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Volumn 22, Issue 4, 2011, Pages 425-433

Functional roles of synapsin: Lessons from invertebrates

Author keywords

Invertebrates; Phylogenetic; Short term synaptic plasticity; Synapsin; Synaptic models

Indexed keywords

SYNAPSIN; SYNAPSIN I; SYNAPSIN II;

EID: 80052744495     PISSN: 10849521     EISSN: 10963634     Source Type: Journal    
DOI: 10.1016/j.semcdb.2011.07.018     Document Type: Review
Times cited : (15)

References (106)
  • 1
    • 0014111301 scopus 로고
    • Transmission in invertebrate and vertebrate ganglia
    • Tauc L. Transmission in invertebrate and vertebrate ganglia. Physiol Rev 1967, 47:521-593.
    • (1967) Physiol Rev , vol.47 , pp. 521-593
    • Tauc, L.1
  • 2
    • 25844489563 scopus 로고    scopus 로고
    • Integrative neuroscience: linking levels of analyses
    • Grillner S., Kozlov A., Kotaleski J.H. Integrative neuroscience: linking levels of analyses. Curr Opin Neurobiol 2005, 15:614-621.
    • (2005) Curr Opin Neurobiol , vol.15 , pp. 614-621
    • Grillner, S.1    Kozlov, A.2    Kotaleski, J.H.3
  • 3
    • 34047159123 scopus 로고    scopus 로고
    • Invertebrate preparations and their contribution to neurobiology in the second half of the 20th century
    • Clarac F., Pearlstein E. Invertebrate preparations and their contribution to neurobiology in the second half of the 20th century. Brain Res Rev 2007, 54:113-161.
    • (2007) Brain Res Rev , vol.54 , pp. 113-161
    • Clarac, F.1    Pearlstein, E.2
  • 4
    • 0004145862 scopus 로고
    • Sinauer Associates, Inc. Publishers, Sunderland, Massachusetts
    • Kuffler S.W., Nicholls J.G. From neuron to brain 1976, Sinauer Associates, Inc. Publishers, Sunderland, Massachusetts.
    • (1976) From neuron to brain
    • Kuffler, S.W.1    Nicholls, J.G.2
  • 5
    • 0015748816 scopus 로고
    • Regulation of endogenous phosphorylation of specific proteins in synaptic membrane fractions from rat brain by adenosine 3':5'-mono-phosphate
    • Ueda T., Maeno H., Greengard P. Regulation of endogenous phosphorylation of specific proteins in synaptic membrane fractions from rat brain by adenosine 3':5'-mono-phosphate. J Biol Chem 1973, 248:8295-8305.
    • (1973) J Biol Chem , vol.248 , pp. 8295-8305
    • Ueda, T.1    Maeno, H.2    Greengard, P.3
  • 6
    • 0001594816 scopus 로고
    • Mechanism of prolonged heterosynaptic facilitation
    • Kandel E.R., Tauc L. Mechanism of prolonged heterosynaptic facilitation. Nature 1964, 202:145-147.
    • (1964) Nature , vol.202 , pp. 145-147
    • Kandel, E.R.1    Tauc, L.2
  • 7
    • 0014964429 scopus 로고
    • Neuronal mechanisms of habituation and dishabituation of the gill-withdrawal reflex in Aplysia
    • Castellucci V., Pinsker H., Kupfermann I., Kandel E.R. Neuronal mechanisms of habituation and dishabituation of the gill-withdrawal reflex in Aplysia. Science 1970, 167:1745-1748.
    • (1970) Science , vol.167 , pp. 1745-1748
    • Castellucci, V.1    Pinsker, H.2    Kupfermann, I.3    Kandel, E.R.4
  • 8
    • 0016815636 scopus 로고
    • Heterosynaptic facilitation in the giant cell of Aplysia
    • Shimahara T., Tauc L. Heterosynaptic facilitation in the giant cell of Aplysia. J Physiol 1975, 247:321-341.
    • (1975) J Physiol , vol.247 , pp. 321-341
    • Shimahara, T.1    Tauc, L.2
  • 10
    • 70149104584 scopus 로고    scopus 로고
    • Identification of a serotonin receptor coupled to adenylyl cyclase involved in learning-related heterosynaptic facilitation in Aplysia
    • Lee Y.S., Choi S.L., Lee S.H., Kim H., Park H., Lee N., et al. Identification of a serotonin receptor coupled to adenylyl cyclase involved in learning-related heterosynaptic facilitation in Aplysia. Proc Natl Acad Sci USA 2009, 106:14634-14639.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14634-14639
    • Lee, Y.S.1    Choi, S.L.2    Lee, S.H.3    Kim, H.4    Park, H.5    Lee, N.6
  • 11
    • 0022835911 scopus 로고
    • A critical period for macromolecular synthesis in long-term heterosynaptic facilitation in Aplysia
    • Montarolo P.G., Goelet P., Castellucci V.F., Morgan J., Kandel E.R., Schacher S. A critical period for macromolecular synthesis in long-term heterosynaptic facilitation in Aplysia. Science 1986, 234:1249-1254.
    • (1986) Science , vol.234 , pp. 1249-1254
    • Montarolo, P.G.1    Goelet, P.2    Castellucci, V.F.3    Morgan, J.4    Kandel, E.R.5    Schacher, S.6
  • 12
    • 0026756423 scopus 로고
    • Inhibitors of protein and RNA synthesis block structural changes that accompany long-term heterosynaptic plasticity in Aplysia
    • Bailey C.H., Montarolo P., Chen M., Kandel E.R., Schacher S. Inhibitors of protein and RNA synthesis block structural changes that accompany long-term heterosynaptic plasticity in Aplysia. Neuron 1992, 9:749-758.
    • (1992) Neuron , vol.9 , pp. 749-758
    • Bailey, C.H.1    Montarolo, P.2    Chen, M.3    Kandel, E.R.4    Schacher, S.5
  • 13
    • 0023950127 scopus 로고
    • Long-term heterosynaptic inhibition in Aplysia
    • Montarolo P.G., Kandel E.R., Schacher S. Long-term heterosynaptic inhibition in Aplysia. Nature 1988, 333:171-174.
    • (1988) Nature , vol.333 , pp. 171-174
    • Montarolo, P.G.1    Kandel, E.R.2    Schacher, S.3
  • 14
    • 0034633737 scopus 로고    scopus 로고
    • A novel function for serotonin-mediated short-term facilitation in Aplysia: conversion of a transient, cell-wide homosynaptic hebbian plasticity into a persistent, protein synthesis-independent synapse-specific enhancement
    • Bailey C.H., Giustetto M., Zhu H., Chen M., Kandel E.R. A novel function for serotonin-mediated short-term facilitation in Aplysia: conversion of a transient, cell-wide homosynaptic hebbian plasticity into a persistent, protein synthesis-independent synapse-specific enhancement. Proc Natl Acad Sci USA 2000, 97:11581-11586.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11581-11586
    • Bailey, C.H.1    Giustetto, M.2    Zhu, H.3    Chen, M.4    Kandel, E.R.5
  • 15
    • 0015799240 scopus 로고
    • Long-lasting potentiation of synaptic transmission in the dentate area of the anaesthetized rabbit following stimulation of the perforant path
    • Bliss T.V., Lomo T. Long-lasting potentiation of synaptic transmission in the dentate area of the anaesthetized rabbit following stimulation of the perforant path. J Physiol 1973, 232:331-356.
    • (1973) J Physiol , vol.232 , pp. 331-356
    • Bliss, T.V.1    Lomo, T.2
  • 16
    • 0242559052 scopus 로고    scopus 로고
    • Learning in Aplysia: looking at synaptic plasticity from both sides
    • Roberts A.C., Glanzman D.L. Learning in Aplysia: looking at synaptic plasticity from both sides. Trends Neurosci 2003, 26:662-670.
    • (2003) Trends Neurosci , vol.26 , pp. 662-670
    • Roberts, A.C.1    Glanzman, D.L.2
  • 17
    • 0032125869 scopus 로고    scopus 로고
    • Postsynaptic induction and PKA-dependent expression of LTP in the lateral amygdala
    • Huang Y.Y., Kandel E.R. Postsynaptic induction and PKA-dependent expression of LTP in the lateral amygdala. Neuron 1998, 21:169-178.
    • (1998) Neuron , vol.21 , pp. 169-178
    • Huang, Y.Y.1    Kandel, E.R.2
  • 18
    • 0346096511 scopus 로고    scopus 로고
    • Presynaptic induction of heterosynaptic associative plasticity in the mammalian brain
    • Humeau Y., Shaban H., Bissiere S., Lüthi A. Presynaptic induction of heterosynaptic associative plasticity in the mammalian brain. Nature 2003, 426:841-845.
    • (2003) Nature , vol.426 , pp. 841-845
    • Humeau, Y.1    Shaban, H.2    Bissiere, S.3    Lüthi, A.4
  • 19
    • 33747610450 scopus 로고    scopus 로고
    • Generalization of amygdala LTP and conditioned fear in the absence of presynaptic inhibition
    • Shaban H., Humeau Y., Herry C., Cassasus G., Shigemoto R., Ciocchi S., et al. Generalization of amygdala LTP and conditioned fear in the absence of presynaptic inhibition. Nat Neurosci 2006, 9:1028-1035.
    • (2006) Nat Neurosci , vol.9 , pp. 1028-1035
    • Shaban, H.1    Humeau, Y.2    Herry, C.3    Cassasus, G.4    Shigemoto, R.5    Ciocchi, S.6
  • 20
    • 15944382338 scopus 로고    scopus 로고
    • The Functioning of the Giant Nerve Fibres of the Squid. 1938 - J. Z. and the discovery of squid giant nerve fibres
    • Young J.Z., Keynes R. The Functioning of the Giant Nerve Fibres of the Squid. 1938 - J. Z. and the discovery of squid giant nerve fibres. J Exp Biol 2005, 208:179-180.
    • (2005) J Exp Biol , vol.208 , pp. 179-180
    • Young, J.Z.1    Keynes, R.2
  • 21
    • 0000345058 scopus 로고
    • Cholinergic transmission mechanisms for both excitation and inhibition in molluscan central synapses
    • Tauc L., Gerschenfeld H.M. Cholinergic transmission mechanisms for both excitation and inhibition in molluscan central synapses. Nature 1962, 192:366-367.
    • (1962) Nature , vol.192 , pp. 366-367
    • Tauc, L.1    Gerschenfeld, H.M.2
  • 22
    • 0342514050 scopus 로고
    • The effect of anion injection and changes in the external potassium and chloride concentration on the reversal potentials of the IPSP and acetylcholine
    • Kerkut G.A., Thomas R.C. The effect of anion injection and changes in the external potassium and chloride concentration on the reversal potentials of the IPSP and acetylcholine. Comp Biochem Physiol 1964, 11:199-213.
    • (1964) Comp Biochem Physiol , vol.11 , pp. 199-213
    • Kerkut, G.A.1    Thomas, R.C.2
  • 23
    • 0014221608 scopus 로고
    • Pharmacological characteristics and ionic bases of a 2 component postsynaptic inhibition
    • Kehoe J. Pharmacological characteristics and ionic bases of a 2 component postsynaptic inhibition. Nature 1967, 215:1503-1505.
    • (1967) Nature , vol.215 , pp. 1503-1505
    • Kehoe, J.1
  • 24
    • 0014123580 scopus 로고
    • A study of synaptic transmission in the absence of nerve impulses
    • Katz B., Miledi R. A study of synaptic transmission in the absence of nerve impulses. J Physiol 1967, 192:407-436.
    • (1967) J Physiol , vol.192 , pp. 407-436
    • Katz, B.1    Miledi, R.2
  • 25
    • 0015836898 scopus 로고
    • Transmitter release induced by injection of calcium ions into nerve terminals
    • Miledi R. Transmitter release induced by injection of calcium ions into nerve terminals. Proc R Soc Lond B Biol Sci 1973, 183:421-425.
    • (1973) Proc R Soc Lond B Biol Sci , vol.183 , pp. 421-425
    • Miledi, R.1
  • 26
    • 0015499125 scopus 로고
    • Calcium transient in presynaptic terminal of squid giant synapse: detection with aequorin
    • Llinás R., Blinks J.R., Nicholson C. Calcium transient in presynaptic terminal of squid giant synapse: detection with aequorin. Science 1972, 176:1127-1129.
    • (1972) Science , vol.176 , pp. 1127-1129
    • Llinás, R.1    Blinks, J.R.2    Nicholson, C.3
  • 27
    • 0019350409 scopus 로고
    • Relationship between presynaptic calcium current and postsynaptic potential in squid giant synapse
    • Llinás R., Steinberg I.Z., Walton K. Relationship between presynaptic calcium current and postsynaptic potential in squid giant synapse. Biophys J 1981, 33:323-351.
    • (1981) Biophys J , vol.33 , pp. 323-351
    • Llinás, R.1    Steinberg, I.Z.2    Walton, K.3
  • 28
    • 0025892022 scopus 로고
    • Regulation by synapsin I and Ca(2+)-calmodulin-dependent protein kinase II of the transmitter release in squid giant synapse
    • Llinás R., Gruner J.A., Sugimori M., McGuinness T.L., Greengard P. Regulation by synapsin I and Ca(2+)-calmodulin-dependent protein kinase II of the transmitter release in squid giant synapse. J Physiol 1991, 436:257-282.
    • (1991) J Physiol , vol.436 , pp. 257-282
    • Llinás, R.1    Gruner, J.A.2    Sugimori, M.3    McGuinness, T.L.4    Greengard, P.5
  • 29
    • 0022270911 scopus 로고
    • Calcium entry and transmitter release at voltage-clamped nerve terminals of squid
    • Augustine G.J., Charlton M.P., Smith S.J. Calcium entry and transmitter release at voltage-clamped nerve terminals of squid. J Physiol 1985, 367:163-181.
    • (1985) J Physiol , vol.367 , pp. 163-181
    • Augustine, G.J.1    Charlton, M.P.2    Smith, S.J.3
  • 30
    • 0018084905 scopus 로고
    • Membrane ultrastructure of the giant synapse of the squid Loligo pealei
    • Pumplin D.W., Reese T.S. Membrane ultrastructure of the giant synapse of the squid Loligo pealei. Neuroscience 1978, 3:685-696.
    • (1978) Neuroscience , vol.3 , pp. 685-696
    • Pumplin, D.W.1    Reese, T.S.2
  • 31
    • 0001034893 scopus 로고
    • Intraterminal injection of synapsin I or calcium/calmodulin-dependent protein kinase II alters neurotransmitter release at the squid giant synapse
    • Llinás R., McGuinness T.L., Leonard C.S., Sugimori M., Greengard P. Intraterminal injection of synapsin I or calcium/calmodulin-dependent protein kinase II alters neurotransmitter release at the squid giant synapse. Proc Natl Acad Sci USA 1985, 82:3035-3039.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 3035-3039
    • Llinás, R.1    McGuinness, T.L.2    Leonard, C.S.3    Sugimori, M.4    Greengard, P.5
  • 32
    • 0026399923 scopus 로고
    • The calcium signal for transmitter secretion from presynaptic nerve terminals
    • Augustine G.J., Adler E.M., Charlton M.P. The calcium signal for transmitter secretion from presynaptic nerve terminals. Ann N Y Acad Sci 1991, 635:365-381.
    • (1991) Ann N Y Acad Sci , vol.635 , pp. 365-381
    • Augustine, G.J.1    Adler, E.M.2    Charlton, M.P.3
  • 33
    • 0016318183 scopus 로고
    • Transmission abolished on a cholinergic synapse after injection of acetylcholinesterase into the presynaptic neurone
    • Tauc L., Hoffmann A., Tsuji S., Hinzen D.H., Faille L. Transmission abolished on a cholinergic synapse after injection of acetylcholinesterase into the presynaptic neurone. Nature 1974, 250:496-498.
    • (1974) Nature , vol.250 , pp. 496-498
    • Tauc, L.1    Hoffmann, A.2    Tsuji, S.3    Hinzen, D.H.4    Faille, L.5
  • 34
    • 0023888382 scopus 로고
    • Neurotransmitter release is blocked intracellularly by botulinum neurotoxin, and this requires uptake of both toxin polypeptides by a process mediated by the larger chain
    • Poulain B., Tauc L., Maisey E.A., Wadsworth J.D., Mohan P.M., Dolly J.O. Neurotransmitter release is blocked intracellularly by botulinum neurotoxin, and this requires uptake of both toxin polypeptides by a process mediated by the larger chain. Proc Natl Acad Sci USA 1988, 85:4090-4094.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4090-4094
    • Poulain, B.1    Tauc, L.2    Maisey, E.A.3    Wadsworth, J.D.4    Mohan, P.M.5    Dolly, J.O.6
  • 35
    • 0025054267 scopus 로고
    • Exogenous mRNA encoding tetanus or botulinum neurotoxins expressed in Aplysia neurons
    • Mochida S., Poulain B., Eisel U., Binz T., Kurazono H., Niemann H., et al. Exogenous mRNA encoding tetanus or botulinum neurotoxins expressed in Aplysia neurons. Proc Natl Acad Sci USA 1990, 87:7844-7848.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7844-7848
    • Mochida, S.1    Poulain, B.2    Eisel, U.3    Binz, T.4    Kurazono, H.5    Niemann, H.6
  • 36
    • 0035875679 scopus 로고    scopus 로고
    • Synapsin controls both reserve and releasable synaptic vesicle pools during neuronal activity and short-term plasticity in Aplysia
    • Humeau Y., Doussau F., Vitiello F., Greengard P., Benfenati F., Poulain B. Synapsin controls both reserve and releasable synaptic vesicle pools during neuronal activity and short-term plasticity in Aplysia. J Neurosci 2001, 21:4195-4206.
    • (2001) J Neurosci , vol.21 , pp. 4195-4206
    • Humeau, Y.1    Doussau, F.2    Vitiello, F.3    Greengard, P.4    Benfenati, F.5    Poulain, B.6
  • 37
    • 0019223370 scopus 로고
    • Quantal release of acetylcholine examined by current fl{ligature}release o analysis at an identified neuroneuronal synapse of Aplysia
    • Simonneau M., Tauc L., Baux G. Quantal release of acetylcholine examined by current fl{ligature}release o analysis at an identified neuroneuronal synapse of Aplysia. Proc Natl Acad Sci USA 1980, 77:1661-1665.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1661-1665
    • Simonneau, M.1    Tauc, L.2    Baux, G.3
  • 38
    • 0025147596 scopus 로고
    • Effects of synapsin I and calcium/calmodulin-dependent protein kinase II on spontaneous neurotransmitter release in the squid giant synapse
    • Lin J.W., Sugimori M., Llinas R.R., McGuinness T.L., Greengard P. Effects of synapsin I and calcium/calmodulin-dependent protein kinase II on spontaneous neurotransmitter release in the squid giant synapse. Proc Natl Acad Sci USA 1990, 87:8257-8261.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8257-8261
    • Lin, J.W.1    Sugimori, M.2    Llinas, R.R.3    McGuinness, T.L.4    Greengard, P.5
  • 40
    • 0037107133 scopus 로고    scopus 로고
    • Rac GTPase plays an essential role in exocytosis by controlling the fusion competence of release sites
    • Humeau Y., Popoff M.R., Kojima H., Doussau F., Poulain B. Rac GTPase plays an essential role in exocytosis by controlling the fusion competence of release sites. J Neurosci 2002, 22:968-7981.
    • (2002) J Neurosci , vol.22 , pp. 968-7981
    • Humeau, Y.1    Popoff, M.R.2    Kojima, H.3    Doussau, F.4    Poulain, B.5
  • 41
    • 0027154822 scopus 로고
    • CAMP and arachidonic acid simulate long-term structural and functional changes produced by neurotransmitters in Aplysia sensory neurons
    • Schacher S., Kandel E.R., Montarolo P. cAMP and arachidonic acid simulate long-term structural and functional changes produced by neurotransmitters in Aplysia sensory neurons. Neuron 1993, 10:1079-1088.
    • (1993) Neuron , vol.10 , pp. 1079-1088
    • Schacher, S.1    Kandel, E.R.2    Montarolo, P.3
  • 42
    • 0030450555 scopus 로고    scopus 로고
    • Synapsin-like molecules in Aplysia punctata and Helix pomatia: identification and distribution in the nervous system and during the formation of synaptic contacts in vitro
    • Cibelli G., Ghirardi M., Onofri F., Casadio A., Benfenati F., Montarolo P.G., et al. Synapsin-like molecules in Aplysia punctata and Helix pomatia: identification and distribution in the nervous system and during the formation of synaptic contacts in vitro. Eur J Neurosci 1996, 8:2530-2543.
    • (1996) Eur J Neurosci , vol.8 , pp. 2530-2543
    • Cibelli, G.1    Ghirardi, M.2    Onofri, F.3    Casadio, A.4    Benfenati, F.5    Montarolo, P.G.6
  • 43
    • 35548955013 scopus 로고    scopus 로고
    • Phosphorylation of synapsin domain A is required for post-tetanic potentiation
    • Fiumara F., Milanese C., Corradi A., Giovedì S., Leitinger G., Menegon A., et al. Phosphorylation of synapsin domain A is required for post-tetanic potentiation. J Cell Sci 2007, 120:3228-3237.
    • (2007) J Cell Sci , vol.120 , pp. 3228-3237
    • Fiumara, F.1    Milanese, C.2    Corradi, A.3    Giovedì, S.4    Leitinger, G.5    Menegon, A.6
  • 44
    • 77951172177 scopus 로고    scopus 로고
    • MAPK/Erk-dependent phosphorylation of synapsin mediates formation of functional synapses and short-term homosynaptic plasticity
    • Giachello C.N., Fiumara F., Giacomini C., Corradi A., Milanese C., Ghirardi, et al. MAPK/Erk-dependent phosphorylation of synapsin mediates formation of functional synapses and short-term homosynaptic plasticity. J Cell Sci 2010, 123:881-893.
    • (2010) J Cell Sci , vol.123 , pp. 881-893
    • Giachello, C.N.1    Fiumara, F.2    Giacomini, C.3    Corradi, A.4    Milanese, C.5    Ghirardi6
  • 45
    • 0024461324 scopus 로고
    • Synapsins: mosaics of shared and individual domains in a family of synaptic vesicle phosphoproteins
    • Südhof T.C., Czernik A.J., Kao H.T., Takei K., Johnston P.A., Horiuchi A., et al. Synapsins: mosaics of shared and individual domains in a family of synaptic vesicle phosphoproteins. Science 1989, 245:1474-1480.
    • (1989) Science , vol.245 , pp. 1474-1480
    • Südhof, T.C.1    Czernik, A.J.2    Kao, H.T.3    Takei, K.4    Johnston, P.A.5    Horiuchi, A.6
  • 46
    • 0344285992 scopus 로고    scopus 로고
    • Characterization of transcripts from the synapsin III gene locus
    • Porton B., Kao H.T., Greengard P. Characterization of transcripts from the synapsin III gene locus. J Neurochem 1999, 73:2266-2271.
    • (1999) J Neurochem , vol.73 , pp. 2266-2271
    • Porton, B.1    Kao, H.T.2    Greengard, P.3
  • 48
    • 0037384351 scopus 로고    scopus 로고
    • Duplication, degeneration and subfunctionalization of the nested synapsin-Timp genes in Fugu
    • Yu W.P., Brenner S., Venkatesh B. Duplication, degeneration and subfunctionalization of the nested synapsin-Timp genes in Fugu. Trends Genet 2003, 19:180-183.
    • (2003) Trends Genet , vol.19 , pp. 180-183
    • Yu, W.P.1    Brenner, S.2    Venkatesh, B.3
  • 51
    • 0036662770 scopus 로고    scopus 로고
    • Byrne, Serotonin stimulates phosphorylation of Aplysia synapsin and alters its subcellular distribution in sensory neurons
    • Angers D., Fioravante J., Chin L.J., Cleary A.J., Bean J.H. Byrne, Serotonin stimulates phosphorylation of Aplysia synapsin and alters its subcellular distribution in sensory neurons. J Neurosci 2002, 22:5412-5422.
    • (2002) J Neurosci , vol.22 , pp. 5412-5422
    • Angers, D.1    Fioravante, J.2    Chin, L.J.3    Cleary, A.J.4    Bean, J.H.5
  • 53
    • 0011628863 scopus 로고
    • Amino acid sequences surrounding the cAMP-dependent and calcium/calmodulin-dependent phosphorylation sites in rat and bovine synapsin I
    • Czernik A.J., Pang D.T., Greengard P. Amino acid sequences surrounding the cAMP-dependent and calcium/calmodulin-dependent phosphorylation sites in rat and bovine synapsin I. Proc Natl Acad Sci USA 1987, 84:7518-7522.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7518-7522
    • Czernik, A.J.1    Pang, D.T.2    Greengard, P.3
  • 54
    • 0029869763 scopus 로고    scopus 로고
    • Neurotrophins stimulate phosphorylation of synapsin I by MAP kinase and regulate synapsin I-actin interactions
    • Jovanovic J.N., Benfenati F., Siow Y.L., Sihra T.S., Sanghera J.S., Pelech S.L., et al. Neurotrophins stimulate phosphorylation of synapsin I by MAP kinase and regulate synapsin I-actin interactions. Proc Natl Acad Sci USA 1996, 93:3679-3683.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3679-3683
    • Jovanovic, J.N.1    Benfenati, F.2    Siow, Y.L.3    Sihra, T.S.4    Sanghera, J.S.5    Pelech, S.L.6
  • 55
    • 0029829890 scopus 로고    scopus 로고
    • Site-specific phosphorylation of synapsin I bymitogen-activated protein kinase and Cdk5 and its effects on physiological functions
    • Matsubara M., Kusubata M., Ishiguro K., Uchida T., Titani K., Taniguchi H. Site-specific phosphorylation of synapsin I bymitogen-activated protein kinase and Cdk5 and its effects on physiological functions. J Biol Chem 1996, 271:21108-21113.
    • (1996) J Biol Chem , vol.271 , pp. 21108-21113
    • Matsubara, M.1    Kusubata, M.2    Ishiguro, K.3    Uchida, T.4    Titani, K.5    Taniguchi, H.6
  • 56
    • 34447550744 scopus 로고    scopus 로고
    • Synapsin phosphorylation by SRC tyrosine kinase enhances SRC activity in synaptic vesicles
    • Onofri F., Messa M., Matafora V., Bonanno G., Corradi A., Bachi A., et al. Synapsin phosphorylation by SRC tyrosine kinase enhances SRC activity in synaptic vesicles. J Biol Chem 2007, 282:15754-15767.
    • (2007) J Biol Chem , vol.282 , pp. 15754-15767
    • Onofri, F.1    Messa, M.2    Matafora, V.3    Bonanno, G.4    Corradi, A.5    Bachi, A.6
  • 57
    • 0141920783 scopus 로고    scopus 로고
    • New aspects of neurotransmitter release and exocytosis: dynamic and differential regulation of synapsin I phosphorylation by acute neuronal excitation in vivo
    • Yamagata Y. New aspects of neurotransmitter release and exocytosis: dynamic and differential regulation of synapsin I phosphorylation by acute neuronal excitation in vivo. J Pharmacol Sci 2003, 93:22-29.
    • (2003) J Pharmacol Sci , vol.93 , pp. 22-29
    • Yamagata, Y.1
  • 58
    • 72449147303 scopus 로고    scopus 로고
    • Cytoplasmic ATM in neurons modulates synaptic function
    • Li J., Han Y.R., Plummer M.R., Herrup K. Cytoplasmic ATM in neurons modulates synaptic function. Curr Biol 2009, 19:2091-2096.
    • (2009) Curr Biol , vol.19 , pp. 2091-2096
    • Li, J.1    Han, Y.R.2    Plummer, M.R.3    Herrup, K.4
  • 59
    • 0023201681 scopus 로고
    • Synapsin I bundles F-actin in a phosphorylation dependent manner
    • Bähler M., Greengard P. Synapsin I bundles F-actin in a phosphorylation dependent manner. Nature 1987, 326:704-707.
    • (1987) Nature , vol.326 , pp. 704-707
    • Bähler, M.1    Greengard, P.2
  • 60
    • 0031428043 scopus 로고    scopus 로고
    • Phosphorylation-dependent effects of synapsin IIa on actin polymerization and network formation
    • Nielander H.B., Onofri F., Schaeffer E., Menegon A., Fesce R., Valtorta F., et al. Phosphorylation-dependent effects of synapsin IIa on actin polymerization and network formation. Eur J Neurosci 1997, 9:2712-2722.
    • (1997) Eur J Neurosci , vol.9 , pp. 2712-2722
    • Nielander, H.B.1    Onofri, F.2    Schaeffer, E.3    Menegon, A.4    Fesce, R.5    Valtorta, F.6
  • 61
    • 0040964284 scopus 로고    scopus 로고
    • Homo- and heterodimerization of synapsins
    • Hosaka M., Sudhof T.C. Homo- and heterodimerization of synapsins. J Biol Chem 1999, 274:16747-16753.
    • (1999) J Biol Chem , vol.274 , pp. 16747-16753
    • Hosaka, M.1    Sudhof, T.C.2
  • 62
    • 0030729884 scopus 로고    scopus 로고
    • Kinetic analysis of the phosphorylation-dependent interactions of synapsin I with rat brain synaptic vesicles
    • Stefani G., Onofri F., Valtorta F., Vaccaro P., Greengard P., Benfenati F. Kinetic analysis of the phosphorylation-dependent interactions of synapsin I with rat brain synaptic vesicles. J Physiol 1997, 504:501-515.
    • (1997) J Physiol , vol.504 , pp. 501-515
    • Stefani, G.1    Onofri, F.2    Valtorta, F.3    Vaccaro, P.4    Greengard, P.5    Benfenati, F.6
  • 63
    • 0036236748 scopus 로고    scopus 로고
    • A protein kinase A-dependent molecular switch in synapsins regulates neurite outgrowth
    • Kao H.T., Song H.J., Porton B., Ming G.L., Hoh J., Abraham M., et al. A protein kinase A-dependent molecular switch in synapsins regulates neurite outgrowth. Nat Neurosci 2002, 5:431-437.
    • (2002) Nat Neurosci , vol.5 , pp. 431-437
    • Kao, H.T.1    Song, H.J.2    Porton, B.3    Ming, G.L.4    Hoh, J.5    Abraham, M.6
  • 64
    • 23744437313 scopus 로고    scopus 로고
    • Phosphorylation of synapsin I by cAMP-dependent protein kinase controls synaptic vesicle dynamics in developing neurons
    • Bonanomi D., Menegon A., Miccio A., Ferrari G., Corradi A., Kao H.T. Phosphorylation of synapsin I by cAMP-dependent protein kinase controls synaptic vesicle dynamics in developing neurons. J Neurosci 2005, 25:7299-7308.
    • (2005) J Neurosci , vol.25 , pp. 7299-7308
    • Bonanomi, D.1    Menegon, A.2    Miccio, A.3    Ferrari, G.4    Corradi, A.5    Kao, H.T.6
  • 65
    • 0035836492 scopus 로고    scopus 로고
    • Intracellular injection of synapsin I induces neurotransmitter release in C1 neurons of Helix pomatia contacting a wrong target
    • Fiumara F., Onofri F., Benfenati F., Montarolo P.G., Ghirardi M. Intracellular injection of synapsin I induces neurotransmitter release in C1 neurons of Helix pomatia contacting a wrong target. Neuroscience 2001, 104:271-280.
    • (2001) Neuroscience , vol.104 , pp. 271-280
    • Fiumara, F.1    Onofri, F.2    Benfenati, F.3    Montarolo, P.G.4    Ghirardi, M.5
  • 67
    • 0024506756 scopus 로고
    • Interactions of synapsin I with small synaptic vesicles: distinct sites in synapsin I bind to vesicle phospholipids and vesicle proteins
    • Benfenati F., Bahler M., Jahn R., Greengard P. Interactions of synapsin I with small synaptic vesicles: distinct sites in synapsin I bind to vesicle phospholipids and vesicle proteins. J CeU Bid 1989, 108:1863-1872.
    • (1989) J CeU Bid , vol.108 , pp. 1863-1872
    • Benfenati, F.1    Bahler, M.2    Jahn, R.3    Greengard, P.4
  • 70
    • 77954202334 scopus 로고    scopus 로고
    • The synapsins: key actors of synapse function and plasticity
    • Cesca F., Baldelli P., Valtorta F., Benfenati F. The synapsins: key actors of synapse function and plasticity. Prog Neurobiol 2010, 91:313-348.
    • (2010) Prog Neurobiol , vol.91 , pp. 313-348
    • Cesca, F.1    Baldelli, P.2    Valtorta, F.3    Benfenati, F.4
  • 71
    • 58149456669 scopus 로고    scopus 로고
    • Synapsin-dependent development of glutamatergic synaptic vesicles and presynaptic plasticity in postnatal mouse brain
    • Bogen I.L., Jensen V., Hvalby O., Walaas S.I. Synapsin-dependent development of glutamatergic synaptic vesicles and presynaptic plasticity in postnatal mouse brain. Neuroscience 2009, 158:231-241.
    • (2009) Neuroscience , vol.158 , pp. 231-241
    • Bogen, I.L.1    Jensen, V.2    Hvalby, O.3    Walaas, S.I.4
  • 72
    • 0028316929 scopus 로고
    • Synapsin IIa accelerates functional development of neuromuscular synapses
    • Schaeffer E., Alder J., Greengard P., Poo M.M. Synapsin IIa accelerates functional development of neuromuscular synapses. Proc Natl Acad Sci USA 1994, 91:3882-3886.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3882-3886
    • Schaeffer, E.1    Alder, J.2    Greengard, P.3    Poo, M.M.4
  • 73
    • 0028895773 scopus 로고
    • Accelerated structural maturation induced by synapsin I at developing neuromuscular synapses of Xenopus laevis
    • Valtorta F., Iezzi N., Benfenati F., Lu B., Poo M.M., Greengard P. Accelerated structural maturation induced by synapsin I at developing neuromuscular synapses of Xenopus laevis. Eur J Neurosci 1995, 7:261-270.
    • (1995) Eur J Neurosci , vol.7 , pp. 261-270
    • Valtorta, F.1    Iezzi, N.2    Benfenati, F.3    Lu, B.4    Poo, M.M.5    Greengard, P.6
  • 74
    • 0030271819 scopus 로고    scopus 로고
    • Expression of synapsin I correlates with maturation of the neuromuscular synapse
    • Lu B., Czernik A.J., Popov S., Wang T., Poo M.M., Greengard P. Expression of synapsin I correlates with maturation of the neuromuscular synapse. Neuroscience 1996, 74:1087-1097.
    • (1996) Neuroscience , vol.74 , pp. 1087-1097
    • Lu, B.1    Czernik, A.J.2    Popov, S.3    Wang, T.4    Poo, M.M.5    Greengard, P.6
  • 75
    • 0034657169 scopus 로고    scopus 로고
    • Synapsin III: developmental expression, subcellular localization, and role in axon formation
    • Ferreira A., Kao H.T., Feng J., Rapoport M., Greengard P. Synapsin III: developmental expression, subcellular localization, and role in axon formation. J Neurosci 2000, 20:3736-3744.
    • (2000) J Neurosci , vol.20 , pp. 3736-3744
    • Ferreira, A.1    Kao, H.T.2    Feng, J.3    Rapoport, M.4    Greengard, P.5
  • 76
    • 2542565848 scopus 로고    scopus 로고
    • Inhibition of neurotransmitter release by a nonphysiological target requires protein synthesis and involves cAMP-dependent and mitogen-activated protein kinases
    • Ghirardi M., Benfenati F., Giovedì S., Fiumara F., Milanese C., Montarolo P.G. Inhibition of neurotransmitter release by a nonphysiological target requires protein synthesis and involves cAMP-dependent and mitogen-activated protein kinases. J Neurosci 2004 May 26, 24(21):5054-5062.
    • (2004) J Neurosci , vol.24 , Issue.21 , pp. 5054-5062
    • Ghirardi, M.1    Benfenati, F.2    Giovedì, S.3    Fiumara, F.4    Milanese, C.5    Montarolo, P.G.6
  • 77
    • 0034014953 scopus 로고    scopus 로고
    • Influence of the target on distribution and functioning of the varicosities of Helix pomatia metacerebral cell C1 in dissociated cell culture
    • Ghirardi M., Casadio A., Naretto G., Levi R., Montarolo P.G. Influence of the target on distribution and functioning of the varicosities of Helix pomatia metacerebral cell C1 in dissociated cell culture. Neuroscience 2000, 96:843-853.
    • (2000) Neuroscience , vol.96 , pp. 843-853
    • Ghirardi, M.1    Casadio, A.2    Naretto, G.3    Levi, R.4    Montarolo, P.G.5
  • 78
    • 8744285529 scopus 로고    scopus 로고
    • Phosphorylation by cAMP-dependent protein kinase is essential for synapsin-induced enhancement of neurotransmitter release in invertebrate neurons
    • Fiumara F., Giovedi S., Menegon A., Milanese C., Merlo D., Montarolo P.G. Phosphorylation by cAMP-dependent protein kinase is essential for synapsin-induced enhancement of neurotransmitter release in invertebrate neurons. J Cell Sci 2004, 117:5145-5154.
    • (2004) J Cell Sci , vol.117 , pp. 5145-5154
    • Fiumara, F.1    Giovedi, S.2    Menegon, A.3    Milanese, C.4    Merlo, D.5    Montarolo, P.G.6
  • 79
    • 0019379357 scopus 로고
    • Serotonin stimulates phosphorylation of protein I in the facial motor nucleus of rat brain
    • Dolphin A.C., Greengard P. Serotonin stimulates phosphorylation of protein I in the facial motor nucleus of rat brain. Nature 1981, 289:76-79.
    • (1981) Nature , vol.289 , pp. 76-79
    • Dolphin, A.C.1    Greengard, P.2
  • 80
    • 0024818015 scopus 로고
    • Phosphorylation-dependent inhibition by synapsin I of organelle movement in squid axoplasm
    • McGuinness T.L., Brady S.T., Gruner J.A., Sugimori M., Llinas R., Greengard P. Phosphorylation-dependent inhibition by synapsin I of organelle movement in squid axoplasm. J Neurosci 1989, 9:4138-4149.
    • (1989) J Neurosci , vol.9 , pp. 4138-4149
    • McGuinness, T.L.1    Brady, S.T.2    Gruner, J.A.3    Sugimori, M.4    Llinas, R.5    Greengard, P.6
  • 81
    • 37549071860 scopus 로고    scopus 로고
    • Synapsin regulates basal synaptic strength, synaptic depression, and serotonin-induced facilitation of sensorimotor synapses in Aplysia
    • Fioravante D., Liu R.Y., Netek A.K., Cleary L.J., Byrne J.H. Synapsin regulates basal synaptic strength, synaptic depression, and serotonin-induced facilitation of sensorimotor synapses in Aplysia. J Neurophysiol 2007, 98:3568-3580.
    • (2007) J Neurophysiol , vol.98 , pp. 3568-3580
    • Fioravante, D.1    Liu, R.Y.2    Netek, A.K.3    Cleary, L.J.4    Byrne, J.H.5
  • 82
    • 0011704440 scopus 로고    scopus 로고
    • MAPK is involved in serotonin-induced short-term facilitation of Aplysia sensorimotor synapses
    • Phares G.A., Byrne J.H. MAPK is involved in serotonin-induced short-term facilitation of Aplysia sensorimotor synapses. Soc Neurosci Abstr 2001, 27:1703.
    • (2001) Soc Neurosci Abstr , vol.27 , pp. 1703
    • Phares, G.A.1    Byrne, J.H.2
  • 83
    • 0036582966 scopus 로고    scopus 로고
    • Transforming growth factor beta1 alters synapsin distribution and modulates synaptic depression in Aplysia
    • Chin J., Angers A., Cleary L.J., Eskin A., Byrne J.H. Transforming growth factor beta1 alters synapsin distribution and modulates synaptic depression in Aplysia. J Neurosci 2002, 22:RC220.
    • (2002) J Neurosci , vol.22
    • Chin, J.1    Angers, A.2    Cleary, L.J.3    Eskin, A.4    Byrne, J.H.5
  • 85
    • 0027050487 scopus 로고
    • Synapsin I partially dissociates from synaptic vesicles during exocytosis induced by electrical stimulation
    • Torri Tarelli F., Bossi M., Fesce R., Greengard P., Valtorta F. Synapsin I partially dissociates from synaptic vesicles during exocytosis induced by electrical stimulation. Neuron 1992, 9:1143-1153.
    • (1992) Neuron , vol.9 , pp. 1143-1153
    • Torri Tarelli, F.1    Bossi, M.2    Fesce, R.3    Greengard, P.4    Valtorta, F.5
  • 87
    • 0034651107 scopus 로고    scopus 로고
    • Switching off and on of synaptic sites at Aplysia sensorimotor synapses
    • Royer S., Coulson R.L., Klein M. Switching off and on of synaptic sites at Aplysia sensorimotor synapses. J Neurosci 2000, 20:626-638.
    • (2000) J Neurosci , vol.20 , pp. 626-638
    • Royer, S.1    Coulson, R.L.2    Klein, M.3
  • 88
    • 0036522973 scopus 로고    scopus 로고
    • Persistent, exocytosis-independent silencing of release sites underlies homosynaptic depression at sensory synapses in Aplysia
    • Gover T.D., Jiang X.Y., Abrams T.W. Persistent, exocytosis-independent silencing of release sites underlies homosynaptic depression at sensory synapses in Aplysia. J Neurosci 2002, 22:1942-1955.
    • (2002) J Neurosci , vol.22 , pp. 1942-1955
    • Gover, T.D.1    Jiang, X.Y.2    Abrams, T.W.3
  • 89
    • 78650039263 scopus 로고    scopus 로고
    • A novel form of presynaptic plasticity based on the fast reactivation of release sites switched off during low-frequency depression
    • Doussau F., Humeau Y., Benfenati F., Poulain B. A novel form of presynaptic plasticity based on the fast reactivation of release sites switched off during low-frequency depression. J Neurosci 2010, 30:16679-16691.
    • (2010) J Neurosci , vol.30 , pp. 16679-16691
    • Doussau, F.1    Humeau, Y.2    Benfenati, F.3    Poulain, B.4
  • 90
    • 33745776535 scopus 로고    scopus 로고
    • Physiological activity depresses synaptic function through an effect on vesicle priming
    • Moulder K.L., Jiang X., Taylor A.A., Olney J.W., Mennerick S. Physiological activity depresses synaptic function through an effect on vesicle priming. J Neurosci 2006, 26:6618-6626.
    • (2006) J Neurosci , vol.26 , pp. 6618-6626
    • Moulder, K.L.1    Jiang, X.2    Taylor, A.A.3    Olney, J.W.4    Mennerick, S.5
  • 91
    • 34548810343 scopus 로고    scopus 로고
    • Fast changes in the functional status of release sites during short-term plasticity: involvement of a frequency-dependent bypass of Rac at Aplysia synapses
    • Humeau Y., Doussau F., Popoff M.R., Benfenati F., Poulain B. Fast changes in the functional status of release sites during short-term plasticity: involvement of a frequency-dependent bypass of Rac at Aplysia synapses. J Physiol 2007, 583:983-1004.
    • (2007) J Physiol , vol.583 , pp. 983-1004
    • Humeau, Y.1    Doussau, F.2    Popoff, M.R.3    Benfenati, F.4    Poulain, B.5
  • 92
    • 0035865411 scopus 로고    scopus 로고
    • Tonically active protein kinase A regulates neurotransmitter release at the squid giant synapse
    • Hilfiker S., Czernik A.J., Greengard P., Augustine G.J. Tonically active protein kinase A regulates neurotransmitter release at the squid giant synapse. J Physiol 2001, 531:141-146.
    • (2001) J Physiol , vol.531 , pp. 141-146
    • Hilfiker, S.1    Czernik, A.J.2    Greengard, P.3    Augustine, G.J.4
  • 93
    • 0031050921 scopus 로고    scopus 로고
    • Multiple overlapping processes underlying short-term synaptic enhancement
    • Review
    • Fisher S.A., Fischer T.M., Carew T.J. Multiple overlapping processes underlying short-term synaptic enhancement. Trends Neurosci 1997, 170-177. Review.
    • (1997) Trends Neurosci , pp. 170-177
    • Fisher, S.A.1    Fischer, T.M.2    Carew, T.J.3
  • 94
    • 0036201201 scopus 로고    scopus 로고
    • Short-term synaptic plasticity
    • Zucker R.S., Regehr W.G. Short-term synaptic plasticity. Annu Rev Physiol 2002, 64:355-405.
    • (2002) Annu Rev Physiol , vol.64 , pp. 355-405
    • Zucker, R.S.1    Regehr, W.G.2
  • 95
    • 7244229524 scopus 로고    scopus 로고
    • Synaptic computation
    • Abbott L.F., Regehr W.G. Synaptic computation. Nature 2004, 431:796-803.
    • (2004) Nature , vol.431 , pp. 796-803
    • Abbott, L.F.1    Regehr, W.G.2
  • 96
    • 0036821729 scopus 로고    scopus 로고
    • Ingestion motor programs of Aplysia are modulated by short-term synaptic enhancement in cerebral-buccal interneuron pathways
    • Sánchez J.A., Kirk M.D. Ingestion motor programs of Aplysia are modulated by short-term synaptic enhancement in cerebral-buccal interneuron pathways. Invert Neurosci 2002, 4:199-212.
    • (2002) Invert Neurosci , vol.4 , pp. 199-212
    • Sánchez, J.A.1    Kirk, M.D.2
  • 98
    • 0027402975 scopus 로고
    • Synaptic vesicle phosphoproteins and regulation of synaptic function
    • Greengard P., Valtorta F., Czernik A.J. Synaptic vesicle phosphoproteins and regulation of synaptic function. Science 1993, 259:780-785.
    • (1993) Science , vol.259 , pp. 780-785
    • Greengard, P.1    Valtorta, F.2    Czernik, A.J.3
  • 99
    • 0029024135 scopus 로고
    • Essential functions of synapsin I and II in synaptic vesicles regulation
    • Rosahl T.W., Spillane D., Missler M., Herz J., Seling O.K., Wolff J.R., et al. Essential functions of synapsin I and II in synaptic vesicles regulation. Nature 1995, 375:488-493.
    • (1995) Nature , vol.375 , pp. 488-493
    • Rosahl, T.W.1    Spillane, D.2    Missler, M.3    Herz, J.4    Seling, O.K.5    Wolff, J.R.6
  • 100
    • 33744990393 scopus 로고    scopus 로고
    • Synapsin utilization differs among functional classes of synapses on thalamocortical cells
    • Kielland A., Erisir A., Walaas S.I., Heggelund P. Synapsin utilization differs among functional classes of synapses on thalamocortical cells. J Neurosci 2006, 26:5786-5793.
    • (2006) J Neurosci , vol.26 , pp. 5786-5793
    • Kielland, A.1    Erisir, A.2    Walaas, S.I.3    Heggelund, P.4
  • 101
    • 0034121745 scopus 로고    scopus 로고
    • How botulinum and tetanus toxins block neurotransmitter release
    • Humeau Y., Doussau F., Grant N., Poulain B. How botulinum and tetanus toxins block neurotransmitter release. Biochimie 2000, 46:427-446.
    • (2000) Biochimie , vol.46 , pp. 427-446
    • Humeau, Y.1    Doussau, F.2    Grant, N.3    Poulain, B.4
  • 102
    • 67649292434 scopus 로고    scopus 로고
    • How do the botulinum neurotoxins block neurotransmitter release: from botulism to the molecular mechanism of action
    • Poulain B., Popoff M.R., Molgo J. How do the botulinum neurotoxins block neurotransmitter release: from botulism to the molecular mechanism of action. Botulinum J 2008, 1:14-87.
    • (2008) Botulinum J , vol.1 , pp. 14-87
    • Poulain, B.1    Popoff, M.R.2    Molgo, J.3
  • 103
    • 0026655015 scopus 로고
    • Tetanus toxin potently stimulates tissue transglutaminase. A possible mechanism of neurotoxicity
    • Facchiano F., Luini A. Tetanus toxin potently stimulates tissue transglutaminase. A possible mechanism of neurotoxicity. J Biol Chem 1992, 267:13267-13271.
    • (1992) J Biol Chem , vol.267 , pp. 13267-13271
    • Facchiano, F.1    Luini, A.2
  • 104
    • 0027480066 scopus 로고
    • Covalent modification of synapsin I by a tetanus toxin-activated transglutaminase
    • Facchiano F., Benfenati F., Valtorta F., Luini A. Covalent modification of synapsin I by a tetanus toxin-activated transglutaminase. J Biol Chem 1993, 268:4588-4591.
    • (1993) J Biol Chem , vol.268 , pp. 4588-4591
    • Facchiano, F.1    Benfenati, F.2    Valtorta, F.3    Luini, A.4
  • 105
    • 77953621824 scopus 로고    scopus 로고
    • Transglutaminase participates in the blockade of neurotransmitter release by tetanus toxin: evidence for a novel biological function
    • Facchiano F., Deloye F., Doussau F., Innamorati G., Ashton A.C., Dolly J.O. Transglutaminase participates in the blockade of neurotransmitter release by tetanus toxin: evidence for a novel biological function. Amino Acids 2010, 39:257-269.
    • (2010) Amino Acids , vol.39 , pp. 257-269
    • Facchiano, F.1    Deloye, F.2    Doussau, F.3    Innamorati, G.4    Ashton, A.C.5    Dolly, J.O.6
  • 106
    • 0036804796 scopus 로고    scopus 로고
    • Transglutaminase 2: an enigmatic enzyme with diverse functions
    • Fesus L., Piacentini M. Transglutaminase 2: an enigmatic enzyme with diverse functions. Trends Biochem Sci 2002, 27:534-539.
    • (2002) Trends Biochem Sci , vol.27 , pp. 534-539
    • Fesus, L.1    Piacentini, M.2


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