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Volumn 52, Issue 6, 2008, Pages 1030-1036

Amyloid-β peptide binds to microtubule-associated protein 1B (MAP1B)

Author keywords

Amyloid beta peptide; Microtubule associated protein 1B (MAP1B); Phage displayed cDNA library

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; MICROTUBULE ASSOCIATED PROTEIN 5;

EID: 40949096957     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2007.10.020     Document Type: Article
Times cited : (26)

References (60)
  • 1
    • 26444588771 scopus 로고    scopus 로고
    • Gradual alteration of mitochondrial structure and function by β-amyloids: importance of membrane viscosity changes, energy deprivation, reactive oxygen species production, and cytochrome c release
    • Aleardi A.M., Benard G., Augereau O., Malgat M., Talbot J.C., Mazat J.P., Letellier T., Dachary-Prigent J., Solaini G.C., and Rossignol R. Gradual alteration of mitochondrial structure and function by β-amyloids: importance of membrane viscosity changes, energy deprivation, reactive oxygen species production, and cytochrome c release. J. Bioenerg. Biomembr. 37 (2005) 207-225
    • (2005) J. Bioenerg. Biomembr. , vol.37 , pp. 207-225
    • Aleardi, A.M.1    Benard, G.2    Augereau, O.3    Malgat, M.4    Talbot, J.C.5    Mazat, J.P.6    Letellier, T.7    Dachary-Prigent, J.8    Solaini, G.C.9    Rossignol, R.10
  • 2
    • 0035985233 scopus 로고    scopus 로고
    • Tau function and dysfunction in neurons. Its role in neurodegenerative disorders
    • Avila J., Lim F., Moreno F., Belmonte C., and Cuello A.C. Tau function and dysfunction in neurons. Its role in neurodegenerative disorders. Mol. Neurobiol. 25 (2002) 213-231
    • (2002) Mol. Neurobiol. , vol.25 , pp. 213-231
    • Avila, J.1    Lim, F.2    Moreno, F.3    Belmonte, C.4    Cuello, A.C.5
  • 3
    • 33644660826 scopus 로고    scopus 로고
    • Cholinergic dysfunction in a mouse model of Alzheimer disease is reversed by an anti-A beta antibody
    • Bales K.R., Tzavara E.T., Wu S., Wade M.R., Bymaster F.P., Paul S.M., and Nomktos G.G. Cholinergic dysfunction in a mouse model of Alzheimer disease is reversed by an anti-A beta antibody. J. Clin. Invest. 116 (2006) 825-832
    • (2006) J. Clin. Invest. , vol.116 , pp. 825-832
    • Bales, K.R.1    Tzavara, E.T.2    Wu, S.3    Wade, M.R.4    Bymaster, F.P.5    Paul, S.M.6    Nomktos, G.G.7
  • 4
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C., Davis J.B., Lesley R., and Schubert D. Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 77 (1994) 817-827
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 5
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal Aβ causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice
    • Billings L.M., Oddo S., Green K.N., McGaugh J.L., and LaFerla F.M. Intraneuronal Aβ causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice. Neuron 45 (2005) 675-688
    • (2005) Neuron , vol.45 , pp. 675-688
    • Billings, L.M.1    Oddo, S.2    Green, K.N.3    McGaugh, J.L.4    LaFerla, F.M.5
  • 6
    • 0034353646 scopus 로고    scopus 로고
    • GABAc receptor sensitivity is modulated by interaction with MAP1B
    • Billups D., Hanley J.G., Orme M., Attwell D., and Moss S.J. GABAc receptor sensitivity is modulated by interaction with MAP1B. J. Neurosci. 20 (2000) 8643-8650
    • (2000) J. Neurosci. , vol.20 , pp. 8643-8650
    • Billups, D.1    Hanley, J.G.2    Orme, M.3    Attwell, D.4    Moss, S.J.5
  • 7
    • 0036434282 scopus 로고    scopus 로고
    • Cytosolic and nuclear aggregation of the amyloid β-peptide following its expression in the endoplasmic reticulum
    • Buckig A., Tikkanen R., Herzog V., and Schmitz A. Cytosolic and nuclear aggregation of the amyloid β-peptide following its expression in the endoplasmic reticulum. Histochem. Cell Biol. 118 (2002) 353-360
    • (2002) Histochem. Cell Biol. , vol.118 , pp. 353-360
    • Buckig, A.1    Tikkanen, R.2    Herzog, V.3    Schmitz, A.4
  • 8
    • 0028986916 scopus 로고
    • Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio J., Lorenzo A., Yeh J., and Yankner B.A. Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron 14 (1995) 879-888
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 9
    • 33947519211 scopus 로고    scopus 로고
    • Microtubule-stabilizing agent prevents protein accumulation-induced loss of synaptic markers
    • Butler D., Bendiske J., Michaelis M.L., Karanian D.A., and Bahr B.A. Microtubule-stabilizing agent prevents protein accumulation-induced loss of synaptic markers. Eur. J. Pharmacol. 562 (2007) 20-27
    • (2007) Eur. J. Pharmacol. , vol.562 , pp. 20-27
    • Butler, D.1    Bendiske, J.2    Michaelis, M.L.3    Karanian, D.A.4    Bahr, B.A.5
  • 10
    • 8744276616 scopus 로고    scopus 로고
    • Amyloid beta-peptide (1-42) contributes to the oxidative stress and neurodegeneration found in Alzheimer disease brain
    • Butterfield D.A., and Boyd-Kimball D. Amyloid beta-peptide (1-42) contributes to the oxidative stress and neurodegeneration found in Alzheimer disease brain. Brain Pathol. 14 (2004) 426-432
    • (2004) Brain Pathol. , vol.14 , pp. 426-432
    • Butterfield, D.A.1    Boyd-Kimball, D.2
  • 11
    • 1542377619 scopus 로고    scopus 로고
    • Toxicity of amyloid β peptide: tales of calcium, mitochondria, and oxidative stress
    • Canevari L., Abramov A.Y., and Duchen M.R. Toxicity of amyloid β peptide: tales of calcium, mitochondria, and oxidative stress. Neurochem. Res. 29 (2004) 637-650
    • (2004) Neurochem. Res. , vol.29 , pp. 637-650
    • Canevari, L.1    Abramov, A.Y.2    Duchen, M.R.3
  • 12
    • 0036272650 scopus 로고    scopus 로고
    • β-Amyloid inhibits integrated mitochondrial respiration and key enzyme activities
    • Casley C.S., Canevari L., Land J.M., Clark J.B., and Sharpe M.A. β-Amyloid inhibits integrated mitochondrial respiration and key enzyme activities. J. Neurochem. 80 (2002) 91-100
    • (2002) J. Neurochem. , vol.80 , pp. 91-100
    • Casley, C.S.1    Canevari, L.2    Land, J.M.3    Clark, J.B.4    Sharpe, M.A.5
  • 17
    • 0035842894 scopus 로고    scopus 로고
    • Microtubule-associated protein 1B: a neuronal binding partner for myelin-associated glycoprotein
    • Franzen R., Tanner S.L., Dashiell S.M., Rottkamp C.A., Hammer J.A., and Quarles R.H. Microtubule-associated protein 1B: a neuronal binding partner for myelin-associated glycoprotein. J. Cell Biol. 155 (2001) 893-898
    • (2001) J. Cell Biol. , vol.155 , pp. 893-898
    • Franzen, R.1    Tanner, S.L.2    Dashiell, S.M.3    Rottkamp, C.A.4    Hammer, J.A.5    Quarles, R.H.6
  • 18
    • 0346750742 scopus 로고    scopus 로고
    • Microtubule-associated protein 1B function during normal development, regeneration, and pathological conditions in the nervous system
    • Gonzalez-Billault C., Jimenez-Mateos E.M., Caceres A., Diaz-Nido J., Wandosell F., and Avila J. Microtubule-associated protein 1B function during normal development, regeneration, and pathological conditions in the nervous system. J. Neurobiol. 58 (2004) 48-59
    • (2004) J. Neurobiol. , vol.58 , pp. 48-59
    • Gonzalez-Billault, C.1    Jimenez-Mateos, E.M.2    Caceres, A.3    Diaz-Nido, J.4    Wandosell, F.5    Avila, J.6
  • 21
    • 0024595972 scopus 로고
    • Synaptic loss in Alzheimer's disease and other dementias
    • Hamos J.E., DeGennaro L.J., and Drachman D.A. Synaptic loss in Alzheimer's disease and other dementias. Neurology 39 (1989) 355-361
    • (1989) Neurology , vol.39 , pp. 355-361
    • Hamos, J.E.1    DeGennaro, L.J.2    Drachman, D.A.3
  • 22
    • 0032562664 scopus 로고    scopus 로고
    • A human brain L-3-hydroxyacyl-coenzyme A dehydrogenase is identical to an amyloid β-peptide-binding protein involved in Alzheimer's disease
    • He X.Y., Schulz H., and Yang S.Y. A human brain L-3-hydroxyacyl-coenzyme A dehydrogenase is identical to an amyloid β-peptide-binding protein involved in Alzheimer's disease. J. Biol. Chem. 273 (1998) 10741-10746
    • (1998) J. Biol. Chem. , vol.273 , pp. 10741-10746
    • He, X.Y.1    Schulz, H.2    Yang, S.Y.3
  • 23
    • 1842504323 scopus 로고    scopus 로고
    • Redox-active metals, oxidative stress, and Alzheimer's disease pathology
    • Huang X., Moir R.D., Tanzi R.E., Bush A.I., and Rogers J.T. Redox-active metals, oxidative stress, and Alzheimer's disease pathology. Ann. NY Acad. Sci. 1012 (2004) 153-163
    • (2004) Ann. NY Acad. Sci. , vol.1012 , pp. 153-163
    • Huang, X.1    Moir, R.D.2    Tanzi, R.E.3    Bush, A.I.4    Rogers, J.T.5
  • 25
    • 11344265672 scopus 로고    scopus 로고
    • Interactions between beta-amyloid and central cholinergic neurons: implications for Alzheimer's disease
    • Kar S., Slowikowski S.P., Westaway D., and Mount H.T. Interactions between beta-amyloid and central cholinergic neurons: implications for Alzheimer's disease. J. Psychiatry Neurosci. 29 (2004) 427-441
    • (2004) J. Psychiatry Neurosci. , vol.29 , pp. 427-441
    • Kar, S.1    Slowikowski, S.P.2    Westaway, D.3    Mount, H.T.4
  • 26
    • 33745901914 scopus 로고    scopus 로고
    • Teasing out the tangles
    • Kins S., and Beyreuther K. Teasing out the tangles. Nat. Med. 12 (2006) 764-765
    • (2006) Nat. Med. , vol.12 , pp. 764-765
    • Kins, S.1    Beyreuther, K.2
  • 27
    • 11844300395 scopus 로고    scopus 로고
    • Soluble Abeta oligomers ultrastructurally localize to cell processes and might be related to synaptic dysfunction in Alzheimer's disease brain
    • Kokubo H., Kayed R., Glabe C.G., and Yamaguchi H. Soluble Abeta oligomers ultrastructurally localize to cell processes and might be related to synaptic dysfunction in Alzheimer's disease brain. Brain Res. 1031 (2005) 222-228
    • (2005) Brain Res. , vol.1031 , pp. 222-228
    • Kokubo, H.1    Kayed, R.2    Glabe, C.G.3    Yamaguchi, H.4
  • 28
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-β in Alzheimer's disease
    • LaFerla F., Green K.N., and Oddo S. Intracellular amyloid-β in Alzheimer's disease. Nat. Rev. Neurosci. 8 (2007) 499-509
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 499-509
    • LaFerla, F.1    Green, K.N.2    Oddo, S.3
  • 29
    • 23444454302 scopus 로고    scopus 로고
    • Amyloid beta peptide binds a novel death-inducing protein
    • Lakshmana M.K., Araki W., and Tabira T. Amyloid beta peptide binds a novel death-inducing protein. AB-DIP FASEB J. 19 (2005) 1362-1364
    • (2005) AB-DIP FASEB J. , vol.19 , pp. 1362-1364
    • Lakshmana, M.K.1    Araki, W.2    Tabira, T.3
  • 34
    • 0032480771 scopus 로고    scopus 로고
    • The presence of amyloid β-protein in the detergent insoluble membrane compartment of human neuroblastoma cells
    • Morishima-Kawashima M., and Ihara Y. The presence of amyloid β-protein in the detergent insoluble membrane compartment of human neuroblastoma cells. Biochemistry 37 (1998) 15247-15253
    • (1998) Biochemistry , vol.37 , pp. 15247-15253
    • Morishima-Kawashima, M.1    Ihara, Y.2
  • 35
    • 0036150827 scopus 로고    scopus 로고
    • Alzheimer's disease-do tauists and Baptists finally shake hands?
    • Mudher A., and Lovestone S. Alzheimer's disease-do tauists and Baptists finally shake hands?. Trends Neurosci. 25 (2002) 22-26
    • (2002) Trends Neurosci. , vol.25 , pp. 22-26
    • Mudher, A.1    Lovestone, S.2
  • 36
    • 33644755673 scopus 로고    scopus 로고
    • Identification of amyloid-beta 1-42 binding protein fragments by screening of a human brain cDNA library
    • Munguia M.E., Govezensky T., Martinez R., Manoutcharian K., and Gevorkian G. Identification of amyloid-beta 1-42 binding protein fragments by screening of a human brain cDNA library. Neurosci. Lett. 397 (2006) 79-82
    • (2006) Neurosci. Lett. , vol.397 , pp. 79-82
    • Munguia, M.E.1    Govezensky, T.2    Martinez, R.3    Manoutcharian, K.4    Gevorkian, G.5
  • 38
    • 4344669435 scopus 로고    scopus 로고
    • Cell degeneration induced by amyloid-beta peptides: implications for Alzheimer's disease
    • Pereira C., Ferreiro E., Cardoso S.M., and de Oliveira C.R. Cell degeneration induced by amyloid-beta peptides: implications for Alzheimer's disease. J. Mol. Neurosci. 23 (2004) 97-104
    • (2004) J. Mol. Neurosci. , vol.23 , pp. 97-104
    • Pereira, C.1    Ferreiro, E.2    Cardoso, S.M.3    de Oliveira, C.R.4
  • 39
    • 16644396858 scopus 로고    scopus 로고
    • Interaction of Alzheimer's disease amyloid beta peptide fragment 25-35 with tau protein, and with a tau peptide containing the microtubule binding domain
    • Perez M., Cuadros R., Benitez M.J., and Jiménez J.S. Interaction of Alzheimer's disease amyloid beta peptide fragment 25-35 with tau protein, and with a tau peptide containing the microtubule binding domain. J. Alzheimer Dis. 6 (2004) 461-467
    • (2004) J. Alzheimer Dis. , vol.6 , pp. 461-467
    • Perez, M.1    Cuadros, R.2    Benitez, M.J.3    Jiménez, J.S.4
  • 40
    • 0026671781 scopus 로고
    • β-Amyloid induces neuritic dystrophy in vitro: similarities with Alzheimer pathology
    • Pike C.J., Cummings B.J., and Cotman C.W. β-Amyloid induces neuritic dystrophy in vitro: similarities with Alzheimer pathology. Neuroreport 3 (1992) 769-772
    • (1992) Neuroreport , vol.3 , pp. 769-772
    • Pike, C.J.1    Cummings, B.J.2    Cotman, C.W.3
  • 41
    • 0030049915 scopus 로고    scopus 로고
    • Filament heterogeneity within the dystrophic neuritis of senile plaques suggests blockage of fast axonal transport in Alzheimer's disease
    • Praprotnik D., Smith M.A., Richey P.L., Vinters H.V., and Perry G. Filament heterogeneity within the dystrophic neuritis of senile plaques suggests blockage of fast axonal transport in Alzheimer's disease. Acta Neuropathol. 91 (1996) 226-235
    • (1996) Acta Neuropathol. , vol.91 , pp. 226-235
    • Praprotnik, D.1    Smith, M.A.2    Richey, P.L.3    Vinters, H.V.4    Perry, G.5
  • 42
    • 33846785588 scopus 로고    scopus 로고
    • Microtubule-associated protein 1B, a growth-associated and phosphorylated scaffold protein
    • Riederer B.M. Microtubule-associated protein 1B, a growth-associated and phosphorylated scaffold protein. Brain Res. Bull. 71 (2007) 541-558
    • (2007) Brain Res. Bull. , vol.71 , pp. 541-558
    • Riederer, B.M.1
  • 44
    • 4644266301 scopus 로고    scopus 로고
    • Glutamate receptor-interacting protein 1 protein binds to the microtubule associated protein
    • Seog D.H. Glutamate receptor-interacting protein 1 protein binds to the microtubule associated protein. Biosci. Biotechnol. Biochem. 68 (2004) 1808-1810
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 1808-1810
    • Seog, D.H.1
  • 45
    • 0037474263 scopus 로고    scopus 로고
    • Apoptotic neuronal cell death induced by the non-fibrillar amyloid-β peptide proceeds through an early reactive oxygen species-dependent cytoskeleton perturbation
    • Sponne I., Fifre A., Drouet B., Klein C., Koziel V., Pincon-Raymond M., Olivier J.L., Chambaz J., and Pillot T. Apoptotic neuronal cell death induced by the non-fibrillar amyloid-β peptide proceeds through an early reactive oxygen species-dependent cytoskeleton perturbation. J. Biol. Chem. 278 (2003) 3437-3445
    • (2003) J. Biol. Chem. , vol.278 , pp. 3437-3445
    • Sponne, I.1    Fifre, A.2    Drouet, B.3    Klein, C.4    Koziel, V.5    Pincon-Raymond, M.6    Olivier, J.L.7    Chambaz, J.8    Pillot, T.9
  • 47
    • 0027102583 scopus 로고
    • Increased microtubule stability and alpha tubulin acetylation in cells transfected with microtubule-associated proteins MAP1B, MAP2 or tau
    • Takemura R., Okabe S., Umeyama T., Kanai Y., Cowan N.J., and Hirokawa N. Increased microtubule stability and alpha tubulin acetylation in cells transfected with microtubule-associated proteins MAP1B, MAP2 or tau. J. Cell Sci. 103 (1992) 953-964
    • (1992) J. Cell Sci. , vol.103 , pp. 953-964
    • Takemura, R.1    Okabe, S.2    Umeyama, T.3    Kanai, Y.4    Cowan, N.J.5    Hirokawa, N.6
  • 49
    • 0033912780 scopus 로고    scopus 로고
    • Evidence for expression of some microtubule-associated protein 1B in neurons as a plasma membrane glycoprotein
    • Tanner S., Franzen R., Jaffe H., and Quarles R.H. Evidence for expression of some microtubule-associated protein 1B in neurons as a plasma membrane glycoprotein. J. Neurochem. 75 (2000) 553-562
    • (2000) J. Neurochem. , vol.75 , pp. 553-562
    • Tanner, S.1    Franzen, R.2    Jaffe, H.3    Quarles, R.H.4
  • 50
    • 0024623621 scopus 로고
    • In situ localization of microtubule-associated protein mRNA in the developing and adult rat brain
    • Tucker R.P., Garner C.C., and Matus A. In situ localization of microtubule-associated protein mRNA in the developing and adult rat brain. Neuron 2 (1989) 1245-1256
    • (1989) Neuron , vol.2 , pp. 1245-1256
    • Tucker, R.P.1    Garner, C.C.2    Matus, A.3
  • 51
    • 0037414777 scopus 로고    scopus 로고
    • Overexpression of full-length but not N-terminal truncated isoform of microtubule-associated protein (MAP) 1B accelerates apoptosis of cultured cortical neurons
    • Uchida Y. Overexpression of full-length but not N-terminal truncated isoform of microtubule-associated protein (MAP) 1B accelerates apoptosis of cultured cortical neurons. J. Biol. Chem. 278 (2003) 366-371
    • (2003) J. Biol. Chem. , vol.278 , pp. 366-371
    • Uchida, Y.1
  • 52
    • 33746859735 scopus 로고    scopus 로고
    • Novel approaches for immunotherapeutic intervention in Alzheimer's disease
    • Vasilevko V., and Cribbs D.H. Novel approaches for immunotherapeutic intervention in Alzheimer's disease. Neurochem. Int. 49 (2006) 113-126
    • (2006) Neurochem. Int. , vol.49 , pp. 113-126
    • Vasilevko, V.1    Cribbs, D.H.2
  • 53
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer's disease
    • Walsh D.M., and Selkoe D.J. Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron 44 (2004) 181-193
    • (2004) Neuron , vol.44 , pp. 181-193
    • Walsh, D.M.1    Selkoe, D.J.2
  • 54
    • 0034609516 scopus 로고    scopus 로고
    • The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain
    • Walsh D.M., Tseng B.P., Rydel R.E., Podlisny M.B., and Selkoe D.J. The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain. Biochemistry 39 (2000) 10831-10839
    • (2000) Biochemistry , vol.39 , pp. 10831-10839
    • Walsh, D.M.1    Tseng, B.P.2    Rydel, R.E.3    Podlisny, M.B.4    Selkoe, D.J.5
  • 55
    • 7244236841 scopus 로고    scopus 로고
    • A modified beta-amyloid hypothesis: intraneuronal accumulation of the beta-amyloid peptide-the first step of a fatal cascade
    • Wirths O., Multhaup G., and Bayer T.A. A modified beta-amyloid hypothesis: intraneuronal accumulation of the beta-amyloid peptide-the first step of a fatal cascade. J. Neurochem. 91 (2004) 513-520
    • (2004) J. Neurochem. , vol.91 , pp. 513-520
    • Wirths, O.1    Multhaup, G.2    Bayer, T.A.3
  • 56
    • 20444441575 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and Alzheimer's disease: role of amyloid-beta peptide alcohol dehydrogenase (ABAD)
    • Yan S.D., and Stern D.M. Mitochondrial dysfunction and Alzheimer's disease: role of amyloid-beta peptide alcohol dehydrogenase (ABAD). Int. J. Exp. Pathol. 86 (2005) 161-171
    • (2005) Int. J. Exp. Pathol. , vol.86 , pp. 161-171
    • Yan, S.D.1    Stern, D.M.2
  • 58
    • 33845291088 scopus 로고    scopus 로고
    • Mitogen activated protein kinase and protein kinase c activation mediate promotion of sAPPa secretion by deprenyl
    • Yang H.Q., Ba M.W., Ren R.J., Zhang Y.H., Ma J.F., Pan J., Lu G.Q., and Chen S.D. Mitogen activated protein kinase and protein kinase c activation mediate promotion of sAPPa secretion by deprenyl. Neurochem. Int. 50 (2007) 74-82
    • (2007) Neurochem. Int. , vol.50 , pp. 74-82
    • Yang, H.Q.1    Ba, M.W.2    Ren, R.J.3    Zhang, Y.H.4    Ma, J.F.5    Pan, J.6    Lu, G.Q.7    Chen, S.D.8
  • 59
    • 27744485233 scopus 로고    scopus 로고
    • Impaired hippocampal long-term potentiation in microtubule-associated protein 1B-deficient mice
    • Zervas M., Opitz T., Edelmann W., Wainer B., Kucherlapati R., and Stanton P.K. Impaired hippocampal long-term potentiation in microtubule-associated protein 1B-deficient mice. J. Neurosci. Res. 82 (2005) 83-92
    • (2005) J. Neurosci. Res. , vol.82 , pp. 83-92
    • Zervas, M.1    Opitz, T.2    Edelmann, W.3    Wainer, B.4    Kucherlapati, R.5    Stanton, P.K.6
  • 60
    • 0027988046 scopus 로고
    • Focal adhesion kinase expressed by nerve cell lines shows increased tyrosine phosporylation in response to Alzheimer's A beta peptide
    • Zhang C., Lambert M.P., Bunch C., Barber K., Wade W.S., Krafft G.A., and Klein W.L. Focal adhesion kinase expressed by nerve cell lines shows increased tyrosine phosporylation in response to Alzheimer's A beta peptide. J. Biol. Chem. 269 (1994) 25247-25250
    • (1994) J. Biol. Chem. , vol.269 , pp. 25247-25250
    • Zhang, C.1    Lambert, M.P.2    Bunch, C.3    Barber, K.4    Wade, W.S.5    Krafft, G.A.6    Klein, W.L.7


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