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Volumn 137, Issue 2, 2014, Pages 537-552

Inositol trisphosphate 3-kinase B is increased in human Alzheimer brain and exacerbates mouse Alzheimer pathology

Author keywords

Alzheimer pathology; inositol (1,3,4,5) tetrakisphosphate; inositol phosphates; ITPKB

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE 1; INOSITOL TRISPHOSPHATE 3 KINASE; INOSITOL TRISPHOSPHATE 3 KINASE B; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 84893828779     PISSN: 00068950     EISSN: 14602156     Source Type: Journal    
DOI: 10.1093/brain/awt344     Document Type: Article
Times cited : (57)

References (46)
  • 1
    • 0029066704 scopus 로고
    • Increased expression and subcellular translocation of the mitogen activated protein kinase kinase and mitogen-Activated protein kinase in alzheimer?s disease
    • Arendt T, Holzer M, Grossmann A, Zedlick D, Bruckner MK. Increased expression and subcellular translocation of the mitogen activated protein kinase kinase and mitogen-Activated protein kinase in Alzheimer?s disease. Neuroscience 1995; 68: 5-18
    • (1995) Neuroscience , vol.68 , pp. 5-18
    • Arendt, T.1    Holzer, M.2    Grossmann, A.3    Zedlick, D.4    Bruckner, M.K.5
  • 2
    • 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 EM, Mandelkow E. Phosphorylation of Ser262 strongly reduces binding of TAU to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding. Neuron 1993; 11: 153-63
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 3
    • 0025863618 scopus 로고
    • Neuropathological stageing of alzheimer-related changes
    • Braak H, Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol (Berl.) 1991; 82: 239-59
    • (1991) Acta Neuropathol (Berl , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 4
    • 0023929799 scopus 로고
    • Both adult and juvenile tau microtubule-Associated proteins are axon specific in the developing and adult rat cerebellum
    • Brion JP, Guilleminot J, Couchie D, Flament-Durand J, Nunez J. Both adult and juvenile TAU microtubule-Associated proteins are axon specific in the developing and adult rat cerebellum. Neuroscience 1988; 25: 139-46
    • (1988) Neuroscience , vol.25 , pp. 139-146
    • Brion, J.P.1    Guilleminot, J.2    Couchie, D.3    Flament-Durand, J.4    Nunez, J.5
  • 5
    • 33846852617 scopus 로고    scopus 로고
    • I ifn--induced bace1 expression is mediated by activation of jak2 and erk1/2 signaling pathways and direct binding of stat1 to bace1 promoter in astrocytes
    • Cho HJ, Kim SK, Jin SM, Hwang EM, Kim YS, Huh K, et al. I. IFN--induced BACE1 expression is mediated by activation of JAK2 and ERK1/2 signaling pathways and direct binding of STAT1 to BACE1 promoter in astrocytes. Glia 2007; 55: 253-62
    • (2007) Glia , vol.55 , pp. 253-262
    • Cho, H.J.1    Kim, S.K.2    Jin, S.M.3    Hwang, E.M.4    Kim, Y.S.5    Huh, K.6
  • 6
    • 84864359816 scopus 로고    scopus 로고
    • Amyloid precursor protein (app) traffics from the cell surface via endosomes for amyloid b (ab) production in the trans-golgi network
    • Choy RW-Y, Cheng Z, Schekman R. Amyloid precursor protein (APP) traffics from the cell surface via endosomes for amyloid b (Ab) production in the trans-Golgi network. Proc Natl Acad Sci USA 2012; 109: E2077-82
    • (2012) Proc Natl Acad Sci USA , vol.109
    • Choy, R.W.-Y.1    Cheng, Z.2    Schekman, R.3
  • 7
    • 0029165902 scopus 로고
    • Molecular study and regulation of D-myo-inositol 1, 4,5-Trisphospahte 3-kinase
    • Communi D, Vanweyenberg V, Erneux C. Molecular study and regulation of D-myo-inositol 1,4,5-Trisphospahte 3-kinase. Cell Signal 1995; 7: 643-50
    • (1995) Cell Signal , vol.7 , pp. 643-650
    • Communi, D.1    Vanweyenberg, V.2    Erneux, C.3
  • 8
    • 0042326882 scopus 로고    scopus 로고
    • The three isoenzymes of human inositol-1, 4,5-Trisphosphate 3-kinase show specific intracellular localization but comparable Ca2+ responses on transfection in Cos-7 cells
    • Dewaste V, Moreau C, De Smedt F, Bex F, De Smedt H, Wuytack F, et al. The three isoenzymes of human inositol-1,4,5-Trisphosphate 3-kinase show specific intracellular localization but comparable Ca2+ responses on transfection in Cos-7 cells. Biochem J 2003; 374: 41-9
    • (2003) Biochem J , vol.374 , pp. 41-49
    • Dewaste, V.1    Moreau, C.2    De Smedt, F.3    Bex, F.4    De Smedt, H.5    Wuytack, F.6
  • 9
    • 0026549985 scopus 로고
    • Mitogen activated protein (map) kinase transforms tau protein into an alzheimer-like state
    • Drewes G, Lichtenberg-Kraag B, Döring F, Mandelkow EM, Biernat J, Goris J, et al. Mitogen activated protein (MAP) kinase transforms TAU protein into an Alzheimer-like state. EMBO J 1992; 11: 2131-8
    • (1992) EMBO J , vol.11 , pp. 2131-2138
    • Drewes, G.1    Lichtenberg-Kraag, B.2    Döring, F.3    Mandelkow, E.M.4    Biernat, J.5    Goris, J.6
  • 10
    • 33244496656 scopus 로고    scopus 로고
    • Alzheimer?s disease: Mrna expression profiles of multiple patients show alterations of genes involved with calcium signaling
    • Emilsson L, Saetre P, Jazin E. Alzheimer?s disease: MRNA expression profiles of multiple patients show alterations of genes involved with calcium signaling. Neurobiol Dis 2006; 21: 618-25
    • (2006) Neurobiol Dis , vol.21 , pp. 618-625
    • Emilsson, L.1    Saetre, P.2    Jazin, E.3
  • 11
    • 0035094403 scopus 로고    scopus 로고
    • Phosphorylated map kinase (erk1, erk2) expression is associated with early tau deposition in neurones and glial cells, but not with increased nuclear dna vulnerability and cell death, in alzheimer?s disease, pick?s disease, progressive supranuclear palsy and corticobasal degeneration
    • Ferrer I, Blanco R, Carmona M, Ribera R, Goutan E, Puig B, et al. Phosphorylated map kinase (ERK1, ERK2) expression is associated with early TAU deposition in neurones and glial cells, but not with increased nuclear DNA vulnerability and cell death, in Alzheimer?s disease, Pick?s disease, progressive supranuclear palsy and corticobasal degeneration. Brain Pathol 2001; 11: 144-58
    • (2001) Brain Pathol , vol.11 , pp. 144-158
    • Ferrer, I.1    Blanco, R.2    Carmona, M.3    Ribera, R.4    Goutan, E.5    Puig, B.6
  • 12
    • 85062139768 scopus 로고
    • Tau phosphorylation in brain slices: Pharmacological evidence for convergent effects of protein phosphatases on tau and mitogenactivated protein kinase
    • Garver TD, Oyler GA, Harris KA, Polavarapu R, Damuni Z, Lehman RA, et al. TAU phosphorylation in brain slices: Pharmacological evidence for convergent effects of protein phosphatases on TAU and mitogenactivated protein kinase. Mol Pharmacol 1995; 47: 745-56
    • (1995) Mol Pharmacol , vol.47 , pp. 745-756
    • Garver, T.D.1    Oyler, G.A.2    Harris, K.A.3    Polavarapu, R.4    Damuni, Z.5    Lehman, R.A.6
  • 13
    • 70349558522 scopus 로고    scopus 로고
    • Genome-wide association study identifies variants at clu and picalm associated with alzheimer?s disease
    • Harold D, Abraham R, Hollingworth P, Sims R, Gerrish A, Hamshere ML, et al. Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer?s disease. Nat Genet 2009; 4: 1088-93
    • (2009) Nat Genet , vol.4 , pp. 1088-1093
    • Harold, D.1    Abraham, R.2    Hollingworth, P.3    Sims, R.4    Gerrish, A.5    Hamshere, M.L.6
  • 14
    • 0030769091 scopus 로고    scopus 로고
    • Distinct sites of intracellular production for alzheimer?s disease ab40/42 amyloid peptides
    • Hartmann T, Bieger SC, Brühl B, Tienari PJ, Ida N, Allsop D, et al. Distinct sites of intracellular production for Alzheimer?s disease Ab40/42 amyloid peptides. Nat Med 1997; 9: 1016-20
    • (1997) Nat Med , vol.9 , pp. 1016-1020
    • Hartmann, T.1    Bieger, S.C.2    Brühl, B.3    Tienari, P.J.4    Ida, N.5    Allsop, D.6
  • 16
    • 0035934224 scopus 로고    scopus 로고
    • Activation of mitogen-Activated protein kinase cascade and phosphorylation of cytoskeletal proteins after neurone-specific activation of p21ras II Cytoskeletal proteinsand dendritic morphology
    • Holzer M, Rödel L, Seeger G, Gärtner U, Narz F, Janke C, et al. Activation of mitogen-Activated protein kinase cascade and phosphorylation of cytoskeletal proteins after neurone-specific activation of p21ras. II. Cytoskeletal proteinsand dendritic morphology. Neuroscience 2001; 105: 1041-54
    • (2001) Neuroscience , vol.105 , pp. 1041-1054
    • Holzer, M.1    Rödel, L.2    Seeger, G.3    Gärtner, U.4    Narz, F.5    Janke, C.6
  • 17
    • 84863337843 scopus 로고    scopus 로고
    • Alzheimer mechanisms and therapeutic strategies
    • Huang Y, Lennart M. Alzheimer mechanisms and therapeutic strategies. Cell 2012; 148: 1205-22
    • (2012) Cell , vol.148 , pp. 1205-1222
    • Huang, Y.1    Lennart, M.2
  • 18
    • 0035347166 scopus 로고    scopus 로고
    • Back in the water: The return of the inositol phosphates
    • Irvine RF, Schell MJ. Back in the water: The return of the inositol phosphates. Nat Rev Mol Cell Biol 2001; 2: 327-38
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 327-338
    • Irvine, R.F.1    Schell, M.J.2
  • 20
    • 42449122333 scopus 로고    scopus 로고
    • Inositol trisphosphate 3-kinase b (insp3kb) as a physiological modulator of myelopoiesis
    • Jia Y, Loison F, Hattori H, Li Y, Erneux C, Park SY, et al. Inositol trisphosphate 3-kinase B (InsP3KB) as a physiological modulator of myelopoiesis. Proc Natl Acad Sci USA 2008; 105: 4739-44
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 4739-4744
    • Jia, Y.1    Loison, F.2    Hattori, H.3    Li, Y.4    Erneux, C.5    Park, S.Y.6
  • 21
    • 78549264026 scopus 로고    scopus 로고
    • Genome-wide association study identifies variants at clu and cr1 associated with alzheimer?s disease
    • Lambert JC, Heath S, Even G, Campion D, Sleegers K, Hiltunen M, et al. Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimer?s disease. Nat Genet 2009; 4: 1094-9
    • (2009) Nat Genet , vol.4 , pp. 1094-1099
    • Lambert, J.C.1    Heath, S.2    Even, G.3    Campion, D.4    Sleegers, K.5    Hiltunen, M.6
  • 23
    • 84869159135 scopus 로고    scopus 로고
    • Lack of tau proteins rescues neuronal cell death and decreases amyloidogenic processing of app in app/ps1 mice
    • Leroy K, Ando K, Laporte V, Dedecker R, Suain V, Authelet M, et al. Lack of TAU proteins rescues neuronal cell death and decreases amyloidogenic processing of APP in APP/PS1 mice. Am J Pathol 2012; 181: 1928-40
    • (2012) Am J Pathol , vol.181 , pp. 1928-1940
    • Leroy, K.1    Ando, K.2    Laporte, V.3    Dedecker, R.4    Suain, V.5    Authelet, M.6
  • 24
    • 0027453202 scopus 로고
    • Functional studies of alzheimer?s disease tau protein
    • Lu Q, Wood JG. Functional studies of Alzheimer?s disease TAU protein. J Neurosci 1993; 13: 508-15
    • (1993) J Neurosci , vol.13 , pp. 508-515
    • Lu, Q.1    Wood, J.G.2
  • 25
    • 0032582516 scopus 로고    scopus 로고
    • The long term adenoviral expression of the human amyloid precursor protein shows different secretase activities in rat cortical neurons and astrocytes
    • Macq AF, Czech C, Essalmani R, Brion JP, Maron A, Mercken L, et al. The long term adenoviral expression of the human amyloid precursor protein shows different secretase activities in rat cortical neurons and astrocytes. J Biol Chem 1998; 273: 28931-6
    • (1998) J Biol Chem , vol.273 , pp. 28931-28936
    • Macq, A.F.1    Czech, C.2    Essalmani, R.3    Brion, J.P.4    Maron, A.5    Mercken, L.6
  • 26
    • 34548745426 scopus 로고    scopus 로고
    • Inositol 1, 3, 4,5-Tetrakisphosphate controls proapoptotic Bim gene expression and survival in B cells
    • Maréchal Y, Pesesse X, Jia Y, Pouillon V, Pérez-Morga D, Daniel J, et al. Inositol 1, 3, 4,5-Tetrakisphosphate controls proapoptotic Bim gene expression and survival in B cells. Proc Natl Acad Sci USA 2007; 104 13978-83
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 13978-13983
    • Maréchal, Y.1    Pesesse, X.2    Jia, Y.3    Pouillon, V.4    Pérez-Morga, D.5    Daniel, J.6
  • 27
    • 78649514132 scopus 로고    scopus 로고
    • Inositol 1,4,5-Trisphosphate 3-kinase b controls survival and prevents anergy in b cells
    • Maréchal Y, Quéant S, Polizzi S, Pouillon V, Schurmans S. Inositol 1,4,5-Trisphosphate 3-kinase B controls survival and prevents anergy in B cells. Immunobiol 2011; 216: 103-109
    • (2011) Immunobiol , vol.216 , pp. 103-109
    • Maréchal, Y.1    Quéant, S.2    Polizzi, S.3    Pouillon, V.4    Schurmans, S.5
  • 28
    • 0029807527 scopus 로고    scopus 로고
    • Control of memory formation through regulated expression of a camkii transgene
    • Mayford M, Bach ME, Huang YY, Wang L, Hawkins RD, Kandel ER. Control of memory formation through regulated expression of a CaMKII transgene. Science 1996; 274: 1678-83
    • (1996) Science , vol.274 , pp. 1678-1683
    • Mayford, M.1    Bach, M.E.2    Huang, Y.Y.3    Wang, L.4    Hawkins, R.D.5    Kandel, E.R.6
  • 29
    • 34247219775 scopus 로고    scopus 로고
    • Production of Ins(1, 3,4,5)P4 mediated by the kinase Itpkb inhibits store-operated calcium channels and regulates B cell selection and activation
    • Miller AT, Sandberg M, Huang YH, Young M, Sutton S, Sauer K, et al. Production of Ins(1,3,4,5)P4 mediated by the kinase Itpkb inhibits store-operated calcium channels and regulates B cell selection and activation. Nat Immunol 2007; 8: 514-21
    • (2007) Nat Immunol , vol.8 , pp. 514-521
    • Miller, A.T.1    Sandberg, M.2    Huang, Y.H.3    Young, M.4    Sutton, S.5    Sauer, K.6
  • 31
    • 0025908356 scopus 로고
    • He consortium to establish a registry for alzheimer?s disease (cerad part ii standardization of the neuropathologic assessment of alzheimer?s disease
    • Mirra SS, Heyman A, McKeel D, Sumi SM, Crain BJ, Brownlee LM, et al. The Consortium to Establish a Registry for Alzheimer?s Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer?s disease. Neurology 1991; 41: 479-86
    • (1991) Neurology , vol.41 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3    Sumi, S.M.4    Crain, B.J.5    Brownlee, L.M.6
  • 32
    • 77952548853 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta and the p25 activator of cyclin dependent kinase 5 increase pausing of mitochondria in neurons
    • Morel M, Authelet M, Dedecker R, Brion JP. Glycogen synthase kinase-3beta and the p25 activator of cyclin dependent kinase 5 increase pausing of mitochondria in neurons. Neuroscience 2010; 167: 1044-56
    • (2010) Neuroscience , vol.167 , pp. 1044-1056
    • Morel, M.1    Authelet, M.2    Dedecker, R.3    Brion, J.P.4
  • 33
    • 33749521100 scopus 로고    scopus 로고
    • Intraneuronal b-Amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer?s disease mutations: Potential factors in amyloid plaque formation
    • Oakley H, Cole SL, Logan S, Maus E, Shao P, Craft J, et al. Intraneuronal b-Amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer?s disease mutations: Potential factors in amyloid plaque formation. J Neurosci 2006; 26: 10129-40
    • (2006) J Neurosci , vol.26 , pp. 10129-10140
    • Oakley, H.1    Cole, S.L.2    Logan, S.3    Maus, E.4    Shao, P.5    Craft, J.6
  • 34
    • 84856060315 scopus 로고    scopus 로고
    • Mutant presenilin 2 increases b-secretase activity through reactive oxygen species-dependent activation of extracellular signal-regulated kinase
    • Park MH, Choi DY, Jin HW, Yoo HS, Han JY, Oh KW, et al. Mutant presenilin 2 increases b-secretase activity through reactive oxygen species-dependent activation of extracellular signal-regulated kinase. J Neuropathol Exp Neurol 2012; 71: 130-9
    • (2012) J Neuropathol Exp Neurol , vol.71 , pp. 130-139
    • Park, M.H.1    Choi, D.Y.2    Jin, H.W.3    Yoo, H.S.4    Han, J.Y.5    Oh, K.W.6
  • 35
    • 1842839883 scopus 로고    scopus 로고
    • Ins(1, 4,5)P3 metabolism and the family of IP3-3 kinases
    • Pattni K, Banting G. Ins(1,4,5)P3 metabolism and the family of IP3-3 kinases. Cell Signal 2004; 16: 643-54
    • (2004) Cell Signal , vol.16 , pp. 643-654
    • Pattni, K.1    Banting, G.2
  • 36
    • 0033516947 scopus 로고    scopus 로고
    • Activation of neuronal extracellular receptor kinase (erk) in alzheimer?s disease links oxidative stress to abnormal phosphorylation
    • Perry G, Roder H, Nunomura A, Takeda A, Friedlich AL, Zhu X, et al. Activation of neuronal extracellular receptor kinase (ERK) in Alzheimer?s disease links oxidative stress to abnormal phosphorylation. Neuroreport 1999; 10: 2411-15
    • (1999) Neuroreport , vol.10 , pp. 2411-2415
    • Perry, G.1    Roder, H.2    Nunomura, A.3    Takeda, A.4    Friedlich, A.L.5    Zhu, X.6
  • 38
    • 79954474007 scopus 로고    scopus 로고
    • Regulation of b cell survival, development and function by inositol 1,4,5-Trisphosphate 3-kinase b (itpkb)
    • Schurmans S, Pouillon V, Maréchal Y. Regulation of B cell survival, development and function by inositol 1,4,5-Trisphosphate 3-kinase B (Itpkb). Adv Enz Reg 2011; 51: 66-73
    • (2011) Adv Enz Reg , vol.51 , pp. 66-73
    • Schurmans, S.1    Pouillon, V.2    Maréchal, Y.3
  • 39
    • 84872347788 scopus 로고    scopus 로고
    • Inositol tetrakisphosphate limits NK cell effector functions by controlling phosphoinositide 3-kinase signaling
    • Sauer K, Park E, Siegemund S, French AR, Wahle JA, Sternberg L, et al. Inositol tetrakisphosphate limits NK cell effector functions by controlling phosphoinositide 3-kinase signaling. Blood 2013; 121: 286-97
    • (2013) Blood , vol.121 , pp. 286-297
    • Sauer, K.1    Park, E.2    Siegemund, S.3    French, A.R.4    Wahle, J.A.5    Sternberg, L.6
  • 40
    • 0025369878 scopus 로고
    • Rat brain inositol 1, 4,5-Trisphosphate 3-kinase Ca2( + )-sensitivity, purification and antibody production
    • Takazawa K, Lemos M, Delvaux A, Lejeune C, Dumont JE, Erneux C. Rat brain inositol 1,4,5-Trisphosphate 3-kinase. Ca2( + )-sensitivity, purification and antibody production. Biochem J 1990; 268: 213-17
    • (1990) Biochem J , vol.268 , pp. 213-217
    • Takazawa, K.1    Lemos, M.2    Delvaux, A.3    Lejeune, C.4    Dumont, J.E.5    Erneux, C.6
  • 41
    • 0029942495 scopus 로고    scopus 로고
    • Metabolism of the swedish amyloid precursor protein variant in neuro2a (n2a) cells
    • Thinakaran G, Teplow DB, Siman R, Greenberg B, Sisodia SS. Metabolism of the Swedish amyloid precursor protein variant in Neuro2a (N2a) cells. J Biol Chem 1996; 271: 9390-7
    • (1996) J Biol Chem , vol.271 , pp. 9390-9397
    • Thinakaran, G.1    Teplow, D.B.2    Siman, R.3    Greenberg, B.4    Sisodia, S.S.5
  • 42
    • 7044220336 scopus 로고    scopus 로고
    • Fibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches
    • Tsai J, Grutzendler J, Duff K, Gan WB. Fibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches. Nat Neurosci 2004; 7: 1181-3
    • (2004) Nat Neurosci , vol.7 , pp. 1181-1183
    • Tsai, J.1    Grutzendler, J.2    Duff, K.3    Gan, W.B.4
  • 43
    • 0028937015 scopus 로고
    • Tissue-And cellspecific expression of Ins(1, 4,5)P3 3-kinase isoenzymes
    • Vanweyenberg V, Communi D, D?Santos CS, Erneux C. Tissue-And cellspecific expression of Ins(1,4,5)P3 3-kinase isoenzymes. Biochem J 1995; 306: 429-35
    • (1995) Biochem J , vol.306 , pp. 429-435
    • Vanweyenberg, V.1    Communi, D.2    D'Santos, C.S.3    Erneux, C.4
  • 44
    • 1842732175 scopus 로고    scopus 로고
    • Inositol (1, 4,5) trisphosphate 3 kinase B controls positive selection of T cells and modulates ERK activity
    • Wen BG, Pletcher MT, Warashina M, Choe SH, Ziaee N, Wiltshire T, et al. Inositol (1,4,5) trisphosphate 3 kinase B controls positive selection of T cells and modulates ERK activity. Proc Natl Acad Sci USA 2004; 101: 5604-9
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 5604-5609
    • Wen, B.G.1    Pletcher, M.T.2    Warashina, M.3    Choe, S.H.4    Ziaee, N.5    Wiltshire, T.6
  • 46
    • 3042712380 scopus 로고    scopus 로고
    • B-secretase bace1 is differentially controlled through muscarinic acetylcholine receptor signling
    • Zuchner T, Perez-Polo JR, Schliebs R. b-secretase BACE1 is differentially controlled through muscarinic acetylcholine receptor signling. J Neurosci Res 2004; 77: 250-257
    • (2004) J Neurosci Res , vol.77 , pp. 250-257
    • Zuchner, T.1    Perez-Polo, J.R.2    Schliebs, R.3


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