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Volumn 2, Issue 1, 2014, Pages

The link between intraneuronal N-truncated amyloid-β peptide and oxidatively modified lipids in idiopathic autism and dup(15q11.2-q13)/autism

Author keywords

4 hydroxy 2 nonenal; Amyloid peptide; Chromosome 15q11.2 q13 duplication; Idiopathic autism; Malondialdehyde; Oxidative stress

Indexed keywords


EID: 85005814220     PISSN: None     EISSN: 20515960     Source Type: Journal    
DOI: 10.1186/2051-5960-1-61     Document Type: Article
Times cited : (24)

References (59)
  • 2
    • 3543038182 scopus 로고    scopus 로고
    • Supernumerary tricentric derivative chromosome 15 in two boys with intractable epilepsy: another mechanism for partial hexasomy
    • Mann SM, Wang NJ, Liu DH, Wang L, Schultz RA: Supernumerary tricentric derivative chromosome 15 in two boys with intractable epilepsy: another mechanism for partial hexasomy. Hum Genet 2004, 115: 104-111.
    • (2004) Hum Genet , vol.115 , pp. 104-111
    • Mann, S.M.1    Wang, N.J.2    Liu, D.H.3    Wang, L.4    Schultz, R.A.5
  • 3
    • 3242710286 scopus 로고    scopus 로고
    • High-resolution molecular characterization of 15q11-q13 rearrangements by array comparative genomic hybridization (array CGH) with detection of gene dosage
    • Wang NJ, Liu D, Parokonny AS, Schanen NC: High-resolution molecular characterization of 15q11-q13 rearrangements by array comparative genomic hybridization (array CGH) with detection of gene dosage. Am J Hum Genet 2004, 75: 267-281. 10.1086/422854
    • (2004) Am J Hum Genet , vol.75 , pp. 267-281
    • Wang, N.J.1    Liu, D.2    Parokonny, A.S.3    Schanen, N.C.4
  • 5
    • 33746049824 scopus 로고    scopus 로고
    • High levels of Alzheimer beta-amyloid precursor protein (APP) in children with severely autistic behavior and aggression
    • Sokol DK, Chen D, Farlow MR, Dunn DW, Maloney B, Zimmer JA, Lahiri DK: High levels of Alzheimer beta-amyloid precursor protein (APP) in children with severely autistic behavior and aggression. J Child Neurol 2006, 21: 444-449.
    • (2006) J Child Neurol , vol.21 , pp. 444-449
    • Sokol, D.K.1    Chen, D.2    Farlow, M.R.3    Dunn, D.W.4    Maloney, B.5    Zimmer, J.A.6    Lahiri, D.K.7
  • 6
    • 79959407483 scopus 로고    scopus 로고
    • Increased secreted amyloid precursor protein-α (sAPPα) in severe autism: proposal of a specific, anabolic pathway and putative biomarker
    • Ray B, Long JM, Sokol DK, Lahiri DK: Increased secreted amyloid precursor protein-α (sAPPα) in severe autism: proposal of a specific, anabolic pathway and putative biomarker. PLoS One 2011, 6: e20405. 1-10 10.1371/journal.pone.0020405
    • (2011) PLoS One , vol.6
    • Ray, B.1    Long, J.M.2    Sokol, D.K.3    Lahiri, D.K.4
  • 7
    • 84860475483 scopus 로고    scopus 로고
    • Abnormal intracellular accumulation and extracellular Aβ deposition in idiopathic and dup15q11.2-q13 autism spectrum disorders
    • Wegiel J, Frackowiak J, Mazur-Kolecka B, Schanen CN, Cook EH, Sigman M, Brown WT, Kuchna I, et al.: Abnormal intracellular accumulation and extracellular Aβ deposition in idiopathic and dup15q11.2-q13 autism spectrum disorders. PLoS One 2012, 7: e35414. 10.1371/journal.pone.0035414
    • (2012) PLoS One , vol.7
    • Wegiel, J.1    Frackowiak, J.2    Mazur-Kolecka, B.3    Schanen, C.N.4    Cook, E.H.5    Sigman, M.6    Brown, W.T.7    Kuchna, I.8
  • 8
    • 12844266117 scopus 로고    scopus 로고
    • The critical role of methionine 35 in Alzheimer's amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity
    • Butterfield DA, Boyd-Kimball D: The critical role of methionine 35 in Alzheimer's amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity. Biochim Biophys Acta 2005, 1703: 149-156. 10.1016/j.bbapap.2004.10.014
    • (2005) Biochim Biophys Acta , vol.1703 , pp. 149-156
    • Butterfield, D.A.1    Boyd-Kimball, D.2
  • 9
    • 84861470082 scopus 로고    scopus 로고
    • Methionine-35 of aβ(1-42): importance for oxidative stress in Alzheimer disease
    • Butterfield DA, Sultana R: Methionine-35 of aβ(1-42): importance for oxidative stress in Alzheimer disease. J Amino Acids 2011, 2011: 198430. doi:10.4061/2011/1984300
    • (2011) J Amino Acids , vol.2011 , pp. 198430
    • Butterfield, D.A.1    Sultana, R.2
  • 10
    • 67649600828 scopus 로고    scopus 로고
    • 2+ coordination of Alzheimer's disease amyloid-β peptide-relevance to N-terminally truncated forms
    • 2+ coordination of Alzheimer's disease amyloid-β peptide-relevance to N-terminally truncated forms. J Am Chem Soc 2009, 131: 8760-8761. 10.1021/ja903669a
    • (2009) J Am Chem Soc , vol.131 , pp. 8760-8761
    • Drew, S.C.1    Masters, C.L.2    Barnham, K.L.3
  • 11
    • 4444347472 scopus 로고    scopus 로고
    • Oxidative stress in autism: increased lipid peroxidation and reduced serum levels of ceruloplasmin and transferrin-the antioxidant proteins
    • Chauhan A, Chauhan V, Brown WT, Cohen I: Oxidative stress in autism: increased lipid peroxidation and reduced serum levels of ceruloplasmin and transferrin-the antioxidant proteins. Life Sci 2004, 75: 2539-2549. 10.1016/j.lfs.2004.04.038
    • (2004) Life Sci , vol.75 , pp. 2539-2549
    • Chauhan, A.1    Chauhan, V.2    Brown, W.T.3    Cohen, I.4
  • 13
    • 12444304256 scopus 로고    scopus 로고
    • Changes in nitric oxide levels and antioxidant enzyme activities may have a role in the pathophysiological mechanisms involved in autism
    • Sogut S, Zoroglu SS, Ozyurt H, Yilmaz HR, Ozugurlu F, Sivasli E, et al.: Changes in nitric oxide levels and antioxidant enzyme activities may have a role in the pathophysiological mechanisms involved in autism. Clin Chim Acta 2003, 331: 111-117. 10.1016/S0009-8981(03)00119-0
    • (2003) Clin Chim Acta , vol.331 , pp. 111-117
    • Sogut, S.1    Zoroglu, S.S.2    Ozyurt, H.3    Yilmaz, H.R.4    Ozugurlu, F.5    Sivasli, E.6
  • 14
    • 80053907390 scopus 로고    scopus 로고
    • Urinary oxidative stress markers in children with autism
    • Damodaran LPM, Arumugam G: Urinary oxidative stress markers in children with autism. Redox Rep 2011, 169: 216-222.
    • (2011) Redox Rep , vol.169 , pp. 216-222
    • Damodaran, L.P.M.1    Arumugam, G.2
  • 16
    • 15244348759 scopus 로고    scopus 로고
    • Metabolic biomarkers of increased oxidative stress and impaired methylation capacity in children with autism
    • James SJ, Cutler P, Melnyk S, Jernigan S, Janak L, Gaylor DW, Neubrander JA: Metabolic biomarkers of increased oxidative stress and impaired methylation capacity in children with autism. Am J Clin Nutr 2004, 80: 1611-1617.
    • (2004) Am J Clin Nutr , vol.80 , pp. 1611-1617
    • James, S.J.1    Cutler, P.2    Melnyk, S.3    Jernigan, S.4    Janak, L.5    Gaylor, D.W.6    Neubrander, J.A.7
  • 18
    • 84863736932 scopus 로고    scopus 로고
    • Evidence of oxidative damage and inflammation associated with low glutathione redox status in the autism brain
    • Rose S, Melnyk S, Pavliv O, Bai S, Nick TG, Frye RE, James SJ: Evidence of oxidative damage and inflammation associated with low glutathione redox status in the autism brain. Transl Psychiatr 2012, 2: e134. doi:10.1038/tp.2012.61 10.1038/tp.2012.61
    • (2012) Transl Psychiatr , vol.2
    • Rose, S.1    Melnyk, S.2    Pavliv, O.3    Bai, S.4    Nick, T.G.5    Frye, R.E.6    James, S.J.7
  • 19
    • 69549111063 scopus 로고    scopus 로고
    • Increase in cerebellar neurotrophin-3 and oxidative stress markers in autism
    • Sajdel-Sulkowska EM, Xu M, Koibuchi N: Increase in cerebellar neurotrophin-3 and oxidative stress markers in autism. Cerebellum 2009, 8: 366-372. 10.1007/s12311-009-0105-9
    • (2009) Cerebellum , vol.8 , pp. 366-372
    • Sajdel-Sulkowska, E.M.1    Xu, M.2    Koibuchi, N.3
  • 20
    • 79952694170 scopus 로고    scopus 로고
    • Brain region-specific changes in oxidative stress and neurotrophin levels in autism spectrum disorders (ASD)
    • Sajdel-Sulkowska EM, Xu M, McGinnis W, Koibuchi N: Brain region-specific changes in oxidative stress and neurotrophin levels in autism spectrum disorders (ASD). Cerebellum 2011, 10: 43-48. 10.1007/s12311-010-0223-4
    • (2011) Cerebellum , vol.10 , pp. 43-48
    • Sajdel-Sulkowska, E.M.1    Xu, M.2    McGinnis, W.3    Koibuchi, N.4
  • 21
    • 84864360468 scopus 로고    scopus 로고
    • Brain region-specific glutathione redox imbalance in autism
    • Chauhan A, Audhya T, Chauhan V: Brain region-specific glutathione redox imbalance in autism. Neurochem Res 2012, 37: 1681-1689. 10.1007/s11064-012-0775-4
    • (2012) Neurochem Res , vol.37 , pp. 1681-1689
    • Chauhan, A.1    Audhya, T.2    Chauhan, V.3
  • 24
    • 20544457861 scopus 로고    scopus 로고
    • Why the frontal cortex in autism might be talking only to itself: local over-connectivity but long-distance disconnection
    • Courchesne E, Pierce K: Why the frontal cortex in autism might be talking only to itself: local over-connectivity but long-distance disconnection. Curr Opin Neurobiol 2005, 15: 225-230. 10.1016/j.conb.2005.03.001
    • (2005) Curr Opin Neurobiol , vol.15 , pp. 225-230
    • Courchesne, E.1    Pierce, K.2
  • 25
  • 26
    • 67649612733 scopus 로고    scopus 로고
    • Accuracy and precision in quantitative fluorescence microscopy
    • Waters JC: Accuracy and precision in quantitative fluorescence microscopy. J Cell Biol 2009, 185: 1135-1148. doi:10.1083/jcb.200903097 10.1083/jcb.200903097
    • (2009) J Cell Biol , vol.185 , pp. 1135-1148
    • Waters, J.C.1
  • 28
    • 1342343006 scopus 로고    scopus 로고
    • Lysosomal deposition of Aβ in cultures of brain vascular smooth muscle cells is enhanced by iron
    • Frackowiak J, Sukontasup T, Potempska A, Mazur-Kolecka B: Lysosomal deposition of Aβ in cultures of brain vascular smooth muscle cells is enhanced by iron. Brain Res 2004, 1002: 67-75. 10.1016/j.brainres.2003.12.015
    • (2004) Brain Res , vol.1002 , pp. 67-75
    • Frackowiak, J.1    Sukontasup, T.2    Potempska, A.3    Mazur-Kolecka, B.4
  • 29
    • 64449085276 scopus 로고    scopus 로고
    • Formation of amyloid-β oligomers in brain vascular smooth muscle cells transiently exposed to iron-induced oxidative stress
    • Frackowiak J, Potempska A, Mazur-Kolecka B: Formation of amyloid-β oligomers in brain vascular smooth muscle cells transiently exposed to iron-induced oxidative stress. Acta Neuropathol 2009, 117: 557-567. 10.1007/s00401-009-0497-0
    • (2009) Acta Neuropathol , vol.117 , pp. 557-567
    • Frackowiak, J.1    Potempska, A.2    Mazur-Kolecka, B.3
  • 30
    • 0025013745 scopus 로고
    • Detection and quantitation of amyloid β-peptide with two monoclonal antibodies
    • Kim KS, Wen GY, Bancher C, Chen CMJ, Sapienza VJ, et al.: Detection and quantitation of amyloid β-peptide with two monoclonal antibodies. Neurosci Res Commun 1990, 7: 113-122.
    • (1990) Neurosci Res Commun , vol.7 , pp. 113-122
    • Kim, K.S.1    Wen, G.Y.2    Bancher, C.3    Chen, C.M.J.4    Sapienza, V.J.5
  • 32
    • 0036471358 scopus 로고    scopus 로고
    • A pH-dependent conformational transition of Aβ peptide and physicochemical properties of the conformers in the glial cell
    • Matsunaga Y, Saito N, Fujii A, Yokotani J, Takakura T, Nishimura T, Esaki H, Yamada T: A pH-dependent conformational transition of Aβ peptide and physicochemical properties of the conformers in the glial cell. Biochem J 2002, 361: 547-556. 10.1042/0264-6021:3610547
    • (2002) Biochem J , vol.361 , pp. 547-556
    • Matsunaga, Y.1    Saito, N.2    Fujii, A.3    Yokotani, J.4    Takakura, T.5    Nishimura, T.6    Esaki, H.7    Yamada, T.8
  • 33
    • 0033008720 scopus 로고    scopus 로고
    • Quantification of sub-femtomole amount of Alzheimer amyloid β peptides
    • Potempska A, Mack K, Mehta P, Kim KS, Miller DL: Quantification of sub-femtomole amount of Alzheimer amyloid β peptides. Amyloid 1999, 6: 14-21. 10.3109/13506129908993283
    • (1999) Amyloid , vol.6 , pp. 14-21
    • Potempska, A.1    Mack, K.2    Mehta, P.3    Kim, K.S.4    Miller, D.L.5
  • 35
    • 79957653811 scopus 로고    scopus 로고
    • Intraneuronal APP, not free Aβ peptides in 3xTg-AD mice: implications for tau versus Aβ-mediated Alzheimer neurodegeneration
    • Winton MJ, Lee EB, Sun E, Wong MM, Leight S, Zhang B, Trojanowski JQ, Lee VM: Intraneuronal APP, not free Aβ peptides in 3xTg-AD mice: implications for tau versus Aβ-mediated Alzheimer neurodegeneration. J Neurosci 2011, 31: 7691-7699. 10.1523/JNEUROSCI.6637-10.2011
    • (2011) J Neurosci , vol.31 , pp. 7691-7699
    • Winton, M.J.1    Lee, E.B.2    Sun, E.3    Wong, M.M.4    Leight, S.5    Zhang, B.6    Trojanowski, J.Q.7    Lee, V.M.8
  • 36
    • 0034644836 scopus 로고    scopus 로고
    • Regulation of APP cleavage by alpha-, beta- and gamma-secretases
    • Nunan J, Small DH: Regulation of APP cleavage by alpha-, beta- and gamma-secretases. FEBS Lett 2000, 483: 6-10. 10.1016/S0014-5793(00)02076-7
    • (2000) FEBS Lett , vol.483 , pp. 6-10
    • Nunan, J.1    Small, D.H.2
  • 38
    • 0030742712 scopus 로고    scopus 로고
    • Heterogeneity of water-soluble amyloid beta-peptide in Alzheimer's disease and Down's syndrome brains
    • Russo C, Saido TC, DeBusk LM, Tabaton M, Gambetti P, Teller JK: Heterogeneity of water-soluble amyloid beta-peptide in Alzheimer's disease and Down's syndrome brains. FEBS Lett 1997, 409: 411-416. 10.1016/S0014-5793(97)00564-4
    • (1997) FEBS Lett , vol.409 , pp. 411-416
    • Russo, C.1    Saido, T.C.2    DeBusk, L.M.3    Tabaton, M.4    Gambetti, P.5    Teller, J.K.6
  • 39
    • 77954460238 scopus 로고    scopus 로고
    • Quantification and calibration of images in fluorescence microscopy
    • Baskin DS, Widmayer MA, Sharpe MA: Quantification and calibration of images in fluorescence microscopy. Anal Biochem 2010, 404: 118-126. doi:10.1016/j.ab.2010.05.029 10.1016/j.ab.2010.05.029
    • (2010) Anal Biochem , vol.404 , pp. 118-126
    • Baskin, D.S.1    Widmayer, M.A.2    Sharpe, M.A.3
  • 40
    • 0028885682 scopus 로고
    • Amino-terminal deletions enhance aggregation of β-amyloid peptides in vitr o
    • Pike CJ, Overman MJ, Cotman CW: Amino-terminal deletions enhance aggregation of β-amyloid peptides in vitr o. J Biol Chem 1995, 270: 23895-23898. 10.1074/jbc.270.41.23895
    • (1995) J Biol Chem , vol.270 , pp. 23895-23898
    • Pike, C.J.1    Overman, M.J.2    Cotman, C.W.3
  • 41
    • 0036707528 scopus 로고    scopus 로고
    • Aβ 17-42 in Alzheimer's disease activates JNK and caspase-8 leading to neuronal apoptosis
    • Wei W, Norton DD, Wang X, Kusiak JW: Aβ 17-42 in Alzheimer's disease activates JNK and caspase-8 leading to neuronal apoptosis. Brain 2002, 125: 2036-2043. 10.1093/brain/awf205
    • (2002) Brain , vol.125 , pp. 2036-2043
    • Wei, W.1    Norton, D.D.2    Wang, X.3    Kusiak, J.W.4
  • 42
    • 84860489415 scopus 로고    scopus 로고
    • Abnormalities in membrane lipids, membrane-associated proteins, and signal transduction in autism
    • In Autism. Edited by: Chauhan A, Chauhan V, Brown WT.. Boca Raton, FL: CRC Press, Taylor and Francis Group
    • Chauhan V, Chauhan A: Abnormalities in membrane lipids, membrane-associated proteins, and signal transduction in autism. Oxidative Stress, Inflammation and Immune Abnormalities. In Autism. Edited by: Chauhan A, Chauhan V, Brown WT.. Boca Raton, FL: CRC Press, Taylor and Francis Group; 2010:177-20651.
    • (2010) Oxidative Stress, Inflammation and Immune Abnormalities , pp. 177-20651
    • Chauhan, V.1    Chauhan, A.2
  • 43
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • Cadenas E, Davies KJ: Mitochondrial free radical generation, oxidative stress, and aging. Free Radic Biol Med 2000, 29: 222-230. 10.1016/S0891-5849(00)00317-8
    • (2000) Free Radic Biol Med , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 44
    • 62349129124 scopus 로고    scopus 로고
    • Neuronal mitochondrial toxicity of malondialdehyde: inhibitory effects on respiratory function and enzyme activities in rat brain mitochondria
    • Long J, Liu C, Sun L, Gao H, Liu J: Neuronal mitochondrial toxicity of malondialdehyde: inhibitory effects on respiratory function and enzyme activities in rat brain mitochondria. Neurochem Res 2009, 34: 786-794. 10.1007/s11064-008-9882-7
    • (2009) Neurochem Res , vol.34 , pp. 786-794
    • Long, J.1    Liu, C.2    Sun, L.3    Gao, H.4    Liu, J.5
  • 48
    • 0024998688 scopus 로고
    • Lipofuscin as an indicator of oxidative stress and aging
    • Sohal RS, Brunk UT: Lipofuscin as an indicator of oxidative stress and aging. Adv Exp Med Biol 1989, 266: 17-26.
    • (1989) Adv Exp Med Biol , vol.266 , pp. 17-26
    • Sohal, R.S.1    Brunk, U.T.2
  • 50
    • 42449143778 scopus 로고    scopus 로고
    • A microscopic study of language-related cortex in autism
    • Lopez-Hurtado E, Prieto JJ: A microscopic study of language-related cortex in autism. Am J Biochem Biotechn 2008, 4: 130-145.
    • (2008) Am J Biochem Biotechn , vol.4 , pp. 130-145
    • Lopez-Hurtado, E.1    Prieto, J.J.2
  • 51
    • 34249043563 scopus 로고    scopus 로고
    • Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry
    • Roe MR, Xie H, Bandhakavi S, Griffin TJ: Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry. Anal Chem 2007, 79: 3747-3756. 10.1021/ac0617971
    • (2007) Anal Chem , vol.79 , pp. 3747-3756
    • Roe, M.R.1    Xie, H.2    Bandhakavi, S.3    Griffin, T.J.4
  • 52
    • 0037379388 scopus 로고    scopus 로고
    • Molecular basis of enzyme inactivation by an endogenous electrophile 4-hydroxy-2-nonenal: identification of modification sites in glyceraldehyde-3-phosphate dehydrogenase
    • Ishii T, Tatsuda E, Kumazawa S, Nakayama T, Uchida K: Molecular basis of enzyme inactivation by an endogenous electrophile 4-hydroxy-2-nonenal: identification of modification sites in glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 2003, 42: 3474-3480. 10.1021/bi027172o
    • (2003) Biochemistry , vol.42 , pp. 3474-3480
    • Ishii, T.1    Tatsuda, E.2    Kumazawa, S.3    Nakayama, T.4    Uchida, K.5
  • 53
    • 28644448115 scopus 로고    scopus 로고
    • Inhibition of defective adenylosuccinate lyase by HNE: a neurological disease that may be affected by oxidative stress
    • Crifò C, Siems W, Soro S, Salerno C: Inhibition of defective adenylosuccinate lyase by HNE: a neurological disease that may be affected by oxidative stress. Biofactors 2005, 24: 131-136. 10.1002/biof.5520240115
    • (2005) Biofactors , vol.24 , pp. 131-136
    • Crifò, C.1    Siems, W.2    Soro, S.3    Salerno, C.4
  • 54
    • 28644434431 scopus 로고    scopus 로고
    • Inhibition of ion transport ATPases by HNE
    • Crifò C, Capuozzo E, Siems W, Salerno C: Inhibition of ion transport ATPases by HNE. Biofactors 2005, 24: 137-140. 10.1002/biof.5520240116
    • (2005) Biofactors , vol.24 , pp. 137-140
    • Crifò, C.1    Capuozzo, E.2    Siems, W.3    Salerno, C.4
  • 55
    • 2442631567 scopus 로고    scopus 로고
    • Malondialdehyde adducts in DNA arrest transcription by T7 RNA polymerase and mammalian RNA polymerase II
    • Cline SD, Riggins JN, Tornaletti S, Marnett LJ, Hanawalt PC: Malondialdehyde adducts in DNA arrest transcription by T7 RNA polymerase and mammalian RNA polymerase II. Proc Natl Acad Sci USA 2004, 101: 7275-7280. 10.1073/pnas.0402252101
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7275-7280
    • Cline, S.D.1    Riggins, J.N.2    Tornaletti, S.3    Marnett, L.J.4    Hanawalt, P.C.5
  • 56
    • 78650922762 scopus 로고    scopus 로고
    • Malondialdehyde inhibits an AMPK-mediated nuclear translocation and repression activity of ALDH2 in transcription
    • Choi JW, Kim JH, Cho SC, Ha MK, Song KY, Youn HD, Park SC: Malondialdehyde inhibits an AMPK-mediated nuclear translocation and repression activity of ALDH2 in transcription. Biochem Biophys Res Commun 2011, 404: 400-406. 10.1016/j.bbrc.2010.11.131
    • (2011) Biochem Biophys Res Commun , vol.404 , pp. 400-406
    • Choi, J.W.1    Kim, J.H.2    Cho, S.C.3    Ha, M.K.4    Song, K.Y.5    Youn, H.D.6    Park, S.C.7
  • 57
    • 33846949357 scopus 로고    scopus 로고
    • The oxidative stress metabolite 4-hydroxynonenal promotes Alzheimer protofibril formation
    • Siegel SJ, Bieschke J, Powers ET, Kelly JW: The oxidative stress metabolite 4-hydroxynonenal promotes Alzheimer protofibril formation. Biochemistry 2007, 46: 1503-1510. 10.1021/bi061853s
    • (2007) Biochemistry , vol.46 , pp. 1503-1510
    • Siegel, S.J.1    Bieschke, J.2    Powers, E.T.3    Kelly, J.W.4
  • 58
    • 19944433845 scopus 로고    scopus 로고
    • Beta-site APP cleaving enzyme up-regulation induced by 4-hydroxynonenal is mediated by stress-activated protein kinases pathways
    • Tamagno E, Parola M, Bardini P, Piccini A, Borghi R, Guglielmotto M, Santoro G, Davit A, et al.: Beta-site APP cleaving enzyme up-regulation induced by 4-hydroxynonenal is mediated by stress-activated protein kinases pathways. J Neurochem 2005, 92: 628-636. 10.1111/j.1471-4159.2004.02895.x
    • (2005) J Neurochem , vol.92 , pp. 628-636
    • Tamagno, E.1    Parola, M.2    Bardini, P.3    Piccini, A.4    Borghi, R.5    Guglielmotto, M.6    Santoro, G.7    Davit, A.8
  • 59
    • 33745999815 scopus 로고    scopus 로고
    • Amyloid-β impairs development of neuronal progenitor cells by oxidative mechanisms
    • Mazur-Kolecka B, Golabek A, Nowicki K, Flory M, Frackowiak J: Amyloid-β impairs development of neuronal progenitor cells by oxidative mechanisms. Neurobiol Aging 2006, 27: 1181-1192. 10.1016/j.neurobiolaging.2005.07.006
    • (2006) Neurobiol Aging , vol.27 , pp. 1181-1192
    • Mazur-Kolecka, B.1    Golabek, A.2    Nowicki, K.3    Flory, M.4    Frackowiak, J.5


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