilayer lipid membrane: mechanisms of ion transport and toxic action. Biochim. Biophys. Acta 862, 185 198.
    • (1986) Biochim. Biophys. Acta , vol.862 , pp. 185-198
    • Mironov, S.L.1    Sokolov, Y.2    Chanturiya, A.N.3    Lishko, V.K.4
  • 81
    • 1842328567 scopus 로고    scopus 로고
    • Binding properties of neuroligin 1 and neurexin 1β reveal function as heterophilic cell adhesion molecules
    • Nguyen T. Sudhof T. C. (1997) Binding properties of neuroligin 1 and neurexin 1β reveal function as heterophilic cell adhesion molecules. J. Biol. Chem. 272, 26032 26039.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26032-26039
    • Nguyen, T.1    Sudhof, T.C.2
  • 82
    • 0020423198 scopus 로고
    • α-Latrotoxin of black widow spider venom depolarizes the plasma membrane, induces massive calcium influx, and stimulates transmitter release in guinea pig brain synaptosomes
    • Nicholls D. G., Rugolo M., Scott I. G. Meldolesi J. (1982) α-Latrotoxin of black widow spider venom depolarizes the plasma membrane, induces massive calcium influx, and stimulates transmitter release in guinea pig brain synaptosomes. Proc. Natl Acad. Sci. USA 79, 7924 7928.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 7924-7928
    • Nicholls, D.G.1    Rugolo, M.2    Scott, I.G.3    Meldolesi, J.4
  • 83
    • 0036402241 scopus 로고    scopus 로고
    • Identification and characterization of heart-specific splicing of human neurexin 3 mRNA (NRXN3)
    • Occhi G., Rampazzo A., Beffagna G. Antonio D. G. (2002) Identification and characterization of heart-specific splicing of human neurexin 3 mRNA (NRXN3). Biochem. Biophys. Res. Commun. 298, 151 155.
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 151-155
    • Occhi, G.1    Rampazzo, A.2    Beffagna, G.3    Antonio, D.G.4
  • 85
    • 0028986457 scopus 로고
    • α-Latrotoxin stimulates glutamate release from cortical astrocytes in cell culture
    • Parpura V., Liu F., Brethorst S., Jeftinija K., Jeftinija S. Haydon P. G. (1995) α-Latrotoxin stimulates glutamate release from cortical astrocytes in cell culture. FEBS Lett. 360, 266 270.
    • (1995) FEBS Lett. , vol.360 , pp. 266-270
    • Parpura, V.1    Liu, F.2    Brethorst, S.3    Jeftinija, K.4    Jeftinija, S.5    Haydon, P.G.6
  • 86
    • 0029032454 scopus 로고
    • The cloning of a cDNA encoding a protein (latrodectin) which co-purifies with the α-latrotoxin from the black widow spider Latrodectus tredecimguttatus (Theridiidae)
    • Pescatori M., Bradbury A., Bouet F., Gargano N., Mastrogiacomo A. Grasso A. (1995) The cloning of a cDNA encoding a protein (latrodectin) which co-purifies with the α-latrotoxin from the black widow spider Latrodectus tredecimguttatus (Theridiidae). Eur. J. Biochem. 230, 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
  • 87
    • 0027254029 scopus 로고
    • α-Latrotoxin receptor. Implications in nerve terminal function
    • Petrenko A. G. (1993) α-Latrotoxin receptor. Implications in nerve terminal function. FEBS Lett. 325, 81 85.
    • (1993) FEBS Lett. , vol.325 , pp. 81-85
    • Petrenko, A.G.1
  • 89
    • 0025776680 scopus 로고
    • Binding of synaptotagmin to the α-latrotoxin receptor implicates both in synaptic vesicle exocytosis
    • Petrenko A. G., Perin M. S., Davletov B. A., Ushkaryov Y. A., Geppert M. Sudhof T. C. (1991) Binding of synaptotagmin to the α-latrotoxin receptor implicates both in synaptic vesicle exocytosis. Nature 353, 65 68.
    • (1991) Nature , vol.353 , pp. 65-68
    • Petrenko, A.G.1    Perin, M.S.2    Davletov, B.A.3    Ushkaryov, Y.A.4    Geppert, M.5    Sudhof, T.C.6
  • 92
    • 34547271016 scopus 로고    scopus 로고
    • Interaction of calcium-independent latrotoxin receptor with intracellular adapter protein TRIP8b
    • Popova N. V., Plotnikov A., Deev I. E. Petrenko A. G. (2007) Interaction of calcium-independent latrotoxin receptor with intracellular adapter protein TRIP8b. Dokl. Biochem. Biophys. 414, 149 151.
    • (2007) Dokl. Biochem. Biophys. , vol.414 , pp. 149-151
    • Popova, N.V.1    Plotnikov, A.2    Deev, I.E.3    Petrenko, A.G.4
  • 94
    • 0029417204 scopus 로고
    • The LAR/PTPδ/PTPσ subfamily of transmembrane protein-tyrosine-phosphatases: Multiple human LAR, PTPδ, and PTPσ isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1
    • Pulido R., Serra-Pages C., Tang M. Streuli M. (1995) The LAR/PTPδ/PTPσ subfamily of transmembrane protein-tyrosine- phosphatases: multiple human LAR, PTPδ, and PTPσ isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1. Proc. Natl Acad. Sci. USA 92, 11686 11690.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 11686-11690
    • Pulido, R.1    Serra-Pages, C.2    Tang, M.3    Streuli, M.4
  • 96
    • 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. (1987) Permeation of divalent cations through α-latrotoxin channels in lipid bilayers: steady-state current-voltage relationships. J. Membr. Biol. 95, 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
  • 97
    • 33847415775 scopus 로고    scopus 로고
    • Insecticidal toxins from black widow spider venom
    • Rohou A., Nield J. Ushkaryov Y. A. (2007) Insecticidal toxins from black widow spider venom. Toxicon 49, 531 549.
    • (2007) Toxicon , vol.49 , pp. 531-549
    • Rohou, A.1    Nield, J.2    Ushkaryov, Y.A.3
  • 100
    • 0037282713 scopus 로고    scopus 로고
    • Isoform-specific binding of the tyrosine phosphatase PTPσ to a ligand in developing muscle
    • Sajnani-Perez G., Chilton J. K., Aricescu A. R., Haj F. Stoker A. W. (2003) Isoform-specific binding of the tyrosine phosphatase PTPσ to a ligand in developing muscle. Mol. Cell. Neurosci. 22, 37 48.
    • (2003) Mol. Cell. Neurosci. , vol.22 , pp. 37-48
    • Sajnani-Perez, G.1    Chilton, J.K.2    Aricescu, A.R.3    Haj, F.4    Stoker, A.W.5
  • 101
    • 7344249869 scopus 로고
    • Pharmacological action of the venom of Latrodectus mactans and other Latrodectus spiders
    • Sampayo R. R. L. (1944) Pharmacological action of the venom of Latrodectus mactans and other Latrodectus spiders. J. Pharmacol. Exp. Ther. 80, 309 322.
    • (1944) J. Pharmacol. Exp. Ther. , vol.80 , pp. 309-322
    • Sampayo, R.R.L.1
  • 102
    • 67249091362 scopus 로고    scopus 로고
    • TRIP8b splice variants form a family of auxiliary subunits that regulate gating and trafficking of HCN channels in the brain
    • Santoro B., Piskorowski R. A., Pian P., Hu L., Liu H. Siegelbaum S. A. (2009) TRIP8b splice variants form a family of auxiliary subunits that regulate gating and trafficking of HCN channels in the brain. Neuron 62, 802 813.
    • (2009) Neuron , vol.62 , pp. 802-813
    • Santoro, B.1    Piskorowski, R.A.2    Pian, P.3    Hu, L.4    Liu, H.5    Siegelbaum, S.A.6
  • 103
    • 0024560686 scopus 로고
    • Interactions between α-latrotoxin and trivalent cations in rat striatal synaptosomal preparations
    • Scheer H. W. (1989) Interactions between α-latrotoxin and trivalent cations in rat striatal synaptosomal preparations. J. Neurochem. 52, 1590 1597.
    • (1989) J. Neurochem. , vol.52 , pp. 1590-1597
    • Scheer, H.W.1
  • 104
    • 0025148243 scopus 로고
    • Interactions between the presynaptically active neurotoxins α-latrotoxin and ω-conotoxin GVIA: Studies on calcium fluxes and binding parameters in rat and chicken synaptosomes
    • Scheer H. W. (1990) Interactions between the presynaptically active neurotoxins α-latrotoxin and ω-conotoxin GVIA: studies on calcium fluxes and binding parameters in rat and chicken synaptosomes. Can. J. Physiol. Pharmacol. 68, 1049 1054.
    • (1990) Can. J. Physiol. Pharmacol. , vol.68 , pp. 1049-1054
    • Scheer, H.W.1
  • 105
    • 0021713743 scopus 로고
    • α-Latrotoxin of black widow spider venom: An interesting neurotoxin and a tool for investigating the process of neurotransmitter release
    • Scheer H., Madeddu L., Dozio N., Gatti G., Vicentini L. M. Meldolesi J. (1984) α-Latrotoxin of black widow spider venom: an interesting neurotoxin and a tool for investigating the process of neurotransmitter release. J. Physiol. (Paris) 79, 216 221.
    • (1984) J. Physiol. (Paris) , vol.79 , pp. 216-221
    • Scheer, H.1    Madeddu, L.2    Dozio, N.3    Gatti, G.4    Vicentini, L.M.5    Meldolesi, J.6
  • 106
    • 0034625250 scopus 로고    scopus 로고
    • Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons
    • Scheiffele P., Fan J., Choih J., Fetter R. Serafini T. (2000) Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons. Cell 101, 657 669.
    • (2000) Cell , vol.101 , pp. 657-669
    • Scheiffele, P.1    Fan, J.2    Choih, J.3    Fetter, R.4    Serafini, T.5
  • 107
    • 61949446367 scopus 로고    scopus 로고
    • Identification of proteins in complexes with α-latrotoxin receptors
    • Serova O. V., Popova N. V., Deev I. E. Petrenko A. G. (2008) Identification of proteins in complexes with α-latrotoxin receptors. Bioorg. Khim. 34, 747 753.
    • (2008) Bioorg. Khim. , vol.34 , pp. 747-753
    • Serova, O.V.1    Popova, N.V.2    Deev, I.E.3    Petrenko, A.G.4
  • 108
    • 0034044563 scopus 로고    scopus 로고
    • The Shank family of scaffold proteins
    • Sheng M. Kim E. (2000) The Shank family of scaffold proteins. J. Cell Sci. 113 (Pt. 11 1851 1856.
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 11 , pp. 1851-1856
    • Sheng, M.1    Kim, E.2
  • 109
    • 65249085110 scopus 로고    scopus 로고
    • Functional cross-interaction of the fragments produced by the cleavage of distinct adhesion G-protein-coupled receptors
    • Silva J. P., Lelianova V., Hopkins C., Volynski K. E. Ushkaryov Y. (2009) Functional cross-interaction of the fragments produced by the cleavage of distinct adhesion G-protein-coupled receptors. J. Biol. Chem. 284, 6495 6506.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6495-6506
    • Silva, J.P.1    Lelianova, V.2    Hopkins, C.3    Volynski, K.E.4    Ushkaryov, Y.5
  • 110
    • 33845763350 scopus 로고    scopus 로고
    • N-cadherin is an in vivo substrate for PTPσ and participates in PTPσ-mediated inhibition of axon growth
    • Siu R., Fladd C. Rotin D. (2006) N-cadherin is an in vivo substrate for PTPσ and participates in PTPσ-mediated inhibition of axon growth. Mol. Cell. Biol. 27, 208 219.
    • (2006) Mol. Cell. Biol. , vol.27 , pp. 208-219
    • Siu, R.1    Fladd, C.2    Rotin, D.3
  • 111
    • 0027997591 scopus 로고
    • GTP cleavage by the small GTP-binding protein Rab3A is associated with exocytosis of synaptic vesicles induced by α-latrotoxin
    • Stahl B., von Mollard G. F., Walch-Solimena C. Jahn R. (1994) GTP cleavage by the small GTP-binding protein Rab3A is associated with exocytosis of synaptic vesicles induced by α-latrotoxin. J. Biol. Chem. 269, 24770 24776.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24770-24776
    • Stahl, B.1    Von Mollard, G.F.2    Walch-Solimena, C.3    Jahn, R.4
  • 112
    • 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. (1998) 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, 32715 32724.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32715-32724
    • Sugita, S.1    Ichtchenko, K.2    Khvotchev, M.3    Südhof, T.C.4
  • 113
    • 0033103549 scopus 로고    scopus 로고
    • Neurexins are functional α-latrotoxin receptors
    • Sugita S., Khvochtev M. Südhof T. C. (1999) Neurexins are functional α-latrotoxin receptors. Neuron 22, 489 496.
    • (1999) Neuron , vol.22 , pp. 489-496
    • Sugita, S.1    Khvochtev, M.2    Südhof, T.C.3
  • 114
    • 33847327313 scopus 로고    scopus 로고
    • Mapping autism risk loci using genetic linkage and chromosomal rearrangements
    • Szatmari P. et al. (2007) Mapping autism risk loci using genetic linkage and chromosomal rearrangements. Nat. Genetics 39, 319 328.
    • (2007) Nat. Genetics , vol.39 , pp. 319-328
    • Szatmari, P.1
  • 115
    • 35148858044 scopus 로고    scopus 로고
    • A neuroligin-3 mutation implicated in autism increases inhibitory synaptic transmission in mice
    • Tabuchi K., Blundell J., Etherton M. R., Hammer R. E., Liu X., Powell C. M. Sudhof T. C. (2007) A neuroligin-3 mutation implicated in autism increases inhibitory synaptic transmission in mice. Science 318, 71 76.
    • (2007) Science , vol.318 , pp. 71-76
    • Tabuchi, K.1    Blundell, J.2    Etherton, M.R.3    Hammer, R.E.4    Liu, X.5    Powell, C.M.6    Sudhof, T.C.7
  • 116
    • 0034680783 scopus 로고    scopus 로고
    • The G protein-coupled receptor CL1 interacts directly with proteins of the Shank family
    • Tobaben S., Sudhof T. C. Stahl B. (2000) The G protein-coupled receptor CL1 interacts directly with proteins of the Shank family. J. Biol. Chem. 275, 36204 36210.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36204-36210
    • Tobaben, S.1    Sudhof, T.C.2    Stahl, B.3
  • 117
    • 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. (2002) Genetic analysis of α-latrotoxin receptors reveals functional interdependence of CIRL/Latrophilin 1 and neurexin Iα. J. Biol. Chem. 277, 6359 6365.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6359-6365
    • Tobaben, S.1    Sudhof, T.C.2    Stahl, B.3
  • 118
    • 33750299450 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: From genes, to function, to disease
    • Tonks N. K. (2006) Protein tyrosine phosphatases: from genes, to function, to disease. Nat. Rev. Mol. Cell Biol. 7, 833 846.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 833-846
    • Tonks, N.K.1
  • 119
    • 0034551770 scopus 로고    scopus 로고
    • α-Latrotoxin releases calcium in frog motor nerve terminals
    • Tsang C. W., Elrick D. B. Charlton M. P. (2000) α-Latrotoxin releases calcium in frog motor nerve terminals. J. Neurosci. 20, 8685 8692.
    • (2000) J. Neurosci. , vol.20 , pp. 8685-8692
    • Tsang, C.W.1    Elrick, D.B.2    Charlton, M.P.3
  • 120
    • 0018394035 scopus 로고
    • The binding interaction between α-latrotoxin from black widow spider venom and a dog cerebral cortex synaptosomal membrane preparation
    • Tzeng M. C. Siekevitz P. (1979) The binding interaction between α-latrotoxin from black widow spider venom and a dog cerebral cortex synaptosomal membrane preparation. J. Neurochem. 33, 263 274.
    • (1979) J. Neurochem. , vol.33 , pp. 263-274
    • Tzeng, M.C.1    Siekevitz, P.2
  • 121
    • 0028969264 scopus 로고
    • Cartography of neurexins: More than 1000 isoforms generated by alternative splicing and expressed in distinct subsets of neurons
    • Ullrich B., Ushkaryov Y. A. Sudhof T. C. (1995) Cartography of neurexins: more than 1000 isoforms generated by alternative splicing and expressed in distinct subsets of neurons. Neuron 14, 497 507.
    • (1995) Neuron , vol.14 , pp. 497-507
    • Ullrich, B.1    Ushkaryov, Y.A.2    Sudhof, T.C.3
  • 122
    • 0036027992 scopus 로고    scopus 로고
    • α-Latrotoxin: From structure to some functions
    • Ushkaryov Y. (2002) α-Latrotoxin: from structure to some functions. Toxicon 40, 1 5.
    • (2002) Toxicon , vol.40 , pp. 1-5
    • Ushkaryov, Y.1
  • 123
    • 0027292233 scopus 로고
    • Neurexin IIIα: Extensive alternative splicing generates membrane-bound and soluble forms
    • Ushkaryov Y. A. Sudhof T. C. (1993) Neurexin IIIα: extensive alternative splicing generates membrane-bound and soluble forms. Proc. Natl Acad. Sci. USA 90, 6410 6414.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6410-6414
    • Ushkaryov, Y.A.1    Sudhof, T.C.2
  • 124
    • 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. (1992) Neurexins: synaptic cell surface proteins related to the α-latrotoxin receptor and laminin. Science 257, 50 56.
    • (1992) Science , vol.257 , pp. 50-56
    • Ushkaryov, Y.A.1    Petrenko, A.G.2    Geppert, M.3    Sudhof, T.C.4
  • 125
    • 0028241554 scopus 로고
    • Conserved domain structure of β-neurexins. Unusual cleaved signal sequences in receptor-like neuronal cell-surface proteins
    • Ushkaryov Y. A., Hata Y., Ichtchenko K., Moomaw C., Afendis S., Slaughter C. A. Sudhof T. C. (1994) Conserved domain structure of β-neurexins. Unusual cleaved signal sequences in receptor-like neuronal cell-surface proteins. J. Biol. Chem. 269, 11987 11992.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11987-11992
    • Ushkaryov, Y.A.1    Hata, Y.2    Ichtchenko, K.3    Moomaw, C.4    Afendis, S.5    Slaughter, C.A.6    Sudhof, T.C.7
  • 126
    • 0024232977 scopus 로고
    • Synaptophysin (p38) at the frog neuromuscular junction: Its incorporation into the axolemma and recycling after intense quantal secretion
    • Valtorta F., Jahn R., Fesce R., Greengard P. Ceccarelli B. (1988) Synaptophysin (p38) at the frog neuromuscular junction: its incorporation into the axolemma and recycling after intense quantal secretion. J. Cell Biol. 107, 2717 2727.
    • (1988) J. Cell Biol. , vol.107 , pp. 2717-2727
    • Valtorta, F.1    Jahn, R.2    Fesce, R.3    Greengard, P.4    Ceccarelli, B.5
  • 129
    • 0021281897 scopus 로고
    • α-Latrotoxin of black widow spider venom binds to a specific receptor coupled to phosphoinositide breakdown in PC12 cells
    • Vicentini L. M. Meldolesi J. (1984) α-Latrotoxin of black widow spider venom binds to a specific receptor coupled to phosphoinositide breakdown in PC12 cells. Biochem. Biophys. Res. Commun. 121, 538 544.
    • (1984) Biochem. Biophys. Res. Commun. , vol.121 , pp. 538-544
    • Vicentini, L.M.1    Meldolesi, J.2
  • 130
    • 0029029647 scopus 로고
    • Low-molecular-weight components from black-widow spider venom
    • Volkova T. M., Pluzhnikov K. A., Woll P. G. Grishin E. V. (1995) Low-molecular-weight components from black-widow spider venom. Toxicon 33, 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
  • 132
    • 0034731437 scopus 로고    scopus 로고
    • Latrophilin, neurexin and their signaling-deficient mutants facilitate α-latrotoxin insertion into membranes but are not involved in pore formation
    • Volynski K. V. et al. (2000) Latrophilin, neurexin and their signaling-deficient mutants facilitate α-latrotoxin insertion into membranes but are not involved in pore formation. J. Biol. Chem. 275, 41175 41183.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41175-41183
    • Volynski, K.V.1
  • 136
    • 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. (1986) α-Latrotoxin of the black widow spider venom opens a small, non-closing cation channel. Biochem. Biophys. Res. Commun. 134, 320 325.
    • (1986) Biochem. Biophys. Res. Commun. , vol.134 , pp. 320-325
    • Wanke, E.1    Ferroni, A.2    Gattanini, P.3    Meldolesi, J.4
  • 138
    • 0029082282 scopus 로고
    • Amperometric detection of stimulus-induced quantal release of catecholamines from cultured superior cervical ganglion neurons
    • Zhou Z. Misler S. (1995) Amperometric detection of stimulus-induced quantal release of catecholamines from cultured superior cervical ganglion neurons. Proc. Natl Acad. Sci. USA 92, 6938 6942.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6938-6942
    • Zhou, Z.1    Misler, S.2


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