메뉴 건너뛰기




Volumn 28, Issue 47, 2008, Pages 12241-12254

Marked calpastatin (CAST) depletion in Alzheimer's disease accelerates cytoskeleton disruption and neurodegeneration: Neuroprotection by CAST overexpression

Author keywords

Apoptosis; Calpain; Caspase; Cdk5; ERK; Tau

Indexed keywords

CALPAIN; CALPAIN 2; CALPASTATIN; CASPASE 3; INTERLEUKIN 1BETA CONVERTING ENZYME; KAINIC ACID; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEINASE; SHORT HAIRPIN RNA; TAU PROTEIN;

EID: 58149397537     PISSN: 02706474     EISSN: 02706474     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.4119-08.2008     Document Type: Article
Times cited : (92)

References (72)
  • 1
    • 0036934648 scopus 로고    scopus 로고
    • Calpain activation in neurodegenerative diseases: Confocal immunofluorescence study with antibodies specifically recognizing the active form of calpain 2
    • Adamec E, Mohan P, Vonsattel JP, Nixon RA (2002) Calpain activation in neurodegenerative diseases: confocal immunofluorescence study with antibodies specifically recognizing the active form of calpain 2. Acta Neuropathol (Berl) 104:92-104.
    • (2002) Acta Neuropathol (Berl) , vol.104 , pp. 92-104
    • Adamec, E.1    Mohan, P.2    Vonsattel, J.P.3    Nixon, R.A.4
  • 6
    • 33749591567 scopus 로고    scopus 로고
    • Calpastatin in rat myoblasts: Transient diminution and decreased phosphorylation depend on myogenin-directed myoblast differentiation
    • Barnoy S, Kosower NS (2007) Calpastatin in rat myoblasts: transient diminution and decreased phosphorylation depend on myogenin-directed myoblast differentiation. Int J Biochem Cell Biol 39:253-261.
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 253-261
    • Barnoy, S.1    Kosower, N.S.2
  • 9
    • 33644897573 scopus 로고    scopus 로고
    • Calpain inhibition: A therapeutic strategy targeting multiple disease states
    • Carragher NO (2006) Calpain inhibition: a therapeutic strategy targeting multiple disease states. Curr Pharm Des 12:615-638.
    • (2006) Curr Pharm Des , vol.12 , pp. 615-638
    • Carragher, N.O.1
  • 10
    • 0025355591 scopus 로고
    • Lysosomal proteinase antigens are prominently localized within senile plaques of Alzheimer's disease: Evidence for a neuronal origin
    • Cataldo AM, Thayer CY, Bird ED, Wheelock TR, Nixon RA (1990) Lysosomal proteinase antigens are prominently localized within senile plaques of Alzheimer's disease: evidence for a neuronal origin. Brain Res 513:181-192.
    • (1990) Brain Res , vol.513 , pp. 181-192
    • Cataldo, A.M.1    Thayer, C.Y.2    Bird, E.D.3    Wheelock, T.R.4    Nixon, R.A.5
  • 12
    • 33846245120 scopus 로고    scopus 로고
    • Kainate induces AKT, ERK and cdk5/GSK3beta pathway deregulation, phosphorylates tau protein in mouse hippocampus
    • Crespo-Biel N, Canudas AM, Camins A, Pallàs M (2007) Kainate induces AKT, ERK and cdk5/GSK3beta pathway deregulation, phosphorylates tau protein in mouse hippocampus. Neurochem Int 50:435-442.
    • (2007) Neurochem Int , vol.50 , pp. 435-442
    • Crespo-Biel, N.1    Canudas, A.M.2    Camins, A.3    Pallàs, M.4
  • 13
    • 0345405447 scopus 로고    scopus 로고
    • Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles
    • Cruz JC, Tseng HC, Goldman JA, Shih H, Tsai LH (2003) Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles. Neuron 40:471-483.
    • (2003) Neuron , vol.40 , pp. 471-483
    • Cruz, J.C.1    Tseng, H.C.2    Goldman, J.A.3    Shih, H.4    Tsai, L.H.5
  • 14
    • 0018172951 scopus 로고
    • Radiolabeling of proteins by reductive alkylation with [14C] formaldehyde and sodium cyanoborohydride
    • Dottavio-Martin D, Ravel JM (1978) Radiolabeling of proteins by reductive alkylation with [14C] formaldehyde and sodium cyanoborohydride. Anal Biochem 87:562-565.
    • (1978) Anal Biochem , vol.87 , pp. 562-565
    • Dottavio-Martin, D.1    Ravel, J.M.2
  • 15
    • 33644853371 scopus 로고    scopus 로고
    • Microtubule-associated protein MAP1A, MAP1B, and MAP2 proteolysis during soluble amyloid beta-peptide-induced neuronal apoptosis. Synergistic involvement of calpain and caspase-3
    • Fifre A, Sponne I, Koziel V, Kriem B, Yen Potin FT, Bihain BE, Olivier JL, Oster T, Pillot T (2006) Microtubule-associated protein MAP1A, MAP1B, and MAP2 proteolysis during soluble amyloid beta-peptide-induced neuronal apoptosis. Synergistic involvement of calpain and caspase-3. J Biol Chem 281:229-240.
    • (2006) J Biol Chem , vol.281 , pp. 229-240
    • Fifre, A.1    Sponne, I.2    Koziel, V.3    Kriem, B.4    Yen Potin, F.T.5    Bihain, B.E.6    Olivier, J.L.7    Oster, T.8    Pillot, T.9
  • 17
    • 0019934878 scopus 로고
    • Intrahippocampal kainic acid, seizures and local neuronal degeneration: Relationships assessed in unanesthetized rats
    • French ED, Aldinio C, Schwarcz R (1982) Intrahippocampal kainic acid, seizures and local neuronal degeneration: relationships assessed in unanesthetized rats. Neuroscience 7:2525-2536.
    • (1982) Neuroscience , vol.7 , pp. 2525-2536
    • French, E.D.1    Aldinio, C.2    Schwarcz, R.3
  • 19
    • 0026911137 scopus 로고
    • Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin?
    • Goll DE, Thompson VF, Taylor RG, Zalewska T (1992) Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin? Bioessays 14:549-556.
    • (1992) Bioessays , vol.14 , pp. 549-556
    • Goll, D.E.1    Thompson, V.F.2    Taylor, R.G.3    Zalewska, T.4
  • 21
    • 0030888520 scopus 로고    scopus 로고
    • Calpains and calpastatin in SH-SY5Y neuroblastoma cells during retinoic acid-induced differentiation and neurite outgrowth: Comparison with the human brain calpain system
    • Grynspan F, Griffin WB, Mohan PS, Shea TB, Nixon RA (1997a) Calpains and calpastatin in SH-SY5Y neuroblastoma cells during retinoic acid-induced differentiation and neurite outgrowth: comparison with the human brain calpain system. J Neurosci Res 48:181-191.
    • (1997) J Neurosci Res , vol.48 , pp. 181-191
    • Grynspan, F.1    Griffin, W.B.2    Mohan, P.S.3    Shea, T.B.4    Nixon, R.A.5
  • 22
    • 0030836467 scopus 로고    scopus 로고
    • Active site-directed antibodies identify calpain II as an early-appearing and pervasive component of neurofibrillary pathology in Alzheimer's disease
    • Grynspan F, Griffin WR, Cataldo A, Katayama S, Nixon RA (1997b) Active site-directed antibodies identify calpain II as an early-appearing and pervasive component of neurofibrillary pathology in Alzheimer's disease. Brain Res 763:145-158.
    • (1997) Brain Res , vol.763 , pp. 145-158
    • Grynspan, F.1    Griffin, W.R.2    Cataldo, A.3    Katayama, S.4    Nixon, R.A.5
  • 23
    • 33645889361 scopus 로고    scopus 로고
    • 3-[2-[4-(3-Chloro-2- methylphenylmethyl)-1-piperazinyl]ethyl]-5,6-dimethoxy -1-(4-imidazolylmethyl)- 1H-indazole dihydro-chloride 3.5 hydrate (DY-9760e) is neuroprotective in rat microsphere embolism: Role of the cross-talk between calpain and caspase-3 through calpastatin
    • Han F, Shirasaki Y, Fukunaga K (2006) 3-[2-[4-(3-Chloro-2- methylphenylmethyl)-1-piperazinyl]ethyl]-5,6-dimethoxy -1-(4-imidazolylmethyl)- 1H-indazole dihydro-chloride 3.5 hydrate (DY-9760e) is neuroprotective in rat microsphere embolism: role of the cross-talk between calpain and caspase-3 through calpastatin. J Pharmacol Exp Ther 317:529-536.
    • (2006) J Pharmacol Exp Ther , vol.317 , pp. 529-536
    • Han, F.1    Shirasaki, Y.2    Fukunaga, K.3
  • 25
    • 0031613125 scopus 로고    scopus 로고
    • Expression of biologically active human calpastatin in baculovirus-infected insect cells and in Escherichia coli
    • Hitomi K, Yokoyama A, Maki M (1998) Expression of biologically active human calpastatin in baculovirus-infected insect cells and in Escherichia coli. Biosci Biotechnol Biochem 62:136-141.
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 136-141
    • Hitomi, K.1    Yokoyama, A.2    Maki, M.3
  • 26
    • 39849110726 scopus 로고    scopus 로고
    • The GSK3 hypothesis of Alzheimer's disease
    • Hooper C, Killick R, Lovestone S (2008) The GSK3 hypothesis of Alzheimer's disease. J Neurochem 104:1433-1439.
    • (2008) J Neurochem , vol.104 , pp. 1433-1439
    • Hooper, C.1    Killick, R.2    Lovestone, S.3
  • 27
    • 0033984684 scopus 로고    scopus 로고
    • Activation of calpain precedes morphological alterations during hydrogen peroxide-induced apoptosis in neuronally differentiated mouse embryonal carcinoma P19 cell line
    • Ishihara I, Minami Y, Nishizaki T, Matsuoka T, Yamamura H (2000) Activation of calpain precedes morphological alterations during hydrogen peroxide-induced apoptosis in neuronally differentiated mouse embryonal carcinoma P19 cell line. Neurosci Lett 279:97-100.
    • (2000) Neurosci Lett , vol.279 , pp. 97-100
    • Ishihara, I.1    Minami, Y.2    Nishizaki, T.3    Matsuoka, T.4    Yamamura, H.5
  • 28
    • 0034739826 scopus 로고    scopus 로고
    • Activation of JNK and p38 in rat hippocampus after kainic acid induced seizure
    • Jeon SH, Kim YS, Bae CD, Park JB (2000) Activation of JNK and p38 in rat hippocampus after kainic acid induced seizure. Exp Mol Med 32:227-230.
    • (2000) Exp Mol Med , vol.32 , pp. 227-230
    • Jeon, S.H.1    Kim, Y.S.2    Bae, C.D.3    Park, J.B.4
  • 30
    • 0034595834 scopus 로고    scopus 로고
    • Calpain-dependent proteolytic cleavage of the p35 cyclin-dependent kinase 5 activator to p25
    • Kusakawa G, Saito T, Onuki R, Ishiguro K, Kishimoto T, Hisanaga S (2000) Calpain-dependent proteolytic cleavage of the p35 cyclin-dependent kinase 5 activator to p25. J Biol Chem 275:17166-17172.
    • (2000) J Biol Chem , vol.275 , pp. 17166-17172
    • Kusakawa, G.1    Saito, T.2    Onuki, R.3    Ishiguro, K.4    Kishimoto, T.5    Hisanaga, S.6
  • 31
    • 0034883504 scopus 로고    scopus 로고
    • Neuroprotective and neurorescuing effects of isoform-specific nitric oxide synthase inhibitors, nitric oxide scavenger, and antioxidant against beta-amyloid toxicity
    • Law A, Gauthier S, Quirion R (2001) Neuroprotective and neurorescuing effects of isoform-specific nitric oxide synthase inhibitors, nitric oxide scavenger, and antioxidant against beta-amyloid toxicity. Br J Pharmacol 133:1114-1124.
    • (2001) Br J Pharmacol , vol.133 , pp. 1114-1124
    • Law, A.1    Gauthier, S.2    Quirion, R.3
  • 32
    • 0038705066 scopus 로고    scopus 로고
    • Cdk5: One of the links between senile plaques and neurofibrillary tangles?
    • Lee MS, Tsai LH (2003) Cdk5: one of the links between senile plaques and neurofibrillary tangles? J Alzheimers Dis 5:127-137.
    • (2003) J Alzheimers Dis , vol.5 , pp. 127-137
    • Lee, M.S.1    Tsai, L.H.2
  • 34
    • 0025904444 scopus 로고    scopus 로고
    • Lee VM, Balin BJ, Otvos L Jr, Trojanowski JQ (1991) A68: a major subunit of paired helical filaments and derivatized forms of normal Tau. Science 251:675-678.
    • Lee VM, Balin BJ, Otvos L Jr, Trojanowski JQ (1991) A68: a major subunit of paired helical filaments and derivatized forms of normal Tau. Science 251:675-678.
  • 35
    • 1542313858 scopus 로고    scopus 로고
    • Taurine prevents the neurotoxicity of beta-amyloid and glutamate receptor agonists: Activation of GABA receptors and possible implications for Alzheimer's disease and other neurological disorders
    • Louzada PR, Lima AC, Mendonca-Silva DL, Noël F, De Mello FG, Ferreira ST (2004) Taurine prevents the neurotoxicity of beta-amyloid and glutamate receptor agonists: activation of GABA receptors and possible implications for Alzheimer's disease and other neurological disorders. FASEB J 18:511-518.
    • (2004) FASEB J , vol.18 , pp. 511-518
    • Louzada, P.R.1    Lima, A.C.2    Mendonca-Silva, D.L.3    Noël, F.4    De Mello, F.G.5    Ferreira, S.T.6
  • 37
    • 33747717424 scopus 로고    scopus 로고
    • Association of calpastatin with inactive calpain: A novel mechanism to control the activation of the protease?
    • Melloni E, Averna M, Stifanese R, De Tullio R, Defranchi E, Salamino F, Pontremoli S (2006) Association of calpastatin with inactive calpain: a novel mechanism to control the activation of the protease? J Biol Chem 281:24945-24954.
    • (2006) J Biol Chem , vol.281 , pp. 24945-24954
    • Melloni, E.1    Averna, M.2    Stifanese, R.3    De Tullio, R.4    Defranchi, E.5    Salamino, F.6    Pontremoli, S.7
  • 38
    • 0141761520 scopus 로고    scopus 로고
    • Seizures in elderly patients with dementia: Epidemiology and management
    • Mendez M, Lim G (2003) Seizures in elderly patients with dementia: epidemiology and management. Drugs Aging 20:791-803.
    • (2003) Drugs Aging , vol.20 , pp. 791-803
    • Mendez, M.1    Lim, G.2
  • 39
    • 0028868307 scopus 로고
    • Purification and properties of high molecular weight calpastatin from bovine brain
    • Mohan PS, Nixon RA (1995) Purification and properties of high molecular weight calpastatin from bovine brain. J Neurochem 64:859-866.
    • (1995) J Neurochem , vol.64 , pp. 859-866
    • Mohan, P.S.1    Nixon, R.A.2
  • 41
    • 0141762744 scopus 로고    scopus 로고
    • The calpains in aging and aging-related diseases
    • Nixon RA (2003) The calpains in aging and aging-related diseases. Ageing Res Rev 2:407-418.
    • (2003) Ageing Res Rev , vol.2 , pp. 407-418
    • Nixon, R.A.1
  • 45
    • 33748752882 scopus 로고    scopus 로고
    • The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation
    • Plattner F, Angelo M, Giese KP (2006) The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation. J Biol Chem 281:25457-25465.
    • (2006) J Biol Chem , vol.281 , pp. 25457-25465
    • Plattner, F.1    Angelo, M.2    Giese, K.P.3
  • 47
    • 0037135978 scopus 로고    scopus 로고
    • Gene replacement in mice reveals that the heavily phosphorylated tail of neurofilament heavy subunit does not affect axonal caliber or the transit of cargoes in slow axonal transport
    • Rao MV, Garcia ML, Miyazaki Y, Gotow T, Yuan A, Mattina S, Ward CM, Calcutt NA, Uchiyama Y, Nixon RA, Cleveland DW (2002) Gene replacement in mice reveals that the heavily phosphorylated tail of neurofilament heavy subunit does not affect axonal caliber or the transit of cargoes in slow axonal transport. J Cell Biol 158:681-693.
    • (2002) J Cell Biol , vol.158 , pp. 681-693
    • Rao, M.V.1    Garcia, M.L.2    Miyazaki, Y.3    Gotow, T.4    Yuan, A.5    Mattina, S.6    Ward, C.M.7    Calcutt, N.A.8    Uchiyama, Y.9    Nixon, R.A.10    Cleveland, D.W.11
  • 48
    • 0027474051 scopus 로고
    • Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: A potential molecular basis for neuronal degeneration
    • Saito K, Elce JS, Hamos JE, Nixon RA (1993) Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration. Proc Natl Acad Sci U S A 90:2628-2632.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2628-2632
    • Saito, K.1    Elce, J.S.2    Hamos, J.E.3    Nixon, R.A.4
  • 49
    • 22844438739 scopus 로고    scopus 로고
    • Tissue processing prior to protein analysis and amyloid-beta quantitation
    • Schmidt SD, Jiang Y, Nixon RA, Mathews PM (2005) Tissue processing prior to protein analysis and amyloid-beta quantitation. Methods Mol Biol 299:267-278.
    • (2005) Methods Mol Biol , vol.299 , pp. 267-278
    • Schmidt, S.D.1    Jiang, Y.2    Nixon, R.A.3    Mathews, P.M.4
  • 50
    • 0029874834 scopus 로고    scopus 로고
    • Calcium influx into human neuroblastoma cells induces ALZ-50 immunoreactivity: Involvement of calpain-mediated hydrolysis of protein kinase C
    • Shea TB, Spencer MJ, Beermann ML, Cressman CM, Nixon RA (1996) Calcium influx into human neuroblastoma cells induces ALZ-50 immunoreactivity: involvement of calpain-mediated hydrolysis of protein kinase C. J Neurochem 66:1539-1549.
    • (1996) J Neurochem , vol.66 , pp. 1539-1549
    • Shea, T.B.1    Spencer, M.J.2    Beermann, M.L.3    Cressman, C.M.4    Nixon, R.A.5
  • 51
    • 0033826589 scopus 로고    scopus 로고
    • Downregulation of the calpain inhibitor protein calpastatin by caspases during renal ischemia-reperfusion
    • Shi Y, Melnikov VY, Schrier RW, Edelstein CL (2000) Downregulation of the calpain inhibitor protein calpastatin by caspases during renal ischemia-reperfusion. Am J Physiol Renal Physiol 279:F509-F517.
    • (2000) Am J Physiol Renal Physiol , vol.279
    • Shi, Y.1    Melnikov, V.Y.2    Schrier, R.W.3    Edelstein, C.L.4
  • 53
    • 0024363137 scopus 로고
    • Calpain I activation is specifically related to excitatory amino acid induction of hippocampal damage
    • Siman R, Noszek JC, Kegerise C (1989) Calpain I activation is specifically related to excitatory amino acid induction of hippocampal damage. J Neurosci 9:1579-1590.
    • (1989) J Neurosci , vol.9 , pp. 1579-1590
    • Siman, R.1    Noszek, J.C.2    Kegerise, C.3
  • 54
    • 0034551780 scopus 로고    scopus 로고
    • Presenilin-1 P264L knock-in mutation: Differential effects on abeta production, amyloid deposition, and neuronal vulnerability
    • Siman R, Reaume AG, Savage MJ, Trusko S, Lin YG, Scott RW, Flood DG (2000) Presenilin-1 P264L knock-in mutation: differential effects on abeta production, amyloid deposition, and neuronal vulnerability. J Neurosci 20:8717-8726.
    • (2000) J Neurosci , vol.20 , pp. 8717-8726
    • Siman, R.1    Reaume, A.G.2    Savage, M.J.3    Trusko, S.4    Lin, Y.G.5    Scott, R.W.6    Flood, D.G.7
  • 55
    • 18144407551 scopus 로고    scopus 로고
    • Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: Evidence from calpastatin mutant mice
    • Takano J, Tomioka M, Tsubuki S, Higuchi M, Iwata N, Itohara S, Maki M, Saido TC (2005) Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: evidence from calpastatin mutant mice. J Biol Chem 280:16175-16184.
    • (2005) J Biol Chem , vol.280 , pp. 16175-16184
    • Takano, J.1    Tomioka, M.2    Tsubuki, S.3    Higuchi, M.4    Iwata, N.5    Itohara, S.6    Maki, M.7    Saido, T.C.8
  • 59
    • 0028674139 scopus 로고
    • Interleukin-1 beta converting enzyme
    • Thornberry NA (1994) Interleukin-1 beta converting enzyme. Methods Enzymol 244:615-631.
    • (1994) Methods Enzymol , vol.244 , pp. 615-631
    • Thornberry, N.A.1
  • 60
    • 17444406677 scopus 로고    scopus 로고
    • Caspase-1 activity is required for neuronal differentiation of PC12 cells: Cross-talk between the caspase and calpain systems
    • Vaisid T, Kosower NS, Barnoy S (2005) Caspase-1 activity is required for neuronal differentiation of PC12 cells: cross-talk between the caspase and calpain systems. Biochim Biophys Acta 1743:223-230.
    • (2005) Biochim Biophys Acta , vol.1743 , pp. 223-230
    • Vaisid, T.1    Kosower, N.S.2    Barnoy, S.3
  • 62
    • 0022539722 scopus 로고
    • Calcium-activated neutral proteinase of human brain: Subunit structure and enzymatic properties of multiple molecular forms
    • Vitto A, Nixon RA (1986) Calcium-activated neutral proteinase of human brain: subunit structure and enzymatic properties of multiple molecular forms. J Neurochem 47:1039-1051.
    • (1986) J Neurochem , vol.47 , pp. 1039-1051
    • Vitto, A.1    Nixon, R.A.2
  • 64
    • 20344388665 scopus 로고    scopus 로고
    • Kainic acid-mediated excitotoxicity as a model for neurodegeneration
    • Wang Q, Yu S, Simonyi A, Sun GY, Sun AY (2005) Kainic acid-mediated excitotoxicity as a model for neurodegeneration. Mol Neurobiol 31:3-16.
    • (2005) Mol Neurobiol , vol.31 , pp. 3-16
    • Wang, Q.1    Yu, S.2    Simonyi, A.3    Sun, G.Y.4    Sun, A.Y.5
  • 66
    • 4644250807 scopus 로고    scopus 로고
    • Higher calpastatin levels correlate with resistance to calpain-mediated proteolysis and neuronal apoptosis in juvenile rats after spinal cord injury
    • Wingrave JM, Sribnick EA, Wilford GG, Matzelle DD, Mou JA, Ray SK, Hogan EL, Banik NL (2004) Higher calpastatin levels correlate with resistance to calpain-mediated proteolysis and neuronal apoptosis in juvenile rats after spinal cord injury. J Neurotrauma 21:1240-1254.
    • (2004) J Neurotrauma , vol.21 , pp. 1240-1254
    • Wingrave, J.M.1    Sribnick, E.A.2    Wilford, G.G.3    Matzelle, D.D.4    Mou, J.A.5    Ray, S.K.6    Hogan, E.L.7    Banik, N.L.8
  • 67
    • 33747870115 scopus 로고    scopus 로고
    • Calpain and synaptic function
    • Wu HY, Lynch DR (2006) Calpain and synaptic function. Mol Neurobiol 33:215-236.
    • (2006) Mol Neurobiol , vol.33 , pp. 215-236
    • Wu, H.Y.1    Lynch, D.R.2
  • 68
    • 33846502748 scopus 로고    scopus 로고
    • Calpain-mediated mGluR1alpha truncation: A key step in excitotoxicity
    • Xu W, Wong TP, Chery N, Gaertner T, Wang YT, Baudry M (2007) Calpain-mediated mGluR1alpha truncation: a key step in excitotoxicity. Neuron 53:399-412.
    • (2007) Neuron , vol.53 , pp. 399-412
    • Xu, W.1    Wong, T.P.2    Chery, N.3    Gaertner, T.4    Wang, Y.T.5    Baudry, M.6
  • 69
    • 0035859053 scopus 로고    scopus 로고
    • p25 protein in neurodegeneration
    • Yoo BC, Lubec G (2001) p25 protein in neurodegeneration. Nature 411:763-764.
    • (2001) Nature , vol.411 , pp. 763-764
    • Yoo, B.C.1    Lubec, G.2
  • 71
    • 0036405495 scopus 로고    scopus 로고
    • Comparison of calpain and caspase activities in the adult rat brain after transient forebrain ischemia
    • Zhang C, Siman R, Xu YA, Mills AM, Frederick JR, Neumar RW (2002) Comparison of calpain and caspase activities in the adult rat brain after transient forebrain ischemia. Neurobiol Dis 10:289-305.
    • (2002) Neurobiol Dis , vol.10 , pp. 289-305
    • Zhang, C.1    Siman, R.2    Xu, Y.A.3    Mills, A.M.4    Frederick, J.R.5    Neumar, R.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.