메뉴 건너뛰기




Volumn 114, Issue 1, 2002, Pages 265-273

Characterization of neuronal dystrophy induced by fibrillar amyloid β: Implications for Alzheimer's disease

Author keywords

Amyloid plaques; Cell adhesion; Cortical cultures; Neuronal plasticity; Neurotoxicity; Synaptic density

Indexed keywords

AMYLOID BETA PROTEIN;

EID: 0037130570     PISSN: 03064522     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0306-4522(02)00241-5     Document Type: Article
Times cited : (151)

References (51)
  • 1
    • 0031745571 scopus 로고    scopus 로고
    • Signal transduction and signal modulation by cell adhesion receptors: The role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins
    • Aplin A.E., Howe A., Alahari S.K., Juliano R.L. Signal transduction and signal modulation by cell adhesion receptors: the role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins. Pharmacol. Rev. 50:1998;197-263.
    • (1998) Pharmacol. Rev. , vol.50 , pp. 197-263
    • Aplin, A.E.1    Howe, A.2    Alahari, S.K.3    Juliano, R.L.4
  • 2
    • 0027757042 scopus 로고
    • Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5
    • Baumann K., Mandelkow E.M., Biernat J., Piwnica-Worms H., Mandelkow E. Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5. FEBS Lett. 336:1993;417-424.
    • (1993) FEBS Lett. , vol.336 , pp. 417-424
    • Baumann, K.1    Mandelkow, E.M.2    Biernat, J.3    Piwnica-Worms, H.4    Mandelkow, E.5
  • 3
    • 0027518937 scopus 로고
    • Alzheimer's disease-like dystrophic neurites characteristically associated with senile plaques are not found within other neurodegenerative diseases unless amyloid beta-protein deposition is present
    • Benzing W.C., Mufson E.J., Armstrong D.M. Alzheimer's disease-like dystrophic neurites characteristically associated with senile plaques are not found within other neurodegenerative diseases unless amyloid beta-protein deposition is present. Brain Res. 606:1993;10-18.
    • (1993) Brain Res. , vol.606 , pp. 10-18
    • Benzing, W.C.1    Mufson, E.J.2    Armstrong, D.M.3
  • 4
    • 0031467020 scopus 로고    scopus 로고
    • Rapid impact of beta-amyloid on paxillin in a neural cell line
    • Berg M.M., Krafft G.A., Klein W.L. Rapid impact of beta-amyloid on paxillin in a neural cell line. J. Neurosci. Res. 50:1997;979-989.
    • (1997) J. Neurosci. Res. , vol.50 , pp. 979-989
    • Berg, M.M.1    Krafft, G.A.2    Klein, W.L.3
  • 5
    • 0027407570 scopus 로고
    • Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells
    • Busciglio J., Gabuzda D.H., Matsudaira P., Yankner B.A. Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells. Proc. Natl. Acad. Sci. USA. 90:1993;2092-2096.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2092-2096
    • Busciglio, J.1    Gabuzda, D.H.2    Matsudaira, P.3    Yankner, B.A.4
  • 6
    • 0026756887 scopus 로고
    • Methodological variables in the assessment of beta amyloid neurotoxicity
    • Busciglio J., Lorenzo A., Yankner B.A. Methodological variables in the assessment of beta amyloid neurotoxicity. Neurobiol. Aging. 13:1992;609-612.
    • (1992) Neurobiol. Aging , vol.13 , pp. 609-612
    • Busciglio, J.1    Lorenzo, A.2    Yankner, B.A.3
  • 7
    • 0029417023 scopus 로고
    • Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro
    • Busciglio J., Yankner B.A. Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro. Nature. 378:1995;776-779.
    • (1995) Nature , vol.378 , pp. 776-779
    • Busciglio, J.1    Yankner, B.A.2
  • 8
    • 0028986916 scopus 로고
    • β-amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio J., Lorenzo A., Yeh J., Yankner B.A. β-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
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X., Sudhof T.C. A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60. Science. 293:2001;115-120.
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 10
    • 0034512244 scopus 로고    scopus 로고
    • The brain's microenvironment, early functional loss, and the conversion to Alzheimer's disease
    • Cotman C.W., Anderson A.J. The brain's microenvironment, early functional loss, and the conversion to Alzheimer's disease. Ann. NY Acad. Sci. 924:2000;112-116.
    • (2000) Ann. NY Acad. Sci. , vol.924 , pp. 112-116
    • Cotman, C.W.1    Anderson, A.J.2
  • 11
    • 0032144786 scopus 로고    scopus 로고
    • Cell adhesion molecules in neural plasticity and pathology: Similar mechanisms, distinct organizations?
    • Cotman C.W., Hailer N.P., Pfister K.K., Soltesz I., Schachner M. Cell adhesion molecules in neural plasticity and pathology: similar mechanisms, distinct organizations? Prog. Neurobiol. 55:1998;659-669.
    • (1998) Prog. Neurobiol. , vol.55 , pp. 659-669
    • Cotman, C.W.1    Hailer, N.P.2    Pfister, K.K.3    Soltesz, I.4    Schachner, M.5
  • 12
    • 0034329543 scopus 로고    scopus 로고
    • Phosphorylation of human tau protein by microtubule-associated kinases: GSK3beta and cdk5 are key participants
    • Flaherty D.B., Soria J.P., Tomasiewicz H.G., Wood J.G. Phosphorylation of human tau protein by microtubule-associated kinases: GSK3beta and cdk5 are key participants. J. Neurosci. Res. 62:2000;463-472.
    • (2000) J. Neurosci. Res. , vol.62 , pp. 463-472
    • Flaherty, D.B.1    Soria, J.P.2    Tomasiewicz, H.G.3    Wood, J.G.4
  • 13
    • 0035477020 scopus 로고    scopus 로고
    • GSK3 takes centre stage more than 20 years after its discovery
    • Frame S., Cohen P. GSK3 takes centre stage more than 20 years after its discovery. Biochem. J. 359:2001;1-16.
    • (2001) Biochem. J. , vol.359 , pp. 1-16
    • Frame, S.1    Cohen, P.2
  • 14
    • 0022891348 scopus 로고
    • Senile plaques as aberrant sprout-stimulating structures
    • Geddes J.W., Anderson K.J., Cotman C.W. Senile plaques as aberrant sprout-stimulating structures. Exp. Neurol. 94:1986;767-776.
    • (1986) Exp. Neurol. , vol.94 , pp. 767-776
    • Geddes, J.W.1    Anderson, K.J.2    Cotman, C.W.3
  • 15
    • 0031824782 scopus 로고    scopus 로고
    • Aging renders the brain vulnerable to amyloid beta-protein neurotoxicity
    • Geula C., Wu C.K., Saroff D., Lorenzo A., Yuan M., Yankner B.A. Aging renders the brain vulnerable to amyloid beta-protein neurotoxicity. Nature Med. 4:1998;827-831.
    • (1998) Nature Med. , vol.4 , pp. 827-831
    • Geula, C.1    Wu, C.K.2    Saroff, D.3    Lorenzo, A.4    Yuan, M.5    Yankner, B.A.6
  • 16
    • 0027082156 scopus 로고
    • A 109-amino-acid C-terminal fragment of Alzheimer's-disease amyloid precursor protein contains a sequence, -RHDS-, that promotes cell adhesion
    • Ghiso J., Rostagno A., Gardella J.E., Liem L., Gorevic P.D., Frangione B. A 109-amino-acid C-terminal fragment of Alzheimer's-disease amyloid precursor protein contains a sequence, -RHDS-, that promotes cell adhesion. Biochem. J. 288:1992;1053-1059.
    • (1992) Biochem. J. , vol.288 , pp. 1053-1059
    • Ghiso, J.1    Rostagno, A.2    Gardella, J.E.3    Liem, L.4    Gorevic, P.D.5    Frangione, B.6
  • 17
    • 0005144326 scopus 로고    scopus 로고
    • Focal adhesion proteins are involved in Aβ-induced neuronal dystrophy
    • Grace E., Busciglio J. Focal adhesion proteins are involved in Aβ-induced neuronal dystrophy. Abstr. Soc. Neurosci. 26:2000;1786.
    • (2000) Abstr. Soc. Neurosci. , vol.26 , pp. 1786
    • Grace, E.1    Busciglio, J.2
  • 18
    • 0034869176 scopus 로고    scopus 로고
    • Protofibrils, the unifying toxic molecule of neurodegenerative disorders?
    • Haass C., Steiner H. Protofibrils, the unifying toxic molecule of neurodegenerative disorders? Nature Neurosci. 4:2001;859-860.
    • (2001) Nature Neurosci. , vol.4 , pp. 859-860
    • Haass, C.1    Steiner, H.2
  • 19
    • 0034056731 scopus 로고    scopus 로고
    • Synapse formation proceeds independently of dendritic elongation in cultured hippocampal neurons
    • Holgado A., Ferreira A. Synapse formation proceeds independently of dendritic elongation in cultured hippocampal neurons. J. Neurobiol. 43:2000;121-131.
    • (2000) J. Neurobiol. , vol.43 , pp. 121-131
    • Holgado, A.1    Ferreira, A.2
  • 21
    • 0034682788 scopus 로고    scopus 로고
    • Inhibition of toxicity in the beta-amyloid peptide fragment beta-(25-35) using N-methylated derivatives: A general strategy to prevent amyloid formation
    • Hughes E., Burke R.M., Doig A.J. Inhibition of toxicity in the beta-amyloid peptide fragment beta-(25-35) using N-methylated derivatives: a general strategy to prevent amyloid formation. J. Biol. Chem. 275:2000;25109-25115.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25109-25115
    • Hughes, E.1    Burke, R.M.2    Doig, A.J.3
  • 22
    • 0030612033 scopus 로고    scopus 로고
    • APPSw transgenic mice develop age-related A beta deposits and neuropil abnormalities, but no neuronal loss in CA1
    • Irizarry M.C., McNamara M., Fedorchak K., Hsiao K., Hyman B.T. APPSw transgenic mice develop age-related A beta deposits and neuropil abnormalities, but no neuronal loss in CA1. J. Neuropathol. Exp. Neurol. 56:1997;965-973.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 965-973
    • Irizarry, M.C.1    McNamara, M.2    Fedorchak, K.3    Hsiao, K.4    Hyman, B.T.5
  • 23
    • 0032433258 scopus 로고    scopus 로고
    • Beta-amyloid induces local neurite degeneration in cultured hippocampal neurons: Evidence for neuritic apoptosis
    • Ivins K.J., Bui E.T., Cotman C.W. Beta-amyloid induces local neurite degeneration in cultured hippocampal neurons: evidence for neuritic apoptosis. Neurobiol. Dis. 5:1998;365-378.
    • (1998) Neurobiol. Dis. , vol.5 , pp. 365-378
    • Ivins, K.J.1    Bui, E.T.2    Cotman, C.W.3
  • 24
    • 0027459771 scopus 로고
    • Signal transduction from the extracellular matrix
    • Juliano R.L., Haskill S. Signal transduction from the extracellular matrix. J. Cell Biol. 120:1993;577-585.
    • (1993) J. Cell Biol. , vol.120 , pp. 577-585
    • Juliano, R.L.1    Haskill, S.2
  • 25
    • 0027288860 scopus 로고
    • Amyloid beta-protein as a substrate interacts with extracellular matrix to promote neurite outgrowth
    • Koo E.H., Park L., Selkoe D.J. Amyloid beta-protein as a substrate interacts with extracellular matrix to promote neurite outgrowth. Proc. Natl. Acad. Sci. USA. 90:1993;4748-4752.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4748-4752
    • Koo, E.H.1    Park, L.2    Selkoe, D.J.3
  • 26
    • 0034663040 scopus 로고    scopus 로고
    • Integrin alpha(1) beta(1)-mediated activation of cyclin-dependent kinase 5 activity is involved in neurite outgrowth and human neurofilament protein H Lys-Ser-Pro tail domain phosphorylation
    • Li B.S., Zhang L., Gu J., Amin N.D., Pant H.C. Integrin alpha(1) beta(1)-mediated activation of cyclin-dependent kinase 5 activity is involved in neurite outgrowth and human neurofilament protein H Lys-Ser-Pro tail domain phosphorylation. J. Neurosci. 20:2000;6055-6062.
    • (2000) J. Neurosci. , vol.20 , pp. 6055-6062
    • Li, B.S.1    Zhang, L.2    Gu, J.3    Amin, N.D.4    Pant, H.C.5
  • 27
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • Lorenzo A., Yankner B.A. Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc. Natl. Acad. Sci. USA. 91:1994;12243-12247.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 31
    • 0025330775 scopus 로고
    • Quantitative immunohistochemistry of synaptophysin in human neocortex: An alternative method to estimate density of presynaptic terminals in paraffin sections
    • Masliah E., Terry R.D., Alford M., DeTeresa R. Quantitative immunohistochemistry of synaptophysin in human neocortex: an alternative method to estimate density of presynaptic terminals in paraffin sections. J. Histochem. Cytochem. 38:1990;837-844.
    • (1990) J. Histochem. Cytochem. , vol.38 , pp. 837-844
    • Masliah, E.1    Terry, R.D.2    Alford, M.3    DeTeresa, R.4
  • 32
    • 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. 12:1992;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
  • 33
    • 0033215252 scopus 로고    scopus 로고
    • 'Apoptotic' biochemical cascades in synaptic compartments: Roles in adaptive plasticity and neurodegenerative disorders
    • Mattson M.P., Duan W. 'Apoptotic' biochemical cascades in synaptic compartments: roles in adaptive plasticity and neurodegenerative disorders. J. Neurosci. Res. 58:1999;152-166.
    • (1999) J. Neurosci. Res. , vol.58 , pp. 152-166
    • Mattson, M.P.1    Duan, W.2
  • 34
    • 0032487648 scopus 로고    scopus 로고
    • Amyloid beta-peptide induces apoptosis-related events in synapses and dendrites
    • Mattson M.P., Partin J., Begley J.G. Amyloid beta-peptide induces apoptosis-related events in synapses and dendrites. Brain Res. 807:1998;167-176.
    • (1998) Brain Res. , vol.807 , pp. 167-176
    • Mattson, M.P.1    Partin, J.2    Begley, J.G.3
  • 35
    • 0033230623 scopus 로고    scopus 로고
    • Neuroplasticity failure in Alzheimer's disease: Bridging the gap between plaques and tangles
    • Mesulam M.M. Neuroplasticity failure in Alzheimer's disease: bridging the gap between plaques and tangles. Neuron. 24:1999;521-529.
    • (1999) Neuron , vol.24 , pp. 521-529
    • Mesulam, M.M.1
  • 37
    • 0032578024 scopus 로고    scopus 로고
    • Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration
    • Pei J.J., Grundke-Iqbal I., Iqbal K., Bogdanovic N., Winblad B., Cowburn R.F. Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration. Brain Res. 797:1998;267-277.
    • (1998) Brain Res. , vol.797 , pp. 267-277
    • Pei, J.J.1    Grundke-Iqbal, I.2    Iqbal, K.3    Bogdanovic, N.4    Winblad, B.5    Cowburn, R.F.6
  • 38
    • 0033215972 scopus 로고    scopus 로고
    • Cerebral amyloid induces aberrant axonal sprouting and ectopic terminal formation in amyloid precursor protein transgenic mice
    • Phinney A.L., Deller T., Stalder M., Calhoun M.E., Frotscher M., Sommer B., Staufenbiel M., Jucker M. Cerebral amyloid induces aberrant axonal sprouting and ectopic terminal formation in amyloid precursor protein transgenic mice. J. Neurosci. 19:1999;8552-8559.
    • (1999) J. Neurosci. , vol.19 , pp. 8552-8559
    • Phinney, A.L.1    Deller, T.2    Stalder, M.3    Calhoun, M.E.4    Frotscher, M.5    Sommer, B.6    Staufenbiel, M.7    Jucker, M.8
  • 39
    • 0035116513 scopus 로고    scopus 로고
    • Presenilin-1 mutations reduce cytoskeletal association, deregulate neurite growth, and potentiate neuronal dystrophy and tau phosphorylation
    • Pigino G., Pelsman A., Mori H., Busciglio J. Presenilin-1 mutations reduce cytoskeletal association, deregulate neurite growth, and potentiate neuronal dystrophy and tau phosphorylation. J. Neurosci. 21:2001;834-842.
    • (2001) J. Neurosci. , vol.21 , pp. 834-842
    • Pigino, G.1    Pelsman, A.2    Mori, H.3    Busciglio, J.4
  • 40
    • 0026671781 scopus 로고
    • Beta-Amyloid induces neuritic dystrophy in vitro: Similarities with Alzheimer pathology
    • Pike C.J., Cummings B.J., Cotman C.W. beta-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
    • 0025733411 scopus 로고
    • Aggregation-related toxicity of synthetic beta-amyloid protein in hippocampal cultures
    • Pike C.J., Walencewicz A.J., Glabe C.G., Cotman C.W. Aggregation-related toxicity of synthetic beta-amyloid protein in hippocampal cultures. Eur. J. Pharmacol. 207:1991;367-368.
    • (1991) Eur. J. Pharmacol. , vol.207 , pp. 367-368
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 42
    • 0028944873 scopus 로고
    • Interaction of beta-amyloid peptides with integrins in a human nerve cell line
    • Sabo S., Lambert M.P., Kessey K., Wade W., Krafft G., Klein W.L. Interaction of beta-amyloid peptides with integrins in a human nerve cell line. Neurosci. Lett. 184:1995;25-28.
    • (1995) Neurosci. Lett. , vol.184 , pp. 25-28
    • Sabo, S.1    Lambert, M.P.2    Kessey, K.3    Wade, W.4    Krafft, G.5    Klein, W.L.6
  • 43
    • 0028799897 scopus 로고
    • Coagulation factor XIa cleaves the RHDS sequence and abolishes the cell adhesive properties of the amyloid beta-protein
    • Saporito-Irwin S.M., Van Nostrand W.E. Coagulation factor XIa cleaves the RHDS sequence and abolishes the cell adhesive properties of the amyloid beta-protein. J. Biol. Chem. 270:1995;26265-26269.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26265-26269
    • Saporito-Irwin, S.M.1    Van Nostrand, W.E.2
  • 44
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe D.J. The molecular pathology of Alzheimer's disease. Neuron. 6:1991;487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 45
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81:2001;741-766.
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 46
    • 0031898770 scopus 로고    scopus 로고
    • The role of the amyloid protein precursor (APP) in Alzheimer's disease: Does the normal function of APP explain the topography of neurodegeneration?
    • Small D.H. The role of the amyloid protein precursor (APP) in Alzheimer's disease: does the normal function of APP explain the topography of neurodegeneration? Neurochem. Res. 23:1998;795-806.
    • (1998) Neurochem. Res. , vol.23 , pp. 795-806
    • Small, D.H.1
  • 47
    • 0033987059 scopus 로고    scopus 로고
    • Cdk5 and munc-18/p67 co-localization in early stage neurofibrillary tangles-bearing neurons in Alzheimer type dementia brains
    • Takahashi M., Iseki E., Kosaka K. Cdk5 and munc-18/p67 co-localization in early stage neurofibrillary tangles-bearing neurons in Alzheimer type dementia brains. J. Neurol. Sci. 172:2000;63-69.
    • (2000) J. Neurol. Sci. , vol.172 , pp. 63-69
    • Takahashi, M.1    Iseki, E.2    Kosaka, K.3
  • 48
    • 0029737421 scopus 로고    scopus 로고
    • Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3 beta and cyclin-dependent kinase 5, a component of TPK II
    • Yamaguchi H., Ishiguro K., Uchida T., Takashima A., Lemere C.A., Imahori K. Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3 beta and cyclin-dependent kinase 5, a component of TPK II. Acta Neuropathol. 92:1996;232-241.
    • (1996) Acta Neuropathol. , vol.92 , pp. 232-241
    • Yamaguchi, H.1    Ishiguro, K.2    Uchida, T.3    Takashima, A.4    Lemere, C.A.5    Imahori, K.6
  • 49
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • Yankner B.A., Duffy L.K., Kirschner D.A. Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides. Science. 250:1990;279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 50
    • 0027988046 scopus 로고
    • Focal adhesion kinase expressed by nerve cell lines shows increased tyrosine phosphorylation in response to Alzheimer's A beta peptide
    • Zhang C., Lambert M.P., Bunch C., Barber K., Wade W.S., Krafft G.A., Klein W.L. Focal adhesion kinase expressed by nerve cell lines shows increased tyrosine phosphorylation 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
  • 51
    • 0030604667 scopus 로고    scopus 로고
    • A beta peptide enhances focal adhesion kinase/Fyn association in a rat CNS nerve cell line
    • Zhang C., Qiu H.E., Krafft G.A., Klein W.L. A beta peptide enhances focal adhesion kinase/Fyn association in a rat CNS nerve cell line. Neurosci. Lett. 211:1996;187-190.
    • (1996) Neurosci. Lett. , vol.211 , pp. 187-190
    • Zhang, C.1    Qiu, H.E.2    Krafft, G.A.3    Klein, W.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.