메뉴 건너뛰기




Volumn 1842, Issue 12, 2014, Pages 2517-2527

Cyclophilin D deficiency rescues Aβ-impaired PKA/CREB signaling and alleviates synaptic degeneration

Author keywords

Alzheimer's disease; Amyloid beta; Mitochondrial permeability transition; Oxidative stress; PKA CREB signaling; Synaptic alteration

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; ANTIOXIDANT; CATALASE; CREB1 PROTEIN, MOUSE; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; CYCLOPHILIN; CYCLOPHILIN D; PROBUCOL; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE;

EID: 84914153002     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2013.03.004     Document Type: Article
Times cited : (74)

References (60)
  • 2
    • 0030464914 scopus 로고    scopus 로고
    • Beta-amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease
    • Cummings B.J., Pike C.J., Shankle R., Cotman C.W. Beta-amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease. Neurobiol. Aging 1996, 17:921-933.
    • (1996) Neurobiol. Aging , vol.17 , pp. 921-933
    • Cummings, B.J.1    Pike, C.J.2    Shankle, R.3    Cotman, C.W.4
  • 3
    • 33747760358 scopus 로고    scopus 로고
    • Hippocampal synaptic loss in early Alzheimer's disease and mild cognitive impairment
    • Scheff S.W., Price D.A., Schmitt F.A., Mufson E.J. Hippocampal synaptic loss in early Alzheimer's disease and mild cognitive impairment. Neurobiol. Aging 2006, 27:1372-1384.
    • (2006) Neurobiol. Aging , vol.27 , pp. 1372-1384
    • Scheff, S.W.1    Price, D.A.2    Schmitt, F.A.3    Mufson, E.J.4
  • 4
    • 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
  • 5
    • 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. U. S. A. 2009, 106:14670-14675.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , 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
  • 8
    • 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
  • 9
    • 33750683018 scopus 로고    scopus 로고
    • Alzheimer's APP mangles mitochondria
    • Lin M.T., Beal M.F. Alzheimer's APP mangles mitochondria. Nat. Med. 2006, 12:1241-1243.
    • (2006) Nat. Med. , vol.12 , pp. 1241-1243
    • Lin, M.T.1    Beal, M.F.2
  • 12
    • 3042513691 scopus 로고    scopus 로고
    • Mitochondria dysfunction of Alzheimer's disease cybrids enhances Abeta toxicity
    • Cardoso S.M., Santana I., Swerdlow R.H., Oliveira C.R. Mitochondria dysfunction of Alzheimer's disease cybrids enhances Abeta toxicity. J. Neurochem. 2004, 89:1417-1426.
    • (2004) J. Neurochem. , vol.89 , pp. 1417-1426
    • Cardoso, S.M.1    Santana, I.2    Swerdlow, R.H.3    Oliveira, C.R.4
  • 14
    • 33745952665 scopus 로고    scopus 로고
    • Mitochondrial trafficking to synapses in cultured primary cortical neurons
    • Chang D.T., Honick A.S., Reynolds I.J. Mitochondrial trafficking to synapses in cultured primary cortical neurons. J. Neurosci. 2006, 26:7035-7045.
    • (2006) J. Neurosci. , vol.26 , pp. 7035-7045
    • Chang, D.T.1    Honick, A.S.2    Reynolds, I.J.3
  • 15
    • 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. U. S. A. 2008, 105:19318-19323.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , 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
  • 16
    • 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
  • 17
    • 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
  • 18
    • 84869012777 scopus 로고    scopus 로고
    • Abnormal interaction of VDAC1 with amyloid beta and phosphorylated tau causes mitochondrial dysfunction in Alzheimer's disease
    • Manczak M., Reddy P.H. Abnormal interaction of VDAC1 with amyloid beta and phosphorylated tau causes mitochondrial dysfunction in Alzheimer's disease. Hum. Mol. Genet. 2012, 21:5131-5146.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 5131-5146
    • Manczak, M.1    Reddy, P.H.2
  • 20
    • 0037100213 scopus 로고    scopus 로고
    • Effect of amyloid beta-peptide on permeability transition pore: a comparative study
    • Moreira P.I., Santos M.S., Moreno A., Rego A.C., Oliveira C. Effect of amyloid beta-peptide on permeability transition pore: a comparative study. J. Neurosci. Res. 2002, 69:257-267.
    • (2002) J. Neurosci. Res. , vol.69 , pp. 257-267
    • Moreira, P.I.1    Santos, M.S.2    Moreno, A.3    Rego, A.C.4    Oliveira, C.5
  • 24
    • 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
  • 25
    • 79952901937 scopus 로고    scopus 로고
    • Cyclophilin D deficiency improves mitochondrial function and learning/memory in aging Alzheimer disease mouse model
    • Du H., Guo L., Zhang W., Rydzewska M., Yan S. Cyclophilin D deficiency improves mitochondrial function and learning/memory in aging Alzheimer disease mouse model. Neurobiol. Aging 2011, 32:398-406.
    • (2011) Neurobiol. Aging , vol.32 , pp. 398-406
    • Du, H.1    Guo, L.2    Zhang, W.3    Rydzewska, M.4    Yan, S.5
  • 27
    • 0842330769 scopus 로고    scopus 로고
    • Regulation of hippocampal synaptic plasticity by cyclic AMP-dependent protein kinases
    • Nguyen P.V., Woo N.H. Regulation of hippocampal synaptic plasticity by cyclic AMP-dependent protein kinases. Prog. Neurobiol. 2003, 71:401-437.
    • (2003) Prog. Neurobiol. , vol.71 , pp. 401-437
    • Nguyen, P.V.1    Woo, N.H.2
  • 28
    • 0141987893 scopus 로고    scopus 로고
    • Phosphorylation of RIM1alpha by PKA triggers presynaptic long-term potentiation at cerebellar parallel fiber synapses
    • Lonart G., Schoch S., Kaeser P.S., Larkin C.J., Sudhof T.C., Linden D.J. Phosphorylation of RIM1alpha by PKA triggers presynaptic long-term potentiation at cerebellar parallel fiber synapses. Cell 2003, 115:49-60.
    • (2003) Cell , vol.115 , pp. 49-60
    • Lonart, G.1    Schoch, S.2    Kaeser, P.S.3    Larkin, C.J.4    Sudhof, T.C.5    Linden, D.J.6
  • 29
    • 28944444811 scopus 로고    scopus 로고
    • Gene targeting of presynaptic proteins in synaptic plasticity and memory: across the great divide
    • Powell C.M. Gene targeting of presynaptic proteins in synaptic plasticity and memory: across the great divide. Neurobiol. Learn. Mem. 2006, 85:2-15.
    • (2006) Neurobiol. Learn. Mem. , vol.85 , pp. 2-15
    • Powell, C.M.1
  • 30
    • 65649108128 scopus 로고    scopus 로고
    • PKA has a critical role in synaptic delivery of GluR1- and GluR4-containing AMPARs during initial stages of acquisition of in vitro classical conditioning
    • Zheng Z., Keifer J. PKA has a critical role in synaptic delivery of GluR1- and GluR4-containing AMPARs during initial stages of acquisition of in vitro classical conditioning. J. Neurophysiol. 2009, 101:2539-2549.
    • (2009) J. Neurophysiol. , vol.101 , pp. 2539-2549
    • Zheng, Z.1    Keifer, J.2
  • 31
    • 0037312605 scopus 로고    scopus 로고
    • PKA phosphorylation of AMPA receptor subunits controls synaptic trafficking underlying plasticity
    • Esteban J.A., Shi S.H., Wilson C., Nuriya M., Huganir R.L., Malinow R. PKA phosphorylation of AMPA receptor subunits controls synaptic trafficking underlying plasticity. Nat. Neurosci. 2003, 6:136-143.
    • (2003) Nat. Neurosci. , vol.6 , pp. 136-143
    • Esteban, J.A.1    Shi, S.H.2    Wilson, C.3    Nuriya, M.4    Huganir, R.L.5    Malinow, R.6
  • 34
    • 41549089757 scopus 로고    scopus 로고
    • Receptor for advanced glycation end product-dependent activation of p38 mitogen-activated protein kinase contributes to amyloid-beta-mediated cortical synaptic dysfunction
    • Origlia N., Righi M., Capsoni S., Cattaneo A., Fang F., Stern D.M., Chen J.X., Schmidt A.M., Arancio O., Yan S.D., Domenici L. Receptor for advanced glycation end product-dependent activation of p38 mitogen-activated protein kinase contributes to amyloid-beta-mediated cortical synaptic dysfunction. J. Neurosci. 2008, 28:3521-3530.
    • (2008) J. Neurosci. , vol.28 , pp. 3521-3530
    • Origlia, N.1    Righi, M.2    Capsoni, S.3    Cattaneo, A.4    Fang, F.5    Stern, D.M.6    Chen, J.X.7    Schmidt, A.M.8    Arancio, O.9    Yan, S.D.10    Domenici, L.11
  • 36
    • 0026734317 scopus 로고
    • Three-dimensional structure of dendritic spines and synapses in rat hippocampus (CA1) at postnatal day 15 and adult ages: implications for the maturation of synaptic physiology and long-term potentiation
    • Harris K.M., Jensen F.E., Tsao B. Three-dimensional structure of dendritic spines and synapses in rat hippocampus (CA1) at postnatal day 15 and adult ages: implications for the maturation of synaptic physiology and long-term potentiation. J. Neurosci. Off. J. Soc. Neurosci. 1992, 12:2685-2705.
    • (1992) J. Neurosci. Off. J. Soc. Neurosci. , vol.12 , pp. 2685-2705
    • Harris, K.M.1    Jensen, F.E.2    Tsao, B.3
  • 37
    • 13244283230 scopus 로고    scopus 로고
    • Enhanced dephosphorylation of cAMP-dependent protein kinase by oxidation and thiol modification
    • Humphries K.M., Deal M.S., Taylor S.S. Enhanced dephosphorylation of cAMP-dependent protein kinase by oxidation and thiol modification. J. Biol. Chem. 2005, 280:2750-2758.
    • (2005) J. Biol. Chem. , vol.280 , pp. 2750-2758
    • Humphries, K.M.1    Deal, M.S.2    Taylor, S.S.3
  • 38
    • 0028304625 scopus 로고
    • Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins
    • Yan S.D., Schmidt A.M., Anderson G.M., Zhang J., Brett J., Zou Y.S., Pinsky D., Stern D. Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins. J. Biol. Chem. 1994, 269:9889-9897.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9889-9897
    • Yan, S.D.1    Schmidt, A.M.2    Anderson, G.M.3    Zhang, J.4    Brett, J.5    Zou, Y.S.6    Pinsky, D.7    Stern, D.8
  • 39
    • 84873130522 scopus 로고    scopus 로고
    • Cyclophilin d deficiency rescues axonal mitochondrial transport in Alzheimer's neurons
    • Guo L., Du H., Yan S., Wu X., McKhann G.M., Chen J.X., Yan S.S. Cyclophilin d deficiency rescues axonal mitochondrial transport in Alzheimer's neurons. PLoS One 2013, 8:e54914.
    • (2013) PLoS One , vol.8 , pp. e54914
    • Guo, L.1    Du, H.2    Yan, S.3    Wu, X.4    McKhann, G.M.5    Chen, J.X.6    Yan, S.S.7
  • 40
    • 0036792096 scopus 로고    scopus 로고
    • Amyloid beta-peptide inhibition of the PKA/CREB pathway and long-term potentiation: reversibility by drugs that enhance cAMP signaling
    • Vitolo O.V., Sant'Angelo A., Costanzo V., Battaglia F., Arancio O., Shelanski M. Amyloid beta-peptide inhibition of the PKA/CREB pathway and long-term potentiation: reversibility by drugs that enhance cAMP signaling. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:13217-13221.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 13217-13221
    • Vitolo, O.V.1    Sant'Angelo, A.2    Costanzo, V.3    Battaglia, F.4    Arancio, O.5    Shelanski, M.6
  • 41
    • 79960985348 scopus 로고    scopus 로고
    • Rapid increase in clusters of synaptophysin at onset of homosynaptic potentiation in Aplysia
    • Jin I., Udo H., Hawkins R.D. Rapid increase in clusters of synaptophysin at onset of homosynaptic potentiation in Aplysia. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:11656-11661.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 11656-11661
    • Jin, I.1    Udo, H.2    Hawkins, R.D.3
  • 42
    • 0027193793 scopus 로고
    • Basal versus apical dendritic long-term potentiation of commissural afferents to hippocampal CA1: a current-source density study
    • Kaibara T., Leung L.S. Basal versus apical dendritic long-term potentiation of commissural afferents to hippocampal CA1: a current-source density study. J. Neurosci. 1993, 13:2391-2404.
    • (1993) J. Neurosci. , vol.13 , pp. 2391-2404
    • Kaibara, T.1    Leung, L.S.2
  • 43
    • 0034928790 scopus 로고    scopus 로고
    • Morphological changes in dendritic spines associated with long-term synaptic plasticity
    • Yuste R., Bonhoeffer T. Morphological changes in dendritic spines associated with long-term synaptic plasticity. Annu. Rev. Neurosci. 2001, 24:1071-1089.
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 1071-1089
    • Yuste, R.1    Bonhoeffer, T.2
  • 44
    • 8444250688 scopus 로고    scopus 로고
    • Mitochondria-derived oxidative stress induces a heat shock protein response
    • Barrett M.J., Alones V., Wang K.X., Phan L., Swerdlow R.H. Mitochondria-derived oxidative stress induces a heat shock protein response. J. Neurosci. Res. 2004, 78:420-429.
    • (2004) J. Neurosci. Res. , vol.78 , pp. 420-429
    • Barrett, M.J.1    Alones, V.2    Wang, K.X.3    Phan, L.4    Swerdlow, R.H.5
  • 45
    • 0037087782 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress and cell death in astrocytes-requirement for stored Ca2+ and sustained opening of the permeability transition pore
    • Jacobson J., Duchen M.R. Mitochondrial oxidative stress and cell death in astrocytes-requirement for stored Ca2+ and sustained opening of the permeability transition pore. J. Cell Sci. 2002, 115:1175-1188.
    • (2002) J. Cell Sci. , vol.115 , pp. 1175-1188
    • Jacobson, J.1    Duchen, M.R.2
  • 46
    • 24644443158 scopus 로고    scopus 로고
    • Oxidative stress in mitochondria: decision to survival and death of neurons in neurodegenerative disorders
    • Naoi M., Maruyama W., Shamoto-Nagai M., Yi H., Akao Y., Tanaka M. Oxidative stress in mitochondria: decision to survival and death of neurons in neurodegenerative disorders. Mol. Neurobiol. 2005, 31:81-93.
    • (2005) Mol. Neurobiol. , vol.31 , pp. 81-93
    • Naoi, M.1    Maruyama, W.2    Shamoto-Nagai, M.3    Yi, H.4    Akao, Y.5    Tanaka, M.6
  • 47
    • 22044455180 scopus 로고    scopus 로고
    • Induction of thioredoxin and mitochondrial survival proteins mediates preconditioning-induced cardioprotection and neuroprotection
    • Chiueh C.C., Andoh T., Chock P.B. Induction of thioredoxin and mitochondrial survival proteins mediates preconditioning-induced cardioprotection and neuroprotection. Ann. N. Y. Acad. Sci. 2005, 1042:403-418.
    • (2005) Ann. N. Y. Acad. Sci. , vol.1042 , pp. 403-418
    • Chiueh, C.C.1    Andoh, T.2    Chock, P.B.3
  • 48
    • 52049115137 scopus 로고    scopus 로고
    • NMDA-induced neuroprotection in hippocampal neurons is mediated through the protein kinase A and CREB (cAMP-response element-binding protein) pathway
    • Valera E., Sanchez-Martin F.J., Ferrer-Montiel A.V., Messeguer A., Merino J.M. NMDA-induced neuroprotection in hippocampal neurons is mediated through the protein kinase A and CREB (cAMP-response element-binding protein) pathway. Neurochem. Int. 2008, 53:148-154.
    • (2008) Neurochem. Int. , vol.53 , pp. 148-154
    • Valera, E.1    Sanchez-Martin, F.J.2    Ferrer-Montiel, A.V.3    Messeguer, A.4    Merino, J.M.5
  • 49
    • 0027436057 scopus 로고
    • The participation of reactive oxygen species and protein thiols in the mechanism of mitochondrial inner membrane permeabilization by calcium plus prooxidants
    • Valle V.G., Fagian M.M., Parentoni L.S., Meinicke A.R., Vercesi A.E. The participation of reactive oxygen species and protein thiols in the mechanism of mitochondrial inner membrane permeabilization by calcium plus prooxidants. Arch. Biochem. Biophys. 1993, 307:1-7.
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 1-7
    • Valle, V.G.1    Fagian, M.M.2    Parentoni, L.S.3    Meinicke, A.R.4    Vercesi, A.E.5
  • 53
    • 0037101605 scopus 로고    scopus 로고
    • Phosphorylation of the postsynaptic density-95 (PSD-95)/discs large/zona occludens-1 binding site of stargazin regulates binding to PSD-95 and synaptic targeting of AMPA receptors
    • Chetkovich D.M., Chen L., Stocker T.J., Nicoll R.A., Bredt D.S. Phosphorylation of the postsynaptic density-95 (PSD-95)/discs large/zona occludens-1 binding site of stargazin regulates binding to PSD-95 and synaptic targeting of AMPA receptors. J. Neurosci. 2002, 22:5791-5796.
    • (2002) J. Neurosci. , vol.22 , pp. 5791-5796
    • Chetkovich, D.M.1    Chen, L.2    Stocker, T.J.3    Nicoll, R.A.4    Bredt, D.S.5
  • 55
    • 15244339852 scopus 로고    scopus 로고
    • Exocytosis and endocytosis of synaptic vesicles and functional roles of vesicle pools: lessons from the Drosophila neuromuscular junction
    • Kuromi H., Kidokoro Y. Exocytosis and endocytosis of synaptic vesicles and functional roles of vesicle pools: lessons from the Drosophila neuromuscular junction. Neuroscientist 2005, 11:138-147.
    • (2005) Neuroscientist , vol.11 , pp. 138-147
    • Kuromi, H.1    Kidokoro, Y.2
  • 56
    • 0027199055 scopus 로고
    • Identification of phosphorylation sites in the recombinant catalytic subunit of cAMP-dependent protein kinase
    • Yonemoto W., Garrod S.M., Bell S.M., Taylor S.S. Identification of phosphorylation sites in the recombinant catalytic subunit of cAMP-dependent protein kinase. J. Biol. Chem. 1993, 268:18626-18632.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18626-18632
    • Yonemoto, W.1    Garrod, S.M.2    Bell, S.M.3    Taylor, S.S.4
  • 57
    • 15744399873 scopus 로고    scopus 로고
    • Consequences of lysine 72 mutation on the phosphorylation and activation state of cAMP-dependent kinase
    • Iyer G.H., Moore M.J., Taylor S.S. Consequences of lysine 72 mutation on the phosphorylation and activation state of cAMP-dependent kinase. J. Biol. Chem. 2005, 280:8800-8807.
    • (2005) J. Biol. Chem. , vol.280 , pp. 8800-8807
    • Iyer, G.H.1    Moore, M.J.2    Taylor, S.S.3
  • 60
    • 33746233393 scopus 로고    scopus 로고
    • Identification of small-molecule inhibitors of the Abeta-ABAD interaction
    • Xie Y., Deng S., Chen Z., Yan S., Landry D.W. Identification of small-molecule inhibitors of the Abeta-ABAD interaction. Bioorg. Med. Chem. Lett. 2006, 16:4657-4660.
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 4657-4660
    • Xie, Y.1    Deng, S.2    Chen, Z.3    Yan, S.4    Landry, D.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.