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Volumn 21, Issue 23, 2012, Pages 5131-5146

Abnormal interaction of VDAC1 with amyloid beta and phosphorylated tau causes mitochondrial dysfunction in Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; MUTANT PROTEIN; TAU PROTEIN; VOLTAGE DEPENDENT ANION CHANNEL 1;

EID: 84869012777     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/dds360     Document Type: Article
Times cited : (268)

References (77)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: genes, proteins, and therapy
    • Selkoe, D.J. (2001) Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev., 81, 741-766.
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 2
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson, M.P. (2004) Pathways towards and away from Alzheimer's disease. Nature, 430, 631-639.
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 3
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer's disease
    • LaFerla, F.M., Green, K.N. and Oddo, S. (2007) Intracellular amyloid-beta in Alzheimer's disease. Nat. Rev. Neurosci., 8, 499-509.
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 499-509
    • LaFerla, F.M.1    Green, K.N.2    Oddo, S.3
  • 4
    • 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. and Beal, M.F. (2008) Amyloid beta, mitochondrial dysfunction and synaptic damage: implications for cognitive decline in aging and Alzheimer's disease. Trends Mol. Med., 14, 45-53.
    • (2008) Trends Mol. Med. , vol.14 , pp. 45-53
    • Reddy, P.H.1    Beal, M.F.2
  • 5
    • 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. and Shirendeb, U. (2010) Amyloid-beta and mitochondria in aging and Alzheimer's disease: implications for synaptic damage and cognitive decline. J. Alzheimers Dis., 20, 499-512.
    • (2010) J. Alzheimers Dis. , vol.20 , pp. 499-512
    • Reddy, P.H.1    Manczak, M.2    Mao, P.3    Calkins, M.J.4    Reddy, A.P.5    Shirendeb, U.6
  • 6
    • 3042806534 scopus 로고    scopus 로고
    • A 'mitochondrial cascade hypothesis' for sporadic Alzheimer's disease
    • Swerdlow, R.H. and Khan, S.M. (2004) A 'mitochondrial cascade hypothesis' for sporadic Alzheimer's disease. Med. Hypotheses, 63, 8-20.
    • (2004) Med. Hypotheses , vol.63 , pp. 8-20
    • Swerdlow, R.H.1    Khan, S.M.2
  • 7
    • 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. and Yan, S.S. (2010) Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model. Proc. Natl Acad. Sci. USA, 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
  • 8
    • 0035875690 scopus 로고    scopus 로고
    • Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis
    • Pratico', D., Uryu, K., Leight, S., Trojanoswki, J.Q. and Lee, V.M. (2001) Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis. J. Neurosci., 21, 4183-4187.
    • (2001) J. Neurosci. , vol.21 , pp. 4183-4187
    • Pratico', D.1    Uryu, K.2    Leight, S.3    Trojanoswki, J.Q.4    Lee, V.M.5
  • 9
    • 2342628596 scopus 로고    scopus 로고
    • Differential expression of oxidative phosphorylation genes in patients with Alzheimer's disease: implications for early mitochondrial dysfunction and oxidative damage
    • Manczak, M., Park, B.S., Jung, Y. and Reddy, P.H. (2004) Differential expression of oxidative phosphorylation genes in patients with Alzheimer's disease: implications for early mitochondrial dysfunction and oxidative damage. Neuromolecular Med., 5, 147-162.
    • (2004) Neuromolecular Med , vol.5 , pp. 147-162
    • Manczak, M.1    Park, B.S.2    Jung, Y.3    Reddy, P.H.4
  • 10
    • 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. and Anandatheerthavarada, H.K. (2006) Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction. J. Neurosci., 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
  • 12
    • 0025024024 scopus 로고
    • Cytochrome oxidase deficiency in Alzheimer's disease
    • Parker, W.D. Jr., Filley, C.M. and Parks, J.K. (1990) Cytochrome oxidase deficiency in Alzheimer's disease. Neurology, 40, 1302-1303.
    • (1990) Neurology , vol.40 , pp. 1302-1303
    • Parker Jr, W.D.1    Filley, C.M.2    Parks, J.K.3
  • 13
    • 0034612075 scopus 로고    scopus 로고
    • A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients
    • Maurer, I., Zierz, S. and Möller, H.J. (2000) A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients. Neurobiol. Aging, 21, 455-462.
    • (2000) Neurobiol. Aging , vol.21 , pp. 455-462
    • Maurer, I.1    Zierz, S.2    Möller, H.J.3
  • 15
    • 3042736860 scopus 로고    scopus 로고
    • Gene expression profiles of transcripts in amyloid precursor protein transgenic mice: up-regulation of mitochondrial metabolism and apoptotic genes is an early cellular change in Alzheimer's disease
    • Reddy, P.H., McWeeney, S., Park, B.S., Manczak, M., Gutala, R.V., Partovi, D., Jung, Y., Yau, V., Searles, R., Mori, M. and Quinn, J. (2004) Gene expression profiles of transcripts in amyloid precursor protein transgenic mice: up-regulation of mitochondrial metabolism and apoptotic genes is an early cellular change in Alzheimer's disease. Hum. Mol. Genet., 13, 1225-1240.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1225-1240
    • Reddy, P.H.1    McWeeney, S.2    Park, B.S.3    Manczak, M.4    Gutala, R.V.5    Partovi, D.6    Jung, Y.7    Yau, V.8    Searles, R.9    Mori, M.10    Quinn, J.11
  • 16
    • 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. and Reddy, P.H. (2006) 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., 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
  • 17
    • 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. and Reddy, P.H. (2011) 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., 20, 2495-2509.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2495-2509
    • Manczak, M.1    Calkins, M.J.2    Reddy, P.H.3
  • 19
    • 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. and Brinton, R.D. (2009) Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease. Proc. Natl Acad. Sci. USA, 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
  • 20
    • 81955164821 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and accumulation of the b-secretase-cleaved C-terminal fragment of APP in Alzheimer's disease transgenic mice
    • Devi, L. and Ohno, M. (2012) Mitochondrial dysfunction and accumulation of the b-secretase-cleaved C-terminal fragment of APP in Alzheimer's disease transgenic mice. Neurobiol. Dis., 45, 417-424.
    • (2012) Neurobiol. Dis. , vol.45 , pp. 417-424
    • Devi, L.1    Ohno, M.2
  • 24
    • 79751537405 scopus 로고    scopus 로고
    • Amyloid beta impairs mitochondrial anterograde transport and degenerates synapses in Alzheimer's disease neurons
    • Calkins, M.J. and Reddy, P.H. (2011) Amyloid beta impairs mitochondrial anterograde transport and degenerates synapses in Alzheimer's disease neurons. Biochim. Biophys. Acta, 1812, 507-513.
    • (2011) Biochim. Biophys. Acta , vol.1812 , pp. 507-513
    • Calkins, M.J.1    Reddy, P.H.2
  • 25
    • 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. and Reddy, P.H. (2011) 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., 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
  • 27
    • 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. and Zhu, X. (2008) Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins. Proc. Natl Acad. Sci. USA, 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
  • 28
    • 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. and Zhu, X. (2009) Impaired balance of mitochondrial fission and fusion in Alzheimer's disease. J. Neurosci., 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
  • 29
    • 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. and Zhu, X. (2010) Amyloid-beta-derived diffusible ligands cause impaired axonal transport of mitochondria in neurons. Neurodegener. Dis., 7, 56-59.
    • (2010) Neurodegener. Dis. , vol.7 , pp. 56-59
    • Wang, X.1    Perry, G.2    Smith, M.A.3    Zhu, X.4
  • 30
    • 39449124353 scopus 로고    scopus 로고
    • Mitochondria morphology and DNA content upon sublethal exposure to beta-amyloid(1-42) peptide
    • Diana, A., Simić, G., Sinforiani, E., Orru', N., Pichiri, G. and Bono, G. (2008) Mitochondria morphology and DNA content upon sublethal exposure to beta-amyloid(1-42) peptide. Coll. Antropol., 32, 51-58.
    • (2008) Coll. Antropol. , vol.32 , pp. 51-58
    • Diana, A.1    Simić, G.2    Sinforiani, E.3    Orru', N.4    Pichiri, G.5    Bono, G.6
  • 31
    • 51949099008 scopus 로고    scopus 로고
    • Amyloid precursor protein and amyloid beta-peptide bind to ATP synthase and regulate its activity at the surface of neural cells
    • Schmidt, C., Lepsverdize, E., Chi, S.L., Das, A.M., Pizzo, S.V., Dityatev, A. and Schachner, M. (2008) Amyloid precursor protein and amyloid beta-peptide bind to ATP synthase and regulate its activity at the surface of neural cells. Mol. Psychiatry, 13, 953-969.
    • (2008) Mol. Psychiatry , vol.13 , pp. 953-969
    • Schmidt, C.1    Lepsverdize, E.2    Chi, S.L.3    Das, A.M.4    Pizzo, S.V.5    Dityatev, A.6    Schachner, M.7
  • 32
    • 31044450074 scopus 로고    scopus 로고
    • Overexpression of amyloid precursor protein induces susceptibility to oxidative stress in human neuroblastoma SH-SY5Y cells
    • Matsumoto, K., Akao, Y., Yi, H., Shamoto-Nagai, M., Maruyama, W. and Naoi, M. (2006) Overexpression of amyloid precursor protein induces susceptibility to oxidative stress in human neuroblastoma SH-SY5Y cells. J. Neural. Transm., 113, 125-135.
    • (2006) J. Neural. Transm. , vol.113 , pp. 125-135
    • Matsumoto, K.1    Akao, Y.2    Yi, H.3    Shamoto-Nagai, M.4    Maruyama, W.5    Naoi, M.6
  • 33
    • 0031737226 scopus 로고    scopus 로고
    • Abnormalities of mitochondrial enzymes in Alzheimer disease
    • Gibson, G.E., Sheu, K.F. and Blass, J.P. (1998) Abnormalities of mitochondrial enzymes in Alzheimer disease. J. Neural. Transm., 105, 855-870.
    • (1998) J. Neural. Transm. , vol.105 , pp. 855-870
    • Gibson, G.E.1    Sheu, K.F.2    Blass, J.P.3
  • 34
    • 18844462415 scopus 로고    scopus 로고
    • Increased oxidative damage in nuclear and mitochondrial DNA in Alzheimer's disease
    • Wang, J., Xiong, S., Xie, C., Markesbery, W.R. and Lovell, M.A. (2005) Increased oxidative damage in nuclear and mitochondrial DNA in Alzheimer's disease. J. Neurochem., 93, 953-962.
    • (2005) J. Neurochem. , vol.93 , pp. 953-962
    • Wang, J.1    Xiong, S.2    Xie, C.3    Markesbery, W.R.4    Lovell, M.A.5
  • 38
    • 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. (2008) Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease. Nat. Med., 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
  • 39
    • 80052846665 scopus 로고    scopus 로고
    • Abnormal tau, mitochondrial dysfunction, impaired axonal transport of mitochondria, and synaptic deprivation in Alzheimer's disease
    • Reddy, P.H. (2011) Abnormal tau, mitochondrial dysfunction, impaired axonal transport of mitochondria, and synaptic deprivation in Alzheimer's disease. Brain Res., 1415, 136-148.
    • (2011) Brain Res , vol.1415 , pp. 136-148
    • Reddy, P.H.1
  • 40
    • 0032476645 scopus 로고    scopus 로고
    • Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease
    • Ebneth, A., Godemann, R., Stamer, K., Illenberger, S., Trinczek, B. and Mandelkow, E. (1998) Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease. J. Cell Biol., 143, 777-794.
    • (1998) J. Cell Biol. , vol.143 , pp. 777-794
    • Ebneth, A.1    Godemann, R.2    Stamer, K.3    Illenberger, S.4    Trinczek, B.5    Mandelkow, E.6
  • 41
    • 0037128935 scopus 로고    scopus 로고
    • Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress
    • Stamer, K., Vogel, R., Thies, E., Mandelkow, E. and Mandelkow, E.M. (2002) Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J. Cell Biol., 156, 1051-1063.
    • (2002) J. Cell Biol. , vol.156 , pp. 1051-1063
    • Stamer, K.1    Vogel, R.2    Thies, E.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 42
    • 0345276565 scopus 로고    scopus 로고
    • Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses
    • Mandelkow, E.M., Stamer, K., Vogel, R., Thies, E. and Mandelkow, E. (2003) Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses. Neurobiol. Aging, 24, 1079-1085.
    • (2003) Neurobiol. Aging , vol.24 , pp. 1079-1085
    • Mandelkow, E.M.1    Stamer, K.2    Vogel, R.3    Thies, E.4    Mandelkow, E.5
  • 43
    • 39449138356 scopus 로고    scopus 로고
    • Tau inhibits anterograde axonal transport and perturbs stability in growing axonal neurites in part by displacing kinesin cargo: neurofilaments attenuate tau-mediated neurite instability
    • Dubey, M., Chaudhury, P., Kabiru, H. and Shea, T.B. (2008) Tau inhibits anterograde axonal transport and perturbs stability in growing axonal neurites in part by displacing kinesin cargo: neurofilaments attenuate tau-mediated neurite instability. Cell Motil. Cytoskeleton, 65, 89-99.
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 89-99
    • Dubey, M.1    Chaudhury, P.2    Kabiru, H.3    Shea, T.B.4
  • 46
    • 42049094912 scopus 로고    scopus 로고
    • Altered oxidant-mediated intraneuronal zinc mobilization in a triple transgenic mouse model of Alzheimer's disease
    • Sensi, S.L., Rapposelli, I.G., Frazzini, V. and Mascetra, N. (2008) Altered oxidant-mediated intraneuronal zinc mobilization in a triple transgenic mouse model of Alzheimer's disease. Exp. Gerontol., 43, 488-492.
    • (2008) Exp. Gerontol. , vol.43 , pp. 488-492
    • Sensi, S.L.1    Rapposelli, I.G.2    Frazzini, V.3    Mascetra, N.4
  • 48
    • 80355148410 scopus 로고    scopus 로고
    • Behavioral deficit, oxidative stress, and mitochondrial dysfunction precede tau pathology in P301S transgenic mice
    • Dumont, M., Stack, C., Elipenahli, C., Jainuddin, S., Gerges, M., Starkova, N.N., Yang, L., Starkov, A.A. and Beal, F. (2011) Behavioral deficit, oxidative stress, and mitochondrial dysfunction precede tau pathology in P301S transgenic mice. FASEB J., 25, 4063-4072.
    • (2011) FASEB J , vol.25 , pp. 4063-4072
    • Dumont, M.1    Stack, C.2    Elipenahli, C.3    Jainuddin, S.4    Gerges, M.5    Starkova, N.N.6    Yang, L.7    Starkov, A.A.8    Beal, F.9
  • 51
    • 34648834538 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in aging and Alzheimer's disease: strategies to protect neurons
    • Reddy, P.H. (2007) Mitochondrial dysfunction in aging and Alzheimer's disease: strategies to protect neurons. Antioxid. Redox Signal., 10, 1647-1658.
    • (2007) Antioxid. Redox Signal. , vol.10 , pp. 1647-1658
    • Reddy, P.H.1
  • 52
    • 0030958679 scopus 로고    scopus 로고
    • Regulation of metabolite flux through voltage-gating of VDAC channels
    • Hodge, T. and Colombini, M. (1997) Regulation of metabolite flux through voltage-gating of VDAC channels. J Membr. Biol., 157, 271-279.
    • (1997) J Membr. Biol. , vol.157 , pp. 271-279
    • Hodge, T.1    Colombini, M.2
  • 53
    • 0030967247 scopus 로고    scopus 로고
    • Autodirected insertion: preinserted VDAC channels greatly shorten the delay to the insertion of new channels
    • Xu, X. and Colombini, M. (1997) Autodirected insertion: preinserted VDAC channels greatly shorten the delay to the insertion of new channels. Biophys. J., 72, 2129-2136.
    • (1997) Biophys. J. , vol.72 , pp. 2129-2136
    • Xu, X.1    Colombini, M.2
  • 54
    • 0030947935 scopus 로고    scopus 로고
    • VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function
    • Rostovtseva, T. and Colombini, M. (1997) VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function. Biophys. J., 72, 1954-1962.
    • (1997) Biophys. J. , vol.72 , pp. 1954-1962
    • Rostovtseva, T.1    Colombini, M.2
  • 55
    • 84859780328 scopus 로고    scopus 로고
    • VDAC structure, selectivity, and dynamics
    • Colombini, M. (2012) VDAC structure, selectivity, and dynamics. Biochim. Biophys. Acta, 1818, 1457-1465.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1457-1465
    • Colombini, M.1
  • 56
    • 0030586893 scopus 로고    scopus 로고
    • A novel mouse mitochondrial voltage-dependent anion channel gene localizes to chromosome 8
    • Sampson, M.J., Lovell, R.S., Davison, D.B. and Craigen, W.J. (1996) A novel mouse mitochondrial voltage-dependent anion channel gene localizes to chromosome 8. Genomics, 36, 192-196.
    • (1996) Genomics , vol.36 , pp. 192-196
    • Sampson, M.J.1    Lovell, R.S.2    Davison, D.B.3    Craigen, W.J.4
  • 57
    • 0029925099 scopus 로고    scopus 로고
    • Isolation, characterization, and mapping of two mouse mitochondrial voltage-dependent anion channel isoforms
    • Sampson, M.J., Lovell, R.S. and Craigen, W.J. (1996) Isolation, characterization, and mapping of two mouse mitochondrial voltage-dependent anion channel isoforms. Genomics, 33, 283-288.
    • (1996) Genomics , vol.33 , pp. 283-288
    • Sampson, M.J.1    Lovell, R.S.2    Craigen, W.J.3
  • 58
    • 52449097233 scopus 로고    scopus 로고
    • Genetic strategies for dissecting mammalian and Drosophila voltage-dependent anion channel functions
    • Craigen, W.J. and Graham, B.H. (2008) Genetic strategies for dissecting mammalian and Drosophila voltage-dependent anion channel functions. J. Bioenerg. Biomembr., 40, 207-212.
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 207-212
    • Craigen, W.J.1    Graham, B.H.2
  • 59
    • 33845405591 scopus 로고    scopus 로고
    • VDAC1, having a shorter N-terminus than VDAC2 but showing the same migration in an SDS-polyacrylamide gel, is the predominant form expressed in mitochondria of various tissues
    • Yamamoto, T., Yamada, A., Watanabe, M., Yoshimura, Y., Yamazaki, N., Yoshimura, Y., Yamauchi, T., Kataoka, M., Nagata, T., Terada, H. and Shinohara, Y. (2006) VDAC1, having a shorter N-terminus than VDAC2 but showing the same migration in an SDS-polyacrylamide gel, is the predominant form expressed in mitochondria of various tissues. J. Proteome Res., 5, 3336-3344.
    • (2006) J. Proteome Res. , vol.5 , pp. 3336-3344
    • Yamamoto, T.1    Yamada, A.2    Watanabe, M.3    Yoshimura, Y.4    Yamazaki, N.5    Yoshimura, Y.6    Yamauchi, T.7    Kataoka, M.8    Nagata, T.9    Terada, H.10    Shinohara, Y.11
  • 60
    • 0032514888 scopus 로고    scopus 로고
    • A novel isoform of the mitochondrial outer membrane protein VDAC3 via alternative splicing of a 3-base exon Functional characteristics and subcellular localization
    • Sampson, M.J., Ross, L., Decker, W.K. and Craigen, W.J. (1998) A novel isoform of the mitochondrial outer membrane protein VDAC3 via alternative splicing of a 3-base exon. Functional characteristics and subcellular localization. J. Biol. Chem., 273, 30482-30486.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30482-30486
    • Sampson, M.J.1    Ross, L.2    Decker, W.K.3    Craigen, W.J.4
  • 61
    • 84859747227 scopus 로고    scopus 로고
    • Voltage-dependant anion channels: novel insights into isoform function through genetic models
    • Raghavan, A., Sheiko, T., Graham, B.H. and Craigen, W.J. (2012) Voltage-dependant anion channels: novel insights into isoform function through genetic models. Biochim. Biophys. Acta, 1818, 1477-1485.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1477-1485
    • Raghavan, A.1    Sheiko, T.2    Graham, B.H.3    Craigen, W.J.4
  • 62
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu, S., Narita, M. and Tsujimoto, Y. (1999) Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature, 399, 483-487.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 63
    • 1442327526 scopus 로고    scopus 로고
    • Essential role of the voltage-dependent anion channel (VDAC) in mitochondrial permeability transition pore opening and cytochrome c release induced by arsenic trioxide
    • Zheng, Y., Shi, Y., Tian, C., Jiang, C., Jin, H., Chen, J., Almasan, A., Tang, H. and Chen, Q. (2004) Essential role of the voltage-dependent anion channel (VDAC) in mitochondrial permeability transition pore opening and cytochrome c release induced by arsenic trioxide. Oncogene, 23, 1239-1247.
    • (2004) Oncogene , vol.23 , pp. 1239-1247
    • Zheng, Y.1    Shi, Y.2    Tian, C.3    Jiang, C.4    Jin, H.5    Chen, J.6    Almasan, A.7    Tang, H.8    Chen, Q.9
  • 64
    • 84859742434 scopus 로고    scopus 로고
    • VDAC inhibition by tubulin and its physiological implications
    • Rostovtseva, T.K. and Bezrukov, S.M. (2012) VDAC inhibition by tubulin and its physiological implications. Biochim. Biophys. Acta, 1818, 1526-1535.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1526-1535
    • Rostovtseva, T.K.1    Bezrukov, S.M.2
  • 66
    • 84859763834 scopus 로고    scopus 로고
    • Regulation of mitochondrial function by voltage dependent anion channels in ethanol metabolism and the Warburg effect
    • Lemasters, J.J., Holmuhamedov, E.L., Czerny, C., Zhong, Z. and Maldonado, E.N. (2012) Regulation of mitochondrial function by voltage dependent anion channels in ethanol metabolism and the Warburg effect. Biochim. Biophys. Acta, 1818, 1536-1544.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1536-1544
    • Lemasters, J.J.1    Holmuhamedov, E.L.2    Czerny, C.3    Zhong, Z.4    Maldonado, E.N.5
  • 68
    • 3543141113 scopus 로고    scopus 로고
    • Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release
    • Choo, Y.S., Johnson, G.V., MacDonald, M., Detloff, P.J. and Lesort, M. (2004) Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release. Hum. Mol. Genet., 13, 1407-1420.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1407-1420
    • Choo, Y.S.1    Johnson, G.V.2    MacDonald, M.3    Detloff, P.J.4    Lesort, M.5
  • 69
    • 79951572740 scopus 로고    scopus 로고
    • Enhanced expression of the voltage-dependent anion channel 1 (VDAC1) in Alzheimer's disease transgenic mice: an insight into the pathogenic effects of amyloid-b
    • Cuadrado-Tejedor, M., Vilarin{ogonek}o, M., Cabodevilla, F., Del Ri{dotless}́o, J., Frechilla, D. and Pérez-Mediavilla, A. (2011) Enhanced expression of the voltage-dependent anion channel 1 (VDAC1) in Alzheimer's disease transgenic mice: an insight into the pathogenic effects of amyloid-b. J. Alzheimers Dis., 23, 195-206.
    • (2011) J. Alzheimers Dis. , vol.23 , pp. 195-206
    • Cuadrado-Tejedor, M.1    Vilariño, M.2    Cabodevilla, F.3    Del Río, J.4    Frechilla, D.5    Pérez-Mediavilla, A.6
  • 70
    • 79960034042 scopus 로고    scopus 로고
    • Apoptogenic interactions of plasmalemmal type-1 VDAC and Ab peptides via GxxxG motifs induce Alzheimer's disease -a basic model of apoptosis?
    • Thinnes, F.P. (2011) Apoptogenic interactions of plasmalemmal type-1 VDAC and Ab peptides via GxxxG motifs induce Alzheimer's disease -a basic model of apoptosis? Wien. Med. Wochenschr., 161, 274-276.
    • (2011) Wien Med. Wochenschr. , vol.161 , pp. 274-276
    • Thinnes, F.P.1
  • 71
    • 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. and Reddy, P.H. (2012) 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., 21, 2538-2547.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 2538-2547
    • Manczak, M.1    Reddy, P.H.2
  • 72
    • 0026134421 scopus 로고
    • Demonstration of amyloid deposits and neurofibrillary changes in whole brain sections
    • Braak, H. and Braak, E. (1991) Demonstration of amyloid deposits and neurofibrillary changes in whole brain sections. Brain Pathol., 1, 213-216.
    • (1991) Brain Pathol , vol.1 , pp. 213-216
    • Braak, H.1    Braak, E.2
  • 73
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice
    • Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F. and Cole, G. (1996) Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice. Science, 274, 99-102.
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3    Eckman, C.4    Harigaya, Y.5    Younkin, S.6    Yang, F.7    Cole, G.8
  • 74
  • 76
    • 84858984845 scopus 로고    scopus 로고
    • Dynamin-related protein 1 heterozygote knockout mice do not have synaptic and mitochondrial deficiencies
    • Manczak, M., Sesaki, H., Kageyama, Y. and Reddy, P.H. (2012) Dynamin-related protein 1 heterozygote knockout mice do not have synaptic and mitochondrial deficiencies. Biochim. Biophys. Acta, 1822, 862-874.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 862-874
    • Manczak, M.1    Sesaki, H.2    Kageyama, Y.3    Reddy, P.H.4
  • 77
    • 84855395163 scopus 로고    scopus 로고
    • Mutant huntingtin's interaction with mitochondrial protein Drp1 impairs mitochondrial biogenesis and causes defective axonal transport and synaptic degeneration in Huntington's disease
    • Shirendeb, U.P., Calkins, M.J., Manczak, M., Anekonda, V., Dufour, B., McBride, J.L., Mao, P. and Reddy, P.H. (2012) Mutant huntingtin's interaction with mitochondrial protein Drp1 impairs mitochondrial biogenesis and causes defective axonal transport and synaptic degeneration in Huntington's disease. Hum. Mol. Genet., 21, 406-420.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 406-420
    • Shirendeb, U.P.1    Calkins, M.J.2    Manczak, M.3    Anekonda, V.4    Dufour, B.5    McBride, J.L.6    Mao, P.7    Reddy, P.H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.