메뉴 건너뛰기




Volumn 78, Issue 1, 2013, Pages 94-108

The CAMKK2-AMPK Kinase Pathway Mediates the Synaptotoxic Effects of Aβ Oligomers through Tau Phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALCIUM ION; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE ALPHA 1; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE ALPHA 2; METFORMIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 84876078566     PISSN: 08966273     EISSN: 10974199     Source Type: Journal    
DOI: 10.1016/j.neuron.2013.02.003     Document Type: Article
Times cited : (289)

References (82)
  • 5
    • 50249135503 scopus 로고    scopus 로고
    • Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease
    • Bezprozvanny I., Mattson M.P. Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease. Trends Neurosci. 2008, 31:454-463.
    • (2008) Trends Neurosci. , vol.31 , pp. 454-463
    • Bezprozvanny, I.1    Mattson, M.P.2
  • 6
    • 0027338266 scopus 로고
    • Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding
    • Biernat J., Gustke N., Drewes G., Mandelkow E.M., Mandelkow E. Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding. Neuron 1993, 11:153-163.
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 7
    • 47249125446 scopus 로고    scopus 로고
    • Investigating the regulation of brain-specific kinases 1 and 2 by phosphorylation
    • Bright N.J., Carling D., Thornton C. Investigating the regulation of brain-specific kinases 1 and 2 by phosphorylation. J. Biol. Chem. 2008, 283:14946-14954.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14946-14954
    • Bright, N.J.1    Carling, D.2    Thornton, C.3
  • 8
    • 57649203362 scopus 로고    scopus 로고
    • Dissociation of tau toxicity and phosphorylation: role of GSK-3beta, MARK and Cdk5 in a Drosophila model
    • Chatterjee S., Sang T.K., Lawless G.M., Jackson G.R. Dissociation of tau toxicity and phosphorylation: role of GSK-3beta, MARK and Cdk5 in a Drosophila model. Hum. Mol. Genet. 2009, 18:164-177.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 164-177
    • Chatterjee, S.1    Sang, T.K.2    Lawless, G.M.3    Jackson, G.R.4
  • 9
    • 62649115914 scopus 로고    scopus 로고
    • Antidiabetic drug metformin (GlucophageR) increases biogenesis of Alzheimer's amyloid peptides via up-regulating BACE1 transcription
    • Chen Y., Zhou K., Wang R., Liu Y., Kwak Y.D., Ma T., Thompson R.C., Zhao Y., Smith L., Gasparini L., et al. Antidiabetic drug metformin (GlucophageR) increases biogenesis of Alzheimer's amyloid peptides via up-regulating BACE1 transcription. Proc. Natl. Acad. Sci. USA 2009, 106:3907-3912.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3907-3912
    • Chen, Y.1    Zhou, K.2    Wang, R.3    Liu, Y.4    Kwak, Y.D.5    Ma, T.6    Thompson, R.C.7    Zhao, Y.8    Smith, L.9    Gasparini, L.10
  • 11
    • 0345276572 scopus 로고    scopus 로고
    • Synaptic slaughter in Alzheimer's disease
    • Coleman P.D., Yao P.J. Synaptic slaughter in Alzheimer's disease. Neurobiol. Aging 2003, 24:1023-1027.
    • (2003) Neurobiol. Aging , vol.24 , pp. 1023-1027
    • Coleman, P.D.1    Yao, P.J.2
  • 12
    • 0034803430 scopus 로고    scopus 로고
    • AMP-activated protein kinase is highly expressed in neurons in the developing rat brain and promotes neuronal survival following glucose deprivation
    • Culmsee C., Monnig J., Kemp B.E., Mattson M.P. AMP-activated protein kinase is highly expressed in neurons in the developing rat brain and promotes neuronal survival following glucose deprivation. J. Mol. Neurosci. 2001, 17:45-58.
    • (2001) J. Mol. Neurosci. , vol.17 , pp. 45-58
    • Culmsee, C.1    Monnig, J.2    Kemp, B.E.3    Mattson, M.P.4
  • 13
    • 0023106967 scopus 로고
    • A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with Alzheimer's disease
    • Davies C.A., Mann D.M., Sumpter P.Q., Yates P.O. A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with Alzheimer's disease. J. Neurol. Sci. 1987, 78:151-164.
    • (1987) J. Neurol. Sci. , vol.78 , pp. 151-164
    • Davies, C.A.1    Mann, D.M.2    Sumpter, P.Q.3    Yates, P.O.4
  • 14
    • 34249672242 scopus 로고    scopus 로고
    • Abeta oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • De Felice F.G., Velasco P.T., Lambert M.P., Viola K., Fernandez S.J., Ferreira S.T., Klein W.L. Abeta oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J. Biol. Chem. 2007, 282:11590-11601.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3    Viola, K.4    Fernandez, S.J.5    Ferreira, S.T.6    Klein, W.L.7
  • 16
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro A., Mina E., Kayed R., Milton S.C., Parker I., Glabe C.G. Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J. Biol. Chem. 2005, 280:17294-17300.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 17
    • 78149449524 scopus 로고    scopus 로고
    • Regulation of synaptic connectivity by glia
    • Eroglu C., Barres B.A. Regulation of synaptic connectivity by glia. Nature 2010, 468:223-231.
    • (2010) Nature , vol.468 , pp. 223-231
    • Eroglu, C.1    Barres, B.A.2
  • 18
    • 76549089547 scopus 로고    scopus 로고
    • Calmodulin-dependent protein kinase kinase-beta activates AMPK without forming a stable complex: synergistic effects of Ca2+ and AMP
    • Fogarty S., Hawley S.A., Green K.A., Saner N., Mustard K.J., Hardie D.G. Calmodulin-dependent protein kinase kinase-beta activates AMPK without forming a stable complex: synergistic effects of Ca2+ and AMP. Biochem. J. 2010, 426:109-118.
    • (2010) Biochem. J. , vol.426 , pp. 109-118
    • Fogarty, S.1    Hawley, S.A.2    Green, K.A.3    Saner, N.4    Mustard, K.J.5    Hardie, D.G.6
  • 20
    • 80053254762 scopus 로고    scopus 로고
    • Characterization of the CaMKKβ-AMPK signaling complex
    • Green M.F., Anderson K.A., Means A.R. Characterization of the CaMKKβ-AMPK signaling complex. Cell. Signal. 2011, 23:2005-2012.
    • (2011) Cell. Signal. , vol.23 , pp. 2005-2012
    • Green, M.F.1    Anderson, K.A.2    Means, A.R.3
  • 21
    • 33748118458 scopus 로고    scopus 로고
    • Neither LKB1 nor AMPK are the direct targets of metformin
    • Hardie D.G. Neither LKB1 nor AMPK are the direct targets of metformin. Gastroenterology 2006, 131:973.
    • (2006) Gastroenterology , vol.131 , pp. 973
    • Hardie, D.G.1
  • 22
    • 34648828532 scopus 로고    scopus 로고
    • AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy
    • Hardie D.G. AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy. Nat. Rev. Mol. Cell Biol. 2007, 8:774-785.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 774-785
    • Hardie, D.G.1
  • 23
    • 0036759508 scopus 로고    scopus 로고
    • Diabetes mellitus is a risk factor for vascular dementia, but not for Alzheimer's disease: a population-based study of the oldest old
    • Hassing L.B., Johansson B., Nilsson S.E., Berg S., Pedersen N.L., Gatz M., McClearn G. Diabetes mellitus is a risk factor for vascular dementia, but not for Alzheimer's disease: a population-based study of the oldest old. Int. Psychogeriatr. 2002, 14:239-248.
    • (2002) Int. Psychogeriatr. , vol.14 , pp. 239-248
    • Hassing, L.B.1    Johansson, B.2    Nilsson, S.E.3    Berg, S.4    Pedersen, N.L.5    Gatz, M.6    McClearn, G.7
  • 24
    • 0345107247 scopus 로고    scopus 로고
    • Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade
    • Hawley S.A., Boudeau J., Reid J.L., Mustard K.J., Udd L., Mäkelä T.P., Alessi D.R., Hardie D.G. Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade. J. Biol. 2003, 2:28.
    • (2003) J. Biol. , vol.2 , pp. 28
    • Hawley, S.A.1    Boudeau, J.2    Reid, J.L.3    Mustard, K.J.4    Udd, L.5    Mäkelä, T.P.6    Alessi, D.R.7    Hardie, D.G.8
  • 29
    • 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
  • 31
    • 23844471263 scopus 로고    scopus 로고
    • The Ca2+/calmodulin-dependent protein kinase kinases are AMP-activated protein kinase kinases
    • Hurley R.L., Anderson K.A., Franzone J.M., Kemp B.E., Means A.R., Witters L.A. The Ca2+/calmodulin-dependent protein kinase kinases are AMP-activated protein kinase kinases. J. Biol. Chem. 2005, 280:29060-29066.
    • (2005) J. Biol. Chem. , vol.280 , pp. 29060-29066
    • Hurley, R.L.1    Anderson, K.A.2    Franzone, J.M.3    Kemp, B.E.4    Means, A.R.5    Witters, L.A.6
  • 32
    • 77957254409 scopus 로고    scopus 로고
    • Tau Ser262 phosphorylation is critical for Abeta42-induced tau toxicity in a transgenic Drosophila model of Alzheimer's disease
    • Iijima K., Gatt A., Iijima-Ando K. Tau Ser262 phosphorylation is critical for Abeta42-induced tau toxicity in a transgenic Drosophila model of Alzheimer's disease. Hum. Mol. Genet. 2010, 19:2947-2957.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 2947-2957
    • Iijima, K.1    Gatt, A.2    Iijima-Ando, K.3
  • 35
    • 14244251499 scopus 로고    scopus 로고
    • Identification of the sucrose non-fermenting related kinase SNRK, as a novel LKB1 substrate
    • Jaleel M., McBride A., Lizcano J.M., Deak M., Toth R., Morrice N.A., Alessi D.R. Identification of the sucrose non-fermenting related kinase SNRK, as a novel LKB1 substrate. FEBS Lett. 2005, 579:1417-1423.
    • (2005) FEBS Lett. , vol.579 , pp. 1417-1423
    • Jaleel, M.1    McBride, A.2    Lizcano, J.M.3    Deak, M.4    Toth, R.5    Morrice, N.A.6    Alessi, D.R.7
  • 36
    • 79955044494 scopus 로고    scopus 로고
    • Soluble amyloid beta-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration
    • Jin M., Shepardson N., Yang T., Chen G., Walsh D., Selkoe D.J. Soluble amyloid beta-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration. Proc. Natl. Acad. Sci. USA 2011, 108:5819-5824.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 5819-5824
    • Jin, M.1    Shepardson, N.2    Yang, T.3    Chen, G.4    Walsh, D.5    Selkoe, D.J.6
  • 38
    • 0035993237 scopus 로고    scopus 로고
    • Abeta toxicity in Alzheimer's disease: globular oligomers (ADDLs) as new vaccine and drug targets
    • Klein W.L. Abeta toxicity in Alzheimer's disease: globular oligomers (ADDLs) as new vaccine and drug targets. Neurochem. Int. 2002, 41:345-352.
    • (2002) Neurochem. Int. , vol.41 , pp. 345-352
    • Klein, W.L.1
  • 41
    • 33846633336 scopus 로고    scopus 로고
    • Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease
    • Lacor P.N., Buniel M.C., Furlow P.W., Clemente A.S., Velasco P.T., Wood M., Viola K.L., Klein W.L. Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease. J. Neurosci. 2007, 27:796-807.
    • (2007) J. Neurosci. , vol.27 , pp. 796-807
    • Lacor, P.N.1    Buniel, M.C.2    Furlow, P.W.3    Clemente, A.S.4    Velasco, P.T.5    Wood, M.6    Viola, K.L.7    Klein, W.L.8
  • 42
    • 84855993170 scopus 로고    scopus 로고
    • Reduced activity of AMP-activated protein kinase protects against genetic models of motor neuron disease
    • Lim M.A., Selak M.A., Xiang Z., Krainc D., Neve R.L., Kraemer B.C., Watts J.L., Kalb R.G. Reduced activity of AMP-activated protein kinase protects against genetic models of motor neuron disease. J. Neurosci. 2012, 32:1123-1141.
    • (2012) J. Neurosci. , vol.32 , pp. 1123-1141
    • Lim, M.A.1    Selak, M.A.2    Xiang, Z.3    Krainc, D.4    Neve, R.L.5    Kraemer, B.C.6    Watts, J.L.7    Kalb, R.G.8
  • 44
    • 33846590099 scopus 로고    scopus 로고
    • Disturbed cross talk between insulin-like growth factor I and AMP-activated protein kinase as a possible cause of vascular dysfunction in the amyloid precursor protein/presenilin 2 mouse model of Alzheimer's disease
    • Lopez-Lopez C., Dietrich M.O., Metzger F., Loetscher H., Torres-Aleman I. Disturbed cross talk between insulin-like growth factor I and AMP-activated protein kinase as a possible cause of vascular dysfunction in the amyloid precursor protein/presenilin 2 mouse model of Alzheimer's disease. J. Neurosci. 2007, 27:824-831.
    • (2007) J. Neurosci. , vol.27 , pp. 824-831
    • Lopez-Lopez, C.1    Dietrich, M.O.2    Metzger, F.3    Loetscher, H.4    Torres-Aleman, I.5
  • 45
    • 0036973393 scopus 로고    scopus 로고
    • Diabetes mellitus and the risk of dementia, Alzheimer's disease and vascular cognitive impairment in the Canadian Study of Health and Aging
    • MacKnight C., Rockwood K., Awalt E., McDowell I. Diabetes mellitus and the risk of dementia, Alzheimer's disease and vascular cognitive impairment in the Canadian Study of Health and Aging. Dement. Geriatr. Cogn. Disord. 2002, 14:77-83.
    • (2002) Dement. Geriatr. Cogn. Disord. , vol.14 , pp. 77-83
    • MacKnight, C.1    Rockwood, K.2    Awalt, E.3    McDowell, I.4
  • 46
    • 84868677556 scopus 로고    scopus 로고
    • Biochemistry and cell biology of tau protein in neurofibrillary degeneration
    • Mandelkow E.M., Mandelkow E. Biochemistry and cell biology of tau protein in neurofibrillary degeneration. Cold Spring Harb. Perspect. Med. 2012, 2:a006247.
    • (2012) Cold Spring Harb. Perspect. Med. , vol.2
    • Mandelkow, E.M.1    Mandelkow, E.2
  • 47
  • 48
    • 0026570528 scopus 로고
    • Beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson M.P., Cheng B., Davis D., Bryant K., Lieberburg I., Rydel R.E. beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 1992, 12:376-389.
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 49
    • 20144368904 scopus 로고    scopus 로고
    • Pharmacological inhibition of AMP-activated protein kinase provides neuroprotection in stroke
    • McCullough L.D., Zeng Z., Li H., Landree L.E., McFadden J., Ronnett G.V. Pharmacological inhibition of AMP-activated protein kinase provides neuroprotection in stroke. J. Biol. Chem. 2005, 280:20493-20502.
    • (2005) J. Biol. Chem. , vol.280 , pp. 20493-20502
    • McCullough, L.D.1    Zeng, Z.2    Li, H.3    Landree, L.E.4    McFadden, J.5    Ronnett, G.V.6
  • 50
    • 80052511813 scopus 로고    scopus 로고
    • The AMPK signalling pathway coordinates cell growth, autophagy and metabolism
    • Mihaylova M.M., Shaw R.J. The AMPK signalling pathway coordinates cell growth, autophagy and metabolism. Nat. Cell Biol. 2011, 13:1016-1023.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1016-1023
    • Mihaylova, M.M.1    Shaw, R.J.2
  • 51
    • 33748747706 scopus 로고    scopus 로고
    • Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates AMP-activated protein kinase in vitro
    • Momcilovic M., Hong S.P., Carlson M. Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates AMP-activated protein kinase in vitro. J. Biol. Chem. 2006, 281:25336-25343.
    • (2006) J. Biol. Chem. , vol.281 , pp. 25336-25343
    • Momcilovic, M.1    Hong, S.P.2    Carlson, M.3
  • 54
    • 1542358895 scopus 로고    scopus 로고
    • PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila
    • Nishimura I., Yang Y., Lu B. PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila. Cell 2004, 116:671-682.
    • (2004) Cell , vol.116 , pp. 671-682
    • Nishimura, I.1    Yang, Y.2    Lu, B.3
  • 55
    • 77954132249 scopus 로고    scopus 로고
    • Amyloid-beta-induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networks
    • Palop J.J., Mucke L. Amyloid-beta-induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networks. Nat. Neurosci. 2010, 13:812-818.
    • (2010) Nat. Neurosci. , vol.13 , pp. 812-818
    • Palop, J.J.1    Mucke, L.2
  • 56
    • 34548264782 scopus 로고    scopus 로고
    • Aberrant excitatory neuronal activity and compensatory remodeling of inhibitory hippocampal circuits in mouse models of Alzheimer's disease
    • Palop J.J., Chin J., Roberson E.D., Wang J., Thwin M.T., Bien-Ly N., Yoo J., Ho K.O., Yu G.Q., Kreitzer A., et al. Aberrant excitatory neuronal activity and compensatory remodeling of inhibitory hippocampal circuits in mouse models of Alzheimer's disease. Neuron 2007, 55:697-711.
    • (2007) Neuron , vol.55 , pp. 697-711
    • Palop, J.J.1    Chin, J.2    Roberson, E.D.3    Wang, J.4    Thwin, M.T.5    Bien-Ly, N.6    Yoo, J.7    Ho, K.O.8    Yu, G.Q.9    Kreitzer, A.10
  • 58
    • 78651506630 scopus 로고    scopus 로고
    • Amyloid-β/Fyn-induced synaptic, network, and cognitive impairments depend on tau levels in multiple mouse models of Alzheimer's disease
    • Roberson E.D., Halabisky B., Yoo J.W., Yao J., Chin J., Yan F., Wu T., Hamto P., Devidze N., Yu G.Q., et al. Amyloid-β/Fyn-induced synaptic, network, and cognitive impairments depend on tau levels in multiple mouse models of Alzheimer's disease. J. Neurosci. 2011, 31:700-711.
    • (2011) J. Neurosci. , vol.31 , pp. 700-711
    • Roberson, E.D.1    Halabisky, B.2    Yoo, J.W.3    Yao, J.4    Chin, J.5    Yan, F.6    Wu, T.7    Hamto, P.8    Devidze, N.9    Yu, G.Q.10
  • 60
    • 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
  • 61
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • Shankar G.M., Bloodgood B.L., Townsend M., Walsh D.M., Selkoe D.J., Sabatini B.L. Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J. Neurosci. 2007, 27:2866-2875.
    • (2007) J. Neurosci. , vol.27 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 63
  • 64
    • 84858336588 scopus 로고    scopus 로고
    • Aβ-induced formation of autophagosomes is mediated by RAGE-CaMKKβ-AMPK signaling
    • 1006.e11-23
    • Son S.M., Jung E.S., Shin H.J., Byun J., Mook-Jung I. Aβ-induced formation of autophagosomes is mediated by RAGE-CaMKKβ-AMPK signaling. Neurobiol. Aging 2012, 33. 1006.e11-23.
    • (2012) Neurobiol. Aging , vol.33
    • Son, S.M.1    Jung, E.S.2    Shin, H.J.3    Byun, J.4    Mook-Jung, I.5
  • 65
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment
    • Terry R.D., Masliah E., Salmon D.P., Butters N., DeTeresa R., Hill R., Hansen L.A., Katzman R. Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann. Neurol. 1991, 30:572-580.
    • (1991) Ann. Neurol. , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    DeTeresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 66
    • 79952135798 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) is a tau kinase, activated in response to amyloid β-peptide exposure
    • Thornton C., Bright N.J., Sastre M., Muckett P.J., Carling D. AMP-activated protein kinase (AMPK) is a tau kinase, activated in response to amyloid β-peptide exposure. Biochem. J. 2011, 434:503-512.
    • (2011) Biochem. J. , vol.434 , pp. 503-512
    • Thornton, C.1    Bright, N.J.2    Sastre, M.3    Muckett, P.J.4    Carling, D.5
  • 67
    • 0037013222 scopus 로고    scopus 로고
    • STO-609, a specific inhibitor of the Ca(2+)/calmodulin-dependent protein kinase kinase
    • Tokumitsu H., Inuzuka H., Ishikawa Y., Ikeda M., Saji I., Kobayashi R. STO-609, a specific inhibitor of the Ca(2+)/calmodulin-dependent protein kinase kinase. J. Biol. Chem. 2002, 277:15813-15818.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15813-15818
    • Tokumitsu, H.1    Inuzuka, H.2    Ishikawa, Y.3    Ikeda, M.4    Saji, I.5    Kobayashi, R.6
  • 69
    • 79251556232 scopus 로고    scopus 로고
    • Novel synthetic small-molecule activators of AMPK as enhancers of autophagy and amyloid-β peptide degradation
    • Vingtdeux V., Chandakkar P., Zhao H., d'Abramo C., Davies P., Marambaud P. Novel synthetic small-molecule activators of AMPK as enhancers of autophagy and amyloid-β peptide degradation. FASEB J. 2011, 25:219-231.
    • (2011) FASEB J. , vol.25 , pp. 219-231
    • Vingtdeux, V.1    Chandakkar, P.2    Zhao, H.3    d'Abramo, C.4    Davies, P.5    Marambaud, P.6
  • 70
    • 79952135316 scopus 로고    scopus 로고
    • AMPK is abnormally activated in tangle- and pre-tangle-bearing neurons in Alzheimer's disease and other tauopathies
    • Vingtdeux V., Davies P., Dickson D.W., Marambaud P. AMPK is abnormally activated in tangle- and pre-tangle-bearing neurons in Alzheimer's disease and other tauopathies. Acta Neuropathol. 2011, 121:337-349.
    • (2011) Acta Neuropathol. , vol.121 , pp. 337-349
    • Vingtdeux, V.1    Davies, P.2    Dickson, D.W.3    Marambaud, P.4
  • 72
    • 79957636327 scopus 로고    scopus 로고
    • Induction of intracellular tau aggregation is promoted by alpha-synuclein seeds and provides novel insights into the hyperphosphorylation of tau
    • Waxman E.A., Giasson B.I. Induction of intracellular tau aggregation is promoted by alpha-synuclein seeds and provides novel insights into the hyperphosphorylation of tau. J. Neurosci. 2011, 31:7604-7618.
    • (2011) J. Neurosci. , vol.31 , pp. 7604-7618
    • Waxman, E.A.1    Giasson, B.I.2
  • 74
    • 41149117383 scopus 로고    scopus 로고
    • LKB1 and AMPK in cell polarity and division
    • Williams T., Brenman J.E. LKB1 and AMPK in cell polarity and division. Trends Cell Biol. 2008, 18:193-198.
    • (2008) Trends Cell Biol. , vol.18 , pp. 193-198
    • Williams, T.1    Brenman, J.E.2
  • 76
  • 77
    • 77954256913 scopus 로고    scopus 로고
    • TGF-beta signaling specifies axons during brain development
    • Yi J.J., Barnes A.P., Hand R., Polleux F., Ehlers M.D. TGF-beta signaling specifies axons during brain development. Cell 2010, 142:144-157.
    • (2010) Cell , vol.142 , pp. 144-157
    • Yi, J.J.1    Barnes, A.P.2    Hand, R.3    Polleux, F.4    Ehlers, M.D.5
  • 79
    • 83855162740 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein tau by AMPK-related kinases
    • Yoshida H., Goedert M. Phosphorylation of microtubule-associated protein tau by AMPK-related kinases. J. Neurochem. 2012, 120:165-176.
    • (2012) J. Neurochem. , vol.120 , pp. 165-176
    • Yoshida, H.1    Goedert, M.2
  • 80
    • 84857676337 scopus 로고    scopus 로고
    • A critical role for the PAR-1/MARK-tau axis in mediating the toxic effects of Aβ on synapses and dendritic spines
    • Yu W., Polepalli J., Wagh D., Rajadas J., Malenka R., Lu B. A critical role for the PAR-1/MARK-tau axis in mediating the toxic effects of Aβ on synapses and dendritic spines. Hum. Mol. Genet. 2012, 21:1384-1390.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1384-1390
    • Yu, W.1    Polepalli, J.2    Wagh, D.3    Rajadas, J.4    Malenka, R.5    Lu, B.6
  • 81
    • 77956587739 scopus 로고    scopus 로고
    • Abeta oligomers cause localized Ca(2+) elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines
    • Zempel H., Thies E., Mandelkow E., Mandelkow E.M. Abeta oligomers cause localized Ca(2+) elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines. J. Neurosci. 2010, 30:11938-11950.
    • (2010) J. Neurosci. , vol.30 , pp. 11938-11950
    • Zempel, H.1    Thies, E.2    Mandelkow, E.3    Mandelkow, E.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.