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Volumn 112, Issue 32, 2015, Pages E4465-E4474

Na, K-ATPase α3 is a death target of Alzheimer patient amyloid-β assembly

(36)  Ohnishi, Takayuki a   Yanazawa, Masako c   Sasahara, Tomoya a,b   Kitamura, Yasuki c   Hiroaki, Hidekazu d   Fukazawa, Yugo e   Kii, Isao b   Nishiyama, Takashi a,b   Kakita, Akiyoshi f   Takeda, Hiroyuki g   Takeuchi, Akihide b   Arai, Yoshie a,b   Ito, Akane c,n   Komura, Hitomi a,b   Hirao, Hajime h   Satomura, Kaori a,b   Inoue, Masafumi a,b   Muramatsu, Shin Ichi i   Matsui, Ko j   Tada, Mari f   more..


Author keywords

Abnormal protein protein interaction in synapse; Computational modeling; Hyperexcitotoxicity; NMR; Protein protein interaction inhibitors

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM) ALPHA 3; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOSPHEROID; CALCIUM CHANNEL N TYPE; GLYCOGEN SYNTHASE KINASE 3BETA; MESSENGER RNA; MICRORNA; MICROTUBULE ASSOCIATED PROTEIN 2; OLIGOMER; SODIUM CALCIUM EXCHANGE PROTEIN; TAU PROTEIN; UNCLASSIFIED DRUG; ATP1A3 PROTEIN, RAT; CALCIUM; PEPTIDE; PROTEIN AGGREGATE; PROTEIN BINDING; SODIUM; SODIUM POTASSIUM ATPASE ALPHA3 SUBUNIT, HUMAN;

EID: 84938948070     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1421182112     Document Type: Article
Times cited : (121)

References (82)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 297(5580): 353-356.
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Aβ oligomers: The solution to an Alzheimer's disease conundrum?
    • Klein WL, Krafft GA, Finch CE (2001) Targeting small Aβ oligomers: The solution to an Alzheimer's disease conundrum? Trends Neurosci 24(4): 219-224.
    • (2001) Trends Neurosci , vol.24 , Issue.4 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 3
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers-A decade of discovery
    • Walsh DM, Selkoe DJ (2007) Aβ oligomers-A decade of discovery. J Neurochem 101(5): 1172-1184.
    • (2007) J Neurochem , vol.101 , Issue.5 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 4
    • 63849197629 scopus 로고    scopus 로고
    • Amyloid β-protein assembly and Alzheimer disease
    • Roychaudhuri R, Yang M, Hoshi MM, Teplow DB (2009) Amyloid β-protein assembly and Alzheimer disease. J Biol Chem 284(8): 4749-4753.
    • (2009) J Biol Chem , vol.284 , Issue.8 , pp. 4749-4753
    • Roychaudhuri, R.1    Yang, M.2    Hoshi, M.M.3    Teplow, D.B.4
  • 5
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti F, Dobson CM (2009) Amyloid formation by globular proteins under native conditions. Nat Chem Biol 5(1): 15-22.
    • (2009) Nat Chem Biol , vol.5 , Issue.1 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 6
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Aβ oligomer and Alzheimer's disease: An emperor in need of clothes
    • Benilova I, Karran E, De Strooper B (2012) The toxic Aβ oligomer and Alzheimer's disease: An emperor in need of clothes. Nat Neurosci 15(3): 349-357.
    • (2012) Nat Neurosci , vol.15 , Issue.3 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 7
    • 0034006944 scopus 로고    scopus 로고
    • β-Amyloid1-42 binds to a7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology
    • Wang HY, et al. (2000) β-Amyloid1-42 binds to a7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology. J Biol Chem 275(8): 5626-5632.
    • (2000) J Biol Chem , vol.275 , Issue.8 , pp. 5626-5632
    • Wang, H.Y.1
  • 8
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
    • Yan SD, et al. (1996) RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease. Nature 382(6593): 685-691.
    • (1996) Nature , vol.382 , Issue.6593 , pp. 685-691
    • Yan, S.D.1
  • 9
    • 78650970378 scopus 로고    scopus 로고
    • Reversing EphB2 depletion rescues cognitive functions in Alzheimer model
    • Cissé M, et al. (2011) Reversing EphB2 depletion rescues cognitive functions in Alzheimer model. Nature 469(7328): 47-52.
    • (2011) Nature , vol.469 , Issue.7328 , pp. 47-52
    • Cissé, M.1
  • 10
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
    • Laur?n J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers. Nature 457(7233): 1128-1132.
    • (2009) Nature , vol.457 , Issue.7233 , pp. 1128-1132
    • Laurén, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 11
    • 84865405744 scopus 로고    scopus 로고
    • Alzheimer's disease, β-amyloid, glutamate, NMDA receptors and memantine-searching for the connections
    • Danysz W, Parsons CG (2012) Alzheimer's disease, β-amyloid, glutamate, NMDA receptors and memantine-searching for the connections. Br J Pharmacol 167(2): 324-352.
    • (2012) Br J Pharmacol , vol.167 , Issue.2 , pp. 324-352
    • Danysz, W.1    Parsons, C.G.2
  • 12
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • Shankar GM, et al. (2008) Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med 14(8): 837-842.
    • (2008) Nat Med , vol.14 , Issue.8 , pp. 837-842
    • Shankar, G.M.1
  • 13
    • 78049326855 scopus 로고    scopus 로고
    • Amyloid β-protein dimers rapidly form stable synaptotoxic protofibrils
    • O'Nuallain B, et al. (2010) Amyloid β-protein dimers rapidly form stable synaptotoxic protofibrils. J Neurosci 30(43): 14411-14419.
    • (2010) J Neurosci , vol.30 , Issue.43 , pp. 14411-14419
    • O'Nuallain, B.1
  • 14
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-β protein assembly in the brain impairs memory
    • Lesn? S, et al. (2006) A specific amyloid-β protein assembly in the brain impairs memory. Nature 440(7082): 352-357.
    • (2006) Nature , vol.440 , Issue.7082 , pp. 352-357
    • Lesné, S.1
  • 15
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins
    • Lambert MP, et al. (1998) Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci USA 95(11): 6448-6453.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.11 , pp. 6448-6453
    • Lambert, M.P.1
  • 16
    • 33846633336 scopus 로고    scopus 로고
    • Aβ oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease
    • Lacor PN, et al. (2007) Aβ oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease. J Neurosci 27(4): 796-807.
    • (2007) J Neurosci , vol.27 , Issue.4 , pp. 796-807
    • Lacor, P.N.1
  • 17
    • 84856414697 scopus 로고    scopus 로고
    • The Alzheimer's Disease Neuroimaging Initiative: A review of papers published since its inception
    • Weiner MW, et al. (2012) The Alzheimer's Disease Neuroimaging Initiative: A review of papers published since its inception. Alzheimer Dement 8(1, Suppl): S1-S68.
    • (2012) Alzheimer Dement , vol.8 , Issue.1 , pp. S1-S68
    • Weiner, M.W.1
  • 18
    • 0037975676 scopus 로고    scopus 로고
    • Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β
    • Hoshi M, et al. (2003) Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β. Proc Natl Acad Sci USA 100(11): 6370-6375.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.11 , pp. 6370-6375
    • Hoshi, M.1
  • 19
    • 70450257636 scopus 로고    scopus 로고
    • Isolation and characterization of patient-derived, toxic, high mass amyloid β-protein (Abeta) assembly from Alzheimer disease brains
    • Noguchi A, et al. (2009) Isolation and characterization of patient-derived, toxic, high mass amyloid β-protein (Abeta) assembly from Alzheimer disease brains. J Biol Chem 284(47): 32895-32905.
    • (2009) J Biol Chem , vol.284 , Issue.47 , pp. 32895-32905
    • Noguchi, A.1
  • 20
    • 79953191504 scopus 로고    scopus 로고
    • Two distinct amyloid β-protein (Aβ) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology, and toxicity analyses
    • Matsumura S, et al. (2011) Two distinct amyloid β-protein (Aβ) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology, and toxicity analyses. J Biol Chem 286(13): 11555-11562.
    • (2011) J Biol Chem , vol.286 , Issue.13 , pp. 11555-11562
    • Matsumura, S.1
  • 21
    • 84860334015 scopus 로고    scopus 로고
    • Inhibitory interneuron deficit links altered network activity and cognitive dysfunction in Alzheimer model
    • Verret L, et al. (2012) Inhibitory interneuron deficit links altered network activity and cognitive dysfunction in Alzheimer model. Cell 149(3): 708-721.
    • (2012) Cell , vol.149 , Issue.3 , pp. 708-721
    • Verret, L.1
  • 22
    • 0031758268 scopus 로고    scopus 로고
    • Isozymes of the Na-K-ATPase: Heterogeneity in structure, diversity in function
    • Blanco G, Mercer RW (1998) Isozymes of the Na-K-ATPase: Heterogeneity in structure, diversity in function. Am J Physiol 275(5 Pt 2): F633-F650.
    • (1998) Am J Physiol , vol.275 , Issue.5 , pp. F633-F650
    • Blanco, G.1    Mercer, R.W.2
  • 23
    • 52049098700 scopus 로고    scopus 로고
    • Calcium channel regulation and presynaptic plasticity
    • Catterall WA, Few AP (2008) Calcium channel regulation and presynaptic plasticity. Neuron 59(6): 882-901.
    • (2008) Neuron , vol.59 , Issue.6 , pp. 882-901
    • Catterall, W.A.1    Few, A.P.2
  • 24
    • 0029737421 scopus 로고    scopus 로고
    • Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3 β and cyclindependent kinase 5, a component of TPK II
    • Yamaguchi H, et al. (1996) Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3 β and cyclindependent kinase 5, a component of TPK II. Acta Neuropathol 92(3): 232-241.
    • (1996) Acta Neuropathol , vol.92 , Issue.3 , pp. 232-241
    • Yamaguchi, H.1
  • 25
    • 0036948067 scopus 로고    scopus 로고
    • Apoptotic volume decrease and the incredible shrinking cell
    • Bortner CD, Cidlowski JA (2002) Apoptotic volume decrease and the incredible shrinking cell. Cell Death Differ 9(12): 1307-1310.
    • (2002) Cell Death Differ , vol.9 , Issue.12 , pp. 1307-1310
    • Bortner, C.D.1    Cidlowski, J.A.2
  • 26
    • 0028334076 scopus 로고
    • Ouabain binding kinetics of the rat alpha two and alpha three isoforms of the sodium-potassium adenosine triphosphate
    • O'Brien WJ, Lingrel JB, Wallick ET (1994) Ouabain binding kinetics of the rat alpha two and alpha three isoforms of the sodium-potassium adenosine triphosphate. Arch Biochem Biophys 310(1): 32-39.
    • (1994) Arch Biochem Biophys , vol.310 , Issue.1 , pp. 32-39
    • O'Brien, W.J.1    Lingrel, J.B.2    Wallick, E.T.3
  • 27
    • 78650254882 scopus 로고    scopus 로고
    • Distribution of Na/K-ATPase alpha 3 isoform, a sodiumpotassium P-type pump associated with rapid-onset of dystonia parkinsonism (RDP) in the adult mouse brain
    • Bøttger P, et al. (2011) Distribution of Na/K-ATPase alpha 3 isoform, a sodiumpotassium P-type pump associated with rapid-onset of dystonia parkinsonism (RDP) in the adult mouse brain. J Comp Neurol 519(2): 376-404.
    • (2011) J Comp Neurol , vol.519 , Issue.2 , pp. 376-404
    • Bøttger, P.1
  • 28
    • 0031305777 scopus 로고    scopus 로고
    • Na,K-ATPase mRNA levels and plaque load in Alzheimer's disease
    • Chauhan NB, Lee JM, Siegel GJ (1997) Na,K-ATPase mRNA levels and plaque load in Alzheimer's disease. J Mol Neurosci 9(3): 151-166.
    • (1997) J Mol Neurosci , vol.9 , Issue.3 , pp. 151-166
    • Chauhan, N.B.1    Lee, J.M.2    Siegel, G.J.3
  • 29
    • 64549140676 scopus 로고    scopus 로고
    • Structural characterization of a soluble amyloid β-peptide oligomer
    • Yu L, et al. (2009) Structural characterization of a soluble amyloid β-peptide oligomer. Biochemistry 48(9): 1870-1877.
    • (2009) Biochemistry , vol.48 , Issue.9 , pp. 1870-1877
    • Yu, L.1
  • 30
    • 79953250721 scopus 로고    scopus 로고
    • Transient formation of intermediate conformational states of amyloid-β peptide revealed by heteronuclear magnetic resonance spectroscopy
    • Yamaguchi T, Matsuzaki K, Hoshino M (2011) Transient formation of intermediate conformational states of amyloid-β peptide revealed by heteronuclear magnetic resonance spectroscopy. FEBS Lett 585(7): 1097-1102.
    • (2011) FEBS Lett , vol.585 , Issue.7 , pp. 1097-1102
    • Yamaguchi, T.1    Matsuzaki, K.2    Hoshino, M.3
  • 31
    • 84930205771 scopus 로고    scopus 로고
    • Structural insight into an Alzheimer's brain-derived spherical assembly of amyloid β by solid-state NMR
    • Parthasarathy S, et al. (2015) Structural insight into an Alzheimer's brain-derived spherical assembly of amyloid β by solid-state NMR. J Am Chem Soc 137(20): 6480-6483.
    • (2015) J Am Chem Soc , vol.137 , Issue.20 , pp. 6480-6483
    • Parthasarathy, S.1
  • 32
    • 37249088547 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump
    • Morth JP, et al. (2007) Crystal structure of the sodium-potassium pump. Nature 450(7172): 1043-1049.
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1043-1049
    • Morth, J.P.1
  • 33
    • 0024401763 scopus 로고
    • Rapid decrease of high affinity ouabain binding sites in hippocampal CA1 region following short-term global cerebral ischemia in rat
    • Pylova SI, Majkowska J, Hilgier W, Kapu-sci-nski A, Albrecht J (1989) Rapid decrease of high affinity ouabain binding sites in hippocampal CA1 region following short-term global cerebral ischemia in rat. Brain Res 490(1): 170-173.
    • (1989) Brain Res , vol.490 , Issue.1 , pp. 170-173
    • Pylova, S.I.1    Majkowska, J.2    Hilgier, W.3    Kapu-sci-nski, A.4    Albrecht, J.5
  • 34
    • 33745029511 scopus 로고    scopus 로고
    • Repeated electroconvulsive shock induces changes in high-affinity [3H]-ouabain binding to rat striatal membranes
    • Bignotto M, Benedito MA (2006) Repeated electroconvulsive shock induces changes in high-affinity [3H]-ouabain binding to rat striatal membranes. Neurochem Res 31(4): 515-521.
    • (2006) Neurochem Res , vol.31 , Issue.4 , pp. 515-521
    • Bignotto, M.1    Benedito, M.A.2
  • 35
    • 0024320720 scopus 로고
    • +-ATPase is the aβ-protomer. Determination by low-angle laser light scattering photometry coupled with high-performance gel chromatography for substantially simultaneous measurement of ATPase activity and molecular weight
    • +-ATPase is the aβ-protomer. Determination by low-angle laser light scattering photometry coupled with high-performance gel chromatography for substantially simultaneous measurement of ATPase activity and molecular weight. Biochim Biophys Acta 983(2): 217-229.
    • (1989) Biochim Biophys Acta , vol.983 , Issue.2 , pp. 217-229
    • Hayashi, Y.1    Mimura, K.2    Matsui, H.3    Takagi, T.4
  • 37
    • 77954952703 scopus 로고    scopus 로고
    • Comments regarding "On the Nature Of Science"
    • Courtney A, Courtney M (2008) Comments regarding "On the Nature Of Science". Physics in Canada 64(3): 7-8.
    • (2008) Physics in Canada , vol.64 , Issue.3 , pp. 7-8
    • Courtney, A.1    Courtney, M.2
  • 38
    • 0025699745 scopus 로고
    • 2+-ATPase and some soluble enzymes related to energy metabolism in brains of patients with Alzheimer's disease
    • 2+-ATPase and some soluble enzymes related to energy metabolism in brains of patients with Alzheimer's disease. Neurosci Lett 112(2-3): 338-342.
    • (1990) Neurosci Lett , vol.112 , Issue.2-3 , pp. 338-342
    • Liguri, G.1
  • 39
    • 0032475514 scopus 로고    scopus 로고
    • +-ATPase activities in Alzheimer's disease brains
    • +-ATPase activities in Alzheimer's disease brains. Neurosci Lett 254(3): 141-144.
    • (1998) Neurosci Lett , vol.254 , Issue.3 , pp. 141-144
    • Hattori, N.1
  • 41
    • 26444552965 scopus 로고    scopus 로고
    • + ATPase by amyloid in APP+PS1 transgenic mice
    • + ATPase by amyloid in APP+PS1 transgenic mice. BMC Neurosci 6: 7.
    • (2005) BMC Neurosci , vol.6 , pp. 7
    • Dickey, C.A.1
  • 43
    • 84911468890 scopus 로고    scopus 로고
    • Alzheimer's therapeutics targeting amyloid beta 1-42 oligomers II: Sigma-2/PGRMC1 receptors mediate Abeta 42 oligomer binding and synaptotoxicity
    • Izzo NJ, et al. (2014) Alzheimer's therapeutics targeting amyloid beta 1-42 oligomers II: Sigma-2/PGRMC1 receptors mediate Abeta 42 oligomer binding and synaptotoxicity. PLoS One 9(11): E111899.
    • (2014) PLoS One , vol.9 , Issue.11 , pp. e111899
    • Izzo, N.J.1
  • 44
    • 52249115856 scopus 로고    scopus 로고
    • Clusters of hyperactive neurons near amyloid plaques in a mouse model of Alzheimer's disease
    • Busche MA, et al. (2008) Clusters of hyperactive neurons near amyloid plaques in a mouse model of Alzheimer's disease. Science 321(5896): 1686-1689.
    • (2008) Science , vol.321 , Issue.5896 , pp. 1686-1689
    • Busche, M.A.1
  • 45
    • 82555174628 scopus 로고    scopus 로고
    • Hippocampal hyperactivation associated with cortical thinning in Alzheimer's disease signature regions in non-demented elderly adults
    • Putcha D, et al. (2011) Hippocampal hyperactivation associated with cortical thinning in Alzheimer's disease signature regions in non-demented elderly adults. J Neurosci 31(48): 17680-17688.
    • (2011) J Neurosci , vol.31 , Issue.48 , pp. 17680-17688
    • Putcha, D.1
  • 46
    • 0025954861 scopus 로고
    • Immunofluorescent localization of three Na,K-ATPase isozymes in the rat central nervous system: Both neurons and glia can express more than one Na,K-ATPase
    • McGrail KM, Phillips JM, Sweadner KJ (1991) Immunofluorescent localization of three Na,K-ATPase isozymes in the rat central nervous system: Both neurons and glia can express more than one Na,K-ATPase. J Neurosci 11(2): 381-391.
    • (1991) J Neurosci , vol.11 , Issue.2 , pp. 381-391
    • McGrail, K.M.1    Phillips, J.M.2    Sweadner, K.J.3
  • 47
    • 0026669417 scopus 로고
    • Isoforms of the Na,K-ATPase are present in both axons and dendrites of hippocampal neurons in culture
    • Pietrini G, Matteoli M, Banker G, Caplan MJ (1992) Isoforms of the Na,K-ATPase are present in both axons and dendrites of hippocampal neurons in culture. Proc Natl Acad Sci USA 89(18): 8414-8418.
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.18 , pp. 8414-8418
    • Pietrini, G.1    Matteoli, M.2    Banker, G.3    Caplan, M.J.4
  • 48
    • 84873828994 scopus 로고    scopus 로고
    • A specific and essential role for Na,K-ATPase a3 in neurons coexpressing a1 and a3
    • Azarias G, et al. (2013) A specific and essential role for Na,K-ATPase a3 in neurons coexpressing a1 and a3. J Biol Chem 288(4): 2734-2743.
    • (2013) J Biol Chem , vol.288 , Issue.4 , pp. 2734-2743
    • Azarias, G.1
  • 49
    • 84855352466 scopus 로고    scopus 로고
    • +-ATPase reduces readily releasable pool size at the avian end-bulb of Held synapse
    • +-ATPase reduces readily releasable pool size at the avian end-bulb of Held synapse. Neurosci Res 72(2): 117-128.
    • (2012) Neurosci Res , vol.72 , Issue.2 , pp. 117-128
    • Taruno, A.1    Ohmori, H.2    Kuba, H.3
  • 51
    • 0034595890 scopus 로고    scopus 로고
    • Immunohistochemical study on the distribution of the voltage-gated calcium channel a1B subunit in the mature rat brain
    • Chung YH, Shin C, Park KH, Cha CI (2000) Immunohistochemical study on the distribution of the voltage-gated calcium channel a1B subunit in the mature rat brain. Brain Res 866(1-2): 274-280.
    • (2000) Brain Res , vol.866 , Issue.1-2 , pp. 274-280
    • Chung, Y.H.1    Shin, C.2    Park, K.H.3    Cha, C.I.4
  • 52
    • 0037480114 scopus 로고    scopus 로고
    • Progressive degeneration of nonphosphorylated neurofilament protein-enriched pyramidal neurons predicts cognitive impairment in Alzheimer's disease: Stereologic analysis of prefrontal cortex area 9
    • Bussière T, et al. (2003) Progressive degeneration of nonphosphorylated neurofilament protein-enriched pyramidal neurons predicts cognitive impairment in Alzheimer's disease: Stereologic analysis of prefrontal cortex area 9. J Comp Neurol 463(3): 281-302.
    • (2003) J Comp Neurol , vol.463 , Issue.3 , pp. 281-302
    • Bussière, T.1
  • 53
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Gong Y, et al. (2003) Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc Natl Acad Sci USA 100(18): 10417-10422.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.18 , pp. 10417-10422
    • Gong, Y.1
  • 54
    • 84898406777 scopus 로고    scopus 로고
    • Distinct neurological disorders with ATP1A3 mutations
    • Heinzen EL, et al.; ATP1A3 Working Group (2014) Distinct neurological disorders with ATP1A3 mutations. Lancet Neurol 13(5): 503-514.
    • (2014) Lancet Neurol , vol.13 , Issue.5 , pp. 503-514
    • Heinzen, E.L.1
  • 55
    • 84883759456 scopus 로고    scopus 로고
    • Seizures and epileptiform activity in the early stages of Alzheimer disease
    • Vossel KA, et al. (2013) Seizures and epileptiform activity in the early stages of Alzheimer disease. JAMA Neurol 70(9): 1158-1166.
    • (2013) JAMA Neurol , vol.70 , Issue.9 , pp. 1158-1166
    • Vossel, K.A.1
  • 57
    • 84867645474 scopus 로고    scopus 로고
    • Levetiracetam suppresses neuronal network dysfunction and reverses synaptic and cognitive deficits in an Alzheimer's disease model
    • Sanchez PE, et al. (2012) Levetiracetam suppresses neuronal network dysfunction and reverses synaptic and cognitive deficits in an Alzheimer's disease model. Proc Natl Acad Sci USA 109(42): E2895-E2903.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.42 , pp. E2895-E2903
    • Sanchez, P.E.1
  • 58
    • 17444380877 scopus 로고    scopus 로고
    • Na,K-ATPase mutations in familial hemiplegic migraine lead to functional inactivation
    • Koenderink JB, et al. (2005) Na,K-ATPase mutations in familial hemiplegic migraine lead to functional inactivation. Biochim Biophys Acta 1669(1): 61-68.
    • (2005) Biochim Biophys Acta , vol.1669 , Issue.1 , pp. 61-68
    • Koenderink, J.B.1
  • 60
    • 80054858598 scopus 로고    scopus 로고
    • A simplified recipe for assigning amide NMR signals using combinatorial 14N amino acid inverse-labeling
    • Hiroaki H, Umetsu Y, Nabeshima Y, Hoshi M, Kohda D (2011) A simplified recipe for assigning amide NMR signals using combinatorial 14N amino acid inverse-labeling. J Struct Funct Genomics 12(3): 167-174.
    • (2011) J Struct Funct Genomics , vol.12 , Issue.3 , pp. 167-174
    • Hiroaki, H.1    Umetsu, Y.2    Nabeshima, Y.3    Hoshi, M.4    Kohda, D.5
  • 61
    • 0026589405 scopus 로고
    • +-adenosine triphosphatase is active and exhibits high ouabain affinity when expressed in transfected fibroblasts
    • +-adenosine triphosphatase is active and exhibits high ouabain affinity when expressed in transfected fibroblasts. FEBS Lett 303(2-3): 147-153.
    • (1992) FEBS Lett , vol.303 , Issue.2-3 , pp. 147-153
    • Kolansky, D.M.1    Brines, M.L.2    Gilmore-Hebert, M.3    Benz, E.J.4
  • 62
    • 0027450805 scopus 로고
    • Functional expression of the a2 and a3 isoforms of the Na,K-ATPase in baculovirus-infected insect cells
    • Blanco G, Xie ZJ, Mercer RW (1993) Functional expression of the a2 and a3 isoforms of the Na,K-ATPase in baculovirus-infected insect cells. Proc Natl Acad Sci USA 90(5): 1824-1828.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.5 , pp. 1824-1828
    • Blanco, G.1    Xie, Z.J.2    Mercer, R.W.3
  • 63
    • 0028984539 scopus 로고
    • Comparison of the enzymatic properties of the Na,K-ATPase a3β1 and a3β2 isozymes
    • Blanco G, Sanchez G, Mercer RW (1995) Comparison of the enzymatic properties of the Na,K-ATPase a3β1 and a3β2 isozymes. Biochemistry 34(31): 9897-9903.
    • (1995) Biochemistry , vol.34 , Issue.31 , pp. 9897-9903
    • Blanco, G.1    Sánchez, G.2    Mercer, R.W.3
  • 65
    • 79953802067 scopus 로고    scopus 로고
    • Production and partial purification of membrane proteins using a liposome-supplemented wheat cell-free translation system
    • Nozawa A, et al. (2011) Production and partial purification of membrane proteins using a liposome-supplemented wheat cell-free translation system. BMC Biotechnol 11: 35.
    • (2011) BMC Biotechnol , vol.11 , pp. 35
    • Nozawa, A.1
  • 66
    • 57349119057 scopus 로고    scopus 로고
    • Efficient cell-free production of olfactory receptors: Detergent optimization, structure, and ligand binding analyses
    • Kaiser L, et al. (2008) Efficient cell-free production of olfactory receptors: Detergent optimization, structure, and ligand binding analyses. Proc Natl Acad Sci USA 105(41): 15726-15731.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.41 , pp. 15726-15731
    • Kaiser, L.1
  • 67
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182(2): 319-326.
    • (1989) Anal Biochem , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 68
    • 33749150163 scopus 로고    scopus 로고
    • Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry
    • Braak H, Alafuzoff I, Arzberger T, Kretzschmar H, Del Tredici K (2006) Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry. Acta Neuropathol 112(4): 389-404.
    • (2006) Acta Neuropathol , vol.112 , Issue.4 , pp. 389-404
    • Braak, H.1    Alafuzoff, I.2    Arzberger, T.3    Kretzschmar, H.4    Del Tredici, K.5
  • 69
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, et al. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3): 277-293.
    • (1995) J Biomol NMR , vol.6 , Issue.3 , pp. 277-293
    • Delaglio, F.1
  • 70
    • 33746335362 scopus 로고    scopus 로고
    • NMR reveals anomalous copper(II) binding to the amyloid Aβ peptide of Alzheimer's disease
    • Hou L, Zagorski MG (2006) NMR reveals anomalous copper(II) binding to the amyloid Aβ peptide of Alzheimer's disease. J Am Chem Soc 128(29): 9260-9261.
    • (2006) J Am Chem Soc , vol.128 , Issue.29 , pp. 9260-9261
    • Hou, L.1    Zagorski, M.G.2
  • 72
    • 79953220788 scopus 로고    scopus 로고
    • 2+-induced permeability transition in brain mitochondria, with relation to the bioenergetic state
    • 2+-induced permeability transition in brain mitochondria, with relation to the bioenergetic state. J Biol Chem 286(8): 6345-6353.
    • (2011) J Biol Chem , vol.286 , Issue.8 , pp. 6345-6353
    • Doczi, J.1
  • 73
    • 84859723641 scopus 로고    scopus 로고
    • A multimodal RAGE-specific inhibitor reduces amyloid β-mediated brain disorder in a mouse model of Alzheimer disease
    • Deane R, et al. (2012) A multimodal RAGE-specific inhibitor reduces amyloid β-mediated brain disorder in a mouse model of Alzheimer disease. J Clin Invest 122(4): 1377-1392.
    • (2012) J Clin Invest , vol.122 , Issue.4 , pp. 1377-1392
    • Deane, R.1
  • 74
    • 84928490153 scopus 로고    scopus 로고
    • Chemical cross-linking/mass spectrometry maps the amyloid β peptide binding region on both apolipoprotein E domains
    • Deroo S, et al. (2015) Chemical cross-linking/mass spectrometry maps the amyloid β peptide binding region on both apolipoprotein E domains. ACS Chem Biol 10(4): 1010-1016.
    • (2015) ACS Chem Biol , vol.10 , Issue.4 , pp. 1010-1016
    • Deroo, S.1
  • 75
    • 0033569717 scopus 로고    scopus 로고
    • Higher avidity binding of apolipoprotein (E-AII) complex than of apolipoprotein E monomer to β-amyloid
    • Yamauchi K, et al. (1999) Higher avidity binding of apolipoprotein (E-AII) complex than of apolipoprotein E monomer to β-amyloid. J Neurosci Res 58(2): 301-307.
    • (1999) J Neurosci Res , vol.58 , Issue.2 , pp. 301-307
    • Yamauchi, K.1
  • 76
    • 23044445669 scopus 로고    scopus 로고
    • Regulation of NMDA receptor trafficking by amyloid-β
    • Snyder EM, et al. (2005) Regulation of NMDA receptor trafficking by amyloid-β. Nat Neurosci 8(8): 1051-1058.
    • (2005) Nat Neurosci , vol.8 , Issue.8 , pp. 1051-1058
    • Snyder, E.M.1
  • 77
    • 84866065959 scopus 로고    scopus 로고
    • Alzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons
    • Um JW, et al. (2012) Alzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons. Nat Neurosci 15(9): 1227-1235.
    • (2012) Nat Neurosci , vol.15 , Issue.9 , pp. 1227-1235
    • Um, J.W.1
  • 78
    • 84909578703 scopus 로고    scopus 로고
    • Apolipoprotein E: Structure and function in lipid metabolism, neurobiology, and Alzheimer's diseases
    • Huang Y, Mahley RW (2014) Apolipoprotein E: Structure and function in lipid metabolism, neurobiology, and Alzheimer's diseases. Neurobiol Dis 72(Pt A): 3-12.
    • (2014) Neurobiol Dis , vol.72 , pp. 3-12
    • Huang, Y.1    Mahley, R.W.2
  • 79
    • 84874585213 scopus 로고    scopus 로고
    • Amyloid-β induced signaling by cellular prion protein and Fyn kinase in Alzheimer disease
    • Um JW, Strittmatter SM (2013) Amyloid-β induced signaling by cellular prion protein and Fyn kinase in Alzheimer disease. Prion 7(1): 37-41.
    • (2013) Prion , vol.7 , Issue.1 , pp. 37-41
    • Um, J.W.1    Strittmatter, S.M.2
  • 80
    • 84866601293 scopus 로고    scopus 로고
    • RAGE is a key cellular target for Abeta-induced perturbation in Alzheimer's disease
    • Yan SS, et al. (2012) RAGE is a key cellular target for Abeta-induced perturbation in Alzheimer's disease. Front Biosci (Schol Ed) 4(4): 240-250.
    • (2012) Front Biosci (Schol Ed) , vol.4 , Issue.4 , pp. 240-250
    • Yan, S.S.1
  • 81
    • 80052033738 scopus 로고    scopus 로고
    • Research update: Alpha7 nicotinic acetylcholine receptor mechanisms in Alzheimer's disease
    • Parri HR, Hernandez CM, Dineley KT (2011) Research update: Alpha7 nicotinic acetylcholine receptor mechanisms in Alzheimer's disease. Biochem Pharmacol 82(8): 931-942.
    • (2011) Biochem Pharmacol , vol.82 , Issue.8 , pp. 931-942
    • Parri, H.R.1    Hernandez, C.M.2    Dineley, K.T.3
  • 82
    • 78650010366 scopus 로고    scopus 로고
    • N-methyl-D-aspartate receptors are required for synaptic targeting of Alzheimer's toxic amyloid-β peptide oligomers
    • Decker H et al. (2010) N-methyl-D-aspartate receptors are required for synaptic targeting of Alzheimer's toxic amyloid-β peptide oligomers. J Neurochem 115(6): 1520-1529.
    • (2010) J Neurochem , vol.115 , Issue.6 , pp. 1520-1529
    • Decker, H.1


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