메뉴 건너뛰기




Volumn 73, Issue 6, 2003, Pages 853-864

Caspase activity is essential for long-term potentiation

Author keywords

CA1; Caspase 3; Hippocampal slices; Long term potentiation (LTP); Z DEVD FMK

Indexed keywords

BENZYLOXYCARBONYLASPARTYLGLUTAMYLVALYLASPARTYL FLUOROMETHYL KETONE; BENZYLOXYCARBONYLPHENYLALANYLALANYL FLUOROMETHYL KETONE; CASPASE; CASPASE 3 INHIBITOR;

EID: 0042338651     PISSN: 03604012     EISSN: None     Source Type: Journal    
DOI: 10.1002/jnr.10730     Document Type: Article
Times cited : (59)

References (123)
  • 1
    • 0032533481 scopus 로고    scopus 로고
    • Caspase-mediated inhibition of human cytosolic phospholipase A2 during apoptosis
    • Adam-Klages S, Schwandner R, Luschen S, Ussat S, Kreder D, Kronke M. 1998. Caspase-mediated inhibition of human cytosolic phospholipase A2 during apoptosis. J Immunol 161:5687-5694.
    • (1998) J Immunol , vol.161 , pp. 5687-5694
    • Adam-Klages, S.1    Schwandner, R.2    Luschen, S.3    Ussat, S.4    Kreder, D.5    Kronke, M.6
  • 2
    • 0034714485 scopus 로고    scopus 로고
    • Expression and subcellular localization of multifunctional calmodulin-dependent protein kinases-I, -11 and -IV are altered in rat hippocampal CA1 neurons after induction of long-term potentiation
    • Ahmed BY, Yamaguchi F, Tsumura T, Gotoh T, Sugimoto K, Tai Y, Konishi R, Kobayashi R, Tokuda M. 2000. Expression and subcellular localization of multifunctional calmodulin-dependent protein kinases-I, -11 and -IV are altered in rat hippocampal CA1 neurons after induction of long-term potentiation. Neurosci Lett 290:149-153.
    • (2000) Neurosci Lett , vol.290 , pp. 149-153
    • Ahmed, B.Y.1    Yamaguchi, F.2    Tsumura, T.3    Gotoh, T.4    Sugimoto, K.5    Tai, Y.6    Konishi, R.7    Kobayashi, R.8    Tokuda, M.9
  • 3
    • 0032826788 scopus 로고    scopus 로고
    • Combined mechanical trauma and metabolic impairment in vitro induces NMDA receptor-dependent neuronal cell death and caspase-3-dependent apoptosis
    • Allen JW, Knoblach SM, Faden AI. 1999. Combined mechanical trauma and metabolic impairment in vitro induces NMDA receptor-dependent neuronal cell death and caspase-3-dependent apoptosis. FASEB J 13:1875-1882.
    • (1999) FASEB J , vol.13 , pp. 1875-1882
    • Allen, J.W.1    Knoblach, S.M.2    Faden, A.I.3
  • 5
    • 0034674786 scopus 로고    scopus 로고
    • Distinct roles of two intracellular phospholipase A2s in fatty acid release in the cell death pathway. Proteolytic fragment of type IVA cytosolic phospholipase A2alpha inhibits stimulus-induced arachidonate release, whereas that of type VI Ca2+-independent phospholipase A2 augments spontaneous fatty acid release
    • Atsumi G, Murakami M, Kojima K, Hadano A, Tajima M, Kudo I. 2000. Distinct roles of two intracellular phospholipase A2s in fatty acid release in the cell death pathway. Proteolytic fragment of type IVA cytosolic phospholipase A2alpha inhibits stimulus-induced arachidonate release, whereas that of type VI Ca2+-independent phospholipase A2 augments spontaneous fatty acid release. J Biol Chem 275:18248-18258.
    • (2000) J Biol Chem , vol.275 , pp. 18248-18258
    • Atsumi, G.1    Murakami, M.2    Kojima, K.3    Hadano, A.4    Tajima, M.5    Kudo, I.6
  • 6
    • 0027476024 scopus 로고
    • A synaptic model of memory: Long-term potentiation in the hippocampus
    • Bliss TV, Collingridge GL. 1993. A synaptic model of memory: long-term potentiation in the hippocampus. Nature 361:31-39.
    • (1993) Nature , vol.361 , pp. 31-39
    • Bliss, T.V.1    Collingridge, G.L.2
  • 7
    • 0031809062 scopus 로고    scopus 로고
    • Bidirectional modulation of AMPA receptor properties by exogenous phospholipase A2 in the hippocampus
    • Chabot C, Gagne J, Giguere C, Bernard J, Baudry M, Massicotte G. 1998. Bidirectional modulation of AMPA receptor properties by exogenous phospholipase A2 in the hippocampus. Hippocampus 8:299-309.
    • (1998) Hippocampus , vol.8 , pp. 299-309
    • Chabot, C.1    Gagne, J.2    Giguere, C.3    Bernard, J.4    Baudry, M.5    Massicotte, G.6
  • 8
    • 0033179170 scopus 로고    scopus 로고
    • Evidence for caspase-mediated cleavage of AMPA receptor subunits in neuronal apoptosis and Alzheimer's disease
    • Chan SL, Griffin WS, Mattson MP. 1999. Evidence for caspase-mediated cleavage of AMPA receptor subunits in neuronal apoptosis and Alzheimer's disease. J Neurosci Res 57:315-323.
    • (1999) J Neurosci Res , vol.57 , pp. 315-323
    • Chan, S.L.1    Griffin, W.S.2    Mattson, M.P.3
  • 9
    • 0033213973 scopus 로고    scopus 로고
    • Caspase and calpain substrates: Roles in synaptic plasticity and cell Death
    • Chan SL, Mattson MP. 1999. Caspase and calpain substrates: roles in synaptic plasticity and cell Death. J Neurosci Res 58:167-190.
    • (1999) J Neurosci Res , vol.58 , pp. 167-190
    • Chan, S.L.1    Mattson, M.P.2
  • 10
    • 0032124903 scopus 로고    scopus 로고
    • Induction of caspase-3-like protease may mediate delayed neuronal death in the hippocampus after transient cerebral ischemia
    • Chen J, Nagayama T, Jin K, Stetler RA, Zhu RL, Graham SH, Simon RP. 1998. Induction of caspase-3-like protease may mediate delayed neuronal death in the hippocampus after transient cerebral ischemia. J Neurosci 18:4914-4928.
    • (1998) J Neurosci , vol.18 , pp. 4914-4928
    • Chen, J.1    Nagayama, T.2    Jin, K.3    Stetler, R.A.4    Zhu, R.L.5    Graham, S.H.6    Simon, R.P.7
  • 12
    • 0029584577 scopus 로고
    • Interactions between arachidonic acid and metabotropic glutamate receptors in the induction of synaptic potentiation in the rat hippocampal slice
    • Collins DR, Smith RC, Davies SN. 1995. Interactions between arachidonic acid and metabotropic glutamate receptors in the induction of synaptic potentiation in the rat hippocampal slice. Eur J Pharmacol 294:147-154.
    • (1995) Eur J Pharmacol , vol.294 , pp. 147-154
    • Collins, D.R.1    Smith, R.C.2    Davies, S.N.3
  • 13
    • 0034699033 scopus 로고    scopus 로고
    • Caspase activity plays an essential role in long-term memory
    • Dash PK, Blum S, Moore AN. 2000. Caspase activity plays an essential role in long-term memory. Neuroreport 11:2811-2816.
    • (2000) Neuroreport , vol.11 , pp. 2811-2816
    • Dash, P.K.1    Blum, S.2    Moore, A.N.3
  • 14
    • 0033784099 scopus 로고    scopus 로고
    • Modeling Alzheimer's disease in transgenic mice: Effect of age and of presenilin 1 on amyloid biochemistry and pathology in APP/London mice
    • Dewachter I, van Dorpe J, Spittaels K, Tesseur I, Van Den Haute C, Moechars D, Van Leuven F. 2000. Modeling Alzheimer's disease in transgenic mice: effect of age and of presenilin 1 on amyloid biochemistry and pathology in APP/London mice. Exp Gerontol 35:831-841.
    • (2000) Exp Gerontol , vol.35 , pp. 831-841
    • Dewachter, I.1    Van Dorpe, J.2    Spittaels, K.3    Tesseur, I.4    Van Den Haute, C.5    Moechars, D.6    Van Leuven, F.7
  • 16
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • Earnshaw WC, Martins LM, Kaufmann SH. 1999. Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu Rev Biochem 68:383-424.
    • (1999) Annu Rev Biochem , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 17
    • 0033908043 scopus 로고    scopus 로고
    • The most unkindest cut of all: On the multiple roles of mammalian caspases
    • Fadeel B, Orrenius S, Zhivotovsky B. 2000. The most unkindest cut of all: on the multiple roles of mammalian caspases. Leukemia 14:1514-1525.
    • (2000) Leukemia , vol.14 , pp. 1514-1525
    • Fadeel, B.1    Orrenius, S.2    Zhivotovsky, B.3
  • 20
    • 0034617378 scopus 로고    scopus 로고
    • Similar levels of long-term potentiation in amyloid precursor protein -null and wild-type mice in the CA1 region of picrotoxin treated slices
    • Fitzjohn SM, Morton RA, Kuenzi F, Davies CH, Seabrook GR, Collingridge GL. 2000. Similar levels of long-term potentiation in amyloid precursor protein -null and wild-type mice in the CA1 region of picrotoxin treated slices. Neurosci Lett 288:9-12.
    • (2000) Neurosci Lett , vol.288 , pp. 9-12
    • Fitzjohn, S.M.1    Morton, R.A.2    Kuenzi, F.3    Davies, C.H.4    Seabrook, G.R.5    Collingridge, G.L.6
  • 21
    • 0033574277 scopus 로고    scopus 로고
    • Cleavage of zetaPKC but not lambda/iota PKC by caspase-3 during UV-induced apoptosis
    • Frutos S, Moscat J, Diaz-Meco MT. 1999. Cleavage of zetaPKC but not lambda/iota PKC by caspase-3 during UV-induced apoptosis. J Biol Chem 274:10765-10770.
    • (1999) J Biol Chem , vol.274 , pp. 10765-10770
    • Frutos, S.1    Moscat, J.2    Diaz-Meco, M.T.3
  • 22
    • 0033785307 scopus 로고    scopus 로고
    • Synaptic plasticity in hippocampal CA1 neurons of mice lacking type 1 inositol-1,4,5-trisphosphate receptors
    • Fujii S, Matsumoto M, Igarashi K, Kato H, Mikoshiba K. 2000. Synaptic plasticity in hippocampal CA1 neurons of mice lacking type 1 inositol-1,4,5-trisphosphate receptors. Learn Mem 7:312-320.
    • (2000) Learn Mem , vol.7 , pp. 312-320
    • Fujii, S.1    Matsumoto, M.2    Igarashi, K.3    Kato, H.4    Mikoshiba, K.5
  • 23
    • 0035073945 scopus 로고    scopus 로고
    • Docosahexaenoic acid improves long-term potentiation attenuated by phospholipase A(2) inhibitor in rat hippocampal slices
    • Fujita S, Ikegaya Y, Nishikawa M, Nishiyama N, Matsuki N. 2001. Docosahexaenoic acid improves long-term potentiation attenuated by phospholipase A(2) inhibitor in rat hippocampal slices. Br J Pharmacol 132:1417-1422.
    • (2001) Br J Pharmacol , vol.132 , pp. 1417-1422
    • Fujita, S.1    Ikegaya, Y.2    Nishikawa, M.3    Nishiyama, N.4    Matsuki, N.5
  • 25
    • 0032479435 scopus 로고    scopus 로고
    • Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide
    • Gervais FG, Thornberry NA, Ruffolo SC, Nicholson DW, Roy S. 1998. Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide. J Biol Chem 273:17102-17108.
    • (1998) J Biol Chem , vol.273 , pp. 17102-17108
    • Gervais, F.G.1    Thornberry, N.A.2    Ruffolo, S.C.3    Nicholson, D.W.4    Roy, S.5
  • 26
    • 0042831025 scopus 로고    scopus 로고
    • Do apoptotic mechanisms regulate synaptic plasticity and growth-cone motility?
    • Gilman CP, Mattson MP. 2002. Do apoptotic mechanisms regulate synaptic plasticity and growth-cone motility? Neuromolecular Med 2:197-214.
    • (2002) Neuromolecular Med , vol.2 , pp. 197-214
    • Gilman, C.P.1    Mattson, M.P.2
  • 27
    • 0034658288 scopus 로고    scopus 로고
    • Caspase-mediated degradation of AMPA receptor subunits: A mechanism for preventing excitotoxic necrosis and ensuring apoptosis
    • Glazner GW, Chan SL, Lu C, Mattson MP. 2000. Caspase-mediated degradation of AMPA receptor subunits: a mechanism for preventing excitotoxic necrosis and ensuring apoptosis. J Neurosci 20:3641-3649.
    • (2000) J Neurosci , vol.20 , pp. 3641-3649
    • Glazner, G.W.1    Chan, S.L.2    Lu, C.3    Mattson, M.P.4
  • 28
    • 0036433355 scopus 로고    scopus 로고
    • Long-term potentiation as a substrate for memory: Evidence from studies of amygdaloid plasticity and Pavlovian fear conditioning
    • Goosens KA, Maren S. 2002. Long-term potentiation as a substrate for memory: evidence from studies of amygdaloid plasticity and Pavlovian fear conditioning. Hippocampus 12:592-599.
    • (2002) Hippocampus , vol.12 , pp. 592-599
    • Goosens, K.A.1    Maren, S.2
  • 29
    • 0027092647 scopus 로고
    • Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice
    • Grant SG, O'Dell TJ, Karl KA, Stein PL, Soriano P, Kandel ER. 1992. Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice. Science 258:1903-1910.
    • (1992) Science , vol.258 , pp. 1903-1910
    • Grant, S.G.1    O'Dell, T.J.2    Karl, K.A.3    Stein, P.L.4    Soriano, P.5    Kandel, E.R.6
  • 30
    • 0035170807 scopus 로고    scopus 로고
    • Hierarchical cleavage of focal adhesion kinase by caspases alters signal transduction during apoptosis of intestinal epithelial cells
    • Grossmann J, Artinger M, Grasso AW, Kung HJ, Scholmerich J, Fiocchi C, Levine AD. 2001. Hierarchical cleavage of focal adhesion kinase by caspases alters signal transduction during apoptosis of intestinal epithelial cells. Gastroenterology 120:79-88.
    • (2001) Gastroenterology , vol.120 , pp. 79-88
    • Grossmann, J.1    Artinger, M.2    Grasso, A.W.3    Kung, H.J.4    Scholmerich, J.5    Fiocchi, C.6    Levine, A.D.7
  • 32
    • 0023765652 scopus 로고
    • Proteolytic processing of human brain alpha spectrin (fodrin): Identification of a hypersensitive site
    • Harris AS, Morrow JS. 1988. Proteolytic processing of human brain alpha spectrin (fodrin): identification of a hypersensitive site. J Neurosci 8:2640-2651.
    • (1988) J Neurosci , vol.8 , pp. 2640-2651
    • Harris, A.S.1    Morrow, J.S.2
  • 33
    • 0033793115 scopus 로고    scopus 로고
    • Degradation of the type I inositol 1,4,5-trisphosphate receptor by caspase-3 in SH-SY5Y neuroblastoma cells undergoing apoptosis
    • Haug LS, Walaas SI, Ostvold AC. 2000. Degradation of the type I inositol 1,4,5-trisphosphate receptor by caspase-3 in SH-SY5Y neuroblastoma cells undergoing apoptosis. J Neurochem 75:1852-1861.
    • (2000) J Neurochem , vol.75 , pp. 1852-1861
    • Haug, L.S.1    Walaas, S.I.2    Ostvold, A.C.3
  • 34
    • 0033607673 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptor type 1 is a substrate for caspase-3 and is cleaved during apoptosis in a caspase-3-dependent manner
    • Hirota J, Furuichi T, Mikoshiba K. 1999. Inositol 1,4,5-trisphosphate receptor type 1 is a substrate for caspase-3 and is cleaved during apoptosis in a caspase-3-dependent manner. J Biol Chem 274:34433-34437.
    • (1999) J Biol Chem , vol.274 , pp. 34433-34437
    • Hirota, J.1    Furuichi, T.2    Mikoshiba, K.3
  • 35
    • 0029799241 scopus 로고    scopus 로고
    • Bidirectional regulation of protein kinase M zeta in the maintenance of long-term potentiation and long-term depression
    • Hrabetova S, Sacktor TC. 1996. Bidirectional regulation of protein kinase M zeta in the maintenance of long-term potentiation and long-term depression. J Neurosci 16:5324-5333.
    • (1996) J Neurosci , vol.16 , pp. 5324-5333
    • Hrabetova, S.1    Sacktor, T.C.2
  • 36
    • 0035906520 scopus 로고    scopus 로고
    • Neuronal plasticity in hippocampal mossy fiber-CA3 synapses of mice lacking the inositol-1,4,5-trisphosphate type 1 receptor
    • Itoh S, Ito K, Fujii S, Kaneko K, Kato K, Mikoshiba K, Kato H. 2001. Neuronal plasticity in hippocampal mossy fiber-CA3 synapses of mice lacking the inositol-1,4,5-trisphosphate type 1 receptor. Brain Res 901:237-246.
    • (2001) Brain Res , vol.901 , pp. 237-246
    • Itoh, S.1    Ito, K.2    Fujii, S.3    Kaneko, K.4    Kato, K.5    Mikoshiba, K.6    Kato, H.7
  • 37
    • 0033623796 scopus 로고    scopus 로고
    • pp60(cSrc) is a caspase-3 substrate and is essential for the transformed phenotype of A431 cells
    • Karni R, Levitzki A. 2000. pp60(cSrc) is a caspase-3 substrate and is essential for the transformed phenotype of A431 cells. Mol Cell Biol Res Commun 3:98-104.
    • (2000) Mol Cell Biol Res Commun , vol.3 , pp. 98-104
    • Karni, R.1    Levitzki, A.2
  • 38
    • 0035968218 scopus 로고    scopus 로고
    • Activation of calcium/ calmodulin-dependent protein kinase IV in long-term potentiation in the rat hippocampal CA1 region
    • Kasahara J, Fukunaga K, Miyamoto E. 2001. Activation of calcium/ calmodulin-dependent protein kinase IV in long-term potentiation in the rat hippocampal CA1 region. J Biol Chem 276:24044-24050.
    • (2001) J Biol Chem , vol.276 , pp. 24044-24050
    • Kasahara, J.1    Fukunaga, K.2    Miyamoto, E.3
  • 39
    • 0034011860 scopus 로고    scopus 로고
    • Caspases cleave the amino-terminal calpain inhibitory unit of calpastatin during apoptosis in human Jurkat T cells
    • Kato M, Nonaka T, Maki M, Kikuchi H, Imajoh-Ohmi S. 2000. Caspases cleave the amino-terminal calpain inhibitory unit of calpastatin during apoptosis in human Jurkat T cells. J Biochem (Tokyo) 127:297-305.
    • (2000) J Biochem (Tokyo) , vol.127 , pp. 297-305
    • Kato, M.1    Nonaka, T.2    Maki, M.3    Kikuchi, H.4    Imajoh-Ohmi, S.5
  • 40
    • 0033152432 scopus 로고    scopus 로고
    • A role of actin filament in synaptic transmission and long-term potentiation
    • Kim CH, Lisman JE. 1999. A role of actin filament in synaptic transmission and long-term potentiation. J Neurosci 19:4314-4324.
    • (1999) J Neurosci , vol.19 , pp. 4314-4324
    • Kim, C.H.1    Lisman, J.E.2
  • 41
    • 0030868903 scopus 로고    scopus 로고
    • Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease
    • Kim TW, Pettingell WH, Jung YK, Kovacs DM, Tanzi RE. 1997. Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease. Science 277:373-376.
    • (1997) Science , vol.277 , pp. 373-376
    • Kim, T.W.1    Pettingell, W.H.2    Jung, Y.K.3    Kovacs, D.M.4    Tanzi, R.E.5
  • 42
    • 0035940412 scopus 로고    scopus 로고
    • Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis
    • Kim YJ, Yi Y, Sapp E, Wang Y, Cuiffo B, Kegel KB, Qin ZH, Aronin N, DiFiglia M. 2001. Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis. Proc Natl Acad Sci USA 98:12784-12789.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12784-12789
    • Kim, Y.J.1    Yi, Y.2    Sapp, E.3    Wang, Y.4    Cuiffo, B.5    Kegel, K.B.6    Qin, Z.H.7    Aronin, N.8    DiFiglia, M.9
  • 43
    • 0035025830 scopus 로고    scopus 로고
    • PKC Activation rescues LTP from NMDA receptor blockade
    • Kleschevnikov AM, Routtenberg A. 2001. PKC Activation rescues LTP from NMDA receptor blockade. Hippocampus 11:168-175.
    • (2001) Hippocampus , vol.11 , pp. 168-175
    • Kleschevnikov, A.M.1    Routtenberg, A.2
  • 44
    • 0030970839 scopus 로고    scopus 로고
    • Rescuing impairment of long-term potentiation in fyn-deficient mice by introducing Fyn transgene
    • Kojima N, Wang J, Mansuy IM, Grant SG, Mayford M, Kandel ER. 1997. Rescuing impairment of long-term potentiation in fyn-deficient mice by introducing Fyn transgene. Proc Natl Acad Sci USA 94:4761-4765.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4761-4765
    • Kojima, N.1    Wang, J.2    Mansuy, I.M.3    Grant, S.G.4    Mayford, M.5    Kandel, E.R.6
  • 45
    • 0033965979 scopus 로고    scopus 로고
    • Intracerebral injection of caspase-3 inhibitor prevents neuronal apoptosis after kainic acid-evoked status epilepticus
    • Kondratyev A, Gale K. 2000. Intracerebral injection of caspase-3 inhibitor prevents neuronal apoptosis after kainic acid-evoked status epilepticus. Brain Res Mol Brain Res 75:216-224.
    • (2000) Brain Res Mol Brain Res , vol.75 , pp. 216-224
    • Kondratyev, A.1    Gale, K.2
  • 46
    • 0034612215 scopus 로고    scopus 로고
    • Dynamic actin filaments are required for stable long-term potentiation (LTP) in area CA1 of the hippocampus
    • Krucker T, Siggins GR, Halpain S. 2000. Dynamic actin filaments are required for stable long-term potentiation (LTP) in area CA1 of the hippocampus. Proc Natl Acad Sci USA 97:6856-6861.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6856-6861
    • Krucker, T.1    Siggins, G.R.2    Halpain, S.3
  • 47
    • 0035980985 scopus 로고    scopus 로고
    • Periods of postnatal maturation of hippocampus: Synaptic modifications and neuronal disconnection
    • Kudryashov IE, Onufriev MV, Kudryashova IV, Gulyaeva NV. 2001. Periods of postnatal maturation of hippocampus: synaptic modifications and neuronal disconnection. Brain Res Dev Brain Res 132:113-120.
    • (2001) Brain Res Dev Brain Res , vol.132 , pp. 113-120
    • Kudryashov, I.E.1    Onufriev, M.V.2    Kudryashova, I.V.3    Gulyaeva, N.V.4
  • 48
    • 0037206649 scopus 로고    scopus 로고
    • Foot-shock stress alters early postnatal development of electrophysiological responses and caspase-3 activity in rat hippocampus
    • Kudryashov IE, Yakovlev AA, Kudryashova I, Gulyaeva NV. 2002. Foot-shock stress alters early postnatal development of electrophysiological responses and caspase-3 activity in rat hippocampus. Neurosci Lett 332:95-98.
    • (2002) Neurosci Lett , vol.332 , pp. 95-98
    • Kudryashov, I.E.1    Yakovlev, A.A.2    Kudryashova, I.3    Gulyaeva, N.V.4
  • 49
    • 0034616245 scopus 로고    scopus 로고
    • High-frequency synaptic stimulation induces association of fyn and c-src to distinct phosphorylated components
    • Lauri SE, Taira T, Rauvala H. 2000. High-frequency synaptic stimulation induces association of fyn and c-src to distinct phosphorylated components. Neuroreport 11:997-1000.
    • (2000) Neuroreport , vol.11 , pp. 997-1000
    • Lauri, S.E.1    Taira, T.2    Rauvala, H.3
  • 53
    • 0036372055 scopus 로고    scopus 로고
    • Direct cleavage of AMPA receptor subunit GluR1 and suppression of AMPA currents by caspase-3: Implications for synaptic plasticity and excitotoxic neuronal death
    • Lu C, Fu W, Salvesen GS, Mattson MP. 2002. Direct cleavage of AMPA receptor subunit GluR1 and suppression of AMPA currents by caspase-3: implications for synaptic plasticity and excitotoxic neuronal death. Neuromolecular Med 1:69-79.
    • (2002) Neuromolecular Med , vol.1 , pp. 69-79
    • Lu, C.1    Fu, W.2    Salvesen, G.S.3    Mattson, M.P.4
  • 54
    • 0034978782 scopus 로고    scopus 로고
    • Proteolysis of glutamate receptor-interacting protein by calpain in rat brain: Implication for synaptic plasticity
    • Lu X, Wyszynski M, Sheng M, Baudry M. 2001. Proteolysis of glutamate receptor-interacting protein by calpain in rat brain: implication for synaptic plasticity. J Neurochem 77:1553-1560.
    • (2001) J Neurochem , vol.77 , pp. 1553-1560
    • Lu, X.1    Wyszynski, M.2    Sheng, M.3    Baudry, M.4
  • 56
    • 0001048711 scopus 로고    scopus 로고
    • Src activation in the induction of long-term potentiation in CA1 hippocampal neurons
    • Lu YM, Roder JC, Davidow J, Salter MW. 1998. Src activation in the induction of long-term potentiation in CA1 hippocampal neurons. Science 279:1363-1367.
    • (1998) Science , vol.279 , pp. 1363-1367
    • Lu, Y.M.1    Roder, J.C.2    Davidow, J.3    Salter, M.W.4
  • 57
    • 0035899499 scopus 로고    scopus 로고
    • Cleavage of Fyn and Lyn in their N-terminal unique regions during induction of apoptosis: A new mechanism for Src kinase regulation
    • Luciano F, Ricci JE, Auberger P. 2001. Cleavage of Fyn and Lyn in their N-terminal unique regions during induction of apoptosis: a new mechanism for Src kinase regulation. Oncogene 20:4935-4941.
    • (2001) Oncogene , vol.20 , pp. 4935-4941
    • Luciano, F.1    Ricci, J.E.2    Auberger, P.3
  • 58
    • 0032122422 scopus 로고    scopus 로고
    • Memory and the brain: Unexpected chemistries and a new pharmacology
    • Lynch G. 1998. Memory and the brain: unexpected chemistries and a new pharmacology. Neurobiol Learn Mem 70:82-100.
    • (1998) Neurobiol Learn Mem , vol.70 , pp. 82-100
    • Lynch, G.1
  • 59
    • 0023239194 scopus 로고
    • Brain spectrin, calpain and long-term changes in synaptic efficacy
    • Lynch G, Baudry M. 1987. Brain spectrin, calpain and long-term changes in synaptic efficacy. Brain Res Bull 18:809-815.
    • (1987) Brain Res Bull , vol.18 , pp. 809-815
    • Lynch, G.1    Baudry, M.2
  • 60
    • 0024156305 scopus 로고
    • Long-term potentiation: Persisting problems and recent results
    • Lynch G, Muller D, Seubert P, Larson J. 1988. Long-term potentiation: persisting problems and recent results. Brain Res Bull 21:363-372.
    • (1988) Brain Res Bull , vol.21 , pp. 363-372
    • Lynch, G.1    Muller, D.2    Seubert, P.3    Larson, J.4
  • 61
    • 0034753649 scopus 로고    scopus 로고
    • Synergistic protective effect of caspase inhibitors and bFGF against brain injury induced by transient focal ischaemia
    • Ma J, Qiu J, Hirt L, Dalkara T, Moskowitz MA. 2001. Synergistic protective effect of caspase inhibitors and bFGF against brain injury induced by transient focal ischaemia. Br J Pharmacol 133:345-350.
    • (2001) Br J Pharmacol , vol.133 , pp. 345-350
    • Ma, J.1    Qiu, J.2    Hirt, L.3    Dalkara, T.4    Moskowitz, M.A.5
  • 62
    • 0035224484 scopus 로고    scopus 로고
    • The molecular biology of the group VIA Ca2+-independent phospholipase A2
    • Ma Z, Turk J. 2001. The molecular biology of the group VIA Ca2+-independent phospholipase A2. Prog Nucleic Acid Res Mol Biol 67:1-33.
    • (2001) Prog Nucleic Acid Res Mol Biol , vol.67 , pp. 1-33
    • Ma, Z.1    Turk, J.2
  • 63
    • 0024393433 scopus 로고
    • An essential role for postsynaptic calmodulin and protein kinase activity in long-term potentiation
    • Malenka RC, Kauer JA, Perkel DJ, Mauk MD, Kelly PT, Nicoll RA, Waxham MN. 1989. An essential role for postsynaptic calmodulin and protein kinase activity in long-term potentiation. Nature 340:554-557.
    • (1989) Nature , vol.340 , pp. 554-557
    • Malenka, R.C.1    Kauer, J.A.2    Perkel, D.J.3    Mauk, M.D.4    Kelly, P.T.5    Nicoll, R.A.6    Waxham, M.N.7
  • 64
    • 0023790503 scopus 로고
    • Persistent protein kinase activity underlying long-term potentiation
    • Malinow R, Madison DV, Tsien RW. 1988. Persistent protein kinase activity underlying long-term potentiation. Nature 335:820-824.
    • (1988) Nature , vol.335 , pp. 820-824
    • Malinow, R.1    Madison, D.V.2    Tsien, R.W.3
  • 65
    • 0036433323 scopus 로고    scopus 로고
    • New life in an old idea: The synaptic plasticity and memory hypothesis revisited
    • Martin SJ, Morris RGM. 2002. New life in an old idea: the synaptic plasticity and memory hypothesis revisited. Hippocampus 12:609-636.
    • (2002) Hippocampus , vol.12 , pp. 609-636
    • Martin, S.J.1    Morris, R.G.M.2
  • 66
    • 0026073468 scopus 로고
    • Modulation of DL-alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid/quisqualate receptors by phospholipase A2: A necessary step in long-term potentiation?
    • Massicotte G, Vanderklish P, Lynch G, Baudry M. 1991. Modulation of DL-alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid/quisqualate receptors by phospholipase A2: a necessary step in long-term potentiation? Proc Natl Acad Sci USA 88:1893-1897.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 1893-1897
    • Massicotte, G.1    Vanderklish, P.2    Lynch, G.3    Baudry, M.4
  • 67
    • 0033785611 scopus 로고    scopus 로고
    • Modification of glutamate receptors by phospholipase A2: Its role in adaptive neural plasticity
    • Massicotte G. 2000. Modification of glutamate receptors by phospholipase A2: its role in adaptive neural plasticity. Cell Mol Life Sci 57:1542-1550.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1542-1550
    • Massicotte, G.1
  • 68
    • 0034029953 scopus 로고    scopus 로고
    • Apoptotic and anti-apoptotic synaptic signaling mechanisms
    • Mattson MP. 2000. Apoptotic and anti-apoptotic synaptic signaling mechanisms. Brain Pathol 10:300-312.
    • (2000) Brain Pathol , vol.10 , pp. 300-312
    • Mattson, M.P.1
  • 69
    • 0033215252 scopus 로고    scopus 로고
    • "Apoptotic" biochemical cascades in synaptic compartments: Roles in adaptive plasticity and neurodegenerative disorders
    • Mattson MP, Duan W. 1999. "Apoptotic" biochemical cascades in synaptic compartments: roles in adaptive plasticity and neurodegenerative disorders. J Neurosci Res 58:152-166.
    • (1999) J Neurosci Res , vol.58 , pp. 152-166
    • Mattson, M.P.1    Duan, W.2
  • 71
    • 0036043866 scopus 로고    scopus 로고
    • Energetics and oxidative stress in synaptic plasticity and neurodegenerative disorders
    • Mattson MP, Liu D. 2002. Energetics and oxidative stress in synaptic plasticity and neurodegenerative disorders. Neuromolecular Med 2:215-231.
    • (2002) Neuromolecular Med , vol.2 , pp. 215-231
    • Mattson, M.P.1    Liu, D.2
  • 72
    • 0032493743 scopus 로고    scopus 로고
    • Calcium/ calmodulin-dependent protein kinase IV is cleaved by caspase-3 and calpain in SH-SY5Y human neuroblastoma cells undergoing apoptosis
    • McGinnis KM, Whitton MM, Gnegy ME, Wang KK. 1998. Calcium/ calmodulin-dependent protein kinase IV is cleaved by caspase-3 and calpain in SH-SY5Y human neuroblastoma cells undergoing apoptosis. J Biol Chem 273:19993-20000.
    • (1998) J Biol Chem , vol.273 , pp. 19993-20000
    • McGinnis, K.M.1    Whitton, M.M.2    Gnegy, M.E.3    Wang, K.K.4
  • 74
    • 0036445741 scopus 로고    scopus 로고
    • IP3 receptor, a Ca2+ oscillator - Role of IP3 receptor in development and neural plasticity
    • Japanese
    • Mikoshiba K. 2002. [IP3 receptor, a Ca2+ oscillator - role of IP3 receptor in development and neural plasticity]. Japanese. Nippon Yakurigaku Zasshi 120:6-10.
    • (2002) Nippon Yakurigaku Zasshi , vol.120 , pp. 6-10
    • Mikoshiba, K.1
  • 79
    • 0028959587 scopus 로고
    • A genetic deficiency in calpastatin and isovalerylcarnitine treatment is associated with enhanced hippocampal long-term potentiation
    • Muller D, Molinari I, Soldati L, Bianchi G. 1995. A genetic deficiency in calpastatin and isovalerylcarnitine treatment is associated with enhanced hippocampal long-term potentiation. Synapse 19:37-45.
    • (1995) Synapse , vol.19 , pp. 37-45
    • Muller, D.1    Molinari, I.2    Soldati, L.3    Bianchi, G.4
  • 81
  • 82
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka Y. 1995. Protein kinase C and lipid signaling for sustained cellular responses. FASEB J 9:484-496.
    • (1995) FASEB J , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 83
    • 0042704497 scopus 로고    scopus 로고
    • The neuroprotective effect of pituitary adenylate cyclase-activating polypeptide on cerebellar granule cells is mediated through inhibition of the CED3-related cysteine protease caspase-3yCPP32
    • Pamantung TF, Fontaine M, Fournier A, Vaudry D, Gonzalez BJ, Basille M, Vaudry H. 2000. The neuroprotective effect of pituitary adenylate cyclase-activating polypeptide on cerebellar granule cells is mediated through inhibition of the CED3-related cysteine protease caspase-3yCPP32. Proc Natl Acad Sci USA 97:6398-6403.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6398-6403
    • Pamantung, T.F.1    Fontaine, M.2    Fournier, A.3    Vaudry, D.4    Gonzalez, B.J.5    Basille, M.6    Vaudry, H.7
  • 84
    • 0032945724 scopus 로고    scopus 로고
    • Synaptic transmission and hippocampal long-term potentiation in transgenic mice expressing FAD-linked presenilin 1
    • Parent A, Linden DJ, Sisodia SS, Borchelt DR. 1999. Synaptic transmission and hippocampal long-term potentiation in transgenic mice expressing FAD-linked presenilin 1. Neurobiol Dis 6:56-62.
    • (1999) Neurobiol Dis , vol.6 , pp. 56-62
    • Parent, A.1    Linden, D.J.2    Sisodia, S.S.3    Borchelt, D.R.4
  • 86
    • 0036209921 scopus 로고    scopus 로고
    • Flies put the buzz back into long-term-potentiation
    • Paulsen O, Morris RGM. 2002. Flies put the buzz back into long-term-potentiation. Nature Neurosci 5:289-290.
    • (2002) Nature Neurosci , vol.5 , pp. 289-290
    • Paulsen, O.1    Morris, R.G.M.2
  • 87
    • 0034800876 scopus 로고    scopus 로고
    • Accumulation of non-erythroid alpha II-spectrin and calpain-cleaved alpha II-spectrin breakdown products in cerebrospinal fluid after traumatic brain injury in rats
    • Pike BR, Flint J, Dutta S, Johnson E, Wang KK, Hayes RL. 2001. Accumulation of non-erythroid alpha II-spectrin and calpain-cleaved alpha II-spectrin breakdown products in cerebrospinal fluid after traumatic brain injury in rats. J Neurochem 78:1297-1306.
    • (2001) J Neurochem , vol.78 , pp. 1297-1306
    • Pike, B.R.1    Flint, J.2    Dutta, S.3    Johnson, E.4    Wang, K.K.5    Hayes, R.L.6
  • 88
    • 0041018181 scopus 로고    scopus 로고
    • Cleavage of the calpain inhibitor, calpastatin, during apoptosis
    • Porn-Ares MI, Samali A, Orrenius S. 1998. Cleavage of the calpain inhibitor, calpastatin, during apoptosis. Cell Death Differ 5:1028-1033.
    • (1998) Cell Death Differ , vol.5 , pp. 1028-1033
    • Porn-Ares, M.I.1    Samali, A.2    Orrenius, S.3
  • 89
    • 0035477406 scopus 로고    scopus 로고
    • Caspase cleavage of exon 9 deleted presenilin-1 is an early event in apoptosis induced by calcium ionophore A 23187 in SH-SY5Y neuroblastoma cells
    • Popescu BO, Cedazo-Minguez A, Popescu LM, Winblad B, Cowburn RF, Ankarcrona M. 2001. Caspase cleavage of exon 9 deleted presenilin-1 is an early event in apoptosis induced by calcium ionophore A 23187 in SH-SY5Y neuroblastoma cells. J Neurosci Res 66:122-134.
    • (2001) J Neurosci Res , vol.66 , pp. 122-134
    • Popescu, B.O.1    Cedazo-Minguez, A.2    Popescu, L.M.3    Winblad, B.4    Cowburn, R.F.5    Ankarcrona, M.6
  • 90
    • 0036490671 scopus 로고    scopus 로고
    • New methodology is a key to progress
    • Robertson JD, Zhivotovsky B. 2002. New methodology is a key to progress. Cell Cycle 1:119-121.
    • (2002) Cell Cycle , vol.1 , pp. 119-121
    • Robertson, J.D.1    Zhivotovsky, B.2
  • 92
    • 0027305085 scopus 로고
    • Sensitizing stimuli cause translocation of protein kinase C in Aplysia sensory neurons
    • Sacktor TC, Schwartz JH. 1993. Sensitizing stimuli cause translocation of protein kinase C in Aplysia sensory neurons. Proc Natl Acad Sci USA 90:8342-8346.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8342-8346
    • Sacktor, T.C.1    Schwartz, J.H.2
  • 93
    • 0036144378 scopus 로고    scopus 로고
    • Caspases: Opening the boxes and interpreting the arrows
    • Salvesen GS. 2002. Caspases: opening the boxes and interpreting the arrows. Cell Death Differ 9:3-5.
    • (2002) Cell Death Differ , vol.9 , pp. 3-5
    • Salvesen, G.S.1
  • 96
    • 0036095459 scopus 로고    scopus 로고
    • Caspase 3-mediated focal adhesion kinase processing in human ovarian cancer cells: Possible regulation by X-linked inhibitor of apoptosis protein
    • Sasaki H, Kotsuji F, Tsang BK. 2002. Caspase 3-mediated focal adhesion kinase processing in human ovarian cancer cells: possible regulation by X-linked inhibitor of apoptosis protein. Gynecol Oncol 85:339-350.
    • (2002) Gynecol Oncol , vol.85 , pp. 339-350
    • Sasaki, H.1    Kotsuji, F.2    Tsang, B.K.3
  • 99
    • 0023161090 scopus 로고
    • Molecular mechanisms for memory: Second-messenger induced modifications of protein kinases in nerve cells
    • Schwartz JH, Greenberg SM. 1987. Molecular mechanisms for memory: second-messenger induced modifications of protein kinases in nerve cells. Annu Rev Neurosci 10:459-476.
    • (1987) Annu Rev Neurosci , vol.10 , pp. 459-476
    • Schwartz, J.H.1    Greenberg, S.M.2
  • 100
    • 0035175495 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase type IV (CaMKIV) inhibits apoptosis induced by potassium deprivation in cerebellar granule neurons
    • See V, Boutillier AL, Bito H, Loeffler JP. 2001. Calcium/calmodulin-dependent protein kinase type IV (CaMKIV) inhibits apoptosis induced by potassium deprivation in cerebellar granule neurons. FASEB J 15:134-144.
    • (2001) FASEB J , vol.15 , pp. 134-144
    • See, V.1    Boutillier, A.L.2    Bito, H.3    Loeffler, J.P.4
  • 102
    • 0033826589 scopus 로고    scopus 로고
    • Downregulation of the calpain inhibitor protein calpastatin by caspases during renal ischemia-reperfusion
    • Shi Y, Melnikov VY, Schrier RW, Edelstein CL. 2000. Downregulation of the calpain inhibitor protein calpastatin by caspases during renal ischemia-reperfusion. Am J Physiol Renal Physiol 279:509-517.
    • (2000) Am J Physiol Renal Physiol , vol.279 , pp. 509-517
    • Shi, Y.1    Melnikov, V.Y.2    Schrier, R.W.3    Edelstein, C.L.4
  • 103
    • 0035930899 scopus 로고    scopus 로고
    • Differential expression of rat brain caspase family proteins during development and aging
    • Shimohama S, Tanino H, Fujimoto S. 2001a. Differential expression of rat brain caspase family proteins during development and aging. Biochem Biophys Res Commun 289:1063-1066.
    • (2001) Biochem Biophys Res Commun , vol.289 , pp. 1063-1066
    • Shimohama, S.1    Tanino, H.2    Fujimoto, S.3
  • 104
    • 0035960537 scopus 로고    scopus 로고
    • Differential subcellular localization of caspase family proteins in the adult rat brain
    • Shimohama S, Tanino H, Fujimoto S. 2001b. Differential subcellular localization of caspase family proteins in the adult rat brain. Neurosci Lett 315:125-128.
    • (2001) Neurosci Lett , vol.315 , pp. 125-128
    • Shimohama, S.1    Tanino, H.2    Fujimoto, S.3
  • 105
    • 0034985915 scopus 로고    scopus 로고
    • mGluR1-mediated potentiation of NMDA receptors involves a rise in intracellular calcium and activation of protein kinase C
    • Skeberdis VA, Lan J, Opitz T, Zheng X, Bennett MV, Zukin RS. 2001. mGluR1-mediated potentiation of NMDA receptors involves a rise in intracellular calcium and activation of protein kinase C. Neuropharmacology 40:856-865.
    • (2001) Neuropharmacology , vol.40 , pp. 856-865
    • Skeberdis, V.A.1    Lan, J.2    Opitz, T.3    Zheng, X.4    Bennett, M.V.5    Zukin, R.S.6
  • 106
    • 0036934466 scopus 로고    scopus 로고
    • Caspase-cleaved amyloid precursor protein and activated caspase-3 are co-localized in the granules of granulovacuolar degeneration in Alzheimer's disease and Down's syndrome brain
    • Su JH, Kesslak JP, Head E, Cotman CW. 2002. Caspase-cleaved amyloid precursor protein and activated caspase-3 are co-localized in the granules of granulovacuolar degeneration in Alzheimer's disease and Down's syndrome brain. Acta Neuropathol (Berl) 104:1-6.
    • (2002) Acta Neuropathol (Berl) , vol.104 , pp. 1-6
    • Su, J.H.1    Kesslak, J.P.2    Head, E.3    Cotman, C.W.4
  • 110
    • 0032897760 scopus 로고    scopus 로고
    • Impaired synaptic plasticity in mice carrying the Huntington's disease mutation
    • Usdin MT, Shelbourne PF, Myers RM, Madison DV. 1999. Impaired synaptic plasticity in mice carrying the Huntington's disease mutation. Hum Mol Genet 8:839-846.
    • (1999) Hum Mol Genet , vol.8 , pp. 839-846
    • Usdin, M.T.1    Shelbourne, P.F.2    Myers, R.M.3    Madison, D.V.4
  • 112
    • 0033532143 scopus 로고    scopus 로고
    • Dephosphorylation of focal adhesion kinase (FAK) and loss of focal contacts precede caspase-mediated cleavage of FAK during apoptosis in renal epithelial cells
    • van de Water B, Nagelkerke JF, Stevens JL. 1999. Dephosphorylation of focal adhesion kinase (FAK) and loss of focal contacts precede caspase-mediated cleavage of FAK during apoptosis in renal epithelial cells. J Biol Chem 274:13328-13337.
    • (1999) J Biol Chem , vol.274 , pp. 13328-13337
    • Van de Water, B.1    Nagelkerke, J.F.2    Stevens, J.L.3
  • 114
    • 0036678723 scopus 로고    scopus 로고
    • Endoplasmic reticulum calcium release is modulated by actin polymerization
    • Wang Y, Mattson MP, Furukawa K. 2002. Endoplasmic reticulum calcium release is modulated by actin polymerization. J Neurochem 82:945-952.
    • (2002) J Neurochem , vol.82 , pp. 945-952
    • Wang, Y.1    Mattson, M.P.2    Furukawa, K.3
  • 115
    • 0033708960 scopus 로고    scopus 로고
    • Huntington disease: New insights on the role of huntingtin cleavage
    • Wellington CL, Leavitt BR, Hayden MR. 2000. Huntington disease: new insights on the role of huntingtin cleavage. J Neural Transm Suppl 58:1-17.
    • (2000) J Neural Transm Suppl , vol.58 , pp. 1-17
    • Wellington, C.L.1    Leavitt, B.R.2    Hayden, M.R.3
  • 116
    • 0032144789 scopus 로고    scopus 로고
    • Molecular mechanisms that underlie structural and functional changes at the postsynaptic membrane during synaptic plasticity
    • Wheal HV, Chen Y, Mitchell J, Schachner M, Maerz W, Wieland H, Van Rossum D, Kirsch J. 1998. Molecular mechanisms that underlie structural and functional changes at the postsynaptic membrane during synaptic plasticity. Prog Neurobiol 55:611-640.
    • (1998) Prog Neurobiol , vol.55 , pp. 611-640
    • Wheal, H.V.1    Chen, Y.2    Mitchell, J.3    Schachner, M.4    Maerz, W.5    Wieland, H.6    Van Rossum, D.7    Kirsch, J.8
  • 117
    • 0029558517 scopus 로고
    • Long-term potentiation requires activation of calcium-independent phospholipase A2
    • Wolf MJ, Izumi Y, Zorumski CF, Gross RW. 1995. Long-term potentiation requires activation of calcium-independent phospholipase A2. FEBS Lett 377:358-362.
    • (1995) FEBS Lett , vol.377 , pp. 358-362
    • Wolf, M.J.1    Izumi, Y.2    Zorumski, C.F.3    Gross, R.W.4
  • 118
    • 0033575255 scopus 로고    scopus 로고
    • Suicidal tendencies: Apoptotic cell death by caspase family proteinases
    • Wolf BB, Green DR. 1999. Suicidal tendencies: apoptotic cell death by caspase family proteinases. J Biol Chem 274:20049-20052.
    • (1999) J Biol Chem , vol.274 , pp. 20049-20052
    • Wolf, B.B.1    Green, D.R.2
  • 119
    • 0036834317 scopus 로고    scopus 로고
    • Genetic and pharmacological demonstration of a role for cyclic AMP-dependent protein kinase-mediated suppression of protein phosphatases in gating the expression of late LTP
    • Woo NH, Abel T, Nguyen PV. 2002. Genetic and pharmacological demonstration of a role for cyclic AMP-dependent protein kinase-mediated suppression of protein phosphatases in gating the expression of late LTP. Eur J Neurosci 16:1871-1876.
    • (2002) Eur J Neurosci , vol.16 , pp. 1871-1876
    • Woo, N.H.1    Abel, T.2    Nguyen, P.V.3
  • 120
    • 0036667154 scopus 로고    scopus 로고
    • "Silent" metaplasticity of the late phase of long-term potentiation requires protein phosphatases
    • Woo NH, Nguyen PV. 2002. "Silent" metaplasticity of the late phase of long-term potentiation requires protein phosphatases. Learn Mem 9:202-213.
    • (2002) Learn Mem , vol.9 , pp. 202-213
    • Woo, N.H.1    Nguyen, P.V.2
  • 121
    • 0035938437 scopus 로고    scopus 로고
    • Expression of active caspase-3 in mitotic and postmitotic cells of the rat forebrain
    • Yan XX, Najbauer J, Woo CC, Dashtipour K, Ribak CE, Leon M. 2001. Expression of active caspase-3 in mitotic and postmitotic cells of the rat forebrain. J Comp Neurol 433:4-22.
    • (2001) J Comp Neurol , vol.433 , pp. 4-22
    • Yan, X.X.1    Najbauer, J.2    Woo, C.C.3    Dashtipour, K.4    Ribak, C.E.5    Leon, M.6
  • 122
    • 0034641936 scopus 로고    scopus 로고
    • Apoptosis in the nervous system
    • Yuan J, Yankner BA. 2000. Apoptosis in the nervous system. Nature 407:802-809.
    • (2000) Nature , vol.407 , pp. 802-809
    • Yuan, J.1    Yankner, B.A.2
  • 123
    • 0037052702 scopus 로고    scopus 로고
    • Preliminary study of the effects of caspase inhibitors on vasospasm in dog penetrating arteries
    • Zubkov AY, Aoki K, Parent AD, Zhang JH. 2002. Preliminary study of the effects of caspase inhibitors on vasospasm in dog penetrating arteries. Life Sci 70:3007-3018.
    • (2002) Life Sci , vol.70 , pp. 3007-3018
    • Zubkov, A.Y.1    Aoki, K.2    Parent, A.D.3    Zhang, J.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.