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Volumn 71, Issue 2, 2012, Pages 116-129

Inhibition of JNK by a peptide inhibitor reduces traumatic brain injury-induced tauopathy in transgenic mice

Author keywords

c Jun N terminal kinase; Controlled cortical impact; D JNKi1; Kinase; Phosphorylation; Tau; Traumatic brain injury

Indexed keywords

BML E1384; BML EI355; BML EI384; PHOSPHOPROTEIN PHOSPHATASE; STRESS ACTIVATED PROTEIN KINASE; STRESS ACTIVATED PROTEIN KINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 84856065447     PISSN: 00223069     EISSN: 15546578     Source Type: Journal    
DOI: 10.1097/NEN.0b013e3182456aed     Document Type: Article
Times cited : (77)

References (97)
  • 1
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • DOI 10.1038/nrn2194, PII NRN2194
    • Ballatore C, Lee VM, Trojanowski JQ. Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat Rev Neurosci 2007;8: 663-72 (Pubitemid 47283144)
    • (2007) Nature Reviews Neuroscience , vol.8 , Issue.9 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.-Y.2    Trojanowski, J.Q.3
  • 4
    • 84856048496 scopus 로고    scopus 로고
    • Widespread tau and amyloid-beta pathology many years after a single traumatic brain injury in humans
    • epub
    • Johnson VE, Stewart W, Smith DH. Widespread tau and amyloid-beta pathology many years after a single traumatic brain injury in humans. Brain Pathol epub 2011;12
    • (2011) Brain Pathol , pp. 12
    • Johnson, V.E.1    Stewart, W.2    Smith, D.H.3
  • 6
    • 0032868750 scopus 로고    scopus 로고
    • Neuronal cytoskeletal changes are an early consequence of repetitive head injury
    • DOI 10.1007/s004010051066
    • Geddes JF, Vowles GH, Nicoll JA, et al. Neuronal cytoskeletal changes are an early consequence of repetitive head injury. Acta Neuropathol 1999;98:171-78 (Pubitemid 29355550)
    • (1999) Acta Neuropathologica , vol.98 , Issue.2 , pp. 171-178
    • Geddes, J.F.1    Vowles, G.H.2    Nicoll, J.A.R.3    Revesz, T.4
  • 8
    • 68249157080 scopus 로고    scopus 로고
    • Chronic traumatic encephalopathy in athletes: Progressive tauopathy after repetitive head injury
    • McKee AC, Cantu RC, Nowinski CJ, et al. Chronic traumatic encephalopathy in athletes: Progressive tauopathy after repetitive head injury. J Neuropathol Exp Neurol 2009;68:709-35
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 709-735
    • McKee, A.C.1    Cantu, R.C.2    Nowinski, C.J.3
  • 10
    • 0034963745 scopus 로고    scopus 로고
    • Tau isoform profile and phosphorylation state in dementia pugilistica recapitulate Alzheimer's disease
    • Schmidt ML, Zhukareva V, Newell KL, et al. Tau isoform profile and phosphorylation state in dementia pugilistica recapitulate Alzheimer's disease. Acta Neuropathol 2001;101:518-24 (Pubitemid 32600142)
    • (2001) Acta Neuropathologica , vol.101 , Issue.5 , pp. 518-524
    • Schmidt, M.L.1    Zhukareva, V.2    Newell, K.L.3    Lee, V.M.-Y.4    Trojanowski, J.Q.5
  • 11
    • 0025784849 scopus 로고
    • Reexamination of ex-boxers' brains using immunohistochemistry with antibodies to amyloid betaprotein and tau protein
    • Tokuda T, Ikeda S, Yanagisawa N, et al. Reexamination of ex-boxers' brains using immunohistochemistry with antibodies to amyloid betaprotein and tau protein. Acta Neuropathol 1991;82:280-85
    • (1991) Acta Neuropathol , vol.82 , pp. 280-285
    • Tokuda, T.1    Ikeda, S.2    Yanagisawa, N.3
  • 13
    • 0028362458 scopus 로고
    • A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads
    • DOI 10.1007/s004010050124
    • Braak E, Braak H, Mandelkow EM. A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads. Acta Neuropathol 1994;87:554-67 (Pubitemid 24158408)
    • (1994) Acta Neuropathologica , vol.87 , Issue.6 , pp. 554-567
    • Braak, E.1    Braaak, H.2    Mandelkow, E.-M.3
  • 14
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel DN, Hyman AA, Cobb MH, et al. Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol Biol Cell 1992;3:1141-54 (Pubitemid 23088964)
    • (1992) Molecular Biology of the Cell , vol.3 , Issue.10 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 16
    • 0027308924 scopus 로고
    • 396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
    • DOI 10.1016/0896-6273(93)90057-X
    • Bramblett GT, Goedert M, Jakes R, et al. Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding. Neuron 1993;10:1089-99 (Pubitemid 23194399)
    • (1993) Neuron , vol.10 , Issue.6 , pp. 1089-1099
    • Bramblett, G.T.1    Goedert, M.2    Jakes, R.3    Merrick, S.E.4    Trojanowski, J.Q.5    Lee -, V.M.Y.6
  • 17
    • 0030813929 scopus 로고    scopus 로고
    • Selective destruction of stable microtubules and axons by inhibitors of protein serine/threonine phosphatases in cultured human neurons (NT2N cells)
    • Merrick SE, Trojanowski JQ, Lee VM. Selective destruction of stable microtubules and axons by inhibitors of protein serine/threonine phosphatases in cultured human neurons. J Neurosci 1997;17:5726-37 (Pubitemid 27310488)
    • (1997) Journal of Neuroscience , vol.17 , Issue.15 , pp. 5726-5737
    • Merrick, S.E.1    Trojanowski, J.Q.2    Lee, V.M.-Y.3
  • 19
    • 77952081276 scopus 로고    scopus 로고
    • Discovery of brain-penetrant, orally bioavailable aminothienopyridazine inhibitors of tau aggregation
    • Ballatore C, Brunden KR, Piscitelli F, et al. Discovery of brain-penetrant, orally bioavailable aminothienopyridazine inhibitors of tau aggregation. J Med Chem 2010;53:3739-47
    • (2010) J Med Chem , vol.53 , pp. 3739-3747
    • Ballatore, C.1    Brunden, K.R.2    Piscitelli, F.3
  • 20
    • 70349638299 scopus 로고    scopus 로고
    • Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies
    • Brunden KR, Trojanowski JQ, Lee VM. Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies. Nat Rev Drug Discov 2009;8:783-93
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 783-793
    • Brunden, K.R.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 22
  • 23
    • 0037125209 scopus 로고    scopus 로고
    • A survey of Cdk5 activator p35 and p25 levels in Alzheimer's disease brains
    • DOI 10.1016/S0014-5793(02)02934-4, PII S0014579302029344
    • Tseng HC, Zhou Y, Shen Y, et al. A survey of Cdk5 activator p35 and p25 levels in Alzheimer's disease brains. FEBS Lett 2002;523:58-62 (Pubitemid 34786058)
    • (2002) FEBS Letters , vol.523 , Issue.1-3 , pp. 58-62
    • Tseng, H.-C.1    Zhou, Y.2    Shen, Y.3    Tsai, L.-H.4
  • 24
    • 1642363745 scopus 로고    scopus 로고
    • Spatial learning deficit in transgenic mice that conditionally over-express GSK-3β in the brain but do not form tau filaments
    • DOI 10.1046/j.1471-4159.2002.01269.x
    • Hernandez F, Borrell J, Guaza C, et al. Spatial learning deficit in transgenic mice that conditionally over-express GSK-3beta in the brain but do not form tau filaments. J Neurochem 2002;83:1529-33 (Pubitemid 35477491)
    • (2002) Journal of Neurochemistry , vol.83 , Issue.6 , pp. 1529-1533
    • Hernandez, F.1    Borrell, J.2    Guaza, C.3    Avila, J.4    Lucas, J.J.5
  • 25
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear β-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3β conditional transgenic mice
    • DOI 10.1093/emboj/20.1.27
    • Lucas JJ, Hernandez F, Gomez-Ramos P, et al. Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice. The EMBO J 2001;20:27-39 (Pubitemid 32099099)
    • (2001) EMBO Journal , vol.20 , Issue.1-2 , pp. 27-39
    • Lucas, J.J.1    Hernandez, F.2    Gomez-Ramos, P.3    Moran, M.A.4    Hen, R.5    Avila, J.6
  • 26
    • 0029113874 scopus 로고
    • Phosphatase activity toward abnormally phosphorylated tau: Decrease in Alzheimer disease brain
    • Gong CX, Shaikh S, Wang JZ, et al. Phosphatase activity toward abnormally phosphorylated tau: Decrease in Alzheimer disease brain. J Neurochem 1995;65:732-38
    • (1995) J Neurochem , vol.65 , pp. 732-738
    • Gong, C.X.1    Shaikh, S.2    Wang, J.Z.3
  • 28
    • 0035851175 scopus 로고    scopus 로고
    • Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice
    • Kins S, Crameri A, Evans DR, et al. Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice. J Biol Chem 2001;276:38193-200
    • (2001) J Biol Chem , vol.276 , pp. 38193-200
    • Kins, S.1    Crameri, A.2    Evans, D.R.3
  • 29
    • 0026597280 scopus 로고
    • Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain
    • Litersky JM, Johnson GV. Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain. J Biol Chem 1992;267: 1563-68
    • (1992) J Biol Chem , vol.267 , pp. 1563-1568
    • Litersky, J.M.1    Johnson, G.V.2
  • 30
    • 33846212717 scopus 로고    scopus 로고
    • Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration
    • DOI 10.1111/j.1460-9568.2006.05226.x
    • Wang JZ, Grundke-Iqbal I, Iqbal K. Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration. Eur J Neurosci 2007;25:59-68 (Pubitemid 46098893)
    • (2007) European Journal of Neuroscience , vol.25 , Issue.1 , pp. 59-68
    • Wang, J.-Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 31
    • 0026549985 scopus 로고
    • Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer-like state
    • Drewes G, Lichtenberg-Kraag B, Doring F, et al. Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer-like state. EMBO J 1992;11:2131-38
    • (1992) EMBO J , vol.11 , pp. 2131-2138
    • Drewes, G.1    Lichtenberg-Kraag, B.2    Doring, F.3
  • 32
    • 0026784416 scopus 로고
    • P42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. Implications for Alzheimer's disease [corrected]
    • Goedert M, Cohen ES, Jakes R, et al. p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. Implications for Alzheimer's disease [corrected]. FEBS Lett 1992;312:95-99
    • (1992) FEBS Lett , vol.312 , pp. 95-99
    • Goedert, M.1    Cohen, E.S.2    Jakes, R.3
  • 33
    • 0037181485 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases in intact cells
    • DOI 10.1016/S0014-5793(02)02460-2, PII S0014579302024602
    • Buee-Scherrer V, Goedert M. Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases in intact cells. FEBS Lett 2002;515:151-54 (Pubitemid 34273915)
    • (2002) FEBS Letters , vol.515 , Issue.1-3 , pp. 151-154
    • Buee-Scherrer, V.1    Goedert, M.2
  • 34
    • 0030963035 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases
    • DOI 10.1016/S0014-5793(97)00483-3, PII S0014579397004833
    • Goedert M, Hasegawa M, Jakes R, et al. Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases. FEBS Lett 1997;409:57-62 (Pubitemid 27248567)
    • (1997) FEBS Letters , vol.409 , Issue.1 , pp. 57-62
    • Goedert, M.1    Hasegawa, M.2    Jakes, R.3    Lawler, S.4    Cuenda, A.5    Cohen, P.6
  • 35
    • 3142712947 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein tau by isoforms of c-Jun N-terminal kinase (JNK)
    • DOI 10.1111/j.1471-4159.2004.02479.x
    • Yoshida H, Hastie CJ, McLauchlan H, et al. Phosphorylation of microtubule-associated protein tau by isoforms of c-Jun N-terminal kinase (JNK). J Neurochem 2004;90:352-58 (Pubitemid 38938221)
    • (2004) Journal of Neurochemistry , vol.90 , Issue.2 , pp. 352-358
    • Yoshida, H.1    Hastie, C.J.2    McLauchlan, H.3    Cohen, P.4    Goedert, M.5
  • 36
    • 69649090119 scopus 로고    scopus 로고
    • The JNK pathway amplifies and drives subcellular changes in tau phosphorylation
    • Vogel J, Anand VS, Ludwig B, et al. The JNK pathway amplifies and drives subcellular changes in tau phosphorylation. Neuropharmacology 2009;57:539-50
    • (2009) Neuropharmacology , vol.57 , pp. 539-550
    • Vogel, J.1    Anand, V.S.2    Ludwig, B.3
  • 37
    • 79959941349 scopus 로고    scopus 로고
    • Controlled cortical impact traumatic brain injury in 3xTg-AD mice causes acute intra-axonal amyloid-beta accumulation and independently accelerates the development of tau abnormalities
    • Tran HT, LaFerla FM, Holtzman DM, et al. Controlled cortical impact traumatic brain injury in 3xTg-AD mice causes acute intra-axonal amyloid-beta accumulation and independently accelerates the development of tau abnormalities. J Neurosci 2011;31:9513-25
    • (2011) J Neurosci , vol.31 , pp. 9513-9525
    • Tran, H.T.1    Laferla, F.M.2    Holtzman, D.M.3
  • 40
    • 12144289492 scopus 로고    scopus 로고
    • Alterations in Glucose Metabolism Induce Hypothermia Leading to Tau Hyperphosphorylation through Differential Inhibition of Kinase and Phosphatase Activities: Implications for Alzheimer's Disease
    • DOI 10.1523/JNEUROSCI.5561-03.2004
    • Planel E, Miyasaka T, Launey T, et al. Alterations in glucose metabolism induce hypothermia leading to tau hyperphosphorylation through differential inhibition of kinase and phosphatase activities: Implications for Alzheimer's disease. J Neurosci 2004;24:2401-11 (Pubitemid 38327953)
    • (2004) Journal of Neuroscience , vol.24 , Issue.10 , pp. 2401-2411
    • Planel, E.1    Miyasaka, T.2    Launey, T.3    Chui, D.-H.4    Tanemura, K.5    Sato, S.6    Murayama, O.7    Ishiguro, K.8    Tatebayashi, Y.9    Takashima, A.10
  • 43
    • 71449125786 scopus 로고    scopus 로고
    • Overexpression of low-density lipoprotein receptor in the brain markedly inhibits amyloid deposition and increases extracellular A beta clearance
    • Kim J, Castellano JM, Jiang H, et al. Overexpression of low-density lipoprotein receptor in the brain markedly inhibits amyloid deposition and increases extracellular A beta clearance. Neuron 2009;64: 632-44
    • (2009) Neuron , vol.64 , pp. 632-644
    • Kim, J.1    Castellano, J.M.2    Jiang, H.3
  • 44
    • 34247368915 scopus 로고    scopus 로고
    • Detection of traumatic axonal injury with diffusion tensor imaging in a mouse model of traumatic brain injury
    • DOI 10.1016/j.expneurol.2007.01.035, PII S0014488607000489
    • Mac Donald CL, Dikranian K, Song SK, et al. Detection of traumatic axonal injury with diffusion tensor imaging in a mouse model of traumatic brain injury. Exp Neurol 2007;205:116-31 (Pubitemid 46629058)
    • (2007) Experimental Neurology , vol.205 , Issue.1 , pp. 116-131
    • Mac Donald, C.L.1    Dikranian, K.2    Song, S.K.3    Bayly, P.V.4    Holtzman, D.M.5    Brody, D.L.6
  • 45
    • 0035152487 scopus 로고    scopus 로고
    • Cell-permeable peptide inhibitors of JNK. Novel blockers of β-cell death
    • Bonny C, Oberson A, Negri S, et al. Cell-permeable peptide inhibitors of JNK: Novel blockers of beta-cell death. Diabetes 2001;50:77-82 (Pubitemid 32047984)
    • (2001) Diabetes , vol.50 , Issue.1 , pp. 77-82
    • Bonny, C.1    Oberson, A.2    Negri, S.3    Sauser, C.4    Schorderet, D.F.5
  • 47
    • 0042380209 scopus 로고    scopus 로고
    • N-methyl-D-aspartate-triggered neuronal death in organotypic hippocampal cultures is endocytic, autophagic and mediated by the c-Jun N-terminal kinase pathway
    • DOI 10.1046/j.1460-9568.2003.02757.x
    • Borsello T, Croquelois K, Hornung JP, et al. N-methyl-D-aspartateY triggered neuronal death in organotypic hippocampal cultures is endocytic, autophagic and mediated by the c-Jun N-terminal kinase pathway. Eur J Neurosci 2003;18:473-85 (Pubitemid 37041099)
    • (2003) European Journal of Neuroscience , vol.18 , Issue.3 , pp. 473-485
    • Borsello, T.1    Croquelois, K.2    Hornung, J.-P.3    Clarke, P.G.H.4
  • 48
    • 0037192843 scopus 로고    scopus 로고
    • Identification of the critical features of a small peptide inhibitor of JNK activity
    • DOI 10.1074/jbc.M107565200
    • Barr RK, Kendrick TS, Bogoyevitch MA. Identification of the critical features of a small peptide inhibitor of JNK activity. J Biol Chem 2002; 277:10987-97 (Pubitemid 34952855)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.13 , pp. 10987-10997
    • Barr, R.K.1    Kendrick, T.S.2    Bogoyevitch, M.A.3
  • 49
    • 0345405447 scopus 로고    scopus 로고
    • Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles
    • DOI 10.1016/S0896-6273(03)00627-5
    • Cruz JC, Tseng HC, Goldman JA, et al. Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles. Neuron 2003;40:471-83 (Pubitemid 37494698)
    • (2003) Neuron , vol.40 , Issue.3 , pp. 471-483
    • Cruz, J.C.1    Tseng, H.-C.2    Goldman, J.A.3    Shih, H.4    Tsai, L.-H.5
  • 50
    • 0031596660 scopus 로고    scopus 로고
    • Phosphorylation of tau, aβ-formation, and apoptosis after in vivo inhibition of PP-1 and PP-2A
    • DOI 10.1016/S0197-4580(98)00003-7, PII S0197458098000037
    • Arendt T, Holzer M, Fruth R, et al. Phosphorylation of tau, Abetaformation, and apoptosis after in vivo inhibition of PP-1 and PP-2A. Neurobiol Aging 1998;19:3-13 (Pubitemid 28167790)
    • (1998) Neurobiology of Aging , vol.19 , Issue.1 , pp. 3-13
    • Arendt, T.1    Holzer, M.2    Fruth, R.3    Bruckner, M.K.4    Gartner, U.5
  • 51
    • 0029899091 scopus 로고    scopus 로고
    • Tau protein is phosphorylated by cyclic AMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II within its microtubule-binding domains at Ser-262 and Ser-356
    • Litersky JM, Johnson GV, Jakes R, et al. Tau protein is phosphorylated by cyclic AMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II within its microtubule-binding domains at Ser-262 and Ser-356. Biochem J 1996;316:655-60 (Pubitemid 26182167)
    • (1996) Biochemical Journal , vol.316 , Issue.2 , pp. 655-660
    • Litersky, J.M.1    Johnson, G.V.W.2    Jakes, R.3    Goedert, M.4    Lee, M.5    Seubert, P.6
  • 53
    • 0028981873 scopus 로고
    • Glycogen synthase kinase-3 beta phosphorylates tau protein at multiple sites in intact cells
    • Sperber BR, Leight S, Goedert M, et al. Glycogen synthase kinase-3 beta phosphorylates tau protein at multiple sites in intact cells. Neurosci Lett 1995;197:149-53
    • (1995) Neurosci Lett , vol.197 , pp. 149-153
    • Sperber, B.R.1    Leight, S.2    Goedert, M.3
  • 54
    • 34249738681 scopus 로고    scopus 로고
    • Phosphorylation of human microtubule-associated protein tau by protein kinases of the AGC subfamily
    • DOI 10.1016/j.febslet.2007.05.009, PII S0014579307005339
    • Virdee K, Yoshida H, Peak-Chew S, et al. Phosphorylation of human microtubule-associated protein tau by protein kinases of the AGC subfamily. FEBS Lett 2007;581:2657-62 (Pubitemid 46829108)
    • (2007) FEBS Letters , vol.581 , Issue.14 , pp. 2657-2662
    • Virdee, K.1    Yoshida, H.2    Peak-Chew, S.3    Goedert, M.4
  • 55
    • 0028898390 scopus 로고
    • Phosphorylation modulates catalytic function and regulation in the cAMP-dependent protein kinase
    • Adams JA, McGlone ML, Gibson R, et al. Phosphorylation modulates catalytic function and regulation in the cAMP-dependent protein kinase. Biochemistry 1995;34:2447-54
    • (1995) Biochemistry , vol.34 , pp. 2447-2454
    • Adams, J.A.1    McGlone, M.L.2    Gibson, R.3
  • 56
    • 0032925146 scopus 로고    scopus 로고
    • The catalytic subunit of cAMP-dependent protein kinase: Prototype for an extended network of communication
    • DOI 10.1016/S0079-6107(98)00059-5, PII S0079610798000595
    • Smith CM, Radzio-Andzelm E, Madhusudan, et al. The catalytic subunit of cAMP-dependent protein kinase: Prototype for an extended network of communication. Prog Biophys Mol Biol 1999;71:313-41 (Pubitemid 29156305)
    • (1999) Progress in Biophysics and Molecular Biology , vol.71 , Issue.3-4 , pp. 313-341
    • Smith, C.M.1    Radzio-Andzelm, E.2    Madhusudan3    Akamine, P.4    Taylor, S.S.5
  • 57
    • 0025120244 scopus 로고
    • Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase
    • Anderson NG, Maller JL, Tonks NK, et al. Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase. Nature 1990;343:651-53
    • (1990) Nature , vol.343 , pp. 651-653
    • Anderson, N.G.1    Maller, J.L.2    Tonks, N.K.3
  • 58
    • 0034696630 scopus 로고    scopus 로고
    • Activation of JNK3α1 requires both MKK4 and MKK7: Kinetic characterization of in vitro phosphorylated JNK3α1
    • DOI 10.1021/bi992410+
    • Lisnock J, Griffin P, Calaycay J, et al. Activation of JNK3 alpha 1 requires both MKK4 and MKK7: Kinetic characterization of in vitro phosphorylated JNK3 alpha 1. Biochemistry 2000;39:3141-48 (Pubitemid 30159421)
    • (2000) Biochemistry , vol.39 , Issue.11 , pp. 3141-3148
    • Lisnock, J.1    Griffin, P.2    Calaycay, J.3    Frantz, B.4    Parsons, J.5    O'Keefe, S.J.6    Lograsso, P.7
  • 59
    • 0035903222 scopus 로고    scopus 로고
    • Impaired synergistic activation of stress-activated protein kinase SAPK/JNK in mouse embryonic stem cells lacking SEK1/MKK4: Different contribution of SEK2/MKK7 isoforms to the synergistic activation
    • Wada T, Nakagawa K, Watanabe T, et al. Impaired synergistic activation of stress-activated protein kinase SAPK/JNK in mouse embryonic stem cells lacking SEK1/MKK4: Different contribution of SEK2/MKK7 isoforms to the synergistic activation. J Biol Chem 2001;276:30892-97
    • (2001) J Biol Chem , vol.276 , pp. 30892-30897
    • Wada, T.1    Nakagawa, K.2    Watanabe, T.3
  • 60
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • DOI 10.1038/378785a0
    • Cross DA, Alessi DR, Cohen P, et al. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 1995;378: 785-89 (Pubitemid 26004411)
    • (1995) Nature , vol.378 , Issue.6559 , pp. 785-789
    • Cross, D.A.E.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 61
    • 0028902487 scopus 로고
    • Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and-2B
    • Wang JZ, Gong CX, Zaidi T, et al. Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and-2B. J Biol Chem 1995;270:4854-60
    • (1995) J Biol Chem , vol.270 , pp. 4854-4860
    • Wang, J.Z.1    Gong, C.X.2    Zaidi, T.3
  • 62
    • 0034088846 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein tau is regulated by protein phosphatase 2A in mammalian brain. Implications for neurofibrillary degeneration in Alzheimer's disease
    • DOI 10.1074/jbc.275.8.5535
    • Gong CX, Lidsky T, Wegiel J, et al. Phosphorylation of microtubuleassociated protein tau is regulated by protein phosphatase 2A in mammalian brain: Implications for neurofibrillary degeneration in Alzheimer's disease. J Biol Chem 2000;275:5535-44 (Pubitemid 30115189)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.8 , pp. 5535-5544
    • Gong, C.-X.1    Lidsky, T.2    Wegiel, J.3    Zuck, L.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 63
    • 0034097748 scopus 로고    scopus 로고
    • Traumatic axonal injury: Practical issues for diagnosis in medicolegal cases
    • DOI 10.1046/j.1365-2990.2000.026002105.x
    • Geddes JF, Whitwell HL, Graham DI. Traumatic axonal injury: Practical issues for diagnosis in medicolegal cases. Neuropathol Appl Neurobiol 2000;26:105-16 (Pubitemid 30251383)
    • (2000) Neuropathology and Applied Neurobiology , vol.26 , Issue.2 , pp. 105-116
    • Geddes, J.F.1    Whitwell, H.L.2    Graham, D.I.3
  • 64
    • 0020369485 scopus 로고
    • Diffuse axonal injury and traumatic coma in the primate
    • DOI 10.1002/ana.410120611
    • Gennarelli TA, Thibault LE, Adams JH, et al. Diffuse axonal injury and traumatic coma in the primate. Ann Neurol 1982;12:564-74 (Pubitemid 13250413)
    • (1982) Annals of Neurology , vol.12 , Issue.6 , pp. 564-574
    • Gennarelli, T.A.1    Thibault, L.E.2    Adams, J.H.3
  • 65
    • 0029010574 scopus 로고
    • Axonal injury: A universal consequence of fatal closed head injury?
    • Gentleman SM, Roberts GW, Gennarelli TA, et al. Axonal injury: A universal consequence of fatal closed head injury? Acta Neuropathol 1995;89:537-43
    • (1995) Acta Neuropathol , vol.89 , pp. 537-543
    • Gentleman, S.M.1    Roberts, G.W.2    Gennarelli, T.A.3
  • 67
    • 0028793071 scopus 로고
    • The pathobiology of traumatically induced axonal injury in animals and humans: A review of current thoughts
    • Povlishock JT, Christman CW. The pathobiology of traumatically induced axonal injury in animals and humans: A review of current thoughts. J Neurotrauma 1995;12:555-64
    • (1995) J Neurotrauma , vol.12 , pp. 555-564
    • Povlishock, J.T.1    Christman, C.W.2
  • 68
    • 0034718421 scopus 로고    scopus 로고
    • Regulation and localization of tyrosine216 phosphorylation of glycogen synthase kinase-3beta in cellular and animal models of neuronal degeneration
    • Bhat RV, Shanley J, Correll MP, et al. Regulation and localization of tyrosine216 phosphorylation of glycogen synthase kinase-3beta in cellular and animal models of neuronal degeneration. Proc Nat Acad Sci USA 2000;97:11074-79
    • (2000) Proc Nat Acad Sci USA , vol.97 , pp. 11074-11079
    • Bhat, R.V.1    Shanley, J.2    Correll, M.P.3
  • 69
    • 0027475421 scopus 로고
    • Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation
    • Hughes K, Nikolakaki E, Plyte SE, et al. Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation. EMBO J 1993;12: 803-8 (Pubitemid 23073729)
    • (1993) EMBO Journal , vol.12 , Issue.2 , pp. 803-808
    • Hughes, K.1    Nikolakaki, E.2    Plyte, S.E.3    Totty, N.F.4    Woodgett, J.R.5
  • 70
    • 0036942638 scopus 로고    scopus 로고
    • The active form of glycogen synthase kinase-3β is associated with granulovacuolar degeneration in neurons in Alzheimers's disease
    • DOI 10.1007/s004010100435
    • Leroy K, Boutajangout A, Authelet M, et al. The active form of glycogen synthase kinase-3beta is associated with granulovacuolar degeneration in neurons in Alzheimer's disease. Acta Neuropathol 2002;103:91-99 (Pubitemid 36067485)
    • (2002) Acta Neuropathologica , vol.103 , Issue.2 , pp. 91-99
    • Leroy, K.1    Boutajangout, A.2    Authelet, M.3    Woodgett, J.R.4    Anderton, B.H.5    Brion, J.-P.6
  • 71
    • 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, Smeal T, et al. Identification of an oncoprotein-and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. Genes Dev 1993;7:2135-48 (Pubitemid 23336140)
    • (1993) Genes and Development , vol.7 , Issue.11 , pp. 2135-2148
    • Hibi, M.1    Lin, A.2    Smeal, T.3    Minden, A.4    Karin, M.5
  • 72
    • 0028987679 scopus 로고
    • Distribution of beta-amyloid protein in the brain following severe head injury
    • Graham DI, Gentleman SM, Lynch A, et al. Distribution of beta-amyloid protein in the brain following severe head injury. Neuropathol Appl Neurobiol 1995;21:27-34
    • (1995) Neuropathol Appl Neurobiol , vol.21 , pp. 27-34
    • Graham, D.I.1    Gentleman, S.M.2    Lynch, A.3
  • 74
    • 0034698233 scopus 로고    scopus 로고
    • Antibodies to the C-terminus of the β-amyloid precursor protein (APP): A site specific marker for the detection of traumatic axonal injury
    • DOI 10.1016/S0006-8993(00)02485-9, PII S0006899300024859
    • Stone JR, Singleton RH, Povlishock JT. Antibodies to the C-terminus of the beta-amyloid precursor protein (APP): A site specific marker for the detection of traumatic axonal injury. Brain Res 2000;871:288-302 (Pubitemid 30433880)
    • (2000) Brain Research , vol.871 , Issue.2 , pp. 288-302
    • Stone, J.R.1    Singleton, R.H.2    Povlishock, J.T.3
  • 75
    • 0035690458 scopus 로고    scopus 로고
    • Intra-axonal neurofilament compaction does not evoke local axonal swelling in all traumatically injured axons
    • DOI 10.1006/exnr.2001.7818
    • Stone JR, Singleton RH, Povlishock JT. Intra-axonal neurofilament compaction does not evoke local axonal swelling in all traumatically injured axons. Exp Neurol 2001;172:320-31 (Pubitemid 34075081)
    • (2001) Experimental Neurology , vol.172 , Issue.2 , pp. 320-331
    • Stone, J.R.1    Singleton, R.H.2    Povlishock, J.T.3
  • 76
    • 0031020909 scopus 로고    scopus 로고
    • Amyloid precursor protein processing and A beta42 deposition in a transgenic mouse model of Alzheimer disease
    • Johnson-Wood K, Lee M, Motter R, et al. Amyloid precursor protein processing and A beta42 deposition in a transgenic mouse model of Alzheimer disease. Proc Natl Acad USA 1997;94:1550-55
    • (1997) Proc Natl Acad USA , vol.94 , pp. 1550-1555
    • Johnson-Wood, K.1    Lee, M.2    Motter, R.3
  • 78
    • 0026501888 scopus 로고
    • Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau
    • Greenberg SG, Davies P, Schein JD, et al. Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau. J Biol Chem 1992;267:564-69
    • (1992) J Biol Chem , vol.267 , pp. 564-569
    • Greenberg, S.G.1    Davies, P.2    Schein, J.D.3
  • 79
    • 0028593606 scopus 로고
    • Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404
    • Otvos L Jr, Feiner L, Lang E, et al. Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404. J Neurosci Res 1994;39:669-73
    • (1994) J Neurosci Res , vol.39 , pp. 669-673
    • Otvos Jr., L.1    Feiner, L.2    Lang, E.3
  • 82
    • 0037819374 scopus 로고    scopus 로고
    • Enhanced activation of axonally transported stress-activated protein kinases in peripheral nerve in diabetic neuropathy is prevented by neurotrophin-3
    • Middlemas A, Delcroix JD, Sayers NM, et al. Enhanced activation of axonally transported stress-activated protein kinases in peripheral nerve in diabetic neuropathy is prevented by neurotrophin-3. Brain 2003;126: 1671-82 (Pubitemid 36834943)
    • (2003) Brain , vol.126 , Issue.7 , pp. 1671-1682
    • Middlemas, A.1    Delcroix, J.-D.2    Sayers, N.M.3    Tomlinson, D.R.4    Fernyhough, P.5
  • 83
    • 0035881379 scopus 로고    scopus 로고
    • Anterograde and retrograde transport of active extracellular signal-related kinase 1 (ERK1) in the ligated rat sciatic nerve
    • DOI 10.1016/S0306-4522(01)00235-4, PII S0306452201002354
    • Reynolds AJ, Hendry IA, Bartlett SE. Anterograde and retrograde transport of active extracellular signalYregulated kinase 1 (ERK1) in the ligated rat sciatic nerve. Neuroscience 2001;105:761-71 (Pubitemid 32769838)
    • (2001) Neuroscience , vol.105 , Issue.3 , pp. 761-771
    • Reynolds, A.J.1    Hendry, I.A.2    Bartlett, S.E.3
  • 84
    • 77958065504 scopus 로고    scopus 로고
    • Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy
    • Brunden KR, Zhang B, Carroll J, et al. Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy. J Neurosci 2010;30:13861-66
    • (2010) J Neurosci , vol.30 , pp. 13861-13866
    • Brunden, K.R.1    Zhang, B.2    Carroll, J.3
  • 86
    • 70349212110 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase pathway activation in human and experimental cerebral contusion
    • Ortolano F, Colombo A, Zanier ER, et al. c-Jun N-terminal kinase pathway activation in human and experimental cerebral contusion. J Neuropathol Exp Neurol 2009;68:964-71
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 964-971
    • Ortolano, F.1    Colombo, A.2    Zanier, E.R.3
  • 88
    • 0036922686 scopus 로고    scopus 로고
    • Temporal and spatial profile of phosphorylated mitogen-activated protein kinase pathways after lateral fluid percussion injury in the cortex of the rat brain
    • Otani N, Nawashiro H, Fukui S, et al. Temporal and spatial profile of phosphorylated mitogenYactivated protein kinase pathways after lateral fluid percussion injury in the cortex of the rat brain. J Neurotrauma 2002; 19:1587-96 (Pubitemid 36026214)
    • (2002) Journal of Neurotrauma , vol.19 , Issue.12 , pp. 1587-1596
    • Otani, N.1    Nawashiro, H.2    Fukui, S.3    Nomura, N.4    Shima, K.5
  • 89
    • 0042986952 scopus 로고    scopus 로고
    • Acute activation of mitogen-activated protein kinases following traumatic brain injury in the rat: Implications for posttraumatic cell death
    • DOI 10.1016/S0014-4886(03)00166-3
    • Raghupathi R, Muir JK, Fulp CT, et al. Acute activation of mitogenactivated protein kinases following traumatic brain injury in the rat: Implications for posttraumatic cell death. Exp Neurol 2003;183:438-48 (Pubitemid 37205085)
    • (2003) Experimental Neurology , vol.183 , Issue.2 , pp. 438-448
    • Raghupathi, R.1    Muir, J.K.2    Fulp, C.T.3    Pittman, R.N.4    McIntosh, T.K.5
  • 90
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • Kyriakis JM, Avruch J. Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol Rev 2001;81:807-69 (Pubitemid 32267078)
    • (2001) Physiological Reviews , vol.81 , Issue.2 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 91
    • 22844445441 scopus 로고    scopus 로고
    • Mixed lineage kinase-c-jun N-terminal kinase signaling pathway: A new therapeutic target in Parkinson's disease
    • DOI 10.1002/mds.20390
    • Silva RM, Kuan CY, Rakic P, et al. Mixed lineage kinase-c-jun N-terminal kinase signaling pathway: A new therapeutic target in Parkinson's disease. Mov Disord 2005;20:653-64 (Pubitemid 41051776)
    • (2005) Movement Disorders , vol.20 , Issue.6 , pp. 653-664
    • Silva, R.M.1    Kuan, C.-Y.2    Rakic, P.3    Burke, R.E.4
  • 93
    • 63649153518 scopus 로고    scopus 로고
    • A dual leucine kinase-dependent axon self-destruction program promotes Wallerian degeneration
    • Miller BR, Press C, Daniels RW, et al. A dual leucine kinase-dependent axon self-destruction program promotes Wallerian degeneration. Nat Neurosci 2009;12:387-89
    • (2009) Nat Neurosci , vol.12 , pp. 387-389
    • Miller, B.R.1    Press, C.2    Daniels, R.W.3
  • 94
    • 79960032374 scopus 로고    scopus 로고
    • Pathogenic forms of tau inhibit kinesin-dependent axonal transport through a mechanism involving activation of axonal phosphotransferases
    • Kanaan NM, Morfini GA, Lapointe NE, et al. Pathogenic forms of tau inhibit kinesin-dependent axonal transport through a mechanism involving activation of axonal phosphotransferases. J Neurosci 2011;31:9858-68
    • (2011) J Neurosci , vol.31 , pp. 9858-9868
    • Kanaan, N.M.1    Morfini, G.A.2    Lapointe, N.E.3
  • 95
    • 79953087890 scopus 로고    scopus 로고
    • The acetylation of tau inhibits its function and promotes pathological tau aggregation
    • Cohen TJ, Guo JL, Hurtado DE, et al. The acetylation of tau inhibits its function and promotes pathological tau aggregation. Nat Commun 2011;2:252
    • (2011) Nat Commun , vol.2 , pp. 252
    • Cohen, T.J.1    Guo, J.L.2    Hurtado, D.E.3
  • 96
    • 77957001697 scopus 로고    scopus 로고
    • Acetylation of tau inhibits its degradation and contributes to tauopathy
    • Min SW, Cho SH, Zhou Y, et al. Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron 2010;67:953-66
    • (2010) Neuron , vol.67 , pp. 953-966
    • Min, S.W.1    Cho, S.H.2    Zhou, Y.3
  • 97
    • 80051519518 scopus 로고    scopus 로고
    • Image-based screening identifies novel roles for i{kappa}b kinase and glycogen synthase kinase 3 in axonal degeneration
    • Gerdts J, Sasaki Y, Vohra B, et al. Image-based screening identifies novel roles for i{kappa}b kinase and glycogen synthase kinase 3 in axonal degeneration. J Biol Chem 2011;286:28011-18
    • (2011) J Biol Chem , vol.286 , pp. 28011-28018
    • Gerdts, J.1    Sasaki, Y.2    Vohra, B.3


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