메뉴 건너뛰기




Volumn 5, Issue 12, 2010, Pages

Amyloid-β triggers the release of neuronal Hexokinase 1 from mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMYLOID BETA PROTEIN[1-42]; DEOXYGLUCOSE; HEXOKINASE 1; OLIGOMER; AMYLOID BETA PROTEIN; HEXOKINASE; HK1 PROTEIN, HUMAN; ISOENZYME; REACTIVE OXYGEN METABOLITE; TETRAZOLIUM; THIAZOLE DERIVATIVE; THIAZOLYL BLUE;

EID: 78650719636     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0015230     Document Type: Article
Times cited : (81)

References (52)
  • 1
    • 0942290437 scopus 로고    scopus 로고
    • In self-defense: Hexokinase promotes voltage-dependent anion channel closure and prevents mitochondria-mediated apoptotic cell death
    • Azoulay-Zohar H, Israelson A, Abu-Hamad S, Shoshan-Barmatz V (2004) In self-defense: hexokinase promotes voltage-dependent anion channel closure and prevents mitochondria-mediated apoptotic cell death. Biochem J 377: 347-355.
    • (2004) Biochem J , vol.377 , pp. 347-355
    • Azoulay-Zohar, H.1    Israelson, A.2    Abu-Hamad, S.3    Shoshan-Barmatz, V.4
  • 2
    • 10644221251 scopus 로고    scopus 로고
    • Insulin enhances mitochondrial inner membrane potential and increases ATP levels through phosphoinositide 3- kinase in adult sensory neurons
    • Huang TJ, Verkhratsky A, Fernyhough P (2005) Insulin enhances mitochondrial inner membrane potential and increases ATP levels through phosphoinositide 3- kinase in adult sensory neurons. Mol Cell Neurosci 28: 42-54.
    • (2005) Mol Cell Neurosci , vol.28 , pp. 42-54
    • Huang, T.J.1    Verkhratsky, A.2    Fernyhough, P.3
  • 3
    • 59149095449 scopus 로고    scopus 로고
    • Mitochondrial hexokinase II promotes neuronal survival and acts downstream of glycogen synthase kinase-3
    • Gimenez-Cassina A, Lim F, Cerrato T, Palomo GM, Diaz-Nido J (2009) Mitochondrial hexokinase II promotes neuronal survival and acts downstream of glycogen synthase kinase-3. J Biol Chem 284: 3001-3011.
    • (2009) J Biol Chem , vol.284 , pp. 3001-3011
    • Gimenez-Cassina, A.1    Lim, F.2    Cerrato, T.3    Palomo, G.M.4    Diaz-Nido, J.5
  • 4
    • 0038714272 scopus 로고    scopus 로고
    • Isozmes of mammalian hexokinase: Structure, subcelular localization and metabolic function
    • Wilson JE (2003) Isozmes of mammalian hexokinase: structure, subcelular localization and metabolic function. J Exp Biol 206: 2049-2057.
    • (2003) J Exp Biol , vol.206 , pp. 2049-2057
    • Wilson, J.E.1
  • 5
    • 0014198143 scopus 로고
    • Mitochondrial hexokinase. Release, rebinding, and location
    • Rose IA, Warms JV (1967) Mitochondrial hexokinase. Release, rebinding, and location. J Biol Chem 242: 1635-1645.
    • (1967) J Biol Chem , vol.242 , pp. 1635-1645
    • Rose, I.A.1    Warms, J.V.2
  • 6
    • 40649099615 scopus 로고    scopus 로고
    • Blockade of hexokinase activity and binding to mitochondria inhibits neurite outgrowth in cultured adult rat sensory neurons
    • Wang Z, Gardiner NJ, Fernyhough P (2008) Blockade of hexokinase activity and binding to mitochondria inhibits neurite outgrowth in cultured adult rat sensory neurons. Neurosci Lett 434: 6-11.
    • (2008) Neurosci Lett , vol.434 , pp. 6-11
    • Wang, Z.1    Gardiner, N.J.2    Fernyhough, P.3
  • 7
    • 0034672943 scopus 로고    scopus 로고
    • Metabolism and functions of glutathione in brain
    • Dringen R (2000) Metabolism and functions of glutathione in brain. Prog Neurobiol 62: 649-671.
    • (2000) Prog Neurobiol , vol.62 , pp. 649-671
    • Dringen, R.1
  • 8
    • 4544355934 scopus 로고    scopus 로고
    • Mitochondrial Bound Hexokinase Activity as a Preventive Antioxidant Defense: Steady-state ADP formation as a regulatory mechanism of membrane potential and reactive species generation in mitochondria
    • da-Silva WS, Gomez-Puyou A, De Gomez-Puyou MT, Moreno-Sanchez R, De Felice FG, et al. (2004) Mitochondrial Bound Hexokinase Activity as a Preventive Antioxidant Defense: steady-state ADP formation as a regulatory mechanism of membrane potential and reactive species generation in mitochondria. J Biol Chem 279: 39846-55.
    • (2004) J Biol Chem , vol.279 , pp. 39846-39855
    • da-Silva, W.S.1    Gomez-Puyou, A.2    De Gomez-Puyou, M.T.3    Moreno-Sanchez, R.4    De Felice, F.G.5
  • 9
    • 0042381676 scopus 로고    scopus 로고
    • The function of complexes between the outer mitochondrial membrane pore (VDAC) and the adenine nucleotide translocase in regulation of energy metabolism and apoptosis
    • Vyssokikh MY, Brdiczka D (2003) The function of complexes between the outer mitochondrial membrane pore (VDAC) and the adenine nucleotide translocase in regulation of energy metabolism and apoptosis. Acta Biochim Pol 50: 389-404.
    • (2003) Acta Biochim Pol , vol.50 , pp. 389-404
    • Vyssokikh, M.Y.1    Brdiczka, D.2
  • 11
    • 8444227821 scopus 로고    scopus 로고
    • Reactive oxygen species and synaptic plasticity in the aging hippocampus
    • Serrano F, Klann E (2004) Reactive oxygen species and synaptic plasticity in the aging hippocampus. Ageing Res Rev 3: 431-443.
    • (2004) Ageing Res Rev , vol.3 , pp. 431-443
    • Serrano, F.1    Klann, E.2
  • 12
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson MP (2004) Pathways towards and away from Alzheimer's disease. Nature 430: 631-639.
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 13
    • 33746089859 scopus 로고    scopus 로고
    • Mitochondrial abnormalities and oxidative imbalance in Alzheimer disease
    • Zhu X, Perry G, Moreira PI, Aliev G, Cash AD, et al. (2006) Mitochondrial abnormalities and oxidative imbalance in Alzheimer disease. J Alzheimers Dis 9: 147-153.
    • (2006) J Alzheimers Dis , vol.9 , pp. 147-153
    • Zhu, X.1    Perry, G.2    Moreira, P.I.3    Aliev, G.4    Cash, A.D.5
  • 14
    • 34249672242 scopus 로고    scopus 로고
    • Abeta oligomers induce neuronal oxidative stress through an N-methyl-Daspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • De Felice FG, Velasco PT, Lambert MP, Viola K, Fernandez SJ, et al. (2007) Abeta oligomers induce neuronal oxidative stress through an N-methyl-Daspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J Biol Chem 282: 11590-601.
    • (2007) J Biol Chem , vol.282 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3    Viola, K.4    Fernandez, S.J.5
  • 15
    • 45249097300 scopus 로고    scopus 로고
    • Amyloid-b peptide and NMDA induce ROS from NADPH oxidase and AA release from cytosolic phospholipase A2 in neurons
    • Shelat PB, Chalimoniuk M, Wang JH, Strosznajder JB, Lee JC, et al. (2008) Amyloid-b peptide and NMDA induce ROS from NADPH oxidase and AA release from cytosolic phospholipase A2 in neurons. J Neurochem 106: 45-55.
    • (2008) J Neurochem , vol.106 , pp. 45-55
    • Shelat, P.B.1    Chalimoniuk, M.2    Wang, J.H.3    Strosznajder, J.B.4    Lee, J.C.5
  • 16
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297: 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 17
    • 2542455537 scopus 로고    scopus 로고
    • Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease
    • Klein WL, Stine WB, Jr., Teplow DB (2004) Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiol Aging 25: 569-580.
    • (2004) Neurobiol Aging , vol.25 , pp. 569-580
    • Klein, W.L.1    Stine Jr., W.B.2    Teplow, D.B.3
  • 18
    • 34248547813 scopus 로고    scopus 로고
    • Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases
    • Ferreira ST, Vieira MN, De Felice FG (2007) Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases. IUBMB Life 59: 332-345.
    • (2007) IUBMB Life , vol.59 , pp. 332-345
    • Ferreira, S.T.1    Vieira, M.N.2    De Felice, F.G.3
  • 19
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8: 101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 20
    • 33748746162 scopus 로고    scopus 로고
    • Formation of soluble oligomers and amyloid fibrils with physical properties of the scrapie isoform of the prion protein from the C-terminal domain of recombinant murine prion protein mPrP-(121-231)
    • Martins SM, Frosoni DJ, Martinez AM, De Felice FG, Ferreira ST (2006) Formation of soluble oligomers and amyloid fibrils with physical properties of the scrapie isoform of the prion protein from the C-terminal domain of recombinant murine prion protein mPrP-(121-231). J Biol Chem 281: 26121-26128.
    • (2006) J Biol Chem , vol.281 , pp. 26121-26128
    • Martins, S.M.1    Frosoni, D.J.2    Martinez, A.M.3    De Felice, F.G.4    Ferreira, S.T.5
  • 21
    • 0035349804 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's disease beta-amyloid aggregation, neurotoxicity, and in vivo deposition by nitrophenols: Implications for Alzheimer's therapy
    • De Felice FG, Houzel JC, Garcia-Abreu J, Louzada PR, Jr., Afonso RC, et al. (2001) Inhibition of Alzheimer's disease beta-amyloid aggregation, neurotoxicity, and in vivo deposition by nitrophenols: implications for Alzheimer's therapy. FASEB J 15: 1297-9.
    • (2001) FASEB J , vol.15 , pp. 1297-1299
    • De Felice, F.G.1    Houzel, J.C.2    Garcia-Abreu, J.3    Louzada Jr., P.R.4    Afonso, R.C.5
  • 22
    • 4344688011 scopus 로고    scopus 로고
    • Targeting the neurotoxic species in Alzheimer's disease: Inhibitors of Abeta oligomerization
    • De Felice FG, Vieira MN, Saraiva LM, Figueroa-Villar JD, Garcia-Abreu J, et al. (2004) Targeting the neurotoxic species in Alzheimer's disease: inhibitors of Abeta oligomerization. FASEB J 12: 1366-72.
    • (2004) FASEB J , vol.12 , pp. 1366-1372
    • De Felice, F.G.1    Vieira, M.N.2    Saraiva, L.M.3    Figueroa-Villar, J.D.4    Garcia-Abreu, J.5
  • 23
    • 27744579437 scopus 로고    scopus 로고
    • Activation of GABA(A) receptors by taurine and muscimol blocks the neurotoxicity of betaamyloid in rat hippocampal and cortical neurons
    • Paula-Lima AC, De Felice FG, Brito-Moreira J, Ferreira ST (2005) Activation of GABA(A) receptors by taurine and muscimol blocks the neurotoxicity of betaamyloid in rat hippocampal and cortical neurons. Neuropharmacology 49: 1140-1148.
    • (2005) Neuropharmacology , vol.49 , pp. 1140-1148
    • Paula-Lima, A.C.1    De Felice, F.G.2    Brito-Moreira, J.3    Ferreira, S.T.4
  • 24
    • 47049120422 scopus 로고    scopus 로고
    • Alzheimer's disease-type neuronal tau hyperphosphorylation induced by A-beta oligomers
    • De Felice FG, Wu D, Lambert MP, Fernandez SJ, Velasco PT, et al. (2008) Alzheimer's disease-type neuronal tau hyperphosphorylation induced by A-beta oligomers. Neurobiol Aging 29: 1334-47.
    • (2008) Neurobiol Aging , vol.29 , pp. 1334-1347
    • De Felice, F.G.1    Wu, D.2    Lambert, M.P.3    Fernandez, S.J.4    Velasco, P.T.5
  • 25
    • 60549084867 scopus 로고    scopus 로고
    • Protection of synapses against Alzheimer's-linked toxins: Insulin signaling prevents the pathogenic binding of Abeta oligomers
    • De Felice FG, Vieira MN, Bomfim TR, Decker H, Velasco PT, et al. (2009) Protection of synapses against Alzheimer's-linked toxins: insulin signaling prevents the pathogenic binding of Abeta oligomers. Proc Natl Acad Sci U S A 106: 1971-6.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 1971-1976
    • De Felice, F.G.1    Vieira, M.N.2    Bomfim, T.R.3    Decker, H.4    Velasco, P.T.5
  • 26
    • 34848887507 scopus 로고    scopus 로고
    • Soluble oligomers from a non-disease related protein mimic Abetainduced tau hyperphosphorylation and neurodegeneration
    • Vieira MN, Forny-Germano L, Saraiva LM, Sebollela A, Martinez AM, et al. (2007) Soluble oligomers from a non-disease related protein mimic Abetainduced tau hyperphosphorylation and neurodegeneration. J Neurochem 103: 736-748.
    • (2007) J Neurochem , vol.103 , pp. 736-748
    • Vieira, M.N.1    Forny-Germano, L.2    Saraiva, L.M.3    Sebollela, A.4    Martinez, A.M.5
  • 28
    • 57049143140 scopus 로고    scopus 로고
    • Mitochondria in neuroplasticity and neurological disorders
    • Mattson MP, Gleichmann M, Cheng A (2008) Mitochondria in neuroplasticity and neurological disorders. Neuron 60: 748-766.
    • (2008) Neuron , vol.60 , pp. 748-766
    • Mattson, M.P.1    Gleichmann, M.2    Cheng, A.3
  • 29
    • 33644663874 scopus 로고    scopus 로고
    • Glucose 6- phosphate release of wild-type and mutant human brain hexokinases from mitochondria
    • Skaff DA, Kim CS, Tsai HJ, Honzatko RB, Fromm HJ (2005) Glucose 6- phosphate release of wild-type and mutant human brain hexokinases from mitochondria. J Biol Chem 280: 38403-38409.
    • (2005) J Biol Chem , vol.280 , pp. 38403-38409
    • Skaff, D.A.1    Kim, C.S.2    Tsai, H.J.3    Honzatko, R.B.4    Fromm, H.J.5
  • 30
    • 9744221185 scopus 로고    scopus 로고
    • Hexokinase-mitochondria interaction mediated by Akt is required to inhibit apoptosis in the presence or absence of Bax and Bak
    • Majewski N, Nogueira V, Bhaskar P, Coy PE, Skeen JE, et al. (2004) Hexokinase-mitochondria interaction mediated by Akt is required to inhibit apoptosis in the presence or absence of Bax and Bak. Mol Cell 16: 819-830.
    • (2004) Mol Cell , vol.16 , pp. 819-830
    • Majewski, N.1    Nogueira, V.2    Bhaskar, P.3    Coy, P.E.4    Skeen, J.E.5
  • 31
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • Lorenzo A, Yankner BA (1994) Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc Natl Acad Sci USA 91: 12243-12247.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 32
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric Ab ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Gong Y, Chang L, Viola KL, Lacor PN, Lambert MP, et al. (2003) Alzheimer's disease-affected brain: presence of oligomeric Ab ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc Natl Acad Sci USA 100: 10417-10422.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3    Lacor, P.N.4    Lambert, M.P.5
  • 33
    • 26644445247 scopus 로고    scopus 로고
    • Beta-amyloid is different in normal aging and in Alzheimer disease
    • Piccini A, Russo C, Gliozzi A, Relini A, Vitali A, et al. (2005) Beta-amyloid is different in normal aging and in Alzheimer disease. J Biol Chem 280: 34186-34192.
    • (2005) J Biol Chem , vol.280 , pp. 34186-34192
    • Piccini, A.1    Russo, C.2    Gliozzi, A.3    Relini, A.4    Vitali, A.5
  • 34
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • Lambert MP, Barlow AK, Chromy BA, Edwards C, Freed R, et al. (1998) Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci USA 95: 6448-6453.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5
  • 35
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal longterm potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, et al. (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal longterm potentiation in vivo. Nature 6880: 535-539.
    • (2002) Nature , vol.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5
  • 36
    • 23944444806 scopus 로고    scopus 로고
    • Molecular, structural, and functional characterization of Alzheimer's disease: Evidence for a relationship between default activity, amyloid, and memory
    • Buckner RL, Snyder AZ, Shannon BJ, LaRossa G, Sachs R, et al. (2005) Molecular, structural, and functional characterization of Alzheimer's disease: evidence for a relationship between default activity, amyloid, and memory. J Neurosci 25: 7709-7717.
    • (2005) J Neurosci , vol.25 , pp. 7709-7717
    • Buckner, R.L.1    Snyder, A.Z.2    Shannon, B.J.3    LaRossa, G.4    Sachs, R.5
  • 37
    • 12244312497 scopus 로고    scopus 로고
    • Cortical glucose metabolism is altered in aged transgenic Tg2576 mice that demonstrate Alzheimer plaque pathology
    • Bigl M, Apelt J, Eschrich K, Schliebs R (2003) Cortical glucose metabolism is altered in aged transgenic Tg2576 mice that demonstrate Alzheimer plaque pathology. J Neural Transm 110: 77-94.
    • (2003) J Neural Transm , vol.110 , pp. 77-94
    • Bigl, M.1    Apelt, J.2    Eschrich, K.3    Schliebs, R.4
  • 38
    • 2442664058 scopus 로고    scopus 로고
    • Amyloid-beta deposition is associated with decreased hippocampal glucose metabolism and spatial memory impairment in APP/PS1 mice
    • Sadowski M, Pankiewicz J, Scholtzova H, Ji Y, Quartermain D, et al. (2004) Amyloid-beta deposition is associated with decreased hippocampal glucose metabolism and spatial memory impairment in APP/PS1 mice. J Neuropathol Exp Neurol 63: 418-428.
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 418-428
    • Sadowski, M.1    Pankiewicz, J.2    Scholtzova, H.3    Ji, Y.4    Quartermain, D.5
  • 40
    • 23444445363 scopus 로고    scopus 로고
    • How astrocytes feed hungry neurons
    • Pellerin L (2005) How astrocytes feed hungry neurons. Mol Neurobiol 32: 59-72.
    • (2005) Mol Neurobiol , vol.32 , pp. 59-72
    • Pellerin, L.1
  • 41
    • 74449087772 scopus 로고    scopus 로고
    • Deciphering neuron-glia compartmentalization in cortical energy metabolism
    • Jolivet R, Magistretti PJ, Weber B (2009) Deciphering neuron-glia compartmentalization in cortical energy metabolism. Front Neuroenergetics 1: 4.
    • (2009) Front Neuroenergetics , vol.1 , pp. 4
    • Jolivet, R.1    Magistretti, P.J.2    Weber, B.3
  • 42
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease
    • Lustbader JW, Cirilli M, Lin C, Xu HW, Takuma K, et al. (2004) ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. Science 304: 448-452.
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3    Xu, H.W.4    Takuma, K.5
  • 44
    • 49649094091 scopus 로고    scopus 로고
    • The role of Wnt signaling in neuronal dysfunction in Alzheimer's Disease
    • Inestrosa NC, Toledo EM (2008) The role of Wnt signaling in neuronal dysfunction in Alzheimer's Disease. Mol Neurodegener 24: 3-9.
    • (2008) Mol Neurodegener , vol.24 , pp. 3-9
    • Inestrosa, N.C.1    Toledo, E.M.2
  • 45
    • 44049089139 scopus 로고    scopus 로고
    • Amyloid-beta binds to the extracellular cysteine-rich domain of Frizzled and inhibits Wnt/beta-catenin signaling
    • Magdesian MH, Carvalho MM, Mendes FA, Saraiva LM, Juliano MA, et al. (2008) Amyloid-beta binds to the extracellular cysteine-rich domain of Frizzled and inhibits Wnt/beta-catenin signaling. J Biol Chem 283: 9359-9368.
    • (2008) J Biol Chem , vol.283 , pp. 9359-9368
    • Magdesian, M.H.1    Carvalho, M.M.2    Mendes, F.A.3    Saraiva, L.M.4    Juliano, M.A.5
  • 46
    • 0030458524 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 alteration in Alzheimer disease is related to neurofibrillary tangle formation
    • Baum L, Hansen L, Masliah E, Saitoh T (1996) Glycogen synthase kinase 3 alteration in Alzheimer disease is related to neurofibrillary tangle formation. Mol Chem Neuropathol 29: 253-261.
    • (1996) Mol Chem Neuropathol , vol.29 , pp. 253-261
    • Baum, L.1    Hansen, L.2    Masliah, E.3    Saitoh, T.4
  • 47
    • 28544436922 scopus 로고    scopus 로고
    • Activation of glycogen synthase kinase 3b disrupts the binding of hkII to mitochondria by phosphorylating voltagedependent anion channel and potentiates chemotherapy-induced cytotoxicity
    • Pastorino GJ, Hoek JB, Shulga N (2005) Activation of glycogen synthase kinase 3b disrupts the binding of hkII to mitochondria by phosphorylating voltagedependent anion channel and potentiates chemotherapy-induced cytotoxicity. Cancer Res 65: 10545-10554.
    • (2005) Cancer Res , vol.65 , pp. 10545-10554
    • Pastorino, G.J.1    Hoek, J.B.2    Shulga, N.3
  • 48
    • 0026570528 scopus 로고
    • Beta- Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson MP, Cheng B, Davis D, Bryant K, Lieberburg I, Rydel RE (1992) Beta- Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J Neurosci 12: 376-389.
    • (1992) J Neurosci , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 49
    • 0031020993 scopus 로고    scopus 로고
    • Amyloid betapeptide impairs glucose transport in hippocampal and cortical neurons: Involvement of membrane lipid peroxidation
    • Mark RJ, Pang Z, Geddes JW, Uchida K, Mattson MP (1997) Amyloid betapeptide impairs glucose transport in hippocampal and cortical neurons: involvement of membrane lipid peroxidation. J Neurosci 17: 1046-1054.
    • (1997) J Neurosci , vol.17 , pp. 1046-1054
    • Mark, R.J.1    Pang, Z.2    Geddes, J.W.3    Uchida, K.4    Mattson, M.P.5
  • 51
    • 33745921507 scopus 로고    scopus 로고
    • Mitochondria at the synapse
    • Ly CV, Verstreken P (2006) Mitochondria at the synapse. Neuroscientist 12: 291-299.
    • (2006) Neuroscientist , vol.12 , pp. 291-299
    • Ly, C.V.1    Verstreken, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.