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Volumn 5, Issue 10, 2012, Pages 1103-1119

Mitochondria-targeted antioxidant SS31 prevents Amyloid beta-induced mitochondrial abnormalities and synaptic degeneration in Alzheimer's disease

Author keywords

Alzheimer's; Antioxidant; Mitochondria; SS31

Indexed keywords

ACETYLCYSTEINE; ALPHA TOCOPHEROL; AMPA RECEPTOR; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; ANTIOXIDANT; CALCIUM ION; CURCUMIN; CYTOCHROME C OXIDASE; DIMEBON; EPIGALLOCATECHIN GALLATE; GINKGO BILOBA EXTRACT; IDEBENONE; MITOCHONDRIAL DNA; MITOCHONDRIAL TRANSCRIPTION FACTOR; MITOCHONDRIAL TRANSCRIPTION FACTOR A; MITOCHONDRIAL TRANSCRIPTION FACTOR B; MITOCHONDRIAL TRANSCRIPTION FACTOR TFB1M; MITOCHONDRIAL TRANSCRIPTION FACTOR TFB2M; NEUROPROTECTIVE AGENT; PEPTIDE SS31; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; PRAMIPEXOLE; RESVERATROL; THIOCTIC ACID; TRANSCRIPTION FACTOR NRF1; TRANSCRIPTION FACTOR NRF2; UBIQUINONE; UNCLASSIFIED DRUG;

EID: 84869231972     PISSN: None     EISSN: 14248247     Source Type: Journal    
DOI: 10.3390/ph5101103     Document Type: Review
Times cited : (62)

References (116)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe, D.J. Alzheimer's disease: Genes, proteins, and therapy. Physiol. Rev. 2001, 81, 741-766.
    • (2001) Physiol. Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 2
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer's disease
    • LaFerla, F.M.; Green, K.N.; Oddo, S. Intracellular amyloid-beta in Alzheimer's disease. Nat. Rev. Neurosci. 2007, 8, 499-509.
    • (2007) Nat. Rev. Neurosci , vol.8 , pp. 499-509
    • Laferla, F.M.1    Green, K.N.2    Oddo, S.3
  • 3
    • 0030966546 scopus 로고    scopus 로고
    • Impairment of glucose and glutamate transport and induction of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid beta-peptide: Role of the lipid peroxidation product 4-hydroxynonenal
    • Keller, J.N.; Pang, Z.; Geddes, J.W.; Begley, J.G.; Germeyer, A.; Waeg, G.; Mattson, M.P. Impairment of glucose and glutamate transport and induction of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid beta-peptide: Role of the lipid peroxidation product 4-hydroxynonenal. J. Neurochem. 1997, 69, 273-284.
    • (1997) J. Neurochem , vol.69 , pp. 273-284
    • Keller, J.N.1    Pang, Z.2    Geddes, J.W.3    Begley, J.G.4    Germeyer, A.5    Waeg, G.6    Mattson, M.P.7
  • 4
    • 3042806534 scopus 로고    scopus 로고
    • A mitochondrial cascade hypothesis for sporadic Alzheimer's disease
    • Swerdlow, R.H.; Khan, S.M. A "mitochondrial cascade hypothesis" for sporadic Alzheimer's disease. Med. Hypotheses 2004, 63, 8-20.
    • (2004) Med. Hypotheses , vol.63 , pp. 8-20
    • Swerdlow, R.H.1    Khan, S.M.2
  • 5
    • 77956224679 scopus 로고    scopus 로고
    • The Alzheimer's disease mitochondrial cascade hypothesis
    • Swerdlow, R.H.; Burns, J.M.; Khan, S.M. The Alzheimer's disease mitochondrial cascade hypothesis. J. Alzheimers Dis. 2010, 20, S265-S279.
    • (2010) J. Alzheimers Dis , vol.20
    • Swerdlow, R.H.1    Burns, J.M.2    Khan, S.M.3
  • 7
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe, D.J. Alzheimer's disease is a synaptic failure. Science 2002, 298, 789-791.
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 8
    • 33748471099 scopus 로고    scopus 로고
    • Inflammation in Alzheimer disease: Driving force, bystander or beneficial response?
    • Wyss-Coray, T. Inflammation in Alzheimer disease: Driving force, bystander or beneficial response? Nat. Med. 2006, 12, 1005-1015.
    • (2006) Nat. Med , vol.12 , pp. 1005-1015
    • Wyss-Coray, T.1
  • 10
    • 28044437122 scopus 로고    scopus 로고
    • Selective butyrylcholinesterase inhibition elevates brain acetylcholine, augments learning and lowers Alzheimer beta-amyloid peptide in rodent
    • Greig, N.H.; Utsuki, T.; Ingram, D.K.; Wang, Y.; Pepeu, G.; Scali, C.; Yu, Q.S.; Mamczarz, J.; Holloway, H.W.; Giordano, T.; et al. Selective butyrylcholinesterase inhibition elevates brain acetylcholine, augments learning and lowers Alzheimer beta-amyloid peptide in rodent. Proc. Natl. Acad. Sci. USA 2005, 102, 17213-17218.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17213-17218
    • Greig, N.H.1    Utsuki, T.2    Ingram, D.K.3    Wang, Y.4    Pepeu, G.5    Scali, C.6    Yu, Q.S.7    Mamczarz, J.8    Holloway, H.W.9    Giordano, T.10
  • 11
    • 0025283380 scopus 로고
    • Morphological adaptive response of the synaptic junctional zones in the human dentate gyrus during aging and Alzheimer's disease
    • Bertoni-Freddari, C.; Fattoretti, P.; Casoli, T.; Meier-Ruge, W.; Ulrich, J. Morphological adaptive response of the synaptic junctional zones in the human dentate gyrus during aging and Alzheimer's disease. Brain Res. 1990, 517, 69-75.
    • (1990) Brain Res , vol.517 , pp. 69-75
    • Bertoni-Freddari, C.1    Fattoretti, P.2    Casoli, T.3    Meier-Ruge, W.4    Ulrich, J.5
  • 12
    • 0030513943 scopus 로고    scopus 로고
    • Structural correlates of cognition in dementia: Quantification and assessment of synapse change
    • DeKosky, S.T.; Scheff, S.W.; Styren, S.D. Structural correlates of cognition in dementia: Quantification and assessment of synapse change. Neurodegeneration 1996, 5, 417-421.
    • (1996) Neurodegeneration , vol.5 , pp. 417-421
    • Dekosky, S.T.1    Scheff, S.W.2    Styren, S.D.3
  • 13
    • 84885915876 scopus 로고    scopus 로고
    • Synapses, synaptic activity and intraneuronal abeta in Alzheimer's disease
    • Tampellini, D.; Gouras, G.K. Synapses, synaptic activity and intraneuronal abeta in Alzheimer's disease. Front. Aging Neurosci. 2010, 2, 13.
    • (2010) Front. Aging Neurosci , vol.2 , pp. 13
    • Tampellini, D.1    Gouras, G.K.2
  • 14
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J.; Selkoe, D.J. The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 2002, 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 15
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers-A decade of discovery
    • Walsh, D.M.; Selkoe, D.J. A beta oligomers-A decade of discovery. J. Neurochem. 2007, 101, 1172-1184.
    • (2007) J. Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 16
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Abeta oligomers: The solution to an Alzheimer's disease conundrum?
    • Klein, W.L.; Krafft, G.A.; Finch, C.E. Targeting small Abeta oligomers: The solution to an Alzheimer's disease conundrum? Trends Neurosci. 2001, 24, 219-224.
    • (2001) Trends Neurosci , vol.24 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 19
    • 79958721260 scopus 로고    scopus 로고
    • Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer's disease: Implications for neuronal damage
    • Manczak, M.; Calkins, M.J.; Reddy, P.H. Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer's disease: Implications for neuronal damage. Hum. Mol. Genet. 2011, 20, 2495-2509.
    • (2011) Hum. Mol. Genet , vol.20 , pp. 2495-2509
    • Manczak, M.1    Calkins, M.J.2    Reddy, P.H.3
  • 20
    • 79951761390 scopus 로고    scopus 로고
    • The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: Oligomer size or conformation?
    • Broersen, K.; Rousseau, F.; Schymkowitz, J. The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: Oligomer size or conformation? Alzheimers Res. Ther. 2010, 2, 12.
    • (2010) Alzheimers Res. Ther , vol.2 , pp. 12
    • Broersen, K.1    Rousseau, F.2    Schymkowitz, J.3
  • 21
    • 77956199725 scopus 로고    scopus 로고
    • Amyloid-beta and mitochondria in aging and Alzheimer's disease: Implications for synaptic damage and cognitive decline
    • Reddy, P.H.; Manczak, M.; Mao, P.; Calkins, M.J.; Reddy, A.P.; Shirendeb, U. Amyloid-beta and mitochondria in aging and Alzheimer's disease: Implications for synaptic damage and cognitive decline. J. Alzheimers Dis. 2010, 20, S499-S512.
    • (2010) J. Alzheimers Dis , vol.20
    • Reddy, P.H.1    Manczak, M.2    Mao, P.3    Calkins, M.J.4    Reddy, A.P.5    Shirendeb, U.6
  • 22
    • 81255190781 scopus 로고    scopus 로고
    • Impaired mitochondrial biogenesis, defective axonal transport of mitochondria, abnormal mitochondrial dynamics and synaptic degeneration in a mouse model of Alzheimer's disease
    • Calkins, M.J.; Manczak, M.; Mao, P.; Shirendeb, U.; Reddy, P.H. Impaired mitochondrial biogenesis, defective axonal transport of mitochondria, abnormal mitochondrial dynamics and synaptic degeneration in a mouse model of Alzheimer's disease. Hum. Mol. Genet. 2011, 20, 4515-4529.
    • (2011) Hum. Mol. Genet , vol.20 , pp. 4515-4529
    • Calkins, M.J.1    Manczak, M.2    Mao, P.3    Shirendeb, U.4    Reddy, P.H.5
  • 23
    • 58049218922 scopus 로고    scopus 로고
    • Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins
    • Wang, X.; Su, B.; Siedlak, S.L.; Moreira, P.I.; Fujioka, H.; Wang, Y.; Casadesus, G.; Zhu, X. Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins. Proc. Natl. Acad. Sci. USA 2008, 105, 19318-19323.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19318-19323
    • Wang, X.1    Su, B.2    Siedlak, S.L.3    Moreira, P.I.4    Fujioka, H.5    Wang, Y.6    Casadesus, G.7    Zhu, X.8
  • 24
    • 67650732998 scopus 로고    scopus 로고
    • Impaired balance of mitochondrial fission and fusion in Alzheimer's disease
    • Wang, X.; Su, B.; Lee, H.G.; Li, X.; Perry, G.; Smith, M.A.; Zhu, X. Impaired balance of mitochondrial fission and fusion in Alzheimer's disease. J. Neurosci. 2009, 29, 9090-9103.
    • (2009) J. Neurosci , vol.29 , pp. 9090-9103
    • Wang, X.1    Su, B.2    Lee, H.G.3    Li, X.4    Perry, G.5    Smith, M.A.6    Zhu, X.7
  • 25
    • 78649815388 scopus 로고    scopus 로고
    • Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model
    • Du, H.; Guo, L.; Yan, S.; Sosunov, A.A.; McKhann, G.M.; Yan, S.S. Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model. Proc. Natl. Acad. Sci. USA 2010, 107, 18670-18675.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 18670-18675
    • Du, H.1    Guo, L.2    Yan, S.3    Sosunov, A.A.4    McKhann, G.M.5    Yan, S.S.6
  • 27
    • 39149122810 scopus 로고    scopus 로고
    • Amyloid beta, mitochondrial dysfunction and synaptic damage: Implications for cognitive decline in aging and Alzheimer's disease
    • Reddy, P.H.; Beal, M.F. Amyloid beta, mitochondrial dysfunction and synaptic damage: Implications for cognitive decline in aging and Alzheimer's disease. Trends Mol. Med. 2008, 14, 45-53.
    • (2008) Trends Mol. Med , vol.14 , pp. 45-53
    • Reddy, P.H.1    Beal, M.F.2
  • 28
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • Manczak, M.; Anekonda, T.S.; Henson, E.; Park, B.S.; Quinn, J.; Reddy, P.H. Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression. Hum. Mol. Genet. 2006, 15, 1437-1449.
    • (2006) Hum. Mol. Genet , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5    Reddy, P.H.6
  • 29
    • 33748283747 scopus 로고    scopus 로고
    • Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction
    • Devi, L.; Prabhu, B.M.; Galati, D.F.; Avadhani, N.G.; Anandatheerthavarada, H.K. Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction. J. Neurosci. 2006, 26, 9057-9068.
    • (2006) J. Neurosci , vol.26 , pp. 9057-9068
    • Devi, L.1    Prabhu, B.M.2    Galati, D.F.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 33
    • 70149093436 scopus 로고    scopus 로고
    • Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease
    • Yao, J.; Irwin, R.W.; Zhao, L.; Nilsen, J.; Hamilton, R.T.; Brinton, R.D. Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease. Proc. Natl. Acad. Sci. USA 2009, 106, 14670-14675.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 14670-14675
    • Yao, J.1    Irwin, R.W.2    Zhao, L.3    Nilsen, J.4    Hamilton, R.T.5    Brinton, R.D.6
  • 35
    • 53549129483 scopus 로고    scopus 로고
    • Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease
    • Du, H.; Guo, L.; Fang, F.; Chen, D.; Sosunov, A.A.; McKhann, G.M.; Yan, Y.; Wang, C.; Zhang, H.; Molkentin, J.D.; et al. Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease. Nat. Med. 2008, 14, 1097-1105.
    • (2008) Nat. Med , vol.14 , pp. 1097-1105
    • Du, H.1    Guo, L.2    Fang, F.3    Chen, D.4    Sosunov, A.A.5    McKhann, G.M.6    Yan, Y.7    Wang, C.8    Zhang, H.9    Molkentin, J.D.10
  • 36
    • 67649803186 scopus 로고    scopus 로고
    • Amyloid beta, mitochondrial structural and functional dynamics in Alzheimer's disease
    • Reddy, P.H. Amyloid beta, mitochondrial structural and functional dynamics in Alzheimer's disease. Exp. Neurol. 2009, 218, 286-292.
    • (2009) Exp. Neurol , vol.218 , pp. 286-292
    • Reddy, P.H.1
  • 37
    • 0034784359 scopus 로고    scopus 로고
    • An energy budget for signaling in the grey matter of the brain
    • Attwell, D.; Laughlin, S.B. An energy budget for signaling in the grey matter of the brain. J. Cereb. Blood Flow Metab. 2001, 21, 1133-1145.
    • (2001) J. Cereb. Blood Flow Metab , vol.21 , pp. 1133-1145
    • Attwell, D.1    Laughlin, S.B.2
  • 38
    • 0033746173 scopus 로고    scopus 로고
    • 3rd. CNS energy metabolism as related to function
    • Ames, A., 3rd. CNS energy metabolism as related to function. Brain Res. Brain Res. Rev. 2000, 34, 42-68.
    • (2000) Brain Res. Brain Res. Rev , vol.34 , pp. 42-68
    • Ames, A.1
  • 39
    • 78650764923 scopus 로고    scopus 로고
    • Food for thought: The importance of glucose and other energy substrates for sustaining brain function under varying levels of activity
    • Pellerin, L. Food for thought: The importance of glucose and other energy substrates for sustaining brain function under varying levels of activity. Diabetes Metab. 2010, 36, S59-S63.
    • (2010) Diabetes Metab , vol.36
    • Pellerin, L.1
  • 41
    • 0024561501 scopus 로고
    • Cytochrome oxidase: An endogenous metabolic marker for neuronal activity
    • Wong-Riley, M.T. Cytochrome oxidase: An endogenous metabolic marker for neuronal activity. Trends Neurosci. 1989, 12, 94-101.
    • (1989) Trends Neurosci , vol.12 , pp. 94-101
    • Wong-Riley, M.T.1
  • 42
    • 84863751189 scopus 로고    scopus 로고
    • Bigenomic regulation of cytochrome C oxidase in neurons and the tight coupling between neuronal activity and energy metabolism
    • Wong-Riley, M.T. Bigenomic regulation of cytochrome C oxidase in neurons and the tight coupling between neuronal activity and energy metabolism. Adv. Exp. Med. Biol. 2012, 748, 283-304.
    • (2012) Adv. Exp. Med. Biol , vol.748 , pp. 283-304
    • Wong-Riley, M.T.1
  • 43
    • 57649148823 scopus 로고    scopus 로고
    • Nuclear control of respiratory chain expression by nuclear respiratory factors and PGC-1-related coactivator
    • Scarpulla, R.C. Nuclear control of respiratory chain expression by nuclear respiratory factors and PGC-1-related coactivator. Ann. NY Acad. Sci. 2008, 1147, 321-334.
    • (2008) Ann. NY Acad. Sci , vol.1147 , pp. 321-334
    • Scarpulla, R.C.1
  • 44
    • 1542373685 scopus 로고    scopus 로고
    • Transcriptional regulatory circuits controlling mitochondrial biogenesis and function
    • Kelly, D.P.; Scarpulla, R.C. Transcriptional regulatory circuits controlling mitochondrial biogenesis and function. Genes Dev. 2004, 18, 357-368.
    • (2004) Genes Dev , vol.18 , pp. 357-368
    • Kelly, D.P.1    Scarpulla, R.C.2
  • 45
    • 79957960940 scopus 로고    scopus 로고
    • Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network
    • Scarpulla, R.C. Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network. Biochim. Biophys. Acta 2011, 1813, 1269-1278.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1269-1278
    • Scarpulla, R.C.1
  • 46
    • 79953210362 scopus 로고    scopus 로고
    • Regulation of PGC-1alpha, a nodal regulator of mitochondrial biogenesis
    • Fernandez-Marcos, P.J.; Auwerx, J. Regulation of PGC-1alpha, a nodal regulator of mitochondrial biogenesis. Am. J. Clin. Nutr. 2011, 93, S884-S890.
    • (2011) Am. J. Clin. Nutr , vol.93
    • Fernandez-Marcos, P.J.1    Auwerx, J.2
  • 47
    • 46749125376 scopus 로고    scopus 로고
    • Transcriptional control of mitochondrial biogenesis: The central role of PGC-1alpha
    • Ventura-Clapier, R.; Garnier, A.; Veksler, V. Transcriptional control of mitochondrial biogenesis: The central role of PGC-1alpha. Cardiovasc. Res. 2008, 79, 208-217.
    • (2008) Cardiovasc. Res , vol.79 , pp. 208-217
    • Ventura-Clapier, R.1    Garnier, A.2    Veksler, V.3
  • 49
    • 0038664183 scopus 로고    scopus 로고
    • Coupling of neuronal activity and mitochondrial metabolism as revealed by NAD(P)H fluorescence signals in organotypic hippocampal slice cultures of the rat
    • Kann, O.; Schuchmann, S.; Buchheim, K.; Heinemann, U. Coupling of neuronal activity and mitochondrial metabolism as revealed by NAD(P)H fluorescence signals in organotypic hippocampal slice cultures of the rat. Neuroscience 2003, 119, 87-100.
    • (2003) Neuroscience , vol.119 , pp. 87-100
    • Kann, O.1    Schuchmann, S.2    Buchheim, K.3    Heinemann, U.4
  • 50
    • 0032526986 scopus 로고    scopus 로고
    • Changes in mitochondrial function resulting from synaptic activity in the rat hippocampal slice
    • Bindokas, V.P.; Lee, C.C.; Colmers, W.F.; Miller, R.J. Changes in mitochondrial function resulting from synaptic activity in the rat hippocampal slice. J. Neurosci. 1998, 18, 4570-4587.
    • (1998) J. Neurosci , vol.18 , pp. 4570-4587
    • Bindokas, V.P.1    Lee, C.C.2    Colmers, W.F.3    Miller, R.J.4
  • 51
    • 0037115108 scopus 로고    scopus 로고
    • Correlated calcium uptake and release by mitochondria and endoplasmic reticulum of CA3 hippocampal dendrites after afferent synaptic stimulation
    • Pivovarova, N.B.; Pozzo-Miller, L.D.; Hongpaisan, J.; Andrews, S.B. Correlated calcium uptake and release by mitochondria and endoplasmic reticulum of CA3 hippocampal dendrites after afferent synaptic stimulation. J. Neurosci. 2002, 22, 10653-10661.
    • (2002) J. Neurosci , vol.22 , pp. 10653-10661
    • Pivovarova, N.B.1    Pozzo-Miller, L.D.2    Hongpaisan, J.3    Andrews, S.B.4
  • 52
    • 0038414654 scopus 로고    scopus 로고
    • 2+ uptake prevents desynchronization of quantal release and minimizes depletion during repetitive stimulation of mouse motor nerve terminals
    • 2+ uptake prevents desynchronization of quantal release and minimizes depletion during repetitive stimulation of mouse motor nerve terminals. J. Physiol. 2003, 548, 425-438.
    • (2003) J. Physiol , vol.548 , pp. 425-438
    • David, G.1    Barrett, E.F.2
  • 54
    • 0036092524 scopus 로고    scopus 로고
    • 2+ buffering regulates synaptic transmission between retinal amacrine cells
    • 2+ buffering regulates synaptic transmission between retinal amacrine cells. J. Neurophysiol. 2002, 87, 1426-1439.
    • (2002) J. Neurophysiol , vol.87 , pp. 1426-1439
    • Medler, K.1    Gleason, E.L.2
  • 56
    • 0033611593 scopus 로고    scopus 로고
    • 2+ exchange and of mitochondria in the regulation of presynaptic Ca2+ and spontaneous glutamate release
    • 2+ exchange and of mitochondria in the regulation of presynaptic Ca2+ and spontaneous glutamate release. Philos. Trans. R. Soc. Lond. B Biol. Sci. 1999, 354, 357-364.
    • (1999) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.354 , pp. 357-364
    • Scotti, A.L.1    Chatton, J.Y.2    Reuter, H.3
  • 57
    • 77952723041 scopus 로고    scopus 로고
    • 2+ channels: Great unknowns with important functions
    • 2+ channels: Great unknowns with important functions. FEBS Lett. 2010, 584, 1942-1947.
    • (2010) FEBS Lett , vol.584 , pp. 1942-1947
    • Malli, R.1    Graier, W.F.2
  • 58
    • 77955793357 scopus 로고    scopus 로고
    • Maturation of the olfactory sensory neurons by Apaf-1/caspase-9-mediated caspase activity
    • Ohsawa, S.; Hamada, S.; Kuida, K.; Yoshida, H.; Igaki, T.; Miura, M. Maturation of the olfactory sensory neurons by Apaf-1/caspase-9-mediated caspase activity. Proc. Natl. Acad. Sci. USA 2010, 107, 13366-13371.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 13366-13371
    • Ohsawa, S.1    Hamada, S.2    Kuida, K.3    Yoshida, H.4    Igaki, T.5    Miura, M.6
  • 59
    • 84862113237 scopus 로고    scopus 로고
    • Apoptotic and non-apoptotic roles of caspases in neuronal physiology and pathophysiology
    • Hyman, B.T.; Yuan, J. Apoptotic and non-apoptotic roles of caspases in neuronal physiology and pathophysiology. Nat. Rev. Neurosci. 2012, 13, 395-406.
    • (2012) Nat. Rev. Neurosci , vol.13 , pp. 395-406
    • Hyman, B.T.1    Yuan, J.2
  • 61
    • 77951667668 scopus 로고    scopus 로고
    • p75NTR-dependent, myelin-mediated axonal degeneration regulates neural connectivity in the adult brain
    • Park, K.J.; Grosso, C.A.; Aubert, I.; Kaplan, D.R.; Miller, F.D. p75NTR-dependent, myelin-mediated axonal degeneration regulates neural connectivity in the adult brain. Nat. Neurosci. 2010, 13, 559-566.
    • (2010) Nat. Neurosci , vol.13 , pp. 559-566
    • Park, K.J.1    Grosso, C.A.2    Aubert, I.3    Kaplan, D.R.4    Miller, F.D.5
  • 62
    • 84860806410 scopus 로고    scopus 로고
    • Caspases in synaptic plasticity
    • Li, Z.; Sheng, M. Caspases in synaptic plasticity. Mol. Brain 2012, 5, 15.
    • (2012) Mol. Brain , vol.5 , pp. 15
    • Li, Z.1    Sheng, M.2
  • 63
    • 9644265305 scopus 로고    scopus 로고
    • Bidirectional activity-dependent morphological plasticity in hippocampal neurons
    • Nagerl, U.V.; Eberhorn, N.; Cambridge, S.B.; Bonhoeffer, T. Bidirectional activity-dependent morphological plasticity in hippocampal neurons. Neuron 2004, 44, 759-767.
    • (2004) Neuron , vol.44 , pp. 759-767
    • Nagerl, U.V.1    Eberhorn, N.2    Cambridge, S.B.3    Bonhoeffer, T.4
  • 64
    • 9644278075 scopus 로고    scopus 로고
    • Shrinkage of dendritic spines associated with long-term depression of hippocampal synapses
    • Zhou, Q.; Homma, K.J.; Poo, M.M. Shrinkage of dendritic spines associated with long-term depression of hippocampal synapses. Neuron 2004, 44, 749-757.
    • (2004) Neuron , vol.44 , pp. 749-757
    • Zhou, Q.1    Homma, K.J.2    Poo, M.M.3
  • 65
    • 7044267351 scopus 로고    scopus 로고
    • Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity
    • Okamoto, K.; Nagai, T.; Miyawaki, A.; Hayashi, Y. Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity. Nat. Neurosci. 2004, 7, 1104-1112.
    • (2004) Nat. Neurosci , vol.7 , pp. 1104-1112
    • Okamoto, K.1    Nagai, T.2    Miyawaki, A.3    Hayashi, Y.4
  • 66
    • 77953271477 scopus 로고    scopus 로고
    • Caspase-3 activation via mitochondria is required for long-term depression and AMPA receptor internalization
    • Li, Z.; Jo, J.; Jia, J.M.; Lo, S.C.; Whitcomb, D.J.; Jiao, S.; Cho, K.; Sheng, M. Caspase-3 activation via mitochondria is required for long-term depression and AMPA receptor internalization. Cell 2010, 141, 859-871.
    • (2010) Cell , vol.141 , pp. 859-871
    • Li, Z.1    Jo, J.2    Jia, J.M.3    Lo, S.C.4    Whitcomb, D.J.5    Jiao, S.6    Cho, K.7    Sheng, M.8
  • 67
    • 79956210669 scopus 로고    scopus 로고
    • Nonapoptotic function of BAD and BAX in long-term depression of synaptic transmission
    • Jiao, S.; Li, Z. Nonapoptotic function of BAD and BAX in long-term depression of synaptic transmission. Neuron 2011, 70, 758-772.
    • (2011) Neuron , vol.70 , pp. 758-772
    • Jiao, S.1    Li, Z.2
  • 68
    • 33845411954 scopus 로고    scopus 로고
    • AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss
    • Hsieh, H.; Boehm, J.; Sato, C.; Iwatsubo, T.; Tomita, T.; Sisodia, S.; Malinow, R. AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss. Neuron 2006, 52, 831-843.
    • (2006) Neuron , vol.52 , pp. 831-843
    • Hsieh, H.1    Boehm, J.2    Sato, C.3    Iwatsubo, T.4    Tomita, T.5    Sisodia, S.6    Malinow, R.7
  • 69
    • 33846068084 scopus 로고    scopus 로고
    • Amyloid precursor protein overexpression depresses excitatory transmission through both presynaptic and postsynaptic mechanisms
    • Ting, J.T.; Kelley, B.G.; Lambert, T.J.; Cook, D.G.; Sullivan, J.M. Amyloid precursor protein overexpression depresses excitatory transmission through both presynaptic and postsynaptic mechanisms. Proc. Natl. Acad. Sci. USA 2007, 104, 353-358.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 353-358
    • Ting, J.T.1    Kelley, B.G.2    Lambert, T.J.3    Cook, D.G.4    Sullivan, J.M.5
  • 71
    • 77950893260 scopus 로고    scopus 로고
    • Inhibition of AMPA receptor trafficking at hippocampal synapses by beta-amyloid oligomers: The mitochondrial contribution
    • Rui, Y.; Gu, J.; Yu, K.; Hartzell, H.C.; Zheng, J.Q. Inhibition of AMPA receptor trafficking at hippocampal synapses by beta-amyloid oligomers: The mitochondrial contribution. Mol. Brain 2010, 3, 10.
    • (2010) Mol. Brain , vol.3 , pp. 10
    • Rui, Y.1    Gu, J.2    Yu, K.3    Hartzell, H.C.4    Zheng, J.Q.5
  • 72
    • 0033179170 scopus 로고    scopus 로고
    • Evidence for caspase-mediated cleavage of AMPA receptor subunits in neuronal apoptosis and Alzheimer's disease
    • Chan, S.L.; Griffin, W.S.; Mattson, M.P. Evidence for caspase-mediated cleavage of AMPA receptor subunits in neuronal apoptosis and Alzheimer's disease. J. Neurosci. Res. 1999, 57, 315-323.
    • (1999) J. Neurosci. Res , vol.57 , pp. 315-323
    • Chan, S.L.1    Griffin, W.S.2    Mattson, M.P.3
  • 73
    • 0029803242 scopus 로고    scopus 로고
    • In situ localization of mitochondrial DNA replication in intact mammalian cells
    • Davis, A.F.; Clayton, D.A. In situ localization of mitochondrial DNA replication in intact mammalian cells. J. Cell Biol. 1996, 135, 883-893.
    • (1996) J. Cell Biol , vol.135 , pp. 883-893
    • Davis, A.F.1    Clayton, D.A.2
  • 74
    • 0029982347 scopus 로고    scopus 로고
    • Mitochondrial DNA polymerase gamma is expressed and translated in the absence of mitochondrial DNA maintenance and replication
    • Davis, A.F.; Ropp, P.A.; Clayton, D.A.; Copeland, W.C. Mitochondrial DNA polymerase gamma is expressed and translated in the absence of mitochondrial DNA maintenance and replication. Nucleic Acids Res. 1996, 24, 2753-2759.
    • (1996) Nucleic Acids Res , vol.24 , pp. 2753-2759
    • Davis, A.F.1    Ropp, P.A.2    Clayton, D.A.3    Copeland, W.C.4
  • 75
    • 0033104147 scopus 로고    scopus 로고
    • Protein-synthesizing machinery in the axon compartment
    • Koenig, E.; Giuditta, A. Protein-synthesizing machinery in the axon compartment. Neuroscience 1999, 89, 5-15.
    • (1999) Neuroscience , vol.89 , pp. 5-15
    • Koenig, E.1    Giuditta, A.2
  • 76
    • 0034287029 scopus 로고    scopus 로고
    • Protein synthesis in axons and terminals: Significance for maintenance, plasticity and regulation of phenotype. With a critique of slow transport theory
    • Alvarez, J.; Giuditta, A.; Koenig, E. Protein synthesis in axons and terminals: Significance for maintenance, plasticity and regulation of phenotype. With a critique of slow transport theory. Prog. Neurobiol. 2000, 62, 1-62.
    • (2000) Prog. Neurobiol , vol.62 , pp. 1-62
    • Alvarez, J.1    Giuditta, A.2    Koenig, E.3
  • 77
    • 33646541355 scopus 로고    scopus 로고
    • New insights into neuronal regeneration: The role of axonal protein synthesis in pathfinding and axonal extension
    • Twiss, J.L.; van Minnen, J. New insights into neuronal regeneration: The role of axonal protein synthesis in pathfinding and axonal extension. J. Neurotrauma 2006, 23, 295-308.
    • (2006) J. Neurotrauma , vol.23 , pp. 295-308
    • Twiss, J.L.1    van Minnen, J.2
  • 78
    • 0035370292 scopus 로고    scopus 로고
    • Local synthesis of nuclear-encoded mitochondrial proteins in the presynaptic nerve terminal
    • Gioio, A.E.; Eyman, M.; Zhang, H.; Lavina, Z.S.; Giuditta, A.; Kaplan, B.B. Local synthesis of nuclear-encoded mitochondrial proteins in the presynaptic nerve terminal. J. Neurosci. Res. 2001, 64, 447-453.
    • (2001) J. Neurosci. Res , vol.64 , pp. 447-453
    • Gioio, A.E.1    Eyman, M.2    Zhang, H.3    Lavina, Z.S.4    Giuditta, A.5    Kaplan, B.B.6
  • 80
    • 0041661881 scopus 로고    scopus 로고
    • Replication of mitochondrial DNA occurs throughout the mitochondria of cultured human cells
    • Magnusson, J.; Orth, M.; Lestienne, P.; Taanman, J.W. Replication of mitochondrial DNA occurs throughout the mitochondria of cultured human cells. Exp. Cell Res. 2003, 289, 133-142.
    • (2003) Exp. Cell Res , vol.289 , pp. 133-142
    • Magnusson, J.1    Orth, M.2    Lestienne, P.3    Taanman, J.W.4
  • 81
    • 51349163907 scopus 로고    scopus 로고
    • Mitochondrial biogenesis in the axons of vertebrate peripheral neurons
    • Amiri, M.; Hollenbeck, P.J. Mitochondrial biogenesis in the axons of vertebrate peripheral neurons. Dev. Neurobiol. 2008, 68, 1348-1361.
    • (2008) Dev. Neurobiol , vol.68 , pp. 1348-1361
    • Amiri, M.1    Hollenbeck, P.J.2
  • 82
    • 79960557491 scopus 로고    scopus 로고
    • Assessment of newly synthesized mitochondrial DNA using BrdU labeling in primary neurons from Alzheimer's disease mice: Implications for impaired mitochondrial biogenesis and synaptic damage
    • Calkins, M.J.; Reddy, P.H. Assessment of newly synthesized mitochondrial DNA using BrdU labeling in primary neurons from Alzheimer's disease mice: Implications for impaired mitochondrial biogenesis and synaptic damage. Biochim. Biophys. Acta 2011, 1812, 1182-1189.
    • (2011) Biochim. Biophys. Acta , vol.1812 , pp. 1182-1189
    • Calkins, M.J.1    Reddy, P.H.2
  • 83
    • 84856056846 scopus 로고    scopus 로고
    • Mitochondrial transport in neurons: Impact on synaptic homeostasis and neurodegeneration
    • Sheng, Z.H.; Cai, Q. Mitochondrial transport in neurons: Impact on synaptic homeostasis and neurodegeneration. Nat. Rev. Neurosci. 2012, 13, 77-93.
    • (2012) Nat. Rev. Neurosci , vol.13 , pp. 77-93
    • Sheng, Z.H.1    Cai, Q.2
  • 84
    • 3242875557 scopus 로고    scopus 로고
    • Axonal mitochondrial transport and potential are correlated
    • Miller, K.E.; Sheetz, M.P. Axonal mitochondrial transport and potential are correlated. J. Cell Sci. 2004, 117, 2791-2804.
    • (2004) J. Cell Sci , vol.117 , pp. 2791-2804
    • Miller, K.E.1    Sheetz, M.P.2
  • 85
    • 51149106133 scopus 로고    scopus 로고
    • Mitochondrial membrane potential in axons increases with local nerve growth factor or semaphorin signaling
    • Verburg, J.; Hollenbeck, P.J. Mitochondrial membrane potential in axons increases with local nerve growth factor or semaphorin signaling. J. Neurosci. 2008, 28, 8306-8315.
    • (2008) J. Neurosci , vol.28 , pp. 8306-8315
    • Verburg, J.1    Hollenbeck, P.J.2
  • 86
    • 79959305691 scopus 로고    scopus 로고
    • Mitochondria: The next (neurode)generation
    • Schon, E.A.; Przedborski, S. Mitochondria: The next (neurode)generation. Neuron 2011, 70, 1033-1053.
    • (2011) Neuron , vol.70 , pp. 1033-1053
    • Schon, E.A.1    Przedborski, S.2
  • 87
    • 84855165944 scopus 로고
    • Mutant huntingtin, abnormal mitochondrial dynamics, defective axonal transport of mitochondria, and selective synaptic degeneration in Huntington's disease
    • Reddy, P.H.; Shirendeb, U.P. Mutant huntingtin, abnormal mitochondrial dynamics, defective axonal transport of mitochondria, and selective synaptic degeneration in Huntington's disease. Biochim. Biophys. Acta 2012, 1822, 101-110.
    • (1822) Biochim. Biophys. Acta , vol.2012 , pp. 101-110
    • Reddy, P.H.1    Shirendeb, U.P.2
  • 88
    • 84857061515 scopus 로고    scopus 로고
    • Mitochondrial pathobiology in ALS
    • Martin, L.J. Mitochondrial pathobiology in ALS. J. Bioenerg. Biomembr. 2011, 43, 569-579.
    • (2011) J. Bioenerg. Biomembr , vol.43 , pp. 569-579
    • Martin, L.J.1
  • 89
    • 79751537405 scopus 로고    scopus 로고
    • Amyloid beta impairs mitochondrial anterograde transport and degenerates synapses in Alzheimer's disease neurons
    • Calkins, M.J.; Reddy, P.H. Amyloid beta impairs mitochondrial anterograde transport and degenerates synapses in Alzheimer's disease neurons. Biochim. Biophys. Acta 2011, 1812, 507-513.
    • (2011) Biochim. Biophys. Acta , vol.1812 , pp. 507-513
    • Calkins, M.J.1    Reddy, P.H.2
  • 90
    • 76549123596 scopus 로고    scopus 로고
    • Amyloid-beta-derived diffusible ligands cause impaired axonal transport of mitochondria in neurons
    • Wang, X.; Perry, G.; Smith, M.A.; Zhu, X. Amyloid-beta-derived diffusible ligands cause impaired axonal transport of mitochondria in neurons. Neurodegener. Dis. 2010, 7, 56-59.
    • (2010) Neurodegener. Dis , vol.7 , pp. 56-59
    • Wang, X.1    Perry, G.2    Smith, M.A.3    Zhu, X.4
  • 91
    • 33749854516 scopus 로고    scopus 로고
    • Acute impairment of mitochondrial trafficking by beta-amyloid peptides in hippocampal neurons
    • Rui, Y.; Tiwari, P.; Xie, Z.; Zheng, J.Q. Acute impairment of mitochondrial trafficking by beta-amyloid peptides in hippocampal neurons. J. Neurosci. 2006, 26, 10480-10487.
    • (2006) J. Neurosci , vol.26 , pp. 10480-10487
    • Rui, Y.1    Tiwari, P.2    Xie, Z.3    Zheng, J.Q.4
  • 92
    • 84862266909 scopus 로고    scopus 로고
    • Oxidative stress inhibits axonal transport: Implications for neurodegenerative diseases
    • Fang, C.; Bourdette, D.; Banker, G. Oxidative stress inhibits axonal transport: Implications for neurodegenerative diseases. Mol. Neurodegener. 2012, 7, 29.
    • (2012) Mol. Neurodegener , vol.7 , pp. 29
    • Fang, C.1    Bourdette, D.2    Banker, G.3
  • 93
    • 77949801029 scopus 로고    scopus 로고
    • Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/Milton complex
    • Misko, A.; Jiang, S.; Wegorzewska, I.; Milbrandt, J.; Baloh, R.H. Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/Milton complex. J. Neurosci. 2010, 30, 4232-4240.
    • (2010) J. Neurosci , vol.30 , pp. 4232-4240
    • Misko, A.1    Jiang, S.2    Wegorzewska, I.3    Milbrandt, J.4    Baloh, R.H.5
  • 94
    • 0037458579 scopus 로고    scopus 로고
    • Atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis
    • Fransson, A.; Ruusala, A.; Aspenstrom, P. Atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. J. Biol. Chem. 2003, 278, 6495-6502.
    • (2003) J. Biol. Chem , vol.278 , pp. 6495-6502
    • Fransson, A.1    Ruusala, A.2    Aspenstrom, P.3
  • 96
    • 84858281225 scopus 로고
    • Abnormal mitochondrial dynamics and synaptic degeneration as early events in Alzheimer's disease: Implications to mitochondria-targeted antioxidant therapeutics
    • Reddy, P.H.; Tripathi, R.; Troung, Q.; Tirumala, K.; Reddy, T.P.; Anekonda, V.; Shirendeb, U.P.; Calkins, M.J.; Reddy, A.P.; Mao, P.; et al. Abnormal mitochondrial dynamics and synaptic degeneration as early events in Alzheimer's disease: Implications to mitochondria-targeted antioxidant therapeutics. Biochim. Biophys. Acta 2012, 1822, 639-649.
    • (1822) Biochim. Biophys. Acta , vol.2012 , pp. 639-649
    • Reddy, P.H.1    Tripathi, R.2    Troung, Q.3    Tirumala, K.4    Reddy, T.P.5    Anekonda, V.6    Shirendeb, U.P.7    Calkins, M.J.8    Reddy, A.P.9    Mao, P.10
  • 97
    • 33646349444 scopus 로고    scopus 로고
    • Mitochondrial oxidative damage in aging and Alzheimer's disease: Implications for mitochondrially targeted antioxidant therapeutics
    • Reddy, P.H. Mitochondrial oxidative damage in aging and Alzheimer's disease: Implications for mitochondrially targeted antioxidant therapeutics. J. Biomed. Biotechnol. 2006, 2006, 31372.
    • (2006) J. Biomed. Biotechnol , vol.2006 , pp. 31372
    • Reddy, P.H.1
  • 98
    • 57649171115 scopus 로고    scopus 로고
    • Mitochondrial approaches for neuroprotection
    • Chaturvedi, R.K.; Beal, M.F. Mitochondrial approaches for neuroprotection. Ann. NY Acad. Sci. 2008, 1147, 395-412.
    • (2008) Ann. NY Acad. Sci , vol.1147 , pp. 395-412
    • Chaturvedi, R.K.1    Beal, M.F.2
  • 99
    • 84858148877 scopus 로고
    • Antioxidant clinical trials in mild cognitive impairment and Alzheimer's disease
    • Mecocci, P.; Polidori, M.C. Antioxidant clinical trials in mild cognitive impairment and Alzheimer's disease. Biochim. Biophys. Acta 2012, 1822, 631-638.
    • (1822) Biochim. Biophys. Acta , vol.2012 , pp. 631-638
    • Mecocci, P.1    Polidori, M.C.2
  • 100
    • 84858161403 scopus 로고
    • Elevation of glutathione as a therapeutic strategy in Alzheimer disease
    • Pocernich, C.B.; Butterfield, D.A. Elevation of glutathione as a therapeutic strategy in Alzheimer disease. Biochim. Biophys. Acta 2012, 1822, 625-630.
    • (1822) Biochim. Biophys. Acta , vol.2012 , pp. 625-630
    • Pocernich, C.B.1    Butterfield, D.A.2
  • 101
    • 33847071146 scopus 로고    scopus 로고
    • Targeting antioxidants to mitochondria by conjugation to lipophilic cations
    • Murphy, M.P.; Smith, R.A. Targeting antioxidants to mitochondria by conjugation to lipophilic cations. Annu. Rev. Pharmacol. Toxicol. 2007, 47, 629-656.
    • (2007) Annu. Rev. Pharmacol. Toxicol , vol.47 , pp. 629-656
    • Murphy, M.P.1    Smith, R.A.2
  • 102
    • 33748201552 scopus 로고    scopus 로고
    • Mitochondria-targeted peptide antioxidants: Novel neuroprotective agents
    • Szeto, H.H. Mitochondria-targeted peptide antioxidants: Novel neuroprotective agents. AAPS J. 2006, 8, E521-E531.
    • (2006) AAPS J , vol.8
    • Szeto, H.H.1
  • 103
    • 29344446328 scopus 로고    scopus 로고
    • Targeting antioxidants to mitochondria: A new therapeutic direction
    • Sheu, S.S.; Nauduri, D.; Anders, M.W. Targeting antioxidants to mitochondria: A new therapeutic direction. Biochim. Biophys. Acta 2006, 1762, 256-265.
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 256-265
    • Sheu, S.S.1    Nauduri, D.2    Anders, M.W.3
  • 105
    • 0345599276 scopus 로고    scopus 로고
    • Comparison of [Dmt1]DALDA and DAMGO in binding and G protein activation at mu, delta, and kappa opioid receptors
    • Zhao, G.M.; Qian, X.; Schiller, P.W.; Szeto, H.H. Comparison of [Dmt1]DALDA and DAMGO in binding and G protein activation at mu, delta, and kappa opioid receptors. J. Pharmacol. Exp. Ther. 2003, 307, 947-954.
    • (2003) J. Pharmacol. Exp. Ther , vol.307 , pp. 947-954
    • Zhao, G.M.1    Qian, X.2    Schiller, P.W.3    Szeto, H.H.4
  • 106
    • 4544370680 scopus 로고    scopus 로고
    • Cell-permeable peptide antioxidants targeted to inner mitochondrial membrane inhibit mitochondrial swelling, oxidative cell death, and reperfusion injury
    • Zhao, K.; Zhao, G.M.; Wu, D.; Soong, Y.; Birk, A.V.; Schiller, P.W.; Szeto, H.H. Cell-permeable peptide antioxidants targeted to inner mitochondrial membrane inhibit mitochondrial swelling, oxidative cell death, and reperfusion injury. J. Biol. Chem. 2004, 279, 34682-34690.
    • (2004) J. Biol. Chem , vol.279 , pp. 34682-34690
    • Zhao, K.1    Zhao, G.M.2    Wu, D.3    Soong, Y.4    Birk, A.V.5    Schiller, P.W.6    Szeto, H.H.7
  • 107
    • 33845979877 scopus 로고    scopus 로고
    • Mitochondrial targeting with antioxidant peptide SS-31 prevents mitochondrial depolarization, reduces islet cell apoptosis, increases islet cell yield, and improves posttransplantation function
    • Thomas, D.A.; Stauffer, C.; Zhao, K.; Yang, H.; Sharma, V.K.; Szeto, H.H.; Suthanthiran, M. Mitochondrial targeting with antioxidant peptide SS-31 prevents mitochondrial depolarization, reduces islet cell apoptosis, increases islet cell yield, and improves posttransplantation function. J. Am. Soc. Nephrol. 2007, 18, 213-222.
    • (2007) J. Am. Soc. Nephrol , vol.18 , pp. 213-222
    • Thomas, D.A.1    Stauffer, C.2    Zhao, K.3    Yang, H.4    Sharma, V.K.5    Szeto, H.H.6    Suthanthiran, M.7
  • 108
    • 34247209532 scopus 로고    scopus 로고
    • Potent mitochondria-targeted peptides reduce myocardial infarction in rats
    • Cho, J.; Won, K.; Wu, D.; Soong, Y.; Liu, S.; Szeto, H.H.; Hong, M.K. Potent mitochondria-targeted peptides reduce myocardial infarction in rats. Coron. Artery Dis. 2007, 18, 215-220.
    • (2007) Coron. Artery Dis , vol.18 , pp. 215-220
    • Cho, J.1    Won, K.2    Wu, D.3    Soong, Y.4    Liu, S.5    Szeto, H.H.6    Hong, M.K.7
  • 109
    • 33947495568 scopus 로고    scopus 로고
    • A novel cell-permeable antioxidant peptide, SS31, attenuates ischemic brain injury by down-regulating CD36
    • Cho, S.; Szeto, H.H.; Kim, E.; Kim, H.; Tolhurst, A.T.; Pinto, J.T. A novel cell-permeable antioxidant peptide, SS31, attenuates ischemic brain injury by down-regulating CD36. J. Biol. Chem. 2007, 282, 4634-4642.
    • (2007) J. Biol. Chem , vol.282 , pp. 4634-4642
    • Cho, S.1    Szeto, H.H.2    Kim, E.3    Kim, H.4    Tolhurst, A.T.5    Pinto, J.T.6
  • 110
    • 33746397617 scopus 로고    scopus 로고
    • Cell-permeable peptide antioxidants as a novel therapeutic approach in a mouse model of amyotrophic lateral sclerosis
    • Petri, S.; Kiaei, M.; Damiano, M.; Hiller, A.; Wille, E.; Manfredi, G.; Calingasan, N.Y.; Szeto, H.H.; Beal, M.F. Cell-permeable peptide antioxidants as a novel therapeutic approach in a mouse model of amyotrophic lateral sclerosis. J. Neurochem. 2006, 98, 1141-1148.
    • (2006) J. Neurochem , vol.98 , pp. 1141-1148
    • Petri, S.1    Kiaei, M.2    Damiano, M.3    Hiller, A.4    Wille, E.5    Manfredi, G.6    Calingasan, N.Y.7    Szeto, H.H.8    Beal, M.F.9
  • 111
    • 1842732209 scopus 로고    scopus 로고
    • Oligomerization of Alzheimer's beta-amyloid within processes and synapses of cultured neurons and brain
    • Takahashi, R.H.; Almeida, C.G.; Kearney, P.F.; Yu, F.; Lin, M.T.; Milner, T.A.; Gouras, G.K. Oligomerization of Alzheimer's beta-amyloid within processes and synapses of cultured neurons and brain. J. Neurosci. 2004, 24, 3592-3599.
    • (2004) J. Neurosci , vol.24 , pp. 3592-3599
    • Takahashi, R.H.1    Almeida, C.G.2    Kearney, P.F.3    Yu, F.4    Lin, M.T.5    Milner, T.A.6    Gouras, G.K.7
  • 112
    • 77249158836 scopus 로고    scopus 로고
    • Amyloid beta induces the morphological neurodegenerative triad of spine loss, dendritic simplification, and neuritic dystrophies through calcineurin activation
    • Wu, H.Y.; Hudry, E.; Hashimoto, T.; Kuchibhotla, K.; Rozkalne, A.; Fan, Z.; Spires-Jones, T.; Xie, H.; Arbel-Ornath, M.; Grosskreutz, C.L.; et al. Amyloid beta induces the morphological neurodegenerative triad of spine loss, dendritic simplification, and neuritic dystrophies through calcineurin activation. J. Neurosci. 2010, 30, 2636-2649.
    • (2010) J. Neurosci , vol.30 , pp. 2636-2649
    • Wu, H.Y.1    Hudry, E.2    Hashimoto, T.3    Kuchibhotla, K.4    Rozkalne, A.5    Fan, Z.6    Spires-Jones, T.7    Xie, H.8    Arbel-Ornath, M.9    Grosskreutz, C.L.10
  • 113
    • 84859525656 scopus 로고    scopus 로고
    • Distinct dendritic spine and nuclear phases of calcineurin activation after exposure to amyloid-beta revealed by a novel fluorescence resonance energy transfer assay
    • Wu, H.Y.; Hudry, E.; Hashimoto, T.; Uemura, K.; Fan, Z.Y.; Berezovska, O.; Grosskreutz, C.L.; Bacskai, B.J.; Hyman, B.T. Distinct dendritic spine and nuclear phases of calcineurin activation after exposure to amyloid-beta revealed by a novel fluorescence resonance energy transfer assay. J. Neurosci. 2012, 32, 5298-5309.
    • (2012) J. Neurosci , vol.32 , pp. 5298-5309
    • Wu, H.Y.1    Hudry, E.2    Hashimoto, T.3    Uemura, K.4    Fan, Z.Y.5    Berezovska, O.6    Grosskreutz, C.L.7    Bacskai, B.J.8    Hyman, B.T.9
  • 114
    • 84861130196 scopus 로고    scopus 로고
    • Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer's disease neurons: Implications for mitochondrial dysfunction and neuronal damage
    • Manczak, M.; Reddy, P.H. Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer's disease neurons: Implications for mitochondrial dysfunction and neuronal damage. Hum. Mol. Genet. 2012, 21, 2538-2547.
    • (2012) Hum. Mol. Genet , vol.21 , pp. 2538-2547
    • Manczak, M.1    Reddy, P.H.2
  • 115
    • 84866241815 scopus 로고    scopus 로고
    • Mitochondrial dynamics and mitophagy in the 6-hydroxydopamine preclinical model of Parkinson's disease
    • 2012
    • Galindo, M.F.; Solesio, M.E.; Atienzar-Aroca, S.; Zamora, M.J.; Jordan Bueso, J. Mitochondrial dynamics and mitophagy in the 6-hydroxydopamine preclinical model of Parkinson's disease. Parkinsons Dis. 2012, 2012, 131058.
    • (2012) Parkinsons Dis , pp. 131058
    • Galindo, M.F.1    Solesio, M.E.2    Atienzar-Aroca, S.3    Zamora, M.J.4    Jordan Bueso, J.5
  • 116
    • 84871270796 scopus 로고    scopus 로고
    • The mitochondria-targeted anti-oxidant MitoQ reduces aspects of mitochondrial fission in the 6-OHDA cell model of Parkinson's disease
    • Acta 2012, in press
    • Solesio, M.E.; Prime, T.A.; Logan, A.; Murphy, M.P.; Del Mar Arroyo-Jimenez, M.; Jordan, J.; Galindo, M.F. The mitochondria-targeted anti-oxidant MitoQ reduces aspects of mitochondrial fission in the 6-OHDA cell model of Parkinson's disease. Biochim. Biophys. Acta 2012, in press.
    • Biochim. Biophys
    • Solesio, M.E.1    Prime, T.A.2    Logan, A.3    Murphy, M.P.4    Del Mar Arroyo-Jimenez, M.5    Jordan, J.6    Galindo, M.F.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.