메뉴 건너뛰기




Volumn 40, Issue C, 2002, Pages 23-62

2 Discovery of Cep-1347/Kt-7515, an Inhibitor of the Jnk/Sapk Pathway for the Treatment of Neurodegenerative Diseases

Author keywords

[No Author keywords available]

Indexed keywords

CARBAZOLE DERIVATIVE; CEP 1347; ENZYME INHIBITOR; INDOLE DERIVATIVE; MITOGEN ACTIVATED PROTEIN KINASE; NOOTROPIC AGENT; STRESS ACTIVATED PROTEIN KINASE; STRESS ACTIVATED PROTEIN KINASE 1;

EID: 0036988312     PISSN: 00796468     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0079-6468(08)70081-X     Document Type: Article
Times cited : (99)

References (174)
  • 1
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease.
    • Thompson C.B. Apoptosis in the pathogenesis and treatment of disease. Science 267 (1995) 1456-1462
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 2
    • 10544253074 scopus 로고    scopus 로고
    • Neuronal death in developmental models: possible implications in neuropathology.
    • Johnson E.M., DeckwerTh T.L., and Deshmukh M. Neuronal death in developmental models: possible implications in neuropathology. Brain Pathology 6 (1996) 397-409
    • (1996) Brain Pathology , vol.6 , pp. 397-409
    • Johnson, E.M.1    DeckwerTh, T.L.2    Deshmukh, M.3
  • 3
    • 0026058318 scopus 로고
    • Cell death during development of the nervous system.
    • Oppenheim R.W. Cell death during development of the nervous system. Ann. Rev. Neurosci. 14 (1991) 453-501
    • (1991) Ann. Rev. Neurosci. , vol.14 , pp. 453-501
    • Oppenheim, R.W.1
  • 4
    • 0033963108 scopus 로고    scopus 로고
    • Apoptosis and neurological disease.
    • Honig L.S., and Rosenburg R.N. Apoptosis and neurological disease. Am. J. Med. 108 (2000) 317-330
    • (2000) Am. J. Med. , vol.108 , pp. 317-330
    • Honig, L.S.1    Rosenburg, R.N.2
  • 5
    • 0031900347 scopus 로고    scopus 로고
    • Sealing one's fate: control of cell death in neurons.
    • Bergeron L., and Yuan J. Sealing one's fate: control of cell death in neurons. Curr. Opin. Neuronal. 8 (1998) 55-63
    • (1998) Curr. Opin. Neuronal. , vol.8 , pp. 55-63
    • Bergeron, L.1    Yuan, J.2
  • 7
    • 0031110054 scopus 로고    scopus 로고
    • Terminal dUTP Nick End Labeling (TUNEL) positive cells in the different regions of the brain in normal aging and Alzheimer patients.
    • Li W.P., Chan W.Y., Lai H.W.L., and Yew D.T. Terminal dUTP Nick End Labeling (TUNEL) positive cells in the different regions of the brain in normal aging and Alzheimer patients. J. Mol. Neurosci. 8 (1997) 75-82
    • (1997) J. Mol. Neurosci. , vol.8 , pp. 75-82
    • Li, W.P.1    Chan, W.Y.2    Lai, H.W.L.3    Yew, D.T.4
  • 8
    • 0033970158 scopus 로고    scopus 로고
    • JNK and p38 stresskinases - degenerative effectors of signal-transduction-cascades in the nervous system.
    • Miellce K., and Herdegen T. JNK and p38 stresskinases - degenerative effectors of signal-transduction-cascades in the nervous system. Prog. Neurobiol. 61 (2000) 45-60
    • (2000) Prog. Neurobiol. , vol.61 , pp. 45-60
    • Miellce, K.1    Herdegen, T.2
  • 9
    • 0027946686 scopus 로고    scopus 로고
    • Altered gene expression in neurons during programmed cell death: Identification of c-Jun as necessary for neuronal apoptosis.
    • Estus S., Zaks W.J., Freeman R.S., Gruda M., Bravo R., and Johnson E.M. Altered gene expression in neurons during programmed cell death: Identification of c-Jun as necessary for neuronal apoptosis. J. Cell. Biol. 127 (1999) 1717-1727
    • (1999) J. Cell. Biol. , vol.127 , pp. 1717-1727
    • Estus, S.1    Zaks, W.J.2    Freeman, R.S.3    Gruda, M.4    Bravo, R.5    Johnson, E.M.6
  • 10
    • 0028631458 scopus 로고
    • The role of Jun transcription factor expression and phosphorylation in neuronal differentiation, neuronal cell death, and plastic adaptations in vivo.
    • Schlingensiepen K.H., Wallnik F., Kunst M., Schlingensiepen R., Herdengen T., and Brysch W. The role of Jun transcription factor expression and phosphorylation in neuronal differentiation, neuronal cell death, and plastic adaptations in vivo. Cell. Mol. Neurobiol. 14 (1994) 487-505
    • (1994) Cell. Mol. Neurobiol. , vol.14 , pp. 487-505
    • Schlingensiepen, K.H.1    Wallnik, F.2    Kunst, M.3    Schlingensiepen, R.4    Herdengen, T.5    Brysch, W.6
  • 11
    • 0029012476 scopus 로고
    • A c-Jun dominant negative mutant protects sympathetic neurons against programmed cell death.
    • Ham J., Babij C., Whitfield J., Pfarr C.M., Lallemand D., Yaniv M., and Rubin L.L. A c-Jun dominant negative mutant protects sympathetic neurons against programmed cell death. Neuron 14 (1995) 927-939
    • (1995) Neuron , vol.14 , pp. 927-939
    • Ham, J.1    Babij, C.2    Whitfield, J.3    Pfarr, C.M.4    Lallemand, D.5    Yaniv, M.6    Rubin, L.L.7
  • 12
    • 0027423418 scopus 로고
    • Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-jun activation domain.
    • Hibi M., Lin A., Stneal T., Minden A., and Karin M. Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-jun activation domain. Genes Dev. 7 (1993) 2135-2148
    • (1993) Genes Dev. , vol.7 , pp. 2135-2148
    • Hibi, M.1    Lin, A.2    Stneal, T.3    Minden, A.4    Karin, M.5
  • 13
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain.
    • Derijard B., Hibi M., Wu I.-H., Barrett T., Su B., Deng T., Karin M., and Davis R.J. JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 76 (1994) 1025-1037
    • (1994) Cell , vol.76 , pp. 1025-1037
    • Derijard, B.1    Hibi, M.2    Wu, I.-H.3    Barrett, T.4    Su, B.5    Deng, T.6    Karin, M.7    Davis, R.J.8
  • 15
    • 0031972678 scopus 로고    scopus 로고
    • Phosphorylation of c-Jun is necessary for apoptosis induced by survival signal withdrawal in cerebellar granule neurons.
    • Watson A., Eilers A., Lallemand D., Kyriakis J., Rubin L.L., and Ham J. Phosphorylation of c-Jun is necessary for apoptosis induced by survival signal withdrawal in cerebellar granule neurons. J. Neurosci. 18 (1998) 751-762
    • (1998) J. Neurosci. , vol.18 , pp. 751-762
    • Watson, A.1    Eilers, A.2    Lallemand, D.3    Kyriakis, J.4    Rubin, L.L.5    Ham, J.6
  • 16
    • 0032937879 scopus 로고    scopus 로고
    • Withdrawal of survival factors results in activation of the JNK pathway in neuronal cells leading to Fas ligand induction and cell death.
    • Le-Ntculescu H., Bonfoco E., Kasuya Y., Claret F.X., Green D.R., and Karin M. Withdrawal of survival factors results in activation of the JNK pathway in neuronal cells leading to Fas ligand induction and cell death. Mol. Cell. Biol. 19 (1999) 751-763
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 751-763
    • Le-Ntculescu, H.1    Bonfoco, E.2    Kasuya, Y.3    Claret, F.X.4    Green, D.R.5    Karin, M.6
  • 17
    • 0028935974 scopus 로고
    • Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms.
    • Deijard B., Raingeaud J., Barrett T., Wu I.H., Han J., Ulevitch R.J., and Davis R.J. Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms. Science 267 (1995) 682-685
    • (1995) Science , vol.267 , pp. 682-685
    • Deijard, B.1    Raingeaud, J.2    Barrett, T.3    Wu, I.H.4    Han, J.5    Ulevitch, R.J.6    Davis, R.J.7
  • 20
    • 0030863983 scopus 로고    scopus 로고
    • SKK4, a novel activator of stress-activated protein kinase-1 (SAPK1/JNK).
    • Lawler S., Cuenda A., Goedert M., and Cohen P. SKK4, a novel activator of stress-activated protein kinase-1 (SAPK1/JNK). FEBS Lett. 414 (1997) 153-158
    • (1997) FEBS Lett. , vol.414 , pp. 153-158
    • Lawler, S.1    Cuenda, A.2    Goedert, M.3    Cohen, P.4
  • 21
    • 0030770419 scopus 로고    scopus 로고
    • Identification of c-Jun NH2-tenninal protein kinase (JNK)-acti-vating kinase 2 as an activator of JNK but not p38.
    • Lu X., Nemoto S., and Lin A. Identification of c-Jun NH2-tenninal protein kinase (JNK)-acti-vating kinase 2 as an activator of JNK but not p38. J. Biol. Chem. 272 (1997) 24751-24754
    • (1997) J. Biol. Chem. , vol.272 , pp. 24751-24754
    • Lu, X.1    Nemoto, S.2    Lin, A.3
  • 22
    • 0030786344 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase.
    • Tournier C., Whitmarsh A., Cavanagh J., Barrett T., and Davis R. Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase. Proc. Natl. Acad. Sci., USA 94 (1997) 7342-7737
    • (1997) Proc. Natl. Acad. Sci., USA , vol.94 , pp. 7342-7737
    • Tournier, C.1    Whitmarsh, A.2    Cavanagh, J.3    Barrett, T.4    Davis, R.5
  • 23
    • 0030689618 scopus 로고    scopus 로고
    • Molecular cloning and characterization of human JNKK2, a novel Jun NH2-terminal kinase-specific kinase.
    • Wu A., Wu J., Jacinto E., and Karin M. Molecular cloning and characterization of human JNKK2, a novel Jun NH2-terminal kinase-specific kinase. Mol. Cell. Biol. 17 (1997) 7407-7416
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 7407-7416
    • Wu, A.1    Wu, J.2    Jacinto, E.3    Karin, M.4
  • 24
    • 0032502772 scopus 로고    scopus 로고
    • Human mitogen-activated protein kinase kinase 7 (MKK7) is a highly conserved c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) activated by environmental stresses and physiological stimuli.
    • Foltz I.N., Gerl R.E., Wieler J.S., Lyckach M., Salmon R.A., and Schrader J.W. Human mitogen-activated protein kinase kinase 7 (MKK7) is a highly conserved c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) activated by environmental stresses and physiological stimuli. J. Biol. Chem. 273 (1998) 9344-9351
    • (1998) J. Biol. Chem. , vol.273 , pp. 9344-9351
    • Foltz, I.N.1    Gerl, R.E.2    Wieler, J.S.3    Lyckach, M.4    Salmon, R.A.5    Schrader, J.W.6
  • 25
    • 0033567291 scopus 로고    scopus 로고
    • The stress-activated protein kinase pathways.
    • Tibbies L.A., and Woodgett J.R. The stress-activated protein kinase pathways. Cell. Mol. Life. Sci. 55 (1998) 1230-1254
    • (1998) Cell. Mol. Life. Sci. , vol.55 , pp. 1230-1254
    • Tibbies, L.A.1    Woodgett, J.R.2
  • 26
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis.
    • Xia Z., Dickens M., Raingeaud J., Davis R.J., and Greenberg M.E. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 270 (1995) 1326-1331
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z.1    Dickens, M.2    Raingeaud, J.3    Davis, R.J.4    Greenberg, M.E.5
  • 27
    • 0033986791 scopus 로고    scopus 로고
    • Role of apoptosis signal-regulating kinase in regulation of the c-Jun N-terminal kinase pathway and apoptosis in sympathetic neurons.
    • Kanamoto T., Mota M., Takefa K., Rubin L., Miyazono K., Ichijo H., and Bazenet C. Role of apoptosis signal-regulating kinase in regulation of the c-Jun N-terminal kinase pathway and apoptosis in sympathetic neurons. Mol. Cell. Biol. 20 (2000) 196-204
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 196-204
    • Kanamoto, T.1    Mota, M.2    Takefa, K.3    Rubin, L.4    Miyazono, K.5    Ichijo, H.6    Bazenet, C.7
  • 28
    • 0029913510 scopus 로고    scopus 로고
    • Signaling from the small GTP-binding proteins Racl and Cdc42 to the c-Jun N-terminal kinase/stress-activated protein kinase pathway. A role for mixed lineage kinase 3/protein tyrosine kinase I, a novel member of the mixed lineage kinase family.
    • Teramoto H., Coso O.A., Miyata H., Igishi T., Miki T., and Gutkind J.S. Signaling from the small GTP-binding proteins Racl and Cdc42 to the c-Jun N-terminal kinase/stress-activated protein kinase pathway. A role for mixed lineage kinase 3/protein tyrosine kinase I, a novel member of the mixed lineage kinase family. J. Biol. Chem. 271 (1996) 27225-27228
    • (1996) J. Biol. Chem. , vol.271 , pp. 27225-27228
    • Teramoto, H.1    Coso, O.A.2    Miyata, H.3    Igishi, T.4    Miki, T.5    Gutkind, J.S.6
  • 29
    • 0032584083 scopus 로고    scopus 로고
    • The small GTP-binding protein Cdc42 is required for nerve growth factor withdrawal-induced neuronal death.
    • Bazenet C.E., Mota M.A., and Rubin L.L. The small GTP-binding protein Cdc42 is required for nerve growth factor withdrawal-induced neuronal death. Proc. Natl. Acad. Sci., USA 95 (1998) 3984-3989
    • (1998) Proc. Natl. Acad. Sci., USA , vol.95 , pp. 3984-3989
    • Bazenet, C.E.1    Mota, M.A.2    Rubin, L.L.3
  • 31
    • 0032979438 scopus 로고    scopus 로고
    • Amino-terminal phosphorylation of c-Jun regulates stress-induced apoptosis and cellular proliferation.
    • Behrens A., Sibilia M., and Wagner E.F. Amino-terminal phosphorylation of c-Jun regulates stress-induced apoptosis and cellular proliferation. Nature Genetics 21 (1999) 326-329
    • (1999) Nature Genetics , vol.21 , pp. 326-329
    • Behrens, A.1    Sibilia, M.2    Wagner, E.F.3
  • 32
    • 0028113035 scopus 로고
    • Induction of c-Jun and suppression of CREB transcription factor proteins in axotomized neurons of substantia nigra and covariation with tyrosine hydroxylase.
    • Brecht S., Gass P., Anton F., Bravo R., Zimmermann M., and Herdegen T. Induction of c-Jun and suppression of CREB transcription factor proteins in axotomized neurons of substantia nigra and covariation with tyrosine hydroxylase. Mol. Cell. Neurosci. 5 (1994) 431-441
    • (1994) Mol. Cell. Neurosci. , vol.5 , pp. 431-441
    • Brecht, S.1    Gass, P.2    Anton, F.3    Bravo, R.4    Zimmermann, M.5    Herdegen, T.6
  • 33
    • 0029080665 scopus 로고
    • Transection of rat fimbria-fornix induces lasting expression of c-Jun protein in axotomized septal neurons immunonegative for choline acetyltransferase and nitric oxide synthase.
    • Brecht S., Martin-Villalba A., Zuschratter W., Bravo B., and Herdegen T. Transection of rat fimbria-fornix induces lasting expression of c-Jun protein in axotomized septal neurons immunonegative for choline acetyltransferase and nitric oxide synthase. Experimental Neurology 134 (1995) 112-125
    • (1995) Experimental Neurology , vol.134 , pp. 112-125
    • Brecht, S.1    Martin-Villalba, A.2    Zuschratter, W.3    Bravo, B.4    Herdegen, T.5
  • 34
    • 0030983123 scopus 로고    scopus 로고
    • Strong c-.lun/AP-1 immunoreactivity is restricted to apoptotic cells following intracerebral ibotenic acid injection in developing rats.
    • Ferrer I., Pozas E., Ballabriga J., and Planas A.M. Strong c-.lun/AP-1 immunoreactivity is restricted to apoptotic cells following intracerebral ibotenic acid injection in developing rats. Neurosci. Res. 28 (1997) 21-31
    • (1997) Neurosci. Res. , vol.28 , pp. 21-31
    • Ferrer, I.1    Pozas, E.2    Ballabriga, J.3    Planas, A.M.4
  • 35
    • 0027416834 scopus 로고
    • C-Jun expression in substantia nigra neurons following striatal 6-hydroxydopamine lesions in the rat.
    • Jenkins R., O'Shea R., Thomas K.L., and Hunt S.P. C-Jun expression in substantia nigra neurons following striatal 6-hydroxydopamine lesions in the rat. Neurosci. 53 (1993) 447-455
    • (1993) Neurosci. , vol.53 , pp. 447-455
    • Jenkins, R.1    O'Shea, R.2    Thomas, K.L.3    Hunt, S.P.4
  • 36
    • 0030608467 scopus 로고    scopus 로고
    • Medial septal cholinergic neurons express c-Jun but do not undergo DNA fragmentation after fornix-fimbria transections.
    • Butterworth N.J., and Dragunow M. Medial septal cholinergic neurons express c-Jun but do not undergo DNA fragmentation after fornix-fimbria transections. Mol. Brain Res. 43 (1996) 1-12
    • (1996) Mol. Brain Res. , vol.43 , pp. 1-12
    • Butterworth, N.J.1    Dragunow, M.2
  • 37
    • 0025935250 scopus 로고
    • Selective expression of Jun proteins following axotomy and axonal-transport block in peripheral nerves in the rat- evidence for a role in the regeneration process.
    • Leah J.D., Herdegen T., and Bravo R. Selective expression of Jun proteins following axotomy and axonal-transport block in peripheral nerves in the rat- evidence for a role in the regeneration process. Brain Res. 566 (1991) 198-207
    • (1991) Brain Res. , vol.566 , pp. 198-207
    • Leah, J.D.1    Herdegen, T.2    Bravo, R.3
  • 38
    • 0028202877 scopus 로고
    • The differential control of c-Jun expression in regenerating sensory neurons and their association with glial cells.
    • Defelipe C., and Hunt S.P. The differential control of c-Jun expression in regenerating sensory neurons and their association with glial cells. J. Neurosci. 14 (1994) 2911-2923
    • (1994) J. Neurosci. , vol.14 , pp. 2911-2923
    • Defelipe, C.1    Hunt, S.P.2
  • 39
    • 0028356223 scopus 로고
    • Immediate-early gene protein expression in neurons undergoing delayed death, but not necrosis, following hypoxic-ischemic injury to the young rat brain
    • Draganow M., Beilharz E., Sirimane E., Lawlor P., Williams C., Brave R., and Gluckman P. Immediate-early gene protein expression in neurons undergoing delayed death, but not necrosis, following hypoxic-ischemic injury to the young rat brain. Mol. Brain Res. 25 (1994) 19-33
    • (1994) Mol. Brain Res. , vol.25 , pp. 19-33
    • Draganow, M.1    Beilharz, E.2    Sirimane, E.3    Lawlor, P.4    Williams, C.5    Brave, R.6    Gluckman, P.7
  • 40
    • 0032909368 scopus 로고    scopus 로고
    • Activity and expression of JNK1, p38 and ERK kinases, c-Jun N-terminal phosphorylation, and c-jun promoter binding in the adult rat brain following kainate-induced seizures.
    • Mielke K., Brecht S., Dorst A., and Herdegen T. Activity and expression of JNK1, p38 and ERK kinases, c-Jun N-terminal phosphorylation, and c-jun promoter binding in the adult rat brain following kainate-induced seizures. Neuroscience 91 (1999) 471-483
    • (1999) Neuroscience , vol.91 , pp. 471-483
    • Mielke, K.1    Brecht, S.2    Dorst, A.3    Herdegen, T.4
  • 41
    • 0032527879 scopus 로고    scopus 로고
    • Lasting N-terminal phosphorylation of c-Jun and activation of c-Jun N-terminal kinases after neuronal injury.
    • Herdegen T., Claret F.X., Kallunli T., Martin-Villalba A., Winter C., Hunter T., and Karin M. Lasting N-terminal phosphorylation of c-Jun and activation of c-Jun N-terminal kinases after neuronal injury. J. Neurosci. 18 (1998) 5124-5135
    • (1998) J. Neurosci. , vol.18 , pp. 5124-5135
    • Herdegen, T.1    Claret, F.X.2    Kallunli, T.3    Martin-Villalba, A.4    Winter, C.5    Hunter, T.6    Karin, M.7
  • 45
    • 0033118607 scopus 로고    scopus 로고
    • The Jnk1 and Jnk2 protein kinases are required for regional specific apoptosis during early brain development.
    • Kuan C.Y., Yang D.D., Samanta D.R., Davis R.J., Rakic P., and Flavell R.A. The Jnk1 and Jnk2 protein kinases are required for regional specific apoptosis during early brain development. Neuron 22 (1999) 667-676
    • (1999) Neuron , vol.22 , pp. 667-676
    • Kuan, C.Y.1    Yang, D.D.2    Samanta, D.R.3    Davis, R.J.4    Rakic, P.5    Flavell, R.A.6
  • 46
    • 0029976253 scopus 로고    scopus 로고
    • DNA damage and apoptosis in Alzheimer's disease: Colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay.
    • Anderson A.J., Su J.H., and Cotman C.W. DNA damage and apoptosis in Alzheimer's disease: Colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay. J. Neurosci. 16 (1996) 1710-1719
    • (1996) J. Neurosci. , vol.16 , pp. 1710-1719
    • Anderson, A.J.1    Su, J.H.2    Cotman, C.W.3
  • 47
    • 0030943263 scopus 로고    scopus 로고
    • Stress-activated protein kinase/c-Jun N-terminal kinase phosphorylates x protein.
    • Reynolds C.H., Utton M.A., Gibb G.M., Yates A., and Anderton B.H. Stress-activated protein kinase/c-Jun N-terminal kinase phosphorylates x protein. J. Neurochem. 68 (1997) 1736-1744
    • (1997) J. Neurochem. , vol.68 , pp. 1736-1744
    • Reynolds, C.H.1    Utton, M.A.2    Gibb, G.M.3    Yates, A.4    Anderton, B.H.5
  • 48
    • 0022500301 scopus 로고
    • K-252a, A potent inhibitor of protein kinase C from microbial origin
    • Kase H., Iwahashi K., and Matsuda Y. K-252a, A potent inhibitor of protein kinase C from microbial origin. J. Antibiot. (Tokyo) 39 (1986) 1059-1065
    • (1986) J. Antibiot. (Tokyo) , vol.39 , pp. 1059-1065
    • Kase, H.1    Iwahashi, K.2    Matsuda, Y.3
  • 50
    • 0026595294 scopus 로고
    • K-252 compounds: modulators of neurotrophic signal transduction.
    • Knusel B., and Hefti F. K-252 compounds: modulators of neurotrophic signal transduction. J. Neurochem. 59 (1992) 1987-1996
    • (1992) J. Neurochem. , vol.59 , pp. 1987-1996
    • Knusel, B.1    Hefti, F.2
  • 51
    • 0028870428 scopus 로고
    • K-252a induces tyrosine phosphorylation of the focal adhesion kinase and neurite outgrowth in human neuroblastoma SH-SY5Y cells.
    • Maroney A.C., Lipfert L., Forbes M.E., Glicksman M.A., Neff N.T., Siman R., and Dionne C.A. K-252a induces tyrosine phosphorylation of the focal adhesion kinase and neurite outgrowth in human neuroblastoma SH-SY5Y cells. J. Neurochem. 64 (1995) 540-549
    • (1995) J. Neurochem. , vol.64 , pp. 540-549
    • Maroney, A.C.1    Lipfert, L.2    Forbes, M.E.3    Glicksman, M.A.4    Neff, N.T.5    Siman, R.6    Dionne, C.A.7
  • 52
    • 0025190264 scopus 로고
    • Differential effects of the protein kinase inhibitor K-252a on the in vitro survival of chick embryonic neurons
    • Borasio G.D. Differential effects of the protein kinase inhibitor K-252a on the in vitro survival of chick embryonic neurons. Neurosci. Lett. 108 (1990) 207-212
    • (1990) Neurosci. Lett. , vol.108 , pp. 207-212
    • Borasio, G.D.1
  • 54
    • 0028938472 scopus 로고
    • K-252a promotes survival and choline acetyltransferase activity in striatal and basal forebrain neuronal cultures.
    • Glicksman M.A., Forbes M.E., Prantner J.E., and Neff N.T. K-252a promotes survival and choline acetyltransferase activity in striatal and basal forebrain neuronal cultures. J. Neurochem. 64 (1995) 1502-1512
    • (1995) J. Neurochem. , vol.64 , pp. 1502-1512
    • Glicksman, M.A.1    Forbes, M.E.2    Prantner, J.E.3    Neff, N.T.4
  • 55
    • 0028220675 scopus 로고
    • Staurosporine, K-252a and K-252b stabilize calcium homeostasis and promote survival of CNS neurons in the absence of glucose.
    • Cheng B., Barger S.W., and Mattson M.P. Staurosporine, K-252a and K-252b stabilize calcium homeostasis and promote survival of CNS neurons in the absence of glucose. J. Neurochem. 62 (1994) 1319-1329
    • (1994) J. Neurochem. , vol.62 , pp. 1319-1329
    • Cheng, B.1    Barger, S.W.2    Mattson, M.P.3
  • 56
    • 0028229755 scopus 로고
    • Staurosporine and K-252a compounds protect hippocampal neurons against amyloid β-peptide toxicity and oxidative injury.
    • Goodman Y., and Mattson M.P. Staurosporine and K-252a compounds protect hippocampal neurons against amyloid β-peptide toxicity and oxidative injury. Brain Res. 650 (1994) 170-174
    • (1994) Brain Res. , vol.650 , pp. 170-174
    • Goodman, Y.1    Mattson, M.P.2
  • 58
    • 0023932343 scopus 로고
    • Inhibition by K-252a, a new inhibitor of protein kinase, of nerve growth factor-induced neurite outgrowth of chick embryo dorsal root ganglion cells.
    • Matsuda Y., and Fukuda J. Inhibition by K-252a, a new inhibitor of protein kinase, of nerve growth factor-induced neurite outgrowth of chick embryo dorsal root ganglion cells. J. Neurosci. Lett. 87 (1988) 11-17
    • (1988) J. Neurosci. Lett. , vol.87 , pp. 11-17
    • Matsuda, Y.1    Fukuda, J.2
  • 59
    • 0024094842 scopus 로고
    • K-252a, a potent protein kinase inhibitor, blocks nerve growth factor-induced neurite outgrowth and changes in the phosphorylation of proteins in PC 12 cells.
    • Hashimoto S. K-252a, a potent protein kinase inhibitor, blocks nerve growth factor-induced neurite outgrowth and changes in the phosphorylation of proteins in PC 12 cells. J. Cell Biol. 107 (1988) 1531-1539
    • (1988) J. Cell Biol. , vol.107 , pp. 1531-1539
    • Hashimoto, S.1
  • 60
    • 0026512998 scopus 로고
    • K-252a inhibits nerve growth factor-induced trk proto-oncogene tyrosine phosphorylation and kinase activity.
    • Berg M.M., Sternberg D.W., Parada L.F., and Chao M.V. K-252a inhibits nerve growth factor-induced trk proto-oncogene tyrosine phosphorylation and kinase activity. J. Biol. Chem. 267 (1992) 13-16
    • (1992) J. Biol. Chem. , vol.267 , pp. 13-16
    • Berg, M.M.1    Sternberg, D.W.2    Parada, L.F.3    Chao, M.V.4
  • 61
    • 0026563244 scopus 로고
    • K-252a is a selective inhibitor of the tyrosine protein kinase activity of the trk family of oncogenes and neurotrophin receptors.
    • Tapley P., Lamballe F., and Barbacid M. K-252a is a selective inhibitor of the tyrosine protein kinase activity of the trk family of oncogenes and neurotrophin receptors. Oncogene 7 (1992) 371-381
    • (1992) Oncogene , vol.7 , pp. 371-381
    • Tapley, P.1    Lamballe, F.2    Barbacid, M.3
  • 62
    • 0026684676 scopus 로고
    • Inhibition of the cellular actions of nerve growth factor by staurosporine and K-252a results from the attenuation of the activity of the trk tyrosine kinase.
    • Ohmichi M., Decker S.J., Pang I., and Saltiel A.R. Inhibition of the cellular actions of nerve growth factor by staurosporine and K-252a results from the attenuation of the activity of the trk tyrosine kinase. Biochemistry 31 (1992) 4034-4039
    • (1992) Biochemistry , vol.31 , pp. 4034-4039
    • Ohmichi, M.1    Decker, S.J.2    Pang, I.3    Saltiel, A.R.4
  • 63
    • 0026648471 scopus 로고
    • Specific inhibition of NGF receptor tyrosine kinase activity by K-252a.
    • Muroya K., Hashimoto Y., Hattori S., and Nakamuru S. Specific inhibition of NGF receptor tyrosine kinase activity by K-252a. Biochim. Biophys. Acta. 1135 (1992) 353-356
    • (1992) Biochim. Biophys. Acta. , vol.1135 , pp. 353-356
    • Muroya, K.1    Hashimoto, Y.2    Hattori, S.3    Nakamuru, S.4
  • 68
    • 0032507611 scopus 로고    scopus 로고
    • CEP-1347/KT7515, a JNK pathway inhibitor supports the in vitro survival of chick embryonic neurons.
    • Borasio G.D., Hostmann S., Anneser J.M.H., Neff N.T., and Glicksman M.A. CEP-1347/KT7515, a JNK pathway inhibitor supports the in vitro survival of chick embryonic neurons. NeuroReport 9 (1998) 1435-1439
    • (1998) NeuroReport , vol.9 , pp. 1435-1439
    • Borasio, G.D.1    Hostmann, S.2    Anneser, J.M.H.3    Neff, N.T.4    Glicksman, M.A.5
  • 70
    • 0028263060 scopus 로고
    • Skeletal muscle-derived trophic factors prevent motoneurons from entering an active cell death program in vitro.
    • Cornelia J.X., Sanz-Rodriguez C., Aldea M., and Esquerda J.E. Skeletal muscle-derived trophic factors prevent motoneurons from entering an active cell death program in vitro. J. Neurosci. 14 (1994) 2674-2686
    • (1994) J. Neurosci. , vol.14 , pp. 2674-2686
    • Cornelia, J.X.1    Sanz-Rodriguez, C.2    Aldea, M.3    Esquerda, J.E.4
  • 71
    • 0028286296 scopus 로고
    • Motoneurons deprived of trophic support in vitro require new gene expression to undergo programmed cell death.
    • Milligan C.E., Oppenheim R.W., and Schwartz L.M. Motoneurons deprived of trophic support in vitro require new gene expression to undergo programmed cell death. J. Neurohiol. 25 (1994) 1005-1016
    • (1994) J. Neurohiol. , vol.25 , pp. 1005-1016
    • Milligan, C.E.1    Oppenheim, R.W.2    Schwartz, L.M.3
  • 72
    • 0025514410 scopus 로고
    • Survival effect of ciliary neurotrophic factor (CNTF) on chick embryonic motoneurons in culture: Comparison with other neurotrophic factors and cytokines.
    • Arakawa Y., Sendtner M., and Thoenen H. Survival effect of ciliary neurotrophic factor (CNTF) on chick embryonic motoneurons in culture: Comparison with other neurotrophic factors and cytokines. J Neurosci. 10 (1990) 3507-3515
    • (1990) J Neurosci. , vol.10 , pp. 3507-3515
    • Arakawa, Y.1    Sendtner, M.2    Thoenen, H.3
  • 73
    • 0027131764 scopus 로고
    • Members of several gene families influence survival of rat motoneuronsin vitro and in vivo
    • Hughes R.A., Sendtner M., and Thoenen H. Members of several gene families influence survival of rat motoneuronsin vitro and in vivo. J. Neurosci. Res. 36 (1993) 663-671
    • (1993) J. Neurosci. Res. , vol.36 , pp. 663-671
    • Hughes, R.A.1    Sendtner, M.2    Thoenen, H.3
  • 77
    • 0029860936 scopus 로고    scopus 로고
    • Ultraviolet light and osmotic stress: Activation of the JNK cascade through multiple growth factor and cytokine receptors.
    • Rosette C., and Karin M. Ultraviolet light and osmotic stress: Activation of the JNK cascade through multiple growth factor and cytokine receptors. Science 274 (1996) 1194-1197
    • (1996) Science , vol.274 , pp. 1194-1197
    • Rosette, C.1    Karin, M.2
  • 78
    • 0030134173 scopus 로고    scopus 로고
    • The stress-activated protein kinase pathway mediates cell death following injury induced bycis-platinum, UV irradiation or heat
    • Zanke B.W., Boudreau K., Rubie E., Winnett E., Tibbies L.A., Zon L., Kyriakis J., Liu F.-F., and Woodgett J.R. The stress-activated protein kinase pathway mediates cell death following injury induced bycis-platinum, UV irradiation or heat. Current Biol. 6 (1996) 606-613
    • (1996) Current Biol. , vol.6 , pp. 606-613
    • Zanke, B.W.1    Boudreau, K.2    Rubie, E.3    Winnett, E.4    Tibbies, L.A.5    Zon, L.6    Kyriakis, J.7    Liu, F.-F.8    Woodgett, J.R.9
  • 79
    • 0028935270 scopus 로고    scopus 로고
    • Proinflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine.
    • Raingeaud J., Gupta S., Rogers J.S., Dickens M., Han J., Ulevitch R.J., and Davis R.J. Proinflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J. Biol. Chem. 270 (1996) 7420-7426
    • (1996) J. Biol. Chem. , vol.270 , pp. 7420-7426
    • Raingeaud, J.1    Gupta, S.2    Rogers, J.S.3    Dickens, M.4    Han, J.5    Ulevitch, R.J.6    Davis, R.J.7
  • 80
    • 0028022750 scopus 로고
    • A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins.
    • Rouse J., Cohen P., Trigon S., Morange M., Alonso-Llamazares A., Zamanillo D., Hunt T., and Nebreda A.R. A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. Cell 78 (1994) 1027-1037
    • (1994) Cell , vol.78 , pp. 1027-1037
    • Rouse, J.1    Cohen, P.2    Trigon, S.3    Morange, M.4    Alonso-Llamazares, A.5    Zamanillo, D.6    Hunt, T.7    Nebreda, A.R.8
  • 81
    • 0028988138 scopus 로고
    • SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1.
    • Cuenda A., Rouse J., Doza Y.R., Meier R., Cohen P., Gallagher T.F., Young P.R., and Lee J.C. SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1. FEBS Lett. 364 (1995) 229-233
    • (1995) FEBS Lett. , vol.364 , pp. 229-233
    • Cuenda, A.1    Rouse, J.2    Doza, Y.R.3    Meier, R.4    Cohen, P.5    Gallagher, T.F.6    Young, P.R.7    Lee, J.C.8
  • 82
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate, and neurodegenerative disorders.
    • Coyle J.T., and Puttfarcken P. Oxidative stress, glutamate, and neurodegenerative disorders. Science 262 (1993) 689-694
    • (1993) Science , vol.262 , pp. 689-694
    • Coyle, J.T.1    Puttfarcken, P.2
  • 83
    • 0029257385 scopus 로고
    • Oxidative stress, age-related neurodegeneration and the potential for neurotrophic treatment. Cerebrovasc.
    • Williams L.R. Oxidative stress, age-related neurodegeneration and the potential for neurotrophic treatment. Cerebrovasc. Brain Metah. Rec. 7 (1993) 55-73
    • (1993) Brain Metah. Rec. , vol.7 , pp. 55-73
    • Williams, L.R.1
  • 85
    • 0032692497 scopus 로고    scopus 로고
    • CEP-1347 (KT7515), an inhibitor of JNK activation, rescues sympathetic neurons and neuronally differentiated PC 12 Cells from death evoked by three distinct insults.
    • Maroney A.C., Finn J.P., Bozyczko-Coyne D., O'Kane T., Neff N.T., Tolkovsky A.M., Park D.S., Yan C.Y.I., Troy C.M., and Greene L.A. CEP-1347 (KT7515), an inhibitor of JNK activation, rescues sympathetic neurons and neuronally differentiated PC 12 Cells from death evoked by three distinct insults. J. Neurochem. 73 (1999) 1901-1912
    • (1999) J. Neurochem. , vol.73 , pp. 1901-1912
    • Maroney, A.C.1    Finn, J.P.2    Bozyczko-Coyne, D.3    O'Kane, T.4    Neff, N.T.5    Tolkovsky, A.M.6    Park, D.S.7    Yan, C.Y.I.8    Troy, C.M.9    Greene, L.A.10
  • 86
    • 0031915545 scopus 로고    scopus 로고
    • Multiple pathways of neuronal death induced by DNA-damaging agents, NGF deprivation, and oxidative stress.
    • Park D.S., Morris E.J., Stefanis L., Troy C.M., Shelanski M.L., Geller H.M., and Greene L.A. Multiple pathways of neuronal death induced by DNA-damaging agents, NGF deprivation, and oxidative stress. J. Neurosci. 18 (1998) 830-840
    • (1998) J. Neurosci. , vol.18 , pp. 830-840
    • Park, D.S.1    Morris, E.J.2    Stefanis, L.3    Troy, C.M.4    Shelanski, M.L.5    Geller, H.M.6    Greene, L.A.7
  • 87
    • 0028924419 scopus 로고
    • Role of mitogen activated protein kinase phosphatase during the cellular response to genotoxic stress.
    • Liu Y., Gorospe M., Yang C., and Holbrook N.J. Role of mitogen activated protein kinase phosphatase during the cellular response to genotoxic stress. J. Biol. Chem. 270 (1995) 8377-8380
    • (1995) J. Biol. Chem. , vol.270 , pp. 8377-8380
    • Liu, Y.1    Gorospe, M.2    Yang, C.3    Holbrook, N.J.4
  • 88
    • 0029753773 scopus 로고    scopus 로고
    • The role of c-Jun N-terminal kinase (JNK) in apoptosis induced by ultraviolet C and y radiation.
    • Chen Y.R., Wang X., Templeton D., David R.J., and Tan T.H. The role of c-Jun N-terminal kinase (JNK) in apoptosis induced by ultraviolet C and y radiation. J. Biol. Chem. 271 (1996) 31929-31936
    • (1996) J. Biol. Chem. , vol.271 , pp. 31929-31936
    • Chen, Y.R.1    Wang, X.2    Templeton, D.3    David, R.J.4    Tan, T.H.5
  • 89
    • 0029890689 scopus 로고    scopus 로고
    • The contrasting roles of ICE family proteases and interleukin 1-β in apoptosis induced by trophic factor withdrawal and by copper/zinc superoxide dismutase down-regulation.
    • Troy C.M., Stefanis L., Prochiantz A., Greene L.A., and Shelanski M.L. The contrasting roles of ICE family proteases and interleukin 1-β in apoptosis induced by trophic factor withdrawal and by copper/zinc superoxide dismutase down-regulation. Proc. Natl. Acad. Sci. USA 93 (1996) 5635-5640
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5635-5640
    • Troy, C.M.1    Stefanis, L.2    Prochiantz, A.3    Greene, L.A.4    Shelanski, M.L.5
  • 90
    • 0030640926 scopus 로고    scopus 로고
    • Mechanisms of neuronal degeneration: A final common pathway?
    • Troy C.M., Stefanis L., Greene L.A., and Shelanski M.L. Mechanisms of neuronal degeneration: A final common pathway?. Neurol. 72 (1997) 103-111
    • (1997) Neurol. , vol.72 , pp. 103-111
    • Troy, C.M.1    Stefanis, L.2    Greene, L.A.3    Shelanski, M.L.4
  • 91
    • 0031018396 scopus 로고    scopus 로고
    • Nedd2 is required for apoptosis after trophic factor withdrawal, but not superoxide dismutase (SOD-1) down regulation, in sympathetic neurons and PC12 cells.
    • Troy C.M., Stefanis L., Greene L.A., and Shelanski M.L. Nedd2 is required for apoptosis after trophic factor withdrawal, but not superoxide dismutase (SOD-1) down regulation, in sympathetic neurons and PC12 cells. J. Neurosci. 17 (1997) 1911-1918
    • (1997) J. Neurosci. , vol.17 , pp. 1911-1918
    • Troy, C.M.1    Stefanis, L.2    Greene, L.A.3    Shelanski, M.L.4
  • 92
    • 0028364545 scopus 로고
    • Activation-induced apoptosis in lymphocytes.
    • Green D.R., and Scott D.W. Activation-induced apoptosis in lymphocytes. Curr. Opin. Immunol. 6 (1994) 476-487
    • (1994) Curr. Opin. Immunol. , vol.6 , pp. 476-487
    • Green, D.R.1    Scott, D.W.2
  • 93
    • 0029892754 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 suppression of tumor necrosis factor α-mediated apoptosis requires RAS and the activation of mitogen-activated protein kinase.
    • Gardner A.M., and Johnson G.L. Fibroblast growth factor-2 suppression of tumor necrosis factor α-mediated apoptosis requires RAS and the activation of mitogen-activated protein kinase. J. Biol. Chem. 271 (1996) 14560-14566
    • (1996) J. Biol. Chem. , vol.271 , pp. 14560-14566
    • Gardner, A.M.1    Johnson, G.L.2
  • 94
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor I effector functions: JNK activation is not linked to apoptosis while NF-κB activation prevents cell death.
    • Liu A.-G., Hsu H., Goeddel D.V., and Karin M. Dissection of TNF receptor I effector functions: JNK activation is not linked to apoptosis while NF-κB activation prevents cell death. Cell 87 (1996) 565-576
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu, A.-G.1    Hsu, H.2    Goeddel, D.V.3    Karin, M.4
  • 97
    • 0031883140 scopus 로고    scopus 로고
    • The c-Jun N-terminal kinase cascade plays a role in stress-induced apoptosis in Jurkat cells by up-regulating Fas ligand expression.
    • Faris M., Kokot N., Latinis K., Kasibhatla S., Green D.R., Koretzky G.A., and Nel A. The c-Jun N-terminal kinase cascade plays a role in stress-induced apoptosis in Jurkat cells by up-regulating Fas ligand expression. J. Immunology 160 (1998) 134-144
    • (1998) J. Immunology , vol.160 , pp. 134-144
    • Faris, M.1    Kokot, N.2    Latinis, K.3    Kasibhatla, S.4    Green, D.R.5    Koretzky, G.A.6    Nel, A.7
  • 100
    • 77956685671 scopus 로고
    • Cell death of motor neurons in the chick embryo spinal cord.
    • Chu-Wang L.-W., and Oppenheimer R.W. Cell death of motor neurons in the chick embryo spinal cord. J. Comp. Neurol. 777 (1978) 33-57
    • (1978) J. Comp. Neurol. , vol.777 , pp. 33-57
    • Chu-Wang, L.-W.1    Oppenheimer, R.W.2
  • 101
    • 0022397928 scopus 로고
    • Androgens prevent normally occurring cell death in a sexually dimorphic spinal nucleus.
    • Nordeen E.J., Nordeen K.W., Sengelaub D.R., and Arnold A.P. Androgens prevent normally occurring cell death in a sexually dimorphic spinal nucleus. Science 229 (1985) 671-673
    • (1985) Science , vol.229 , pp. 671-673
    • Nordeen, E.J.1    Nordeen, K.W.2    Sengelaub, D.R.3    Arnold, A.P.4
  • 102
    • 0026058318 scopus 로고
    • Cell death during development of the nervous system.
    • Oppenheim R.W. Cell death during development of the nervous system. Ann. Rev. Neurosci. 14 (1991) 453-501
    • (1991) Ann. Rev. Neurosci. , vol.14 , pp. 453-501
    • Oppenheim, R.W.1
  • 103
    • 0019972810 scopus 로고
    • The cholinergic hypothesis of geriatric memory dysfunction.
    • Bartus R.T., Dean R.L., Beer B., and Lippa A.S. The cholinergic hypothesis of geriatric memory dysfunction. Science 217 (1982) 408-414
    • (1982) Science , vol.217 , pp. 408-414
    • Bartus, R.T.1    Dean, R.L.2    Beer, B.3    Lippa, A.S.4
  • 104
    • 0025938569 scopus 로고
    • The basal forebrain-cortical cholinergic system: interpreting the function consequences of excitotoxic lesions.
    • Dunnett S.B., Everitt B.J., and Robbins T.W. The basal forebrain-cortical cholinergic system: interpreting the function consequences of excitotoxic lesions. Trends Neurosci. 14 (1991) 494-501
    • (1991) Trends Neurosci. , vol.14 , pp. 494-501
    • Dunnett, S.B.1    Everitt, B.J.2    Robbins, T.W.3
  • 105
    • 0041125361 scopus 로고
    • The organization and some projections of cholinergic neurons of the mammalian forebrain.
    • Fibiger H.C. The organization and some projections of cholinergic neurons of the mammalian forebrain. Brain Res. Rev. 4 (1982) 327-388
    • (1982) Brain Res. Rev. , vol.4 , pp. 327-388
    • Fibiger, H.C.1
  • 106
    • 0025782928 scopus 로고
    • Cholinergic mechanisms in learning memory and dementia: a review of recent evidence.
    • Fibiger H.C. Cholinergic mechanisms in learning memory and dementia: a review of recent evidence. Trends Neurosci. 14 (1991) 220-223
    • (1991) Trends Neurosci. , vol.14 , pp. 220-223
    • Fibiger, H.C.1
  • 107
    • 0020072221 scopus 로고
    • Alzheimer's disease and senile dementia: Loss of neurons in the basal forebrain.
    • Whitehouse P.J., Price D.L., Struble R.O., Clark A.W., and Delong M.R. Alzheimer's disease and senile dementia: Loss of neurons in the basal forebrain. Science 215 (1982) 237-1239
    • (1982) Science , vol.215 , pp. 237-1239
    • Whitehouse, P.J.1    Price, D.L.2    Struble, R.O.3    Clark, A.W.4    Delong, M.R.5
  • 108
    • 0002083998 scopus 로고
    • Dementia: animal models of the cognitive impairments produced by degeneration of the basal forebrain cholinergic system
    • Meltzer H.Y. (Ed), Raven Press, New York
    • Olton D.S., and Wenk G.L. Dementia: animal models of the cognitive impairments produced by degeneration of the basal forebrain cholinergic system. In: Meltzer H.Y. (Ed). Psychopharma-cology: The Third Generation of Progress (1987), Raven Press, New York 941-953
    • (1987) Psychopharma-cology: The Third Generation of Progress , pp. 941-953
    • Olton, D.S.1    Wenk, G.L.2
  • 109
    • 0023929304 scopus 로고
    • Animal models of Alzheimer's disease: experimental cholinergic denervation.
    • Smith G. Animal models of Alzheimer's disease: experimental cholinergic denervation. Brain Res. Rev. 13 (1988) 103-118
    • (1988) Brain Res. Rev. , vol.13 , pp. 103-118
    • Smith, G.1
  • 110
    • 0034125843 scopus 로고    scopus 로고
    • On neurodegenerative diseases, models, and treatment strategies: lessons learned and lessons forgotten a generation following the cholinergic hypothesis.
    • Bartus R.T. On neurodegenerative diseases, models, and treatment strategies: lessons learned and lessons forgotten a generation following the cholinergic hypothesis. Exp. Neurol. 163 (2000) 495-529
    • (2000) Exp. Neurol. , vol.163 , pp. 495-529
    • Bartus, R.T.1
  • 111
    • 0022639418 scopus 로고
    • Pilocarpine and physostigmine attenuate spatial memory impairments produced by lesions of the NBM.
    • Murray C.L., and Fibiger H.C. Pilocarpine and physostigmine attenuate spatial memory impairments produced by lesions of the NBM. Behav. Neurosci. 100 (1986) 23-32
    • (1986) Behav. Neurosci. , vol.100 , pp. 23-32
    • Murray, C.L.1    Fibiger, H.C.2
  • 112
    • 0024309694 scopus 로고
    • Spatial learning in rats: correlation with cortical choline acetyltransferase and improvement with NGF following nbm damage.
    • Mandel R.J., Gage F.H., and Thai L.J. Spatial learning in rats: correlation with cortical choline acetyltransferase and improvement with NGF following nbm damage. Exp. Neurol. 104 (1989) 208-217
    • (1989) Exp. Neurol. , vol.104 , pp. 208-217
    • Mandel, R.J.1    Gage, F.H.2    Thai, L.J.3
  • 113
    • 0026598881 scopus 로고
    • Widespread neuronal degeneration after ibotenic acid lesioning of cholinergic neurons in the nucleus basalis revealed by in situ hybridization.
    • Lindefors N., Boatel M.L., Mahy N., and Persson H. Widespread neuronal degeneration after ibotenic acid lesioning of cholinergic neurons in the nucleus basalis revealed by in situ hybridization. Neurosci. Lett. 135 (1992) 262-264
    • (1992) Neurosci. Lett. , vol.135 , pp. 262-264
    • Lindefors, N.1    Boatel, M.L.2    Mahy, N.3    Persson, H.4
  • 114
    • 0020686674 scopus 로고
    • AD: a disorder of cortical cholinergic innervation.
    • Coyle J.T. AD: a disorder of cortical cholinergic innervation. Science 219 (1983) 1184-1190
    • (1983) Science , vol.219 , pp. 1184-1190
    • Coyle, J.T.1
  • 115
    • 0027087240 scopus 로고
    • Basal forebrain neurons and memory: A biochemical, histological, and behavioral study of differential vulnerability to ibotenate and quisqualate
    • Wenk G.L., Harrington C.A., Tucker D.A., Ranee N.E., and Walker L.C. Basal forebrain neurons and memory: A biochemical, histological, and behavioral study of differential vulnerability to ibotenate and quisqualate. Behav. Neurosci. (1992) 909-923
    • (1992) Behav. Neurosci. , pp. 909-923
    • Wenk, G.L.1    Harrington, C.A.2    Tucker, D.A.3    Ranee, N.E.4    Walker, L.C.5
  • 116
    • 0032100520 scopus 로고    scopus 로고
    • Preservation of cholinergic activity and prevention of neuron death by CEP-1347/KT-7515 following excitotoxic injury of the nucleus basalis magnocellularis.
    • Saporito M.S., Brown E.R., Miller M.S., Murakata C., Neff N.H., Vaught J.L., and Carswell S. Preservation of cholinergic activity and prevention of neuron death by CEP-1347/KT-7515 following excitotoxic injury of the nucleus basalis magnocellularis. Neuroscience 86 (1998) 461-472
    • (1998) Neuroscience , vol.86 , pp. 461-472
    • Saporito, M.S.1    Brown, E.R.2    Miller, M.S.3    Murakata, C.4    Neff, N.H.5    Vaught, J.L.6    Carswell, S.7
  • 117
    • 0021988440 scopus 로고
    • Cholinergic projections from the basal forebrain to the basolateral amygdaloid complex: A combined retrograde fluorescent and immunohistochemical study.
    • Carlsen J., Zaborszky L., and Heimer L. Cholinergic projections from the basal forebrain to the basolateral amygdaloid complex: A combined retrograde fluorescent and immunohistochemical study. J. Comp. Neurol. 234 (1985) 155-167
    • (1985) J. Comp. Neurol. , vol.234 , pp. 155-167
    • Carlsen, J.1    Zaborszky, L.2    Heimer, L.3
  • 118
    • 0030004870 scopus 로고    scopus 로고
    • Behavioral vigilance following infusions of 192 IgG-saporin into the basal forebrain: selectivity of the behavioral impairment and relation to cortical AChE-positive fiber density.
    • Mcgaughy J., Kaiser T., and Sarter M. Behavioral vigilance following infusions of 192 IgG-saporin into the basal forebrain: selectivity of the behavioral impairment and relation to cortical AChE-positive fiber density. Behav. Neurosci. 110 (1996) 247-265
    • (1996) Behav. Neurosci. , vol.110 , pp. 247-265
    • Mcgaughy, J.1    Kaiser, T.2    Sarter, M.3
  • 119
    • 0026724263 scopus 로고
    • Attentional functions of the forebrain cholinergic systems: effects of intraventricular hemicholinium, physostigmine, basal forebrain lesions and intracortical grafts on a multiple-choice serial reaction time task.
    • Muir J.L., Dunnett S.B., Robbins T.W., and Everitt B.J. Attentional functions of the forebrain cholinergic systems: effects of intraventricular hemicholinium, physostigmine, basal forebrain lesions and intracortical grafts on a multiple-choice serial reaction time task. Exp. Brain Res. 89 (1992) 611-622
    • (1992) Exp. Brain Res. , vol.89 , pp. 611-622
    • Muir, J.L.1    Dunnett, S.B.2    Robbins, T.W.3    Everitt, B.J.4
  • 120
    • 0028316603 scopus 로고
    • AMPA-induced excitotoxic lesions of the basal forebrain: a significant role for the cortical cholinergic system in attentional function.
    • Muir J.L., Everitt B.J., and Robbins T.W. AMPA-induced excitotoxic lesions of the basal forebrain: a significant role for the cortical cholinergic system in attentional function. J. Neurosci. 14 (1994) 2313-2326
    • (1994) J. Neurosci. , vol.14 , pp. 2313-2326
    • Muir, J.L.1    Everitt, B.J.2    Robbins, T.W.3
  • 121
    • 0028090036 scopus 로고
    • Behavioural, histochemical and biochemical consequences of selective immunolesions in discrete regions of the basal forebrain cholinergic system.
    • Torres E.M., Perry T.A., Blockland A., Wilkinson L.S., Wiley R.G., Lappi D.A., and Dunnet S.B. Behavioural, histochemical and biochemical consequences of selective immunolesions in discrete regions of the basal forebrain cholinergic system. Neuroscience 63 (1994) 95-122
    • (1994) Neuroscience , vol.63 , pp. 95-122
    • Torres, E.M.1    Perry, T.A.2    Blockland, A.3    Wilkinson, L.S.4    Wiley, R.G.5    Lappi, D.A.6    Dunnet, S.B.7
  • 122
    • 0031981009 scopus 로고    scopus 로고
    • Light deprivation accelerates recovery from frontal cortical neglect: relation to locomotion and striatal Fos expression.
    • Vargo J.M., Lai H.V., and Marshall J.F. Light deprivation accelerates recovery from frontal cortical neglect: relation to locomotion and striatal Fos expression. Behav. Neurosci. 112 (1998) 387-398
    • (1998) Behav. Neurosci. , vol.112 , pp. 387-398
    • Vargo, J.M.1    Lai, H.V.2    Marshall, J.F.3
  • 123
    • 58149205575 scopus 로고
    • Attention and brain function in Alzheimer's Disease: a review.
    • Parasuraman R., and Haxby J.V. Attention and brain function in Alzheimer's Disease: a review. Neuropsychology 7 (1993) 242-272
    • (1993) Neuropsychology , vol.7 , pp. 242-272
    • Parasuraman, R.1    Haxby, J.V.2
  • 125
    • 0026654156 scopus 로고
    • Effect of delayed treatment with nerve growth factor on choline acetyltransferase activity in the cortex of rats with lesions of the nucleus basalis magno-cellularis: dose requirements.
    • Dekker A.J., and Thai L.J. Effect of delayed treatment with nerve growth factor on choline acetyltransferase activity in the cortex of rats with lesions of the nucleus basalis magno-cellularis: dose requirements. Brain Res. 584 (1992) 55-63
    • (1992) Brain Res. , vol.584 , pp. 55-63
    • Dekker, A.J.1    Thai, L.J.2
  • 126
    • 0028353076 scopus 로고
    • Grafting of nerve growth factor-producing fibroblasts reduces behavioral deficits in rats with lesions of the nucleus basalis magnocellularis.
    • Dekker A.J., Winkler J., Ray J., Thai L.J., and Gage F.H. Grafting of nerve growth factor-producing fibroblasts reduces behavioral deficits in rats with lesions of the nucleus basalis magnocellularis. Neuroscience 60 (1994) 299-309
    • (1994) Neuroscience , vol.60 , pp. 299-309
    • Dekker, A.J.1    Winkler, J.2    Ray, J.3    Thai, L.J.4    Gage, F.H.5
  • 127
    • 0024354790 scopus 로고
    • Attenuation of nucleus basalis of Meynert lesion-induced cholinergic deficits by nerve growth factor.
    • Haroutunian V., Kanof P.D., and Davis K.L. Attenuation of nucleus basalis of Meynert lesion-induced cholinergic deficits by nerve growth factor. Brain Res. 487 (1989) 200-203
    • (1989) Brain Res. , vol.487 , pp. 200-203
    • Haroutunian, V.1    Kanof, P.D.2    Davis, K.L.3
  • 128
    • 0031022977 scopus 로고    scopus 로고
    • Differential modulation of the cholinergic phenotype of the nucleus basalis magnocelluaris neurons by applying NGF at the cell body or cortical terminal fields.
    • Hu L., Cote S.L., and Cuello C. Differential modulation of the cholinergic phenotype of the nucleus basalis magnocelluaris neurons by applying NGF at the cell body or cortical terminal fields. Exp. Neurol. 143 (1997) 162-171
    • (1997) Exp. Neurol. , vol.143 , pp. 162-171
    • Hu, L.1    Cote, S.L.2    Cuello, C.3
  • 129
    • 0032100674 scopus 로고    scopus 로고
    • Chronic sparing of delayed alternation performance and choline acetyltransferase activity by CEP-1347/KT-7515 in rats with lesions of nucleus basalis magnocellularis.
    • DiCamillo A.M., Neff N.T., Carswell S., and Haun F.A. Chronic sparing of delayed alternation performance and choline acetyltransferase activity by CEP-1347/KT-7515 in rats with lesions of nucleus basalis magnocellularis. Neuroscience 86 (1998) 473-483
    • (1998) Neuroscience , vol.86 , pp. 473-483
    • DiCamillo, A.M.1    Neff, N.T.2    Carswell, S.3    Haun, F.A.4
  • 130
    • 0038397221 scopus 로고
    • Animal models of Alzheimer's disease and dementia (with an emphasis on cortical cholinergic systems)
    • Willner P. (Ed), Cambridge University Press, London
    • Dunnett S.B., and Barth T.M. Animal models of Alzheimer's disease and dementia (with an emphasis on cortical cholinergic systems). In: Willner P. (Ed). Behavioural Models in Psychopharmacology (1991), Cambridge University Press, London 359-418
    • (1991) Behavioural Models in Psychopharmacology , pp. 359-418
    • Dunnett, S.B.1    Barth, T.M.2
  • 131
    • 0023835556 scopus 로고
    • Morphological response of axotomized septal neurons to nerve growth factor.
    • Gage F.H., Armstrong D.M., Williams L.R., and Varon S. Morphological response of axotomized septal neurons to nerve growth factor. J. Comp. Neurol. 269 (1988) 147-155
    • (1988) J. Comp. Neurol. , vol.269 , pp. 147-155
    • Gage, F.H.1    Armstrong, D.M.2    Williams, L.R.3    Varon, S.4
  • 132
    • 0025780387 scopus 로고
    • Recombinant human nerve growth factor prevents retrograde degeneration of axotomized basal forebrain cholinergic neurons in the rat.
    • Koliatsos V.E., Applegate M.D., Knusel B., Junard E.O., Burton L.E., Mobley W.C., Hefti F.F., and Price D.L. Recombinant human nerve growth factor prevents retrograde degeneration of axotomized basal forebrain cholinergic neurons in the rat. Exp. Neurol. 112 (1991) 161-173
    • (1991) Exp. Neurol. , vol.112 , pp. 161-173
    • Koliatsos, V.E.1    Applegate, M.D.2    Knusel, B.3    Junard, E.O.4    Burton, L.E.5    Mobley, W.C.6    Hefti, F.F.7    Price, D.L.8
  • 134
    • 0025000718 scopus 로고
    • Human brain cholinergic pathways.
    • Mesulam M.M. Human brain cholinergic pathways. Prog. Brain Res. 84 (1990) 231-241
    • (1990) Prog. Brain Res. , vol.84 , pp. 231-241
    • Mesulam, M.M.1
  • 135
    • 0030437247 scopus 로고    scopus 로고
    • Glial cell line-derived neurotrophic factor sustains axotomized basal forebrain cholinergic neurons in vivo: doseresponse comparison to nerve growth factor and brain-derived neurotrophic factor.
    • Williams L.R., Inouye G., Cummins V., and Pelleymounter M.A. Glial cell line-derived neurotrophic factor sustains axotomized basal forebrain cholinergic neurons in vivo: doseresponse comparison to nerve growth factor and brain-derived neurotrophic factor. J. Pharmacol. Exp. Ther. 277 (1996) 1140-1151
    • (1996) J. Pharmacol. Exp. Ther. , vol.277 , pp. 1140-1151
    • Williams, L.R.1    Inouye, G.2    Cummins, V.3    Pelleymounter, M.A.4
  • 136
    • 0026574673 scopus 로고
    • Brain-derived neurotrophic factor administration protects basal forebrain cholinergic but not nigral dopaminergic neurons from degenerative changes after axotomy in the adult rat brain.
    • Knusel B., Beck K.D., Winslow J., Rosenthal A., Burton L.E., Widmer H.R., Nikolics K., and Hefti F. Brain-derived neurotrophic factor administration protects basal forebrain cholinergic but not nigral dopaminergic neurons from degenerative changes after axotomy in the adult rat brain. J. Neurosci. 12 (1992) 4391-4402
    • (1992) J. Neurosci. , vol.12 , pp. 4391-4402
    • Knusel, B.1    Beck, K.D.2    Winslow, J.3    Rosenthal, A.4    Burton, L.E.5    Widmer, H.R.6    Nikolics, K.7    Hefti, F.8
  • 137
    • 0022486717 scopus 로고
    • Nerve growth factor promotes survival of septal cholinergic neurons after fimbrial transactions.
    • Hefti F. Nerve growth factor promotes survival of septal cholinergic neurons after fimbrial transactions. J. Neurosci. 6 (1986) 2155-2162
    • (1986) J. Neurosci. , vol.6 , pp. 2155-2162
    • Hefti, F.1
  • 138
    • 0025893945 scopus 로고
    • Parkinson's disease: pathophysiology.
    • Agid Y. Parkinson's disease: pathophysiology. The Lancet 337 (1991) 1321-1324
    • (1991) The Lancet , vol.337 , pp. 1321-1324
    • Agid, Y.1
  • 139
    • 0029751103 scopus 로고    scopus 로고
    • The etiology of Parkinson's disease with emphasis on the MPTP story
    • Langston J.W. The etiology of Parkinson's disease with emphasis on the MPTP story. Neurology 47 (1996) S153-S160
    • (1996) Neurology , vol.47
    • Langston, J.W.1
  • 140
    • 0025023096 scopus 로고
    • The nigrostriatal system in Parkinson's disease.
    • Graybiel A.M., Hirsch E.C., and Agid Y. The nigrostriatal system in Parkinson's disease. Adv. Neurol. 53 (1990) 17-29
    • (1990) Adv. Neurol. , vol.53 , pp. 17-29
    • Graybiel, A.M.1    Hirsch, E.C.2    Agid, Y.3
  • 141
    • 0029269229 scopus 로고
    • The rationale for the use of dopamine agonists in Parkinson's disease.
    • Jenner P. The rationale for the use of dopamine agonists in Parkinson's disease. Neurology 45 (1995) S6-12
    • (1995) Neurology , vol.45
    • Jenner, P.1
  • 142
    • 0032829657 scopus 로고    scopus 로고
    • Dopamine receptorsphysiological understanding to therapeutic intervention potential.
    • Emilien G., Maloteaux J.M., Geurts M., Hoogenberg K., and Cragg S. Dopamine receptorsphysiological understanding to therapeutic intervention potential. Pharmacol. Ther. 84 (1999) 133-156
    • (1999) Pharmacol. Ther. , vol.84 , pp. 133-156
    • Emilien, G.1    Maloteaux, J.M.2    Geurts, M.3    Hoogenberg, K.4    Cragg, S.5
  • 143
    • 0021224694 scopus 로고
    • Protection against the dopaminergic neurotoxicity of 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine by monoamine oxidase inhibitors.
    • Heikkila R.E., Manzino L., Cabbat F.S., and Duvoisin R.C. Protection against the dopaminergic neurotoxicity of 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine by monoamine oxidase inhibitors. Nature 311 (1984) 467-469
    • (1984) Nature , vol.311 , pp. 467-469
    • Heikkila, R.E.1    Manzino, L.2    Cabbat, F.S.3    Duvoisin, R.C.4
  • 144
    • 0021280826 scopus 로고
    • Dopaminergic neurotoxicity of 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine in mice.
    • Heikkila R.E., Hess A., and Duvoisín R.C. Dopaminergic neurotoxicity of 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine in mice. Science 224 (1984) 1451-1453
    • (1984) Science , vol.224 , pp. 1451-1453
    • Heikkila, R.E.1    Hess, A.2    Duvoisín, R.C.3
  • 145
    • 0032191183 scopus 로고    scopus 로고
    • Chronic exposure to MPTP as a primate model of progressive parkinsonism: a pilot study with a free radical scavenger.
    • Blanchet P.J., Konitsiotis S., Hyland K., Arnold L.A., Pettigrew K.D., and Chase T.N. Chronic exposure to MPTP as a primate model of progressive parkinsonism: a pilot study with a free radical scavenger. Exp. Neurol. 153 (1998) 214-222
    • (1998) Exp. Neurol. , vol.153 , pp. 214-222
    • Blanchet, P.J.1    Konitsiotis, S.2    Hyland, K.3    Arnold, L.A.4    Pettigrew, K.D.5    Chase, T.N.6
  • 146
    • 0028784523 scopus 로고
    • Time course and morphology of dopaminergic neuronal death caused by the neurotoxin 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine.
    • Jackson-Lewis V., Jakowec M., Burke R.E., and Przedborski S. Time course and morphology of dopaminergic neuronal death caused by the neurotoxin 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine. Neurodegeneration 4 (1995) 257-269
    • (1995) Neurodegeneration , vol.4 , pp. 257-269
    • Jackson-Lewis, V.1    Jakowec, M.2    Burke, R.E.3    Przedborski, S.4
  • 147
    • 0000340348 scopus 로고
    • Parkinsonism-inducing neurotoxin, N-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine: uptake of the metabolite N-methyl-4-phenylpyridine by dopamine neurons explains selective toxicity.
    • Javitch J.A., D'Amato R.J., Strittmatter S.M., and Snyder S.H. Parkinsonism-inducing neurotoxin, N-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine: uptake of the metabolite N-methyl-4-phenylpyridine by dopamine neurons explains selective toxicity. Proc. Nail. Acad. Sci. U.S.A. 82 (1985) 2173-2177
    • (1985) Proc. Nail. Acad. Sci. U.S.A. , vol.82 , pp. 2173-2177
    • Javitch, J.A.1    D'Amato, R.J.2    Strittmatter, S.M.3    Snyder, S.H.4
  • 148
    • 0027504297 scopus 로고
    • Advances in our understanding of the mechanisms of the neurotoxicity of MPTP and related compounds.
    • Tipton K.F., and Singer T.P. Advances in our understanding of the mechanisms of the neurotoxicity of MPTP and related compounds. J. Neurochem. 61 (1993) 1191-1206
    • (1993) J. Neurochem. , vol.61 , pp. 1191-1206
    • Tipton, K.F.1    Singer, T.P.2
  • 149
    • 0026754078 scopus 로고
    • Dopaminergic neurotoxicity of 1-methyl-4-phenylpyridinium analogs in cultured mesencephalon: relationship to dopamine uptake affinity and inhibition of mitochondrial respiration.
    • Saporito M.S., Heikkila R.E., Youngster S.K., Nicklas W.J., and Geller H.M. Dopaminergic neurotoxicity of 1-methyl-4-phenylpyridinium analogs in cultured mesencephalon: relationship to dopamine uptake affinity and inhibition of mitochondrial respiration. J. Pharmacol. Exp. Ther. 260 (1992) 1400-1409
    • (1992) J. Pharmacol. Exp. Ther. , vol.260 , pp. 1400-1409
    • Saporito, M.S.1    Heikkila, R.E.2    Youngster, S.K.3    Nicklas, W.J.4    Geller, H.M.5
  • 150
    • 0021810979 scopus 로고
    • Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenylpyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1, 2, 5, 6-tetrahydropyridine.
    • Nicklas W.J., Vyas I., and Heikkila R.E. Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenylpyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1, 2, 5, 6-tetrahydropyridine. Life Sci. 36 (1985) 2503-2508
    • (1985) Life Sci. , vol.36 , pp. 2503-2508
    • Nicklas, W.J.1    Vyas, I.2    Heikkila, R.E.3
  • 151
    • 0023525982 scopus 로고
    • Mitochondrial and metabolic toxicity of 1-methyl-4-(2′-methylphenyl)-1, 2, 3, 6-tetrahydropyridine.
    • Kindt M.V., Heikkila R.E., and Nicklas W.J. Mitochondrial and metabolic toxicity of 1-methyl-4-(2′-methylphenyl)-1, 2, 3, 6-tetrahydropyridine. J. Pharmacol. Exp. Ther. 242 (1987) 858-863
    • (1987) J. Pharmacol. Exp. Ther. , vol.242 , pp. 858-863
    • Kindt, M.V.1    Heikkila, R.E.2    Nicklas, W.J.3
  • 152
    • 0022503139 scopus 로고
    • Studies on the neurotoxicity of 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine: inhibition of NAD-linked substrate oxidation by its metabolite, 1-methyl-4-phenylpyridinium.
    • Vyas I., Heikkila R.E., and Nicklas W.J. Studies on the neurotoxicity of 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine: inhibition of NAD-linked substrate oxidation by its metabolite, 1-methyl-4-phenylpyridinium. J. Neurochem. 46 (1986) 1501-1507
    • (1986) J. Neurochem. , vol.46 , pp. 1501-1507
    • Vyas, I.1    Heikkila, R.E.2    Nicklas, W.J.3
  • 155
    • 0026345867 scopus 로고
    • Apoptosis and DNA degradation induced by 1-methyl-4-phenylpyridinium in neurons.
    • Dipasquale B., Marini A.M., and Youle R.J. Apoptosis and DNA degradation induced by 1-methyl-4-phenylpyridinium in neurons. Biochem. Biophys. Res. Commun. 181 (1991) 1442-1448
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 1442-1448
    • Dipasquale, B.1    Marini, A.M.2    Youle, R.J.3
  • 156
    • 84975751684 scopus 로고
    • Complex I inhibitors induce dose-dependent apoptosis in PC12 cells; Relevance to Parkinson's disease.
    • Hartley A., Stone J.M., Heron C., Cooper J.M., and Schapira A.H. Complex I inhibitors induce dose-dependent apoptosis in PC12 cells; Relevance to Parkinson's disease. J. Neurochem. 63 (1994) 1987-1990
    • (1994) J. Neurochem. , vol.63 , pp. 1987-1990
    • Hartley, A.1    Stone, J.M.2    Heron, C.3    Cooper, J.M.4    Schapira, A.H.5
  • 158
    • 0030888286 scopus 로고    scopus 로고
    • In situ detection of apoptotic nuclei in the substantia nigra compacta of 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine-treated mice using terminal deoxynucleotidyl transferase labelling and acridine orange staining
    • Tatton N.A., and Kish S.J. In situ detection of apoptotic nuclei in the substantia nigra compacta of 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine-treated mice using terminal deoxynucleotidyl transferase labelling and acridine orange staining. Neuroscience 77 (1997) 1037-1048
    • (1997) Neuroscience , vol.77 , pp. 1037-1048
    • Tatton, N.A.1    Kish, S.J.2
  • 159
    • 0033104442 scopus 로고    scopus 로고
    • +-induced apoptosis in numan SH-SY5Y neuroblastoma cells.
    • +-induced apoptosis in numan SH-SY5Y neuroblastoma cells. J. Neurosci. Res. 55 (1999) 620-628
    • (1999) J. Neurosci. Res. , vol.55 , pp. 620-628
    • Fall, C.P.1    Bennett Jr., J.P.2
  • 160
    • 0032510758 scopus 로고    scopus 로고
    • Transgenic mice expressing human Bc1-2 in their neurons are resistant to 6-hydroxydopamine and 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine neurotoxicity.
    • Offen D., Beart P.M., Cheung N.S., Pascoe C.J., Hocham A., Oorodin S., Melamed E., Bernard R., and Bernard O. Transgenic mice expressing human Bc1-2 in their neurons are resistant to 6-hydroxydopamine and 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine neurotoxicity. Proc. Natl. Acad. Sci. USA 95 (1998) 5789-5794
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5789-5794
    • Offen, D.1    Beart, P.M.2    Cheung, N.S.3    Pascoe, C.J.4    Hocham, A.5    Oorodin, S.6    Melamed, E.7    Bernard, R.8    Bernard, O.9
  • 161
    • 0030249597 scopus 로고    scopus 로고
    • Dopamine neurons from transgenic mice with knockout of the p53 gene resist MPTP neurotoxicity.
    • Trimmer P.A., Smith T.S., Jung A.B., and Bennett J.P. Dopamine neurons from transgenic mice with knockout of the p53 gene resist MPTP neurotoxicity. Neurodegeneration 5 (1996) 233-239
    • (1996) Neurodegeneration , vol.5 , pp. 233-239
    • Trimmer, P.A.1    Smith, T.S.2    Jung, A.B.3    Bennett, J.P.4
  • 164
    • 0033029823 scopus 로고    scopus 로고
    • CEP-1347/K.T-7515. An inhibititor of c-jun N-terminal kinase activation attenuates the 1-methyl-4-phenyl tetrahydropyridinemediated loss of nigrostriatal dopaminergic neurons in vivo.
    • Saporito M.S., Brown E.M., Miller M.S., and Carswell S. CEP-1347/K.T-7515. An inhibititor of c-jun N-terminal kinase activation attenuates the 1-methyl-4-phenyl tetrahydropyridinemediated loss of nigrostriatal dopaminergic neurons in vivo. J. Pharmacol. Exp. Ther. 288 (1999) 421-427
    • (1999) J. Pharmacol. Exp. Ther. , vol.288 , pp. 421-427
    • Saporito, M.S.1    Brown, E.M.2    Miller, M.S.3    Carswell, S.4
  • 166
    • 0033840581 scopus 로고    scopus 로고
    • MPTP activates c-Jun NH(2)-terminal kinase (JNK) and its upstream regulatory kinase MKK4 in nigrostriatal neurons in vivo.
    • Saporito M.S., Thomas B.A., and Scott R.W. MPTP activates c-Jun NH(2)-terminal kinase (JNK) and its upstream regulatory kinase MKK4 in nigrostriatal neurons in vivo. J. Neurochem. 75 (2000) 1200-1208
    • (2000) J. Neurochem. , vol.75 , pp. 1200-1208
    • Saporito, M.S.1    Thomas, B.A.2    Scott, R.W.3
  • 169
    • 0025945089 scopus 로고
    • Rapid ATP loss caused by 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine in mouse brain.
    • Chan P., DeLanney L.E., Irwin I., Langston J.W., and Di Monte D. Rapid ATP loss caused by 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine in mouse brain. J. Neurochem. 57 (1991) 348-351
    • (1991) J. Neurochem. , vol.57 , pp. 348-351
    • Chan, P.1    DeLanney, L.E.2    Irwin, I.3    Langston, J.W.4    Di Monte, D.5
  • 170
    • 0025864532 scopus 로고
    • Correlation between the neostriatal content of the 1-methyl-4-phenylpyridinium species and dopaminergic neurotoxicity following 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine administration to several strains of mice.
    • Giovanni A., Sieber B.A., Heikkila R.E., and Sonsalia P.K. Correlation between the neostriatal content of the 1-methyl-4-phenylpyridinium species and dopaminergic neurotoxicity following 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine administration to several strains of mice. J. Pharmacol. Exp. Ther. 257 (1991) 691-697
    • (1991) J. Pharmacol. Exp. Ther. , vol.257 , pp. 691-697
    • Giovanni, A.1    Sieber, B.A.2    Heikkila, R.E.3    Sonsalia, P.K.4
  • 171
    • 0030175359 scopus 로고    scopus 로고
    • Striatal MPP+ levels do not necessarily correlate with striatal dopamine levels after MPTP treatment in mice.
    • Vaglini F., Fascetti F., Tedeschi D., Cavalletti M., Fornai F., and Corsini G.U. Striatal MPP+ levels do not necessarily correlate with striatal dopamine levels after MPTP treatment in mice. Neurodegeneration 5 (1996) 129-136
    • (1996) Neurodegeneration , vol.5 , pp. 129-136
    • Vaglini, F.1    Fascetti, F.2    Tedeschi, D.3    Cavalletti, M.4    Fornai, F.5    Corsini, G.U.6
  • 172
    • 0024460034 scopus 로고
    • Attenuation by dopamine uptake blockers of the inhibitory effects of 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine and some of its analogs on NADH-linked metabolism in mouse neostriatal slices.
    • Ofori S., Heikkila R.E., and Nicklas W.J. Attenuation by dopamine uptake blockers of the inhibitory effects of 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine and some of its analogs on NADH-linked metabolism in mouse neostriatal slices. J. Pharmacol. Exp. Ther. 251 (1989) 258-266
    • (1989) J. Pharmacol. Exp. Ther. , vol.251 , pp. 258-266
    • Ofori, S.1    Heikkila, R.E.2    Nicklas, W.J.3
  • 173
    • 0023943559 scopus 로고
    • MPP+-induced efflux of dopamine and lactate from rat striatum have similar time courses as shown by in vivo brain dialysis
    • Rollema H., Kuhr W.G., Kranenborg G., De Vries J., and Van den Berg C. MPP+-induced efflux of dopamine and lactate from rat striatum have similar time courses as shown by in vivo brain dialysis. J. Pharmacol. Exp. Ther. 245 (1988) 858-866
    • (1988) J. Pharmacol. Exp. Ther. , vol.245 , pp. 858-866
    • Rollema, H.1    Kuhr, W.G.2    Kranenborg, G.3    De Vries, J.4    Van den Berg, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.