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Volumn 146, Issue 4, 2007, Pages 1640-1651

Retracted: "Oxidative damage of 14-3-3 zeta and gamma isoforms in Alzheimer's disease and cerebral amyloid angiopathy" [Neuroscience 146 (2007) 1640-1651] (DOI:10.1016/j.neuroscience.2007.03.013);Oxidative damage of 14-3-3 zeta and gamma isoforms in Alzheimer's disease and cerebral amyloid angiopathy

Author keywords

14 3 3; Alzheimer's disease; A ; cerebral amyloid angiopathy; lipoxidation; oxidative stress

Indexed keywords

4 HYDROXYNONENAL; MALONALDEHYDE;

EID: 34249314785     PISSN: 03064522     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuroscience.2009.05.001     Document Type: Erratum
Times cited : (14)

References (55)
  • 1
    • 0037631324 scopus 로고    scopus 로고
    • 14-3-3 Connects glycogen synthase kinase-3 beta to tau within a brain microtubule-associated tau phosphorylation complex
    • Agarwal-Mawal A., Qureshi H.Y., Cafferty P.W., Yuan Z., Han D., Lin R., and Paudel H.K. 14-3-3 Connects glycogen synthase kinase-3 beta to tau within a brain microtubule-associated tau phosphorylation complex. J Biol Chem 278 (2003) 12722-12728
    • (2003) J Biol Chem , vol.278 , pp. 12722-12728
    • Agarwal-Mawal, A.1    Qureshi, H.Y.2    Cafferty, P.W.3    Yuan, Z.4    Han, D.5    Lin, R.6    Paudel, H.K.7
  • 2
    • 33646926129 scopus 로고    scopus 로고
    • 14-3-3 Proteins: a historic overview
    • Aitken A. 14-3-3 Proteins: a historic overview. Semin Cancer Biol 16 (2006) 162-172
    • (2006) Semin Cancer Biol , vol.16 , pp. 162-172
    • Aitken, A.1
  • 3
    • 0035208849 scopus 로고    scopus 로고
    • Activation of the JNK/p38 pathway occurs in diseases characterized by tau protein pathology and is related to tau phosphorylation but not to apoptosis
    • Atzori C., Ghetti B., Piva R., Srinivasan A.N., Zolo P., Delisle M.B., Mirra S.S., and Migheli A. Activation of the JNK/p38 pathway occurs in diseases characterized by tau protein pathology and is related to tau phosphorylation but not to apoptosis. J Neuropathol Exp Neurol 60 (2001) 1190-1197
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 1190-1197
    • Atzori, C.1    Ghetti, B.2    Piva, R.3    Srinivasan, A.N.4    Zolo, P.5    Delisle, M.B.6    Mirra, S.S.7    Migheli, A.8
  • 4
    • 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
  • 5
    • 0141722623 scopus 로고    scopus 로고
    • 14-3-3 Proteins in the nervous system
    • Berg D., Holzmann C., and Riess O. 14-3-3 Proteins in the nervous system. Nat Rev Neurosci 4 (2003) 752-762
    • (2003) Nat Rev Neurosci , vol.4 , pp. 752-762
    • Berg, D.1    Holzmann, C.2    Riess, O.3
  • 6
    • 15744387176 scopus 로고    scopus 로고
    • Proteomic identification of proteins specifically oxidized by intracerebral injection of amyloid β-peptide (1-42) into rat brain: implications for Alzheimer's disease
    • Boyd-Kimball D., Sultana R., Fai Poon H., Lynn B.C., Casamenti F., Pepeu G., Klein J.B., and Butterfield D.A. Proteomic identification of proteins specifically oxidized by intracerebral injection of amyloid β-peptide (1-42) into rat brain: implications for Alzheimer's disease. Neuroscience 132 (2005) 313-324
    • (2005) Neuroscience , vol.132 , pp. 313-324
    • Boyd-Kimball, D.1    Sultana, R.2    Fai Poon, H.3    Lynn, B.C.4    Casamenti, F.5    Pepeu, G.6    Klein, J.B.7    Butterfield, D.A.8
  • 8
    • 33644877400 scopus 로고    scopus 로고
    • 14-3-3 Proteins: a number of functions for a numbered protein
    • 2005: re10
    • Bridges D., and Moorhead G.B. 14-3-3 Proteins: a number of functions for a numbered protein. Sci STKE (2005) 2005: re10
    • (2005) Sci STKE
    • Bridges, D.1    Moorhead, G.B.2
  • 9
    • 0033850407 scopus 로고    scopus 로고
    • Tau protein isoforms, phosphorylation and role in neurodegenerative disorders
    • Buee L., Bussiere T., Buee-Scherrer V., Delacourte A., and Hof P.R. Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res Rev 33 (2000) 95-130
    • (2000) Brain Res Rev , vol.33 , pp. 95-130
    • Buee, L.1    Bussiere, T.2    Buee-Scherrer, V.3    Delacourte, A.4    Hof, P.R.5
  • 10
    • 0344824654 scopus 로고    scopus 로고
    • Amyloid beta-peptide (1-42)-associated free radical-induced oxidative stress and neurodegeneration in Alzheimer's disease brain: mechanisms and consequences
    • Butterfield D.A. Amyloid beta-peptide (1-42)-associated free radical-induced oxidative stress and neurodegeneration in Alzheimer's disease brain: mechanisms and consequences. Curr Med Chem 10 (2003) 2651-2659
    • (2003) Curr Med Chem , vol.10 , pp. 2651-2659
    • Butterfield, D.A.1
  • 11
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzheimer's disease brain: central role for β-amyloid peptide
    • Butterfield D.A., Drake J., Pocernich C., and Castegna A. Evidence of oxidative damage in Alzheimer's disease brain: central role for β-amyloid peptide. Trends Mol Med 7 (2001) 548-554
    • (2001) Trends Mol Med , vol.7 , pp. 548-554
    • Butterfield, D.A.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 12
    • 0036591849 scopus 로고    scopus 로고
    • Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress
    • Butterfield D.A., and Lauderback C.M. Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress. Free Rad Biol Med 32 (2002) 1050-1060
    • (2002) Free Rad Biol Med , vol.32 , pp. 1050-1060
    • Butterfield, D.A.1    Lauderback, C.M.2
  • 13
    • 33747036919 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease brain: New insights from redox proteomics
    • Butterfield D.A., Perluigi M., and Sultana R. Oxidative stress in Alzheimer's disease brain: New insights from redox proteomics. Eur J Pharmacol 545 (2006) 39-50
    • (2006) Eur J Pharmacol , vol.545 , pp. 39-50
    • Butterfield, D.A.1    Perluigi, M.2    Sultana, R.3
  • 15
    • 33745727582 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease
    • Chauhan V., and Chauhan A. Oxidative stress in Alzheimer's disease. Pathophysiology 3 (2006) 195-208
    • (2006) Pathophysiology , vol.3 , pp. 195-208
    • Chauhan, V.1    Chauhan, A.2
  • 16
    • 33344470872 scopus 로고    scopus 로고
    • C-terminal binding: an expanded repertoire and function of 14-3-3 proteins
    • Coblitz B., Wu M., Shikano S., and Li M. C-terminal binding: an expanded repertoire and function of 14-3-3 proteins. FEBS Lett 580 (2006) 1531-1535
    • (2006) FEBS Lett , vol.580 , pp. 1531-1535
    • Coblitz, B.1    Wu, M.2    Shikano, S.3    Li, M.4
  • 17
    • 25144441037 scopus 로고    scopus 로고
    • Role of 14-3-3 proteins in eukaryotic signaling and development
    • Darling D.L., Yingling J., and Wynshaw-Boris A. Role of 14-3-3 proteins in eukaryotic signaling and development. Curr Top Dev Biol 68 (2005) 281-315
    • (2005) Curr Top Dev Biol , vol.68 , pp. 281-315
    • Darling, D.L.1    Yingling, J.2    Wynshaw-Boris, A.3
  • 18
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • Davies K.J. Degradation of oxidized proteins by the 20S proteasome. Biochimie 83 (2001) 301-310
    • (2001) Biochimie , vol.83 , pp. 301-310
    • Davies, K.J.1
  • 19
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals. I. general aspects
    • Davies K.J. Protein damage and degradation by oxygen radicals. I. general aspects. J Biol Chem 262 (1987) 9895-9901
    • (1987) J Biol Chem , vol.262 , pp. 9895-9901
    • Davies, K.J.1
  • 20
    • 2942552470 scopus 로고    scopus 로고
    • Unlocking the code 14-3-3
    • Dougherty M.K., and Morrison D.K. Unlocking the code 14-3-3. J Cell Sci 117 (2004) 1875-1884
    • (2004) J Cell Sci , vol.117 , pp. 1875-1884
    • Dougherty, M.K.1    Morrison, D.K.2
  • 21
    • 12244281810 scopus 로고    scopus 로고
    • Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid beta-peptide1-42 in a transgenic Caenorhabditis elegans model
    • Drake J., Link C.D., and Butterfied D.A. Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid beta-peptide1-42 in a transgenic Caenorhabditis elegans model. Neurobiol Aging 24 (2003) 415-420
    • (2003) Neurobiol Aging , vol.24 , pp. 415-420
    • Drake, J.1    Link, C.D.2    Butterfied, D.A.3
  • 24
    • 0035659377 scopus 로고    scopus 로고
    • Phosphorylated mitogen-activated protein kinase (MAPK/ERK-P), protein kinase of 38 kDa (p38-P), stress-activated protein kinase (SAPK/JNK-P), and calcium/calmodulin-dependent kinase II (CaM kinase II) are differentially expressed in tau deposits in neurons and glial cells in tauopathies
    • Ferrer I., Blanco R., Carmona M., and Puig B. Phosphorylated mitogen-activated protein kinase (MAPK/ERK-P), protein kinase of 38 kDa (p38-P), stress-activated protein kinase (SAPK/JNK-P), and calcium/calmodulin-dependent kinase II (CaM kinase II) are differentially expressed in tau deposits in neurons and glial cells in tauopathies. J Neural Transm 108 (2001) 1397-1415
    • (2001) J Neural Transm , vol.108 , pp. 1397-1415
    • Ferrer, I.1    Blanco, R.2    Carmona, M.3    Puig, B.4
  • 25
    • 25844458239 scopus 로고    scopus 로고
    • Current advances on different kinases involved in tau phosphorylation, and implications in Alzheimer's disease and tauopathies
    • Ferrer I., Gomez-Isla T., Puig B., Freixes M., Ribe E., Dalfó E., and Avila J. Current advances on different kinases involved in tau phosphorylation, and implications in Alzheimer's disease and tauopathies. Curr Alzheimer Res 2 (2005) 3-18
    • (2005) Curr Alzheimer Res , vol.2 , pp. 3-18
    • Ferrer, I.1    Gomez-Isla, T.2    Puig, B.3    Freixes, M.4    Ribe, E.5    Dalfó, E.6    Avila, J.7
  • 26
    • 0032585827 scopus 로고    scopus 로고
    • Increased levels of 14-3-3 gamma and epsilon proteins in brain of patients with Alzheimer's disease and Down syndrome
    • Fountoulakis M., Cairns N., and Lubec G. Increased levels of 14-3-3 gamma and epsilon proteins in brain of patients with Alzheimer's disease and Down syndrome. J Neural Transm Suppl 57 (1999) 323-335
    • (1999) J Neural Transm Suppl , vol.57 , pp. 323-335
    • Fountoulakis, M.1    Cairns, N.2    Lubec, G.3
  • 27
    • 0034117078 scopus 로고    scopus 로고
    • Masters, 14-3-3 proteins: structure, function, and regulation
    • Fu R.R., and Subramanian S.C. Masters, 14-3-3 proteins: structure, function, and regulation. Annu Rev Pharmacol Toxicol 40 (2000) 617-647
    • (2000) Annu Rev Pharmacol Toxicol , vol.40 , pp. 617-647
    • Fu, R.R.1    Subramanian, S.C.2
  • 28
    • 84961061408 scopus 로고
    • Radiation-induced oxidation of protein in aqueous solution
    • Garrison W.M., Jayko M.E., and Bennet W. Radiation-induced oxidation of protein in aqueous solution. Radiat Res 16 (1962) 483-502
    • (1962) Radiat Res , vol.16 , pp. 483-502
    • Garrison, W.M.1    Jayko, M.E.2    Bennet, W.3
  • 29
    • 0034682667 scopus 로고    scopus 로고
    • 14-3-3 Zeta is an effector of tau protein phosphorylation
    • Hashiguchi M., Sobue K., and Paudel H.K. 14-3-3 Zeta is an effector of tau protein phosphorylation. J Biol Chem 275 (2000) 25247-25254
    • (2000) J Biol Chem , vol.275 , pp. 25247-25254
    • Hashiguchi, M.1    Sobue, K.2    Paudel, H.K.3
  • 30
    • 33744544172 scopus 로고    scopus 로고
    • 14-3-3 Proteins in cell cycle regulation
    • Hermeking H., and Benzinger A. 14-3-3 Proteins in cell cycle regulation. Semin Cancer Biol 16 (2006) 183-192
    • (2006) Semin Cancer Biol , vol.16 , pp. 183-192
    • Hermeking, H.1    Benzinger, A.2
  • 31
    • 1242337344 scopus 로고    scopus 로고
    • Zeta 14-3-3 protein favors the formation of human tau fibrillar polymers
    • Hernández F., Cuadros R., and Avila J. Zeta 14-3-3 protein favors the formation of human tau fibrillar polymers. Neurosci Lett 357 (2004) 143-146
    • (2004) Neurosci Lett , vol.357 , pp. 143-146
    • Hernández, F.1    Cuadros, R.2    Avila, J.3
  • 32
  • 35
    • 24344460521 scopus 로고    scopus 로고
    • 14-3-3 Proteins. An update
    • Mhawech P. 14-3-3 Proteins. An update. Cell Res 15 (2005) 228-236
    • (2005) Cell Res , vol.15 , pp. 228-236
    • Mhawech, P.1
  • 36
    • 15944412545 scopus 로고    scopus 로고
    • The protective role of vitamin E in vascular amyloid beta-mediated damage
    • Muñoz F.J., Sole M., and Coma M. The protective role of vitamin E in vascular amyloid beta-mediated damage. Subcell Biochem 38 (2005) 147-165
    • (2005) Subcell Biochem , vol.38 , pp. 147-165
    • Muñoz, F.J.1    Sole, M.2    Coma, M.3
  • 37
    • 15544385930 scopus 로고    scopus 로고
    • Differential functions of 14-3-3 isoforms in vertebrate development
    • Muslin A.J., and Lau J.M. Differential functions of 14-3-3 isoforms in vertebrate development. Curr Top Dev Biol 65 (2005) 211-228
    • (2005) Curr Top Dev Biol , vol.65 , pp. 211-228
    • Muslin, A.J.1    Lau, J.M.2
  • 41
    • 20444373701 scopus 로고    scopus 로고
    • Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation. Effects of Alzheimer disease and identification of lipoxidation targets
    • Pamplona R., Dalfó E., Ayala V., Bellmunt J., Prat J., Ferrer I., and Portero M. Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation. Effects of Alzheimer disease and identification of lipoxidation targets. J Biol Chem 280 (2005) 21522-21530
    • (2005) J Biol Chem , vol.280 , pp. 21522-21530
    • Pamplona, R.1    Dalfó, E.2    Ayala, V.3    Bellmunt, J.4    Prat, J.5    Ferrer, I.6    Portero, M.7
  • 42
    • 0035087703 scopus 로고    scopus 로고
    • Localization of active forms of c-Jun kinase (JNK) and p38 kinase in Alzheimer's disease brains at different stages of neurofibrillary degeneration
    • Pei J.J., Braak E., Braak H., Grundque-Iqbal K., Winblad W., and Cowburn R.F. Localization of active forms of c-Jun kinase (JNK) and p38 kinase in Alzheimer's disease brains at different stages of neurofibrillary degeneration. J Alzheimer's Dis 3 (2001) 41-48
    • (2001) J Alzheimer's Dis , vol.3 , pp. 41-48
    • Pei, J.J.1    Braak, E.2    Braak, H.3    Grundque-Iqbal, K.4    Winblad, W.5    Cowburn, R.F.6
  • 43
    • 7044284920 scopus 로고    scopus 로고
    • Expression of stress-activated kinase c-Jun N-terminal kinase (SAPK/JNK-P) and p38 (p38-P), and tau hyperphosphorylation in neurites surrounding βA plaques in APP Tg2576 mice
    • Puig B., Gómez-Isla T., Ribé E., Cuadrado M., Torrejón-Escribano B., Dalfó E., and Ferrer I. Expression of stress-activated kinase c-Jun N-terminal kinase (SAPK/JNK-P) and p38 (p38-P), and tau hyperphosphorylation in neurites surrounding βA plaques in APP Tg2576 mice. Neuropathol Appl Neurobiol 30 (2004) 491-502
    • (2004) Neuropathol Appl Neurobiol , vol.30 , pp. 491-502
    • Puig, B.1    Gómez-Isla, T.2    Ribé, E.3    Cuadrado, M.4    Torrejón-Escribano, B.5    Dalfó, E.6    Ferrer, I.7
  • 45
    • 10944223484 scopus 로고    scopus 로고
    • Tau protein as a differential biomarker of tauopathies
    • Sergeant N., Delacourte A., and Buee L. Tau protein as a differential biomarker of tauopathies. Biochim Biophys Acta 1739 (2005) 179-197
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 179-197
    • Sergeant, N.1    Delacourte, A.2    Buee, L.3
  • 46
    • 3242680852 scopus 로고    scopus 로고
    • Examination of stress-related genes in human temporal versus occipital cortex in the course of neurodegeneration: involvement of 14-3-3 zeta in this dynamic process
    • Soulié C., Nicole A., Delacourte A., and Ceballos-Picot I. Examination of stress-related genes in human temporal versus occipital cortex in the course of neurodegeneration: involvement of 14-3-3 zeta in this dynamic process. Neurosci Lett 365 (2004) 1-5
    • (2004) Neurosci Lett , vol.365 , pp. 1-5
    • Soulié, C.1    Nicole, A.2    Delacourte, A.3    Ceballos-Picot, I.4
  • 47
    • 0003374626 scopus 로고    scopus 로고
    • Tau protein pathology in neurodegenerative diseases
    • Spillantini M.G., and Goedert M. Tau protein pathology in neurodegenerative diseases. Trends Neurosci 21 (1998) 428-433
    • (1998) Trends Neurosci , vol.21 , pp. 428-433
    • Spillantini, M.G.1    Goedert, M.2
  • 49
    • 0038724088 scopus 로고    scopus 로고
    • The 14-3-3 proteins: gene, gene expression, and function
    • Takahashi Y. The 14-3-3 proteins: gene, gene expression, and function. Neurochem Res 28 (2003) 1265-1273
    • (2003) Neurochem Res , vol.28 , pp. 1265-1273
    • Takahashi, Y.1
  • 50
    • 4844230325 scopus 로고    scopus 로고
    • 14-3-3 Proteins and zeta isoform containing neurofibrillary tangles in patients with Alzheimer's disease
    • Umahara T., Uchihara T., Tsuchiya K., Nakamura A., Iwamoto T., Ikeda K., and Takasaki M. 14-3-3 Proteins and zeta isoform containing neurofibrillary tangles in patients with Alzheimer's disease. Acta Neuropathol 108 (2004) 279-286
    • (2004) Acta Neuropathol , vol.108 , pp. 279-286
    • Umahara, T.1    Uchihara, T.2    Tsuchiya, K.3    Nakamura, A.4    Iwamoto, T.5    Ikeda, K.6    Takasaki, M.7
  • 51
    • 27444433260 scopus 로고    scopus 로고
    • 14-3-3 Proteins: regulators of numerous eukaryotic proteins
    • van Heusden G.P. 14-3-3 Proteins: regulators of numerous eukaryotic proteins. IUBMB Life 57 (2005) 623-629
    • (2005) IUBMB Life , vol.57 , pp. 623-629
    • van Heusden, G.P.1
  • 52
    • 0033860372 scopus 로고    scopus 로고
    • Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity
    • Varadarajan S., Yatin S., Aksenova M., and Butterfield D.A. Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity. J Struct Biol 130 (2000) 184-208
    • (2000) J Struct Biol , vol.130 , pp. 184-208
    • Varadarajan, S.1    Yatin, S.2    Aksenova, M.3    Butterfield, D.A.4
  • 53
    • 2942755865 scopus 로고    scopus 로고
    • 14-3-3 binds to and mediates phosphorylation of microtubule-associated tau protein by Ser9-phosphorylated glycogen synthase kinase 3β in the brain
    • Yuan Z., Agarwal-Marwal A., and Paudel H.K. 14-3-3 binds to and mediates phosphorylation of microtubule-associated tau protein by Ser9-phosphorylated glycogen synthase kinase 3β in the brain. J Biol Chem 279 (2004) 26105-26114
    • (2004) J Biol Chem , vol.279 , pp. 26105-26114
    • Yuan, Z.1    Agarwal-Marwal, A.2    Paudel, H.K.3
  • 54
    • 0035142804 scopus 로고    scopus 로고
    • Activation and redistribution of c-Jun N-terminal kinase/stress activated protein kinase in degenerating neurons in Alzheimer's disease
    • Zhu X., Raina A.K., Rottkamp C.A., Aliev G., Perry G., Boux H., and Smith M.A. Activation and redistribution of c-Jun N-terminal kinase/stress activated protein kinase in degenerating neurons in Alzheimer's disease. J Neurochem 76 (2001) 435-441
    • (2001) J Neurochem , vol.76 , pp. 435-441
    • Zhu, X.1    Raina, A.K.2    Rottkamp, C.A.3    Aliev, G.4    Perry, G.5    Boux, H.6    Smith, M.A.7
  • 55
    • 0033782845 scopus 로고    scopus 로고
    • Activation of p38 kinase links tau phosphorylation, oxidative stress, and cell cycle-related events in Alzheimer disease
    • Zhu X., Rottkamp C.A., Boux H., Takeda A., Perry G., and Smith M.A. Activation of p38 kinase links tau phosphorylation, oxidative stress, and cell cycle-related events in Alzheimer disease. J Neuropathol Exp Neurol 59 (2000) 880-888
    • (2000) J Neuropathol Exp Neurol , vol.59 , pp. 880-888
    • Zhu, X.1    Rottkamp, C.A.2    Boux, H.3    Takeda, A.4    Perry, G.5    Smith, M.A.6


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