메뉴 건너뛰기




Volumn 7, Issue 1-2, 2013, Pages 109-122

Apolipoprotein A-I: Insights from redox proteomics for its role in neurodegeneration

Author keywords

Alzheimer disease; Apolipoprotein A I; Neurodegeneration; Tumor necrosis factor

Indexed keywords

4 HYDROXYNONENAL; ABC TRANSPORTER A1; ACROLEIN; ANTHRACYCLINE; APOLIPOPROTEIN A1; CHOLESTEROL; DOXORUBICIN; HIGH DENSITY LIPOPROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LIPOPROTEIN; LOW DENSITY LIPOPROTEIN; PROTEIN KINASE C ZETA; TRIACYLGLYCEROL; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR 1; TUMOR NECROSIS FACTOR RECEPTOR 2;

EID: 84872717635     PISSN: 18628346     EISSN: 18628354     Source Type: Journal    
DOI: 10.1002/prca.201200087     Document Type: Review
Times cited : (64)

References (148)
  • 1
    • 21044437207 scopus 로고    scopus 로고
    • The use of proteomics in biomarker discovery in neurodegenerative diseases
    • Davidsson, P., Sjogren, M., The use of proteomics in biomarker discovery in neurodegenerative diseases. Dis. Markers 2005, 21, 81-92.
    • (2005) Dis. Markers , vol.21 , pp. 81-92
    • Davidsson, P.1    Sjogren, M.2
  • 2
    • 78649372310 scopus 로고    scopus 로고
    • Tetranectin and apolipoprotein A-I in cerebrospinal fluid as potential biomarkers for Parkinson's disease
    • Wang, E. S., Sun, Y., Guo, J. G., Gao, X. et al., Tetranectin and apolipoprotein A-I in cerebrospinal fluid as potential biomarkers for Parkinson's disease. Acta Neurol. Scand. 2010, 122, 350-359.
    • (2010) Acta Neurol. Scand. , vol.122 , pp. 350-359
    • Wang, E.S.1    Sun, Y.2    Guo, J.G.3    Gao, X.4
  • 3
    • 52349099782 scopus 로고    scopus 로고
    • Peptides and proteins in plasma and cerebrospinal fluid as biomarkers for the prediction, diagnosis, and monitoring of therapeutic efficacy of Alzheimer's disease
    • Aluise, C. D., Sowell, R. A., Butterfield, D. A., Peptides and proteins in plasma and cerebrospinal fluid as biomarkers for the prediction, diagnosis, and monitoring of therapeutic efficacy of Alzheimer's disease. Biochim. Biophys. Acta 2008, 1782, 549-558.
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 549-558
    • Aluise, C.D.1    Sowell, R.A.2    Butterfield, D.A.3
  • 5
    • 77956832045 scopus 로고    scopus 로고
    • Protein oxidation processes in aging brain
    • Butterfield, D. A., Stadtman, E. R.
    • Butterfield, D. A., Stadtman, E. R., Protein oxidation processes in aging brain. Cell Aging Gerontol. 1997, 2, 161-191.
    • (1997) Cell Aging Gerontol , vol.2 , pp. 161-191
  • 6
    • 12444296480 scopus 로고    scopus 로고
    • Proteins as biomarkers of oxidative/nitrosative stress in diseases: the contribution of redox proteomics
    • Dalle-Donne, I., Scaloni, A., Giustarini, D., Cavarra, E. et al., Proteins as biomarkers of oxidative/nitrosative stress in diseases: the contribution of redox proteomics. Mass Spectrom. Rev. 2005, 24, 55-99.
    • (2005) Mass Spectrom. Rev. , vol.24 , pp. 55-99
    • Dalle-Donne, I.1    Scaloni, A.2    Giustarini, D.3    Cavarra, E.4
  • 7
    • 0346100510 scopus 로고    scopus 로고
    • Proteomics for the identification of specifically oxidized proteins in brain: technology and application to the study of neurodegenerative disorders
    • Butterfield, D. A., Castegna, A., Proteomics for the identification of specifically oxidized proteins in brain: technology and application to the study of neurodegenerative disorders. Amino Acids 2003, 25, 419-425.
    • (2003) Amino Acids , vol.25 , pp. 419-425
    • Butterfield, D.A.1    Castegna, A.2
  • 8
    • 0141767139 scopus 로고    scopus 로고
    • Proteomics in Alzheimer's disease: insights into potential mechanisms of neurodegeneration
    • Butterfield, D. A., Boyd-Kimball, D., Castegna, A., Proteomics in Alzheimer's disease: insights into potential mechanisms of neurodegeneration. J. Neurochem. 2003, 86, 1313-1327.
    • (2003) J. Neurochem. , vol.86 , pp. 1313-1327
    • Butterfield, D.A.1    Boyd-Kimball, D.2    Castegna, A.3
  • 11
    • 21044435930 scopus 로고    scopus 로고
    • Validation of a prefractionation method followed by two-dimensional electrophoresis-Applied to cerebrospinal fluid proteins from frontotemporal dementia patients
    • Hansson, S. F., Puchades, M., Blennow, K., Sjögren, M. et al., Validation of a prefractionation method followed by two-dimensional electrophoresis-Applied to cerebrospinal fluid proteins from frontotemporal dementia patients. Proteome Science 2004, 2, 7.
    • (2004) Proteome Science , vol.2 , pp. 7
    • Hansson, S.F.1    Puchades, M.2    Blennow, K.3    Sjögren, M.4
  • 12
    • 80755166682 scopus 로고    scopus 로고
    • Lipid transport by mammalian ABC proteins
    • Quazi, F., Molday, R. S., Lipid transport by mammalian ABC proteins. Essays Biochem. 2011, 50, 265-290.
    • (2011) Essays Biochem. , vol.50 , pp. 265-290
    • Quazi, F.1    Molday, R.S.2
  • 13
    • 0035871793 scopus 로고    scopus 로고
    • Apolipoprotein A-I inhibits the production of interleukin-1beta and tumor necrosis factor-alpha by blocking contact-mediated activation of monocytes by T lymphocytes
    • Hyka, N., Dayer, J. M., Modoux, C., Kohno, T. et al., Apolipoprotein A-I inhibits the production of interleukin-1beta and tumor necrosis factor-alpha by blocking contact-mediated activation of monocytes by T lymphocytes. Blood 2001, 97, 2381-2389.
    • (2001) Blood , vol.97 , pp. 2381-2389
    • Hyka, N.1    Dayer, J.M.2    Modoux, C.3    Kohno, T.4
  • 14
    • 39749145196 scopus 로고    scopus 로고
    • Translating molecular discoveries into new therapies for atherosclerosis
    • Rader, D. J., Daugherty, A., Translating molecular discoveries into new therapies for atherosclerosis. Nature 2008, 451, 904-913.
    • (2008) Nature , vol.451 , pp. 904-913
    • Rader, D.J.1    Daugherty, A.2
  • 15
    • 0025273159 scopus 로고
    • Apolipoprotein A-I and apolipoprotein SAA half-lives during acute inflammation and amyloidogenesis
    • Tape, C., Kisilevsky, R., Apolipoprotein A-I and apolipoprotein SAA half-lives during acute inflammation and amyloidogenesis. Biochim. Biophys. Acta 1990, 1043, 295-300.
    • (1990) Biochim. Biophys. Acta , vol.1043 , pp. 295-300
    • Tape, C.1    Kisilevsky, R.2
  • 16
    • 0031027667 scopus 로고    scopus 로고
    • Marked increases in concentrations of apolipoprotein in the cerebrospinal fluid of poliovirus-infected macaques: relations between apolipoprotein concentrations and severity of brain injury
    • Saito, K., Seishima, M., Heyes, M. P., Song, H. et al., Marked increases in concentrations of apolipoprotein in the cerebrospinal fluid of poliovirus-infected macaques: relations between apolipoprotein concentrations and severity of brain injury. Biochem. J. 1997, 321 (Pt 1), 145-149.
    • (1997) Biochem. J. , vol.321 , Issue.PART 1 , pp. 145-149
    • Saito, K.1    Seishima, M.2    Heyes, M.P.3    Song, H.4
  • 17
    • 0029034940 scopus 로고
    • Intracellular cholesterol transport and compartmentation
    • Liscum, L., Underwood, K. W., Intracellular cholesterol transport and compartmentation. J. Biol. Chem. 1995, 270, 15443-15446.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15443-15446
    • Liscum, L.1    Underwood, K.W.2
  • 18
    • 0037063998 scopus 로고    scopus 로고
    • Sphingolipid and cholesterol dependence of alphavirus membrane fusion. Lack of correlation with lipid raft formation in target liposomes
    • Waarts, B. L., Bittman, R., Wilschut, J., Sphingolipid and cholesterol dependence of alphavirus membrane fusion. Lack of correlation with lipid raft formation in target liposomes. J. Biol. Chem. 2002, 277, 38141-38147.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38141-38147
    • Waarts, B.L.1    Bittman, R.2    Wilschut, J.3
  • 19
    • 3142724785 scopus 로고    scopus 로고
    • Cholesterol efflux alters lipid raft stability and distribution during capacitation of boar spermatozoa
    • Shadan, S., James, P. S., Howes, E. A., Jones, R., Cholesterol efflux alters lipid raft stability and distribution during capacitation of boar spermatozoa. Biol. Reprod. 2004, 71, 253-265.
    • (2004) Biol. Reprod. , vol.71 , pp. 253-265
    • Shadan, S.1    James, P.S.2    Howes, E.A.3    Jones, R.4
  • 20
    • 34347246377 scopus 로고    scopus 로고
    • Cholesterol level of lipid raft microdomains regulates apoptotic cell death in prostate cancer cells through EGFR-mediated Akt and ERK signal transduction
    • Oh, H. Y., Lee, E. J., Yoon, S., Chung, B. H. et al., Cholesterol level of lipid raft microdomains regulates apoptotic cell death in prostate cancer cells through EGFR-mediated Akt and ERK signal transduction. The Prostate 2007, 67, 1061-1069.
    • (2007) The Prostate , vol.67 , pp. 1061-1069
    • Oh, H.Y.1    Lee, E.J.2    Yoon, S.3    Chung, B.H.4
  • 21
    • 78649789514 scopus 로고    scopus 로고
    • Transbilayer organization of membrane cholesterol at low concentrations: implications in health and disease
    • Chaudhuri, A., Chattopadhyay, A., Transbilayer organization of membrane cholesterol at low concentrations: implications in health and disease. Biochim. Biophys. Acta 2011, 1808, 19-25.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 19-25
    • Chaudhuri, A.1    Chattopadhyay, A.2
  • 22
    • 0034746809 scopus 로고    scopus 로고
    • Risk factors for coronary disease: the time for a paradigm shift?
    • Dominiczak, M. H., Risk factors for coronary disease: the time for a paradigm shift? Clin. Chem. Lab. Med.: CCLM/FESCC 2001, 39, 907-919.
    • (2001) Clin. Chem. Lab. Med.: CCLM/FESCC , vol.39 , pp. 907-919
    • Dominiczak, M.H.1
  • 23
    • 84856010494 scopus 로고    scopus 로고
    • Apolipoproteins: metabolic role and clinical biochemistry applications
    • Dominiczak, M. H., Caslake, M. J., Apolipoproteins: metabolic role and clinical biochemistry applications. Annals of Clin. Biochem. 2011, 48, 498-515.
    • (2011) Annals of Clin. Biochem. , vol.48 , pp. 498-515
    • Dominiczak, M.H.1    Caslake, M.J.2
  • 24
    • 0030689641 scopus 로고    scopus 로고
    • Reverse cholesterol transport-a review of the process and its clinical implications
    • Hill, S. A., McQueen, M. J., Reverse cholesterol transport-a review of the process and its clinical implications. Clin. Biochem. 1997, 30, 517-525.
    • (1997) Clin. Biochem. , vol.30 , pp. 517-525
    • Hill, S.A.1    McQueen, M.J.2
  • 25
    • 77952715110 scopus 로고    scopus 로고
    • A genome-wide linkage scan identifies multiple quantitative trait loci for HDL-cholesterol levels in families with premature CAD and MI
    • Yang, R., Li, L., Seidelmann, S. B., Shen, G. Q. et al., A genome-wide linkage scan identifies multiple quantitative trait loci for HDL-cholesterol levels in families with premature CAD and MI. J. Lipid Res. 2010, 51, 1442-1451.
    • (2010) J. Lipid Res. , vol.51 , pp. 1442-1451
    • Yang, R.1    Li, L.2    Seidelmann, S.B.3    Shen, G.Q.4
  • 26
    • 84858201901 scopus 로고    scopus 로고
    • The interaction of ApoA-I and ABCA1 triggers signal transduction pathways to mediate efflux of cellular lipids
    • Zhao, G. J., Yin, K., Fu, Y. C., Tang, C. K., The interaction of ApoA-I and ABCA1 triggers signal transduction pathways to mediate efflux of cellular lipids. Mol. Med. 2012, 18, 149-158.
    • (2012) Mol. Med. , vol.18 , pp. 149-158
    • Zhao, G.J.1    Yin, K.2    Fu, Y.C.3    Tang, C.K.4
  • 28
    • 77954661945 scopus 로고    scopus 로고
    • Effect of ApoA-I on cholesterol release and apoE secretion in human mature adipocytes
    • Bencharif, K., Hoareau, L., Murumalla, R. K., Tarnus, E. et al., Effect of ApoA-I on cholesterol release and apoE secretion in human mature adipocytes. Lipids in Health and Disease 2010, 9, 75.
    • (2010) Lipids in Health and Disease , vol.9 , pp. 75
    • Bencharif, K.1    Hoareau, L.2    Murumalla, R.K.3    Tarnus, E.4
  • 29
    • 71449125360 scopus 로고    scopus 로고
    • Modification of high density lipoprotein by myeloperoxidase generates a pro-inflammatory particle
    • Undurti, A., Huang, Y., Lupica, J. A., Smith, J. D. et al., Modification of high density lipoprotein by myeloperoxidase generates a pro-inflammatory particle. J. Biol. Chem. 2009, 284, 30825-30835.
    • (2009) J. Biol. Chem. , vol.284 , pp. 30825-30835
    • Undurti, A.1    Huang, Y.2    Lupica, J.A.3    Smith, J.D.4
  • 30
    • 77953257870 scopus 로고    scopus 로고
    • Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease
    • Butterfield, D. A., Bader Lange, M. L., Sultana, R., Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease. Biochim. Biophys. Acta 2010, 1801, 924-929.
    • (2010) Biochim. Biophys. Acta , vol.1801 , pp. 924-929
    • Butterfield, D.A.1    Bader Lange, M.L.2    Sultana, R.3
  • 31
    • 71049139267 scopus 로고    scopus 로고
    • An azido-biotin reagent for use in the isolation of protein adducts of lipid-derived electrophiles by streptavidin catch and photorelease
    • Kim, H. Y., Tallman, K. A., Liebler, D. C., Porter, N. A., An azido-biotin reagent for use in the isolation of protein adducts of lipid-derived electrophiles by streptavidin catch and photorelease. Mol. Cell Proteomics 2009, 8, 2080-2089.
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 2080-2089
    • Kim, H.Y.1    Tallman, K.A.2    Liebler, D.C.3    Porter, N.A.4
  • 32
    • 38949089246 scopus 로고    scopus 로고
    • Protein damage by reactive electrophiles: targets and consequences
    • Liebler, D. C., Protein damage by reactive electrophiles: targets and consequences. Chem. Res. Toxicol 2008, 21, 117-128.
    • (2008) Chem. Res. Toxicol , vol.21 , pp. 117-128
    • Liebler, D.C.1
  • 33
    • 0030746621 scopus 로고    scopus 로고
    • The lipid peroxidation product, 4-hydroxy-2-trans-nonenal, alters the conformation of cortical synaptosomal membrane proteins
    • Subramaniam, R., Roediger, F., Jordan, B., Mattson, M. P. et al., The lipid peroxidation product, 4-hydroxy-2-trans-nonenal, alters the conformation of cortical synaptosomal membrane proteins. J. Neurochem. 1997, 69, 1161-1169.
    • (1997) J. Neurochem. , vol.69 , pp. 1161-1169
    • Subramaniam, R.1    Roediger, F.2    Jordan, B.3    Mattson, M.P.4
  • 34
    • 55949122145 scopus 로고    scopus 로고
    • Identification of proteins adducted by lipid peroxidation products in plasma and modifications of apolipoprotein A1 with a novel biotinylated phospholipid probe
    • Szapacs, M. E., Kim, H. Y., Porter, N. A., Liebler, D. C., Identification of proteins adducted by lipid peroxidation products in plasma and modifications of apolipoprotein A1 with a novel biotinylated phospholipid probe. J. Proteome Res. 2008, 7, 4237-4246.
    • (2008) J. Proteome Res. , vol.7 , pp. 4237-4246
    • Szapacs, M.E.1    Kim, H.Y.2    Porter, N.A.3    Liebler, D.C.4
  • 35
    • 77956841888 scopus 로고    scopus 로고
    • The HDL hypothesis: does high-density lipoprotein protect from atherosclerosis?
    • Vergeer, M., Holleboom, A. G., Kastelein, J. J., Kuivenhoven, J. A., The HDL hypothesis: does high-density lipoprotein protect from atherosclerosis? J. Lipid Res. 2010, 51, 2058-2073.
    • (2010) J. Lipid Res. , vol.51 , pp. 2058-2073
    • Vergeer, M.1    Holleboom, A.G.2    Kastelein, J.J.3    Kuivenhoven, J.A.4
  • 36
    • 64749104937 scopus 로고    scopus 로고
    • ABCA1 mutants reveal an interdependency between lipid export function, ApoA-I binding activity, and Janus kinase 2 activation
    • Vaughan, A. M., Tang, C., Oram, J. F., ABCA1 mutants reveal an interdependency between lipid export function, ApoA-I binding activity, and Janus kinase 2 activation. J. Lipid Res. 2009, 50, 285-292.
    • (2009) J. Lipid Res. , vol.50 , pp. 285-292
    • Vaughan, A.M.1    Tang, C.2    Oram, J.F.3
  • 37
    • 1542320076 scopus 로고    scopus 로고
    • Janus kinase 2 modulates the apolipoprotein interactions with ABCA1 required for removing cellular cholesterol
    • Tang, C., Vaughan, A. M., Oram, J. F., Janus kinase 2 modulates the apolipoprotein interactions with ABCA1 required for removing cellular cholesterol. J. Biolog. Chem. 2004, 279, 7622-7628.
    • (2004) J. Biolog. Chem. , vol.279 , pp. 7622-7628
    • Tang, C.1    Vaughan, A.M.2    Oram, J.F.3
  • 38
    • 30844445600 scopus 로고    scopus 로고
    • Janus kinase 2 modulates the lipid-removing but not protein-stabilizing interactions of amphipathic helices with ABCA1
    • Tang, C., Vaughan, A. M., Anantharamaiah, G. M., Oram, J. F., Janus kinase 2 modulates the lipid-removing but not protein-stabilizing interactions of amphipathic helices with ABCA1. J. Lipid Res. 2006, 47, 107-114.
    • (2006) J. Lipid Res. , vol.47 , pp. 107-114
    • Tang, C.1    Vaughan, A.M.2    Anantharamaiah, G.M.3    Oram, J.F.4
  • 39
    • 0035964745 scopus 로고    scopus 로고
    • ATP-binding cassette transporter-1 induces rearrangement of actin cytoskeletons possibly through Cdc42/N-WASP
    • Tsukamoto, K., Hirano, K., Tsujii, K., Ikegami, C. et al., ATP-binding cassette transporter-1 induces rearrangement of actin cytoskeletons possibly through Cdc42/N-WASP. Biochem. Biophys. Res. Comm. 2001, 287, 757-765.
    • (2001) Biochem. Biophys. Res. Comm. , vol.287 , pp. 757-765
    • Tsukamoto, K.1    Hirano, K.2    Tsujii, K.3    Ikegami, C.4
  • 40
    • 77953933427 scopus 로고    scopus 로고
    • Calmodulin interacts with ATP binding cassette transporter A1 to protect from calpain-mediated degradation and upregulates high-density lipoprotein generation
    • Iwamoto, N., Lu, R., Tanaka, N., Abe-Dohmae, S. et al., Calmodulin interacts with ATP binding cassette transporter A1 to protect from calpain-mediated degradation and upregulates high-density lipoprotein generation. Arterioscler. Thromb. Vasc. Biol. 2010, 30, 1446-1452.
    • (2010) Arterioscler. Thromb. Vasc. Biol. , vol.30 , pp. 1446-1452
    • Iwamoto, N.1    Lu, R.2    Tanaka, N.3    Abe-Dohmae, S.4
  • 41
    • 0025846967 scopus 로고
    • Apolipoprotein A-I deficiency due to a codon 84 nonsense mutation of the apolipoprotein A-I gene
    • Matsunaga, T., Hiasa, Y., Yanagi, H., Maeda, T. et al., Apolipoprotein A-I deficiency due to a codon 84 nonsense mutation of the apolipoprotein A-I gene. Proc. Nat. Acad. Sci. USA 1991, 88, 2793-2797.
    • (1991) Proc. Nat. Acad. Sci. USA , vol.88 , pp. 2793-2797
    • Matsunaga, T.1    Hiasa, Y.2    Yanagi, H.3    Maeda, T.4
  • 42
    • 79954601097 scopus 로고    scopus 로고
    • Tristetraprolin-dependent post-transcriptional regulation of inflammatory cytokine mRNA expression by apolipoprotein A-I: role of ATP-binding membrane cassette transporter A1 and signal transducer and activator of transcription 3
    • Yin, K., Deng, X., Mo, Z. C., Zhao, G. J. et al., Tristetraprolin-dependent post-transcriptional regulation of inflammatory cytokine mRNA expression by apolipoprotein A-I: role of ATP-binding membrane cassette transporter A1 and signal transducer and activator of transcription 3. J. Biol. Chem. 2011, 286, 13834-13845.
    • (2011) J. Biol. Chem. , vol.286 , pp. 13834-13845
    • Yin, K.1    Deng, X.2    Mo, Z.C.3    Zhao, G.J.4
  • 43
    • 33745700364 scopus 로고    scopus 로고
    • Understanding and exploiting the endogenous interleukin-10/STAT3-mediated anti-inflammatory response
    • Murray, P. J., Understanding and exploiting the endogenous interleukin-10/STAT3-mediated anti-inflammatory response. Curr. Op. Pharmacol. 2006, 6, 379-386.
    • (2006) Curr. Op. Pharmacol. , vol.6 , pp. 379-386
    • Murray, P.J.1
  • 44
    • 70450255118 scopus 로고    scopus 로고
    • The macrophage cholesterol exporter ABCA1 functions as an anti-inflammatory receptor
    • Tang, C., Liu, Y., Kessler, P. S., Vaughan, A. M. et al., The macrophage cholesterol exporter ABCA1 functions as an anti-inflammatory receptor. J. Biol. Chem. 2009, 284, 32336-32343.
    • (2009) J. Biol. Chem. , vol.284 , pp. 32336-32343
    • Tang, C.1    Liu, Y.2    Kessler, P.S.3    Vaughan, A.M.4
  • 45
    • 78650018621 scopus 로고    scopus 로고
    • Ca2+/calmodulin-stimulated PDE1 regulates the beta-catenin/TCF signaling through PP2A B56 gamma subunit in proliferating vascular smooth muscle cells
    • Jeon, K. I., Jono, H., Miller, C. L., Cai, Y. et al., Ca2+/calmodulin-stimulated PDE1 regulates the beta-catenin/TCF signaling through PP2A B56 gamma subunit in proliferating vascular smooth muscle cells. FEBS J. 2010, 277, 5026-5039.
    • (2010) FEBS J. , vol.277 , pp. 5026-5039
    • Jeon, K.I.1    Jono, H.2    Miller, C.L.3    Cai, Y.4
  • 46
    • 34548563810 scopus 로고    scopus 로고
    • Effect of apolipoprotein A-I on expression and function of ATP-binding cassette transporter A1 through PKA signaling
    • Yang, J. H., Dai, X. Y., Ou, X., Hao, X. R. et al., Effect of apolipoprotein A-I on expression and function of ATP-binding cassette transporter A1 through PKA signaling. Prog. Biochem. Biophys. 2007, 34, 611-619.
    • (2007) Prog. Biochem. Biophys. , vol.34 , pp. 611-619
    • Yang, J.H.1    Dai, X.Y.2    Ou, X.3    Hao, X.R.4
  • 47
    • 67349173154 scopus 로고    scopus 로고
    • Eicosapentaenoic acid reduces ABCA1 serine phosphorylation and impairs ABCA1-dependent cholesterol efflux through cyclic AMP/protein kinase A signaling pathway in THP-1 macrophage-derived foam cells
    • Hu, Y. W., Ma, X., Li, X. X., Liu, X. H. et al., Eicosapentaenoic acid reduces ABCA1 serine phosphorylation and impairs ABCA1-dependent cholesterol efflux through cyclic AMP/protein kinase A signaling pathway in THP-1 macrophage-derived foam cells. Atherosclerosis 2009, 204, e35-e43.
    • (2009) Atherosclerosis , vol.204
    • Hu, Y.W.1    Ma, X.2    Li, X.X.3    Liu, X.H.4
  • 48
    • 0347918856 scopus 로고    scopus 로고
    • Apolipoprotein A-I activates protein kinase C alpha signaling to phosphorylate and stabilize ATP binding cassette transporter A1 for the high density lipoprotein assembly
    • Yamauchi, Y., Hayashi, M., Abe-Dohmae, S., Yokoyama, S., Apolipoprotein A-I activates protein kinase C alpha signaling to phosphorylate and stabilize ATP binding cassette transporter A1 for the high density lipoprotein assembly. J. Biol. Chem. 2003, 278, 47890-47897.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47890-47897
    • Yamauchi, Y.1    Hayashi, M.2    Abe-Dohmae, S.3    Yokoyama, S.4
  • 49
    • 16644368329 scopus 로고    scopus 로고
    • Intracellular cholesterol mobilization involved in the ABCA1/apolipoprotein-mediated assembly of high density lipoprotein in fibroblasts
    • Yamauchi, Y., Chang, C. C., Hayashi, M., Abe-Dohmae, S. et al., Intracellular cholesterol mobilization involved in the ABCA1/apolipoprotein-mediated assembly of high density lipoprotein in fibroblasts. J. Lipid Res. 2004, 45, 1943-1951.
    • (2004) J. Lipid Res. , vol.45 , pp. 1943-1951
    • Yamauchi, Y.1    Chang, C.C.2    Hayashi, M.3    Abe-Dohmae, S.4
  • 50
    • 79953221107 scopus 로고    scopus 로고
    • Transcriptional regulation of ATP-binding cassette transporter A1 expression by a novel signaling pathway
    • Chen, X., Zhao, Y., Guo, Z., Zhou, L. et al., Transcriptional regulation of ATP-binding cassette transporter A1 expression by a novel signaling pathway. J. Biol. Chem. 2011, 286, 8917-8923.
    • (2011) J. Biol. Chem. , vol.286 , pp. 8917-8923
    • Chen, X.1    Zhao, Y.2    Guo, Z.3    Zhou, L.4
  • 51
    • 4344577056 scopus 로고    scopus 로고
    • Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease
    • Zheng, L., Nukuna, B., Brennan, M. L., Sun, M. et al., Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease. J. Clin. Invest. 2004, 114, 529-541.
    • (2004) J. Clin. Invest. , vol.114 , pp. 529-541
    • Zheng, L.1    Nukuna, B.2    Brennan, M.L.3    Sun, M.4
  • 52
    • 34548501273 scopus 로고    scopus 로고
    • The refined structure of nascent HDL reveals a key functional domain for particle maturation and dysfunction
    • Wu, Z., Wagner, M. A., Zheng, L., Parks, J. S. et al., The refined structure of nascent HDL reveals a key functional domain for particle maturation and dysfunction. Nat. Struct. Mol. Biol. 2007, 14, 861-868.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 861-868
    • Wu, Z.1    Wagner, M.A.2    Zheng, L.3    Parks, J.S.4
  • 53
    • 38849155723 scopus 로고    scopus 로고
    • An apolipoprotein A-I gene promoter polymorphism associated with cognitive decline, but not with Alzheimer's disease
    • Helbecque, N., Codron, V., Cottel, D., Amouyel, P., An apolipoprotein A-I gene promoter polymorphism associated with cognitive decline, but not with Alzheimer's disease. Dement. Geriatr. Cogn. Disord. 2008, 25, 97-102.
    • (2008) Dement. Geriatr. Cogn. Disord. , vol.25 , pp. 97-102
    • Helbecque, N.1    Codron, V.2    Cottel, D.3    Amouyel, P.4
  • 54
    • 4444341939 scopus 로고    scopus 로고
    • Compartmentalization of TNF receptor 1 signaling: internalized TNF receptosomes as death signaling vesicles
    • Schneider-Brachert, W., Tchikov, V., Neumeyer, J., Jakob, M. et al., Compartmentalization of TNF receptor 1 signaling: internalized TNF receptosomes as death signaling vesicles. Immunity 2004, 21, 415-428.
    • (2004) Immunity , vol.21 , pp. 415-428
    • Schneider-Brachert, W.1    Tchikov, V.2    Neumeyer, J.3    Jakob, M.4
  • 55
    • 68149150836 scopus 로고    scopus 로고
    • Activation of caspase-8 by tumour necrosis factor receptor 1 is necessary for caspase-3 activation and apoptosis in oxygen-glucose deprived cultured cortical cells
    • Badiola, N., Malagelada, C., Llecha, N., Hidalgo, J. et al., Activation of caspase-8 by tumour necrosis factor receptor 1 is necessary for caspase-3 activation and apoptosis in oxygen-glucose deprived cultured cortical cells. Neurobiol. Dis. 2009, 35, 438-447.
    • (2009) Neurobiol. Dis. , vol.35 , pp. 438-447
    • Badiola, N.1    Malagelada, C.2    Llecha, N.3    Hidalgo, J.4
  • 56
    • 0025092159 scopus 로고
    • Proliferation of astrocytes in vitro in response to cytokines. A primary role for tumor necrosis factor
    • Selmaj, K. W., Farooq, M., Norton, W. T., Raine, C. S. et al., Proliferation of astrocytes in vitro in response to cytokines. A primary role for tumor necrosis factor. J. Immunol. 1990, 144, 129-135.
    • (1990) J. Immunol. , vol.144 , pp. 129-135
    • Selmaj, K.W.1    Farooq, M.2    Norton, W.T.3    Raine, C.S.4
  • 57
    • 13544258066 scopus 로고    scopus 로고
    • Role of NF-kappaB signaling pathway in increased tumor necrosis factor-alpha-induced apoptosis of lymphocytes in aged humans
    • Gupta, S., Bi, R., Kim, C., Chiplunkar, S. et al., Role of NF-kappaB signaling pathway in increased tumor necrosis factor-alpha-induced apoptosis of lymphocytes in aged humans. Cell Death Diff. 2005, 12, 177-183.
    • (2005) Cell Death Diff. , vol.12 , pp. 177-183
    • Gupta, S.1    Bi, R.2    Kim, C.3    Chiplunkar, S.4
  • 58
    • 84861078831 scopus 로고    scopus 로고
    • A review: inflammatory process in Alzheimer's disease, role of cytokines
    • Rubio-Perez, J. M., Morillas-Ruiz, J. M., A review: inflammatory process in Alzheimer's disease, role of cytokines. Sci. World J. 2012, 2012, 756357.
    • (2012) Sci. World J. , vol.2012 , pp. 756357
    • Rubio-Perez, J.M.1    Morillas-Ruiz, J.M.2
  • 59
    • 0036121098 scopus 로고    scopus 로고
    • TNF receptor subtype signalling: differences and cellular consequences
    • MacEwan, D. J., TNF receptor subtype signalling: differences and cellular consequences. Cell. Signal 2002, 14, 477-492.
    • (2002) Cell. Signal , vol.14 , pp. 477-492
    • MacEwan, D.J.1
  • 61
    • 12644272789 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-mediated kinase cascades: bifurcation of nuclear factor-kappaB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2
    • Song, H. Y., Regnier, C. H., Kirschning, C. J., Goeddel, D. V. et al., Tumor necrosis factor (TNF)-mediated kinase cascades: bifurcation of nuclear factor-kappaB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2. Proc. Nat. Acad. Sci. USA 1997, 94, 9792-9796.
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 9792-9796
    • Song, H.Y.1    Regnier, C.H.2    Kirschning, C.J.3    Goeddel, D.V.4
  • 62
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death
    • Liu, Z. G., Hsu, H., Goeddel, D. V., Karin, M., Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death. Cell 1996, 87, 565-576.
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu, Z.G.1    Hsu, H.2    Goeddel, D.V.3    Karin, M.4
  • 63
    • 0037204948 scopus 로고    scopus 로고
    • TNF-R1 signaling: a beautiful pathway
    • Chen, G., Goeddel, D. V., TNF-R1 signaling: a beautiful pathway. Science 2002, 296, 1634-1635.
    • (2002) Science , vol.296 , pp. 1634-1635
    • Chen, G.1    Goeddel, D.V.2
  • 64
    • 0032158987 scopus 로고    scopus 로고
    • ASK1 is essential for JNK/SAPK activation by TRAF2
    • Nishitoh, H., Saitoh, M., Mochida, Y., Takeda, K. et al., ASK1 is essential for JNK/SAPK activation by TRAF2. Molec. Cell 1998, 2, 389-395.
    • (1998) Molec. Cell , vol.2 , pp. 389-395
    • Nishitoh, H.1    Saitoh, M.2    Mochida, Y.3    Takeda, K.4
  • 65
    • 33746354022 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha induces neurotoxicity via glutamate release from hemichannels of activated microglia in an autocrine manner
    • Takeuchi, H., Jin, S., Wang, J., Zhang, G. et al., Tumor necrosis factor-alpha induces neurotoxicity via glutamate release from hemichannels of activated microglia in an autocrine manner. J. Biol. Chem. 2006, 281, 21362-21368.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21362-21368
    • Takeuchi, H.1    Jin, S.2    Wang, J.3    Zhang, G.4
  • 66
    • 37849010216 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha-mediated nitric oxide production enhances manganese superoxide dismutase nitration and mitochondrial dysfunction in primary neurons: an insight into the role of glial cells
    • Tangpong, J., Sompol, P., Vore, M., St Clair, W. et al., Tumor necrosis factor alpha-mediated nitric oxide production enhances manganese superoxide dismutase nitration and mitochondrial dysfunction in primary neurons: an insight into the role of glial cells. Neuroscience 2008, 151, 622-629.
    • (2008) Neuroscience , vol.151 , pp. 622-629
    • Tangpong, J.1    Sompol, P.2    Vore, M.3    St Clair, W.4
  • 67
    • 33744909882 scopus 로고    scopus 로고
    • Caspase-3 cleaves and inactivates the glutamate transporter EAAT2
    • Boston-Howes, W., Gibb, S. L., Williams, E. O., Pasinelli, P. et al., Caspase-3 cleaves and inactivates the glutamate transporter EAAT2. J. Biol. Chem. 2006, 281, 14076-14084.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14076-14084
    • Boston-Howes, W.1    Gibb, S.L.2    Williams, E.O.3    Pasinelli, P.4
  • 68
    • 14844316278 scopus 로고    scopus 로고
    • Positive and negative regulation of EAAT2 by NF-kappaB: a role for N-myc in TNFalpha-controlled repression
    • Sitcheran, R., Gupta, P., Fisher, P. B., Baldwin, A. S., Positive and negative regulation of EAAT2 by NF-kappaB: a role for N-myc in TNFalpha-controlled repression. EMBO J. 2005, 24, 510-520.
    • (2005) EMBO J. , vol.24 , pp. 510-520
    • Sitcheran, R.1    Gupta, P.2    Fisher, P.B.3    Baldwin, A.S.4
  • 69
    • 13844270562 scopus 로고    scopus 로고
    • TNF alpha potentiates glutamate neurotoxicity by inhibiting glutamate uptake in organotypic brain slice cultures: neuroprotection by NF kappa B inhibition
    • Zou, J. Y., Crews, F. T., TNF alpha potentiates glutamate neurotoxicity by inhibiting glutamate uptake in organotypic brain slice cultures: neuroprotection by NF kappa B inhibition. Brain Res. 2005, 1034, 11-24.
    • (2005) Brain Res. , vol.1034 , pp. 11-24
    • Zou, J.Y.1    Crews, F.T.2
  • 70
    • 33750801663 scopus 로고    scopus 로고
    • Involvement of TNF-alpha in glutamate-induced apoptosis in a differentiated neuronal cell line
    • Kogo, J., Takeba, Y., Kumai, T., Kitaoka, Y. et al., Involvement of TNF-alpha in glutamate-induced apoptosis in a differentiated neuronal cell line. Brain Res. 2006, 1122, 201-208.
    • (2006) Brain Res. , vol.1122 , pp. 201-208
    • Kogo, J.1    Takeba, Y.2    Kumai, T.3    Kitaoka, Y.4
  • 71
    • 16244376446 scopus 로고    scopus 로고
    • Differential regulation of AMPA receptor and GABA receptor trafficking by tumor necrosis factor-alpha
    • Stellwagen, D., Beattie, E. C., Seo, J. Y., Malenka, R. C., Differential regulation of AMPA receptor and GABA receptor trafficking by tumor necrosis factor-alpha. J. Neurosci. 2005, 25, 3219-3228.
    • (2005) J. Neurosci. , vol.25 , pp. 3219-3228
    • Stellwagen, D.1    Beattie, E.C.2    Seo, J.Y.3    Malenka, R.C.4
  • 72
    • 79955574686 scopus 로고    scopus 로고
    • 2-mercaptoethane sulfonate prevents doxorubicin-induced plasma protein oxidation and TNF-alpha release: implications for the reactive oxygen species-mediated mechanisms of chemobrain
    • Aluise, C. D., Miriyala, S., Noel, T., Sultana, R. et al., 2-mercaptoethane sulfonate prevents doxorubicin-induced plasma protein oxidation and TNF-alpha release: implications for the reactive oxygen species-mediated mechanisms of chemobrain. Free Radic. Biol. Med. 2011, 50, 1630-1638.
    • (2011) Free Radic. Biol. Med. , vol.50 , pp. 1630-1638
    • Aluise, C.D.1    Miriyala, S.2    Noel, T.3    Sultana, R.4
  • 73
    • 0028856460 scopus 로고
    • An English translation of Alzheimer's 1907 paper, "Uber eine eigenartige Erkankung der Hirnrinde"
    • Alzheimer, A., Stelzmann, R. A., Schnitzlein, H. N., Murtagh, F. R., An English translation of Alzheimer's 1907 paper, "Uber eine eigenartige Erkankung der Hirnrinde". Clin. Anat. 1995, 8, 429-431.
    • (1995) Clin. Anat. , vol.8 , pp. 429-431
    • Alzheimer, A.1    Stelzmann, R.A.2    Schnitzlein, H.N.3    Murtagh, F.R.4
  • 74
    • 0023009658 scopus 로고
    • Microtubule-associated protein tau. A component of Alzheimer paired helical filaments
    • Grundke-Iqbal, I., Iqbal, K., Quinlan, M., Tung, Y. C. et al., Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. J. Biol. Chem. 1986, 261, 6084-6089.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6084-6089
    • Grundke-Iqbal, I.1    Iqbal, K.2    Quinlan, M.3    Tung, Y.C.4
  • 75
  • 76
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang, J., Lemaire, H. G., Unterbeck, A., Salbaum, J. M. et al., The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 1987, 325, 733-736.
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3    Salbaum, J.M.4
  • 77
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • Goldgaber, D., Lerman, M. I., McBride, O. W., Saffiotti, U. et al., Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science 1987, 235, 877-880.
    • (1987) Science , vol.235 , pp. 877-880
    • Goldgaber, D.1    Lerman, M.I.2    McBride, O.W.3    Saffiotti, U.4
  • 78
    • 0023109592 scopus 로고
    • Amyloid beta protein gene: cDNA, mRNA distribution, and genetic linkage near the Alzheimer locus
    • Tanzi, R. E., Gusella, J. F., Watkins, P. C., Bruns, G. A. et al., Amyloid beta protein gene: cDNA, mRNA distribution, and genetic linkage near the Alzheimer locus. Science 1987, 235, 880-884.
    • (1987) Science , vol.235 , pp. 880-884
    • Tanzi, R.E.1    Gusella, J.F.2    Watkins, P.C.3    Bruns, G.A.4
  • 79
    • 34547102265 scopus 로고    scopus 로고
    • Roles of amyloid beta-peptide-associated oxidative stress and brain protein modifications in the pathogenesis of Alzheimer's disease and mild cognitive impairment
    • Butterfield, D. A., Reed, T., Newman, S. F., Sultana, R., Roles of amyloid beta-peptide-associated oxidative stress and brain protein modifications in the pathogenesis of Alzheimer's disease and mild cognitive impairment. Free Radic. Biol. Med. 2007, 43, 658-677.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 658-677
    • Butterfield, D.A.1    Reed, T.2    Newman, S.F.3    Sultana, R.4
  • 80
    • 33748423353 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: an approach to understand pathological and biochemical alterations in AD
    • Sultana, R., Boyd-Kimball, D., Poon, H. F., Cai, J. et al., Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: an approach to understand pathological and biochemical alterations in AD. Neurobiol. Aging 2006, 27, 1564-1576.
    • (2006) Neurobiol. Aging , vol.27 , pp. 1564-1576
    • Sultana, R.1    Boyd-Kimball, D.2    Poon, H.F.3    Cai, J.4
  • 81
    • 0024436506 scopus 로고
    • Relationship of microglia and astrocytes to amyloid deposits of Alzheimer disease
    • Itagaki, S., McGeer, P. L., Akiyama, H., Zhu, S. et al., Relationship of microglia and astrocytes to amyloid deposits of Alzheimer disease. J. Neuroimmunol. 1989, 24, 173-182.
    • (1989) J. Neuroimmunol. , vol.24 , pp. 173-182
    • Itagaki, S.1    McGeer, P.L.2    Akiyama, H.3    Zhu, S.4
  • 82
    • 33845286140 scopus 로고    scopus 로고
    • Convergence of genes implicated in Alzheimer's disease on the cerebral cholesterol shuttle: APP, cholesterol, lipoproteins, and atherosclerosis
    • Carter, C. J., Convergence of genes implicated in Alzheimer's disease on the cerebral cholesterol shuttle: APP, cholesterol, lipoproteins, and atherosclerosis. Neurochem. Int. 2007, 50, 12-38.
    • (2007) Neurochem. Int. , vol.50 , pp. 12-38
    • Carter, C.J.1
  • 83
    • 0027407565 scopus 로고
    • Apolipoprotein E: high-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease
    • Strittmatter, W. J., Saunders, A. M., Schmechel, D., Pericak-Vance, M. et al., Apolipoprotein E: high-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease. Proc. Natl. Acad. Sci. USA 1993, 90, 1977-1981.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1977-1981
    • Strittmatter, W.J.1    Saunders, A.M.2    Schmechel, D.3    Pericak-Vance, M.4
  • 84
    • 34247140072 scopus 로고    scopus 로고
    • Invited commentary: lipoproteins and dementia - is it the apolipoprotein A-I?
    • Scarmeas, N., Invited commentary: lipoproteins and dementia - is it the apolipoprotein A-I? Am. J. Epidemiol. 2007, 165, 993-997.
    • (2007) Am. J. Epidemiol. , vol.165 , pp. 993-997
    • Scarmeas, N.1
  • 85
    • 0033958076 scopus 로고    scopus 로고
    • Serum cholesterol, APOE genotype, and the risk of Alzheimer's disease: a population-based study of African Americans
    • Evans, R. M., Emsley, C. L., Gao, S., Sahota, A. et al., Serum cholesterol, APOE genotype, and the risk of Alzheimer's disease: a population-based study of African Americans. Neurology 2000, 54, 240-242.
    • (2000) Neurology , vol.54 , pp. 240-242
    • Evans, R.M.1    Emsley, C.L.2    Gao, S.3    Sahota, A.4
  • 86
    • 7244258941 scopus 로고    scopus 로고
    • Association of gamma-secretase with lipid rafts in post-Golgi and endosome membranes
    • Vetrivel, K. S., Cheng, H., Lin, W., Sakurai, T. et al., Association of gamma-secretase with lipid rafts in post-Golgi and endosome membranes. J. Biol. Chem. 2004, 279, 44945-44954.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44945-44954
    • Vetrivel, K.S.1    Cheng, H.2    Lin, W.3    Sakurai, T.4
  • 87
    • 0036776991 scopus 로고    scopus 로고
    • Function of beta-amyloid in cholesterol transport: a lead to neurotoxicity
    • Yao, Z. X., Papadopoulos, V., Function of beta-amyloid in cholesterol transport: a lead to neurotoxicity. FASEB J. 2002, 16, 1677-1679.
    • (2002) FASEB J. , vol.16 , pp. 1677-1679
    • Yao, Z.X.1    Papadopoulos, V.2
  • 88
    • 78651365099 scopus 로고    scopus 로고
    • Atorvastatin and pitavastatin improve cognitive function and reduce senile plaque and phosphorylated tau in aged APP mice
    • Kurata, T., Miyazaki, K., Kozuki, M., Panin, V. L. et al., Atorvastatin and pitavastatin improve cognitive function and reduce senile plaque and phosphorylated tau in aged APP mice. Brain Res. 2011, 1371, 161-170.
    • (2011) Brain Res. , vol.1371 , pp. 161-170
    • Kurata, T.1    Miyazaki, K.2    Kozuki, M.3    Panin, V.L.4
  • 89
    • 58249089520 scopus 로고    scopus 로고
    • Statins are associated with a reduced risk of Alzheimer disease regardless of lipophilicity. The Rotterdam Study
    • Haag, M. D., Hofman, A., Koudstaal, P. J., Stricker, B. H. et al., Statins are associated with a reduced risk of Alzheimer disease regardless of lipophilicity. The Rotterdam Study. J. Neurol. Neurosurg. Psychiat. 2009, 80, 13-17.
    • (2009) J. Neurol. Neurosurg. Psychiat. , vol.80 , pp. 13-17
    • Haag, M.D.1    Hofman, A.2    Koudstaal, P.J.3    Stricker, B.H.4
  • 90
    • 33745739157 scopus 로고    scopus 로고
    • Circulating cholesterol levels, apolipoprotein E genotype and dementia severity influence the benefit of atorvastatin treatment in Alzheimer's disease: results of the Alzheimer's disease cholesterol-lowering treatment (ADCLT) trial
    • Sparks, D. L., Connor, D. J., Sabbagh, M. N., Petersen, R. B. et al., Circulating cholesterol levels, apolipoprotein E genotype and dementia severity influence the benefit of atorvastatin treatment in Alzheimer's disease: results of the Alzheimer's disease cholesterol-lowering treatment (ADCLT) trial. Acta Neurol. Scand. 2006, 185, 3-7.
    • (2006) Acta Neurol. Scand. , vol.185 , pp. 3-7
    • Sparks, D.L.1    Connor, D.J.2    Sabbagh, M.N.3    Petersen, R.B.4
  • 91
    • 0036305918 scopus 로고    scopus 로고
    • The impact of the use of statins on the prevalence of dementia and the progression of cognitive impairment
    • Hajjar, I., Schumpert, J., Hirth, V., Wieland, D. et al., The impact of the use of statins on the prevalence of dementia and the progression of cognitive impairment. J. Gerontol. A Biol. Sci. Med. Sci. 2002, 57, M414-M418.
    • (2002) J. Gerontol. A Biol. Sci. Med. Sci. , vol.57
    • Hajjar, I.1    Schumpert, J.2    Hirth, V.3    Wieland, D.4
  • 92
    • 79851511930 scopus 로고    scopus 로고
    • Atorvastatin and Abeta(1-40): not as simple as cholesterol reduction in brain and relevance to Alzheimer disease
    • Butterfield, D. A., Atorvastatin and Abeta(1-40): not as simple as cholesterol reduction in brain and relevance to Alzheimer disease. Exp. Neurol. 2011, 228, 15-18.
    • (2011) Exp. Neurol. , vol.228 , pp. 15-18
    • Butterfield, D.A.1
  • 93
    • 84864349775 scopus 로고    scopus 로고
    • Atorvastatin treatment in a dog preclinical model of Alzheimer's disease leads to up-regulation of haem oxygenase-1 and is associated with reduced oxidative stress in brain
    • Butterfield, D. A., Barone, E., Di Domenico, F., Cenini, G. et al., Atorvastatin treatment in a dog preclinical model of Alzheimer's disease leads to up-regulation of haem oxygenase-1 and is associated with reduced oxidative stress in brain. Int. J. Neuropsychopharmacol. 2012, 15, 981-987.
    • (2012) Int. J. Neuropsychopharmacol. , vol.15 , pp. 981-987
    • Butterfield, D.A.1    Barone, E.2    Di Domenico, F.3    Cenini, G.4
  • 94
    • 79959953827 scopus 로고    scopus 로고
    • Cholesterol-independent neuroprotective and neurotoxic activities of statins: perspectives for statin use in Alzheimer disease and other age-related neurodegenerative disorders
    • Butterfield, D. A., Barone, E., Mancuso, C., Cholesterol-independent neuroprotective and neurotoxic activities of statins: perspectives for statin use in Alzheimer disease and other age-related neurodegenerative disorders. Pharmacol. Res. 2011, 64, 180-186.
    • (2011) Pharmacol. Res. , vol.64 , pp. 180-186
    • Butterfield, D.A.1    Barone, E.2    Mancuso, C.3
  • 95
    • 79751532850 scopus 로고    scopus 로고
    • Long-term high-dose atorvastatin decreases brain oxidative and nitrosative stress in a preclinical model of Alzheimer disease: a novel mechanism of action
    • Barone, E., Cenini, G., Di Domenico, F., Martin, S. et al., Long-term high-dose atorvastatin decreases brain oxidative and nitrosative stress in a preclinical model of Alzheimer disease: a novel mechanism of action. Pharmacol. Res. 2011, 63, 172-180.
    • (2011) Pharmacol. Res. , vol.63 , pp. 172-180
    • Barone, E.1    Cenini, G.2    Di Domenico, F.3    Martin, S.4
  • 96
    • 0029643560 scopus 로고
    • Marked decrease of plasma apolipoprotein AI and AII in Japanese patients with late-onset non-familial Alzheimer's disease
    • Kawano, M., Kawakami, M., Otsuka, M., Yashima, H. et al., Marked decrease of plasma apolipoprotein AI and AII in Japanese patients with late-onset non-familial Alzheimer's disease. Clin. Chim. Acta 1995, 239, 209-211.
    • (1995) Clin. Chim. Acta , vol.239 , pp. 209-211
    • Kawano, M.1    Kawakami, M.2    Otsuka, M.3    Yashima, H.4
  • 97
    • 0034594467 scopus 로고    scopus 로고
    • Decreased high-density lipoprotein cholesterol and serum apolipoprotein AI concentrations are highly correlated with the severity of Alzheimer's disease
    • Merched, A., Xia, Y., Visvikis, S., Serot, J. M. et al., Decreased high-density lipoprotein cholesterol and serum apolipoprotein AI concentrations are highly correlated with the severity of Alzheimer's disease. Neurobiol. Aging. 2000, 21, 27-30.
    • (2000) Neurobiol. Aging. , vol.21 , pp. 27-30
    • Merched, A.1    Xia, Y.2    Visvikis, S.3    Serot, J.M.4
  • 98
    • 32044446447 scopus 로고    scopus 로고
    • Proteomic identification of lower apolipoprotein A-I in Alzheimer's disease
    • Liu, H. C., Hu, C. J., Chang, J. G., Sung, S. M. et al., Proteomic identification of lower apolipoprotein A-I in Alzheimer's disease. Dement. Geriatr. Cogn. Disord. 2006, 21, 155-161.
    • (2006) Dement. Geriatr. Cogn. Disord. , vol.21 , pp. 155-161
    • Liu, H.C.1    Hu, C.J.2    Chang, J.G.3    Sung, S.M.4
  • 99
    • 34247103970 scopus 로고    scopus 로고
    • The relation between apolipoprotein A-I and dementia: the Honolulu-Asia aging study
    • Saczynski, J. S., White, L., Peila, R. L., Rodriguez, B. L. et al., The relation between apolipoprotein A-I and dementia: the Honolulu-Asia aging study. Am. J. Epidemiol. 2007, 165, 985-992.
    • (2007) Am. J. Epidemiol. , vol.165 , pp. 985-992
    • Saczynski, J.S.1    White, L.2    Peila, R.L.3    Rodriguez, B.L.4
  • 100
    • 0030763288 scopus 로고    scopus 로고
    • Cerebrospinal fluid apo E and apo A-I concentrations in early- and late-onset Alzheimer's disease
    • Song, H., Saito, K., Seishima, M., Noma, A. et al., Cerebrospinal fluid apo E and apo A-I concentrations in early- and late-onset Alzheimer's disease. Neurosci. Lett. 1997, 231, 175-178.
    • (1997) Neurosci. Lett. , vol.231 , pp. 175-178
    • Song, H.1    Saito, K.2    Seishima, M.3    Noma, A.4
  • 101
    • 0141957321 scopus 로고    scopus 로고
    • Proteomic studies of potential cerebrospinal fluid protein markers for Alzheimer's disease
    • Puchades, M., Hansson, S. F., Nilsson, C. L., Andreasen, N. et al., Proteomic studies of potential cerebrospinal fluid protein markers for Alzheimer's disease. Brain Res. Mol. Brain Res. 2003, 118, 140-146.
    • (2003) Brain Res. Mol. Brain Res. , vol.118 , pp. 140-146
    • Puchades, M.1    Hansson, S.F.2    Nilsson, C.L.3    Andreasen, N.4
  • 102
    • 33645776682 scopus 로고    scopus 로고
    • Comparative proteomics of cerebrospinal fluid in neuropathologically-confirmed Alzheimer's disease and non-demented elderly subjects
    • Castano, E. M., Roher, A. E., Esh, C. L., Kokjohn, T. A. et al., Comparative proteomics of cerebrospinal fluid in neuropathologically-confirmed Alzheimer's disease and non-demented elderly subjects. Neurol. Res. 2006, 28, 155-163.
    • (2006) Neurol. Res. , vol.28 , pp. 155-163
    • Castano, E.M.1    Roher, A.E.2    Esh, C.L.3    Kokjohn, T.A.4
  • 103
    • 0029063033 scopus 로고
    • Amyloid beta binding proteins in vitro and in normal human cerebrospinal fluid
    • Golabek, A., Marques, M. A., Lalowski, M., Wisniewski, T., Amyloid beta binding proteins in vitro and in normal human cerebrospinal fluid. Neurosci. Lett. 1995, 191, 79-82.
    • (1995) Neurosci. Lett. , vol.191 , pp. 79-82
    • Golabek, A.1    Marques, M.A.2    Lalowski, M.3    Wisniewski, T.4
  • 104
    • 0029081399 scopus 로고
    • Conformational mimicry in Alzheimer's disease. Role of apolipoproteins in amyloidogenesis
    • Wisniewski, T., Golabek, A. A., Kida, E., Wisniewski, K. E. et al., Conformational mimicry in Alzheimer's disease. Role of apolipoproteins in amyloidogenesis. Am. J. Pathol. 1995, 147, 238-244.
    • (1995) Am. J. Pathol. , vol.147 , pp. 238-244
    • Wisniewski, T.1    Golabek, A.A.2    Kida, E.3    Wisniewski, K.E.4
  • 105
    • 0035957222 scopus 로고    scopus 로고
    • Apolipoprotein A-I directly interacts with amyloid precursor protein and inhibits A beta aggregation and toxicity
    • Koldamova, R. P., Lefterov, I. M., Lefterova, M. I., Lazo, J. S., Apolipoprotein A-I directly interacts with amyloid precursor protein and inhibits A beta aggregation and toxicity. Biochemistry 2001, 40, 3553-3560.
    • (2001) Biochemistry , vol.40 , pp. 3553-3560
    • Koldamova, R.P.1    Lefterov, I.M.2    Lefterova, M.I.3    Lazo, J.S.4
  • 106
    • 78449255602 scopus 로고    scopus 로고
    • Overexpression of human apolipoprotein A-I preserves cognitive function and attenuates neuroinflammation and cerebral amyloid angiopathy in a mouse model of Alzheimer disease
    • Lewis, T. L., Cao, D., Lu, H., Mans, R. A. et al., Overexpression of human apolipoprotein A-I preserves cognitive function and attenuates neuroinflammation and cerebral amyloid angiopathy in a mouse model of Alzheimer disease. J. Biol. Chem. 2010, 285, 36958-36968.
    • (2010) J. Biol. Chem. , vol.285 , pp. 36958-36968
    • Lewis, T.L.1    Cao, D.2    Lu, H.3    Mans, R.A.4
  • 107
    • 78449232720 scopus 로고    scopus 로고
    • Apolipoprotein A-I deficiency increases cerebral amyloid angiopathy and cognitive deficits in APP/PS1DeltaE9 mice
    • Lefterov, I., Fitz, N. F., Cronican, A. A., Fogg, A. et al., Apolipoprotein A-I deficiency increases cerebral amyloid angiopathy and cognitive deficits in APP/PS1DeltaE9 mice. J. Biol. Chem. 2010, 285, 36945-36957.
    • (2010) J. Biol. Chem. , vol.285 , pp. 36945-36957
    • Lefterov, I.1    Fitz, N.F.2    Cronican, A.A.3    Fogg, A.4
  • 108
    • 0032837741 scopus 로고    scopus 로고
    • The levels of soluble versus insoluble brain Abeta distinguish Alzheimer's disease from normal and pathologic aging
    • Wang, J., Dickson, D. W., Trojanowski, J. Q., Lee, V. M., The levels of soluble versus insoluble brain Abeta distinguish Alzheimer's disease from normal and pathologic aging. Exp. Neurol. 1999, 158, 328-337.
    • (1999) Exp. Neurol. , vol.158 , pp. 328-337
    • Wang, J.1    Dickson, D.W.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 109
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • McLean, C. A., Cherny, R. A., Fraser, F. W., Fuller, S. J. et al., Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann. Neurol. 1999, 46, 860-866.
    • (1999) Ann. Neurol. , vol.46 , pp. 860-866
    • McLean, C.A.1    Cherny, R.A.2    Fraser, F.W.3    Fuller, S.J.4
  • 110
    • 84855583479 scopus 로고    scopus 로고
    • Oxidative stress and Down syndrome: a route toward Alzheimer-like dementia
    • Perluigi, M., Butterfield, D. A., Oxidative stress and Down syndrome: a route toward Alzheimer-like dementia. Curr. Gerontol. Geriatr. Res. 2012, 2012, 724904.
    • (2012) Curr. Gerontol. Geriatr. Res. , vol.2012 , pp. 724904
    • Perluigi, M.1    Butterfield, D.A.2
  • 111
    • 70449245071 scopus 로고
    • (Study of somatic chromosomes from 9 mongoloid children)
    • Lejeune, J., Gautier, M., Turpin, R., (Study of somatic chromosomes from 9 mongoloid children). C R Hebd Seances Acad. Sci. 1959, 248, 1721-1722.
    • (1959) C R Hebd Seances Acad. Sci. , vol.248 , pp. 1721-1722
    • Lejeune, J.1    Gautier, M.2    Turpin, R.3
  • 112
    • 0036261357 scopus 로고    scopus 로고
    • Genetic and host factors for dementia in Down's syndrome
    • Schupf, N., Sergievsky, G. H., Genetic and host factors for dementia in Down's syndrome. Br. J. Psychiat. 2002, 180, 405-410.
    • (2002) Br. J. Psychiat. , vol.180 , pp. 405-410
    • Schupf, N.1    Sergievsky, G.H.2
  • 113
    • 0015539755 scopus 로고
    • Neurofibrillary tangles in patients with Down's syndrome: a light and electron microscopic study
    • Schochet, S. S., Jr., Lampert, P. W., McCormick, W. F., Neurofibrillary tangles in patients with Down's syndrome: a light and electron microscopic study. Acta Neuropathol. 1973, 23, 342-346.
    • (1973) Acta Neuropathol. , vol.23 , pp. 342-346
    • Schochet Jr., S.S.1    Lampert, P.W.2    McCormick, W.F.3
  • 114
    • 33847349325 scopus 로고    scopus 로고
    • Oxidative stress: a bridge between Down's syndrome and Alzheimer's disease
    • Zana, M., Janka, Z., Kalman, J., Oxidative stress: a bridge between Down's syndrome and Alzheimer's disease. Neurobiol. Aging 2007, 28, 648-676.
    • (2007) Neurobiol. Aging , vol.28 , pp. 648-676
    • Zana, M.1    Janka, Z.2    Kalman, J.3
  • 115
    • 83055187877 scopus 로고    scopus 로고
    • Association between frontal cortex oxidative damage and beta-amyloid as a function of age in Down syndrome
    • Cenini, G., Dowling, A. L., Beckett, T. L., Barone, E. et al., Association between frontal cortex oxidative damage and beta-amyloid as a function of age in Down syndrome. Biochim. Biophys. Acta 2012, 1822, 130-138.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 130-138
    • Cenini, G.1    Dowling, A.L.2    Beckett, T.L.3    Barone, E.4
  • 116
    • 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 1995, 378, 776-779.
    • (1995) Nature , vol.378 , pp. 776-779
    • Busciglio, J.1    Yankner, B.A.2
  • 117
    • 79953120069 scopus 로고    scopus 로고
    • Oxidative stress occurs early in Down syndrome pregnancy: a redox proteomics analysis of amniotic fluid
    • Perluigi, M., Di Domenico, F., Fiorini, A., Cocciolo, A. et al., Oxidative stress occurs early in Down syndrome pregnancy: a redox proteomics analysis of amniotic fluid. Proteomics Clin. Appl. 2011, 5, 167-178.
    • (2011) Proteomics Clin. Appl. , vol.5 , pp. 167-178
    • Perluigi, M.1    Di Domenico, F.2    Fiorini, A.3    Cocciolo, A.4
  • 119
    • 74049085513 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of maternal plasma in Down syndrome pregnancies using isobaric tagging reagent (iTRAQ)
    • Kolla, V., Jeno, P., Moes, S., Tercanli, S. et al., Quantitative proteomics analysis of maternal plasma in Down syndrome pregnancies using isobaric tagging reagent (iTRAQ). J. Biomed. Biotechnol. 2010, 2010, 952047.
    • (2010) J. Biomed. Biotechnol. , vol.2010 , pp. 952047
    • Kolla, V.1    Jeno, P.2    Moes, S.3    Tercanli, S.4
  • 120
    • 84863364358 scopus 로고    scopus 로고
    • Identification of novel candidate maternal serum protein markers for Down syndrome by integrated proteomic and bioinformatic analysis
    • Kang, Y., Dong, X., Zhou, Q., Zhang, Y. et al., Identification of novel candidate maternal serum protein markers for Down syndrome by integrated proteomic and bioinformatic analysis. Prenat. Diagn. 2012, 32, 284-292.
    • (2012) Prenat. Diagn. , vol.32 , pp. 284-292
    • Kang, Y.1    Dong, X.2    Zhou, Q.3    Zhang, Y.4
  • 121
    • 69749098657 scopus 로고    scopus 로고
    • Bead-based multiplexed immunoassays to identify new biomarkers in maternal serum to improve first trimester Down syndrome screening
    • Koster, M. P., Pennings, J. L., Imholz, S., Rodenburg, W. et al., Bead-based multiplexed immunoassays to identify new biomarkers in maternal serum to improve first trimester Down syndrome screening. Prenat. Diagn. 2009, 29, 857-862.
    • (2009) Prenat. Diagn. , vol.29 , pp. 857-862
    • Koster, M.P.1    Pennings, J.L.2    Imholz, S.3    Rodenburg, W.4
  • 122
    • 33646868385 scopus 로고    scopus 로고
    • Proteomic analysis of Down's syndrome patients with gout
    • Chen, Y. C., Wang, P. W., Pan, T. L., Wallace, C. G. et al., Proteomic analysis of Down's syndrome patients with gout. Clin. Chim. Acta 2006, 369, 89-94.
    • (2006) Clin. Chim. Acta , vol.369 , pp. 89-94
    • Chen, Y.C.1    Wang, P.W.2    Pan, T.L.3    Wallace, C.G.4
  • 123
    • 77954961914 scopus 로고    scopus 로고
    • Comparative proteomic analysis of human amniotic fluid supernatants with Down syndrome using mass spectrometry
    • Park, J., Cha, D. H., Jung, J. W., Kim, Y. H. et al., Comparative proteomic analysis of human amniotic fluid supernatants with Down syndrome using mass spectrometry. J. Microbiol. Biotechnol. 2010, 20, 959-967.
    • (2010) J. Microbiol. Biotechnol. , vol.20 , pp. 959-967
    • Park, J.1    Cha, D.H.2    Jung, J.W.3    Kim, Y.H.4
  • 124
    • 34248148090 scopus 로고    scopus 로고
    • Proteomic analysis of maternal serum in Down syndrome: identification of novel protein biomarkers
    • Nagalla, S. R., Canick, J. A., Jacob, T., Schneider, K. A. et al., Proteomic analysis of maternal serum in Down syndrome: identification of novel protein biomarkers. J. Proteome Res. 2007, 6, 1245-1257.
    • (2007) J. Proteome Res. , vol.6 , pp. 1245-1257
    • Nagalla, S.R.1    Canick, J.A.2    Jacob, T.3    Schneider, K.A.4
  • 125
    • 0032936755 scopus 로고    scopus 로고
    • Etiology and pathogenesis of Parkinson's disease
    • Olanow, C. W., Tatton, W. G., Etiology and pathogenesis of Parkinson's disease. Annu. Rev. Neurosci. 1999, 22, 123-144.
    • (1999) Annu. Rev. Neurosci. , vol.22 , pp. 123-144
    • Olanow, C.W.1    Tatton, W.G.2
  • 126
    • 0029917194 scopus 로고    scopus 로고
    • Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson disease
    • Yoritaka, A., Hattori, N., Uchida, K., Tanaka, M. et al., Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson disease. Proc. Natl. Acad. Sci. USA 1996, 93, 2696-2701.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2696-2701
    • Yoritaka, A.1    Hattori, N.2    Uchida, K.3    Tanaka, M.4
  • 127
    • 0030805622 scopus 로고    scopus 로고
    • A generalised increase in protein carbonyls in the brain in Parkinson's but not incidental Lewy body disease
    • Alam, Z. I., Daniel, S. E., Lees, A. J., Marsden, D. C. et al., A generalised increase in protein carbonyls in the brain in Parkinson's but not incidental Lewy body disease. J. Neurochem. 1997, 69, 1326-1329.
    • (1997) J. Neurochem. , vol.69 , pp. 1326-1329
    • Alam, Z.I.1    Daniel, S.E.2    Lees, A.J.3    Marsden, D.C.4
  • 128
    • 0036197296 scopus 로고    scopus 로고
    • Systemic increase of oxidative nucleic acid damage in Parkinson's disease and multiple system atrophy
    • Kikuchi, A., Takeda, A., Onodera, H., Kimpara, T. et al., Systemic increase of oxidative nucleic acid damage in Parkinson's disease and multiple system atrophy. Neurobiol. Dis. 2002, 9, 244-248.
    • (2002) Neurobiol. Dis. , vol.9 , pp. 244-248
    • Kikuchi, A.1    Takeda, A.2    Onodera, H.3    Kimpara, T.4
  • 129
    • 74149087316 scopus 로고    scopus 로고
    • Oxidative damage in Parkinson disease: measurement using accurate biomarkers
    • Seet, R. C., Lee, C. Y., Lim, E. C., Tan, J. J. et al., Oxidative damage in Parkinson disease: measurement using accurate biomarkers. Free Radic. Biol. Med. 2010, 48, 560-566.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 560-566
    • Seet, R.C.1    Lee, C.Y.2    Lim, E.C.3    Tan, J.J.4
  • 130
    • 58849085001 scopus 로고    scopus 로고
    • Different patterns of oxidized lipid products in plasma and urine of dengue fever, stroke, and Parkinson's disease patients: cautions in the use of biomarkers of oxidative stress
    • Lee, C. Y., Seet, R. C., Huang, S. H., Long, L. H. et al., Different patterns of oxidized lipid products in plasma and urine of dengue fever, stroke, and Parkinson's disease patients: cautions in the use of biomarkers of oxidative stress. Antioxid. Redox Signal 2009, 11, 407-420.
    • (2009) Antioxid. Redox Signal , vol.11 , pp. 407-420
    • Lee, C.Y.1    Seet, R.C.2    Huang, S.H.3    Long, L.H.4
  • 131
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease
    • discussion S36-28.
    • Jenner, P., Oxidative stress in Parkinson's disease. Ann. Neurol. 2003, 53 Suppl 3, S26-S36; discussion S36-28.
    • (2003) Ann. Neurol. , vol.53 , Issue.SUPPL. 3
    • Jenner, P.1
  • 132
    • 62949121626 scopus 로고    scopus 로고
    • Neuronal pentraxin receptor in cerebrospinal fluid as a potential biomarker for neurodegenerative diseases
    • Yin, G. N., Lee, H. W., Cho, J. Y., Suk, K., Neuronal pentraxin receptor in cerebrospinal fluid as a potential biomarker for neurodegenerative diseases. Brain Res. 2009, 1265, 158-170.
    • (2009) Brain Res. , vol.1265 , pp. 158-170
    • Yin, G.N.1    Lee, H.W.2    Cho, J.Y.3    Suk, K.4
  • 133
    • 83455203344 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of serum proteins in patients with Parkinson's disease using an isobaric tag for relative and absolute quantification labeling, two-dimensional liquid chromatography, and tandem mass spectrometry
    • Zhang, X., Yin, X., Yu, H., Liu, X. et al., Quantitative proteomic analysis of serum proteins in patients with Parkinson's disease using an isobaric tag for relative and absolute quantification labeling, two-dimensional liquid chromatography, and tandem mass spectrometry. Analyst. 2012, 137, 490-495.
    • (2012) Analyst. , vol.137 , pp. 490-495
    • Zhang, X.1    Yin, X.2    Yu, H.3    Liu, X.4
  • 134
    • 33645465212 scopus 로고    scopus 로고
    • Is 'chemo-fog'/'chemo-brain' caused by cancer chemotherapy?
    • Raffa, R. B., Duong, P. V., Finney, J., Garber, D. A. et al., Is 'chemo-fog'/'chemo-brain' caused by cancer chemotherapy? J. Clin. Pharm. Ther. 2006, 31, 129-138.
    • (2006) J. Clin. Pharm. Ther. , vol.31 , pp. 129-138
    • Raffa, R.B.1    Duong, P.V.2    Finney, J.3    Garber, D.A.4
  • 135
    • 0017703085 scopus 로고
    • Anthracycline antibiotic augmentation of microsomal electron transport and free radical formation
    • Bachur, N. R., Gordon, S. L., Gee, M. V., Anthracycline antibiotic augmentation of microsomal electron transport and free radical formation. Mol. Pharmacol. 1977, 13, 901-910.
    • (1977) Mol. Pharmacol. , vol.13 , pp. 901-910
    • Bachur, N.R.1    Gordon, S.L.2    Gee, M.V.3
  • 136
    • 19944400407 scopus 로고    scopus 로고
    • Prevention of doxorubicin-induced acute cardiotoxicity by an experimental antioxidant compound
    • Deres, P., Halmosi, R., Toth, A., Kovacs, K. et al., Prevention of doxorubicin-induced acute cardiotoxicity by an experimental antioxidant compound. J. Cardiovasc Pharmacol. 2005, 45, 36-43.
    • (2005) J. Cardiovasc Pharmacol. , vol.45 , pp. 36-43
    • Deres, P.1    Halmosi, R.2    Toth, A.3    Kovacs, K.4
  • 137
    • 0028348480 scopus 로고
    • Interference by doxorubicin with DNA unwinding in MCF-7 breast tumor cells
    • Fornari, F. A., Randolph, J. K., Yalowich, J. C., Ritke, M. K. et al., Interference by doxorubicin with DNA unwinding in MCF-7 breast tumor cells. Mol. Pharmacol. 1994, 45, 649-656.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 649-656
    • Fornari, F.A.1    Randolph, J.K.2    Yalowich, J.C.3    Ritke, M.K.4
  • 138
    • 34347394526 scopus 로고    scopus 로고
    • Collateral damage in cancer chemotherapy: oxidative stress in nontargeted tissues
    • Chen, Y., Jungsuwadee, P., Vore, M., Butterfield, D. A. et al., Collateral damage in cancer chemotherapy: oxidative stress in nontargeted tissues. Mol. Interv. 2007, 7, 147-156.
    • (2007) Mol. Interv. , vol.7 , pp. 147-156
    • Chen, Y.1    Jungsuwadee, P.2    Vore, M.3    Butterfield, D.A.4
  • 139
    • 33845195053 scopus 로고    scopus 로고
    • Increase in Mrp1 expression and 4-hydroxy-2-nonenal adduction in heart tissue of Adriamycin-treated C57BL/6 mice
    • Jungsuwadee, P., Cole, M. P., Sultana, R., Joshi, G. et al., Increase in Mrp1 expression and 4-hydroxy-2-nonenal adduction in heart tissue of Adriamycin-treated C57BL/6 mice. Mol. Cancer Ther. 2006, 5, 2851-2860.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 2851-2860
    • Jungsuwadee, P.1    Cole, M.P.2    Sultana, R.3    Joshi, G.4
  • 140
    • 77956633238 scopus 로고    scopus 로고
    • Chemo brain (chemo fog) as a potential side effect of doxorubicin administration: role of cytokine-induced, oxidative/nitrosative stress in cognitive dysfunction
    • Aluise, C. D., Sultana, R., Tangpong, J., Vore, M. et al., Chemo brain (chemo fog) as a potential side effect of doxorubicin administration: role of cytokine-induced, oxidative/nitrosative stress in cognitive dysfunction. Adv. Exp. Med. Biol. 2010, 678, 147-156.
    • (2010) Adv. Exp. Med. Biol. , vol.678 , pp. 147-156
    • Aluise, C.D.1    Sultana, R.2    Tangpong, J.3    Vore, M.4
  • 141
    • 0027517309 scopus 로고
    • Murine tumor necrosis factor alpha is transported from blood to brain in the mouse
    • Gutierrez, E. G., Banks, W. A., Kastin, A. J., Murine tumor necrosis factor alpha is transported from blood to brain in the mouse. J. Neuroimmunol. 1993, 47, 169-176.
    • (1993) J. Neuroimmunol. , vol.47 , pp. 169-176
    • Gutierrez, E.G.1    Banks, W.A.2    Kastin, A.J.3
  • 142
    • 0036838512 scopus 로고    scopus 로고
    • Effect of endotoxin on expression of TNF receptors and transport of TNF-alpha at the blood-brain barrier of the rat
    • Osburg, B., Peiser, C., Domling, D., Schomburg, L. et al., Effect of endotoxin on expression of TNF receptors and transport of TNF-alpha at the blood-brain barrier of the rat. Am. J. Physiol. Endocrinol. Metab. 2002, 283, E899-E908.
    • (2002) Am. J. Physiol. Endocrinol. Metab. , vol.283
    • Osburg, B.1    Peiser, C.2    Domling, D.3    Schomburg, L.4
  • 143
    • 33746882124 scopus 로고    scopus 로고
    • Adriamycin-induced, TNF-alpha-mediated central nervous system toxicity
    • Tangpong, J., Cole, M. P., Sultana, R., Joshi, G. et al., Adriamycin-induced, TNF-alpha-mediated central nervous system toxicity. Neurobiol. Dis. 2006, 23, 127-139.
    • (2006) Neurobiol. Dis. , vol.23 , pp. 127-139
    • Tangpong, J.1    Cole, M.P.2    Sultana, R.3    Joshi, G.4
  • 144
    • 33846203801 scopus 로고    scopus 로고
    • Adriamycin-mediated nitration of manganese superoxide dismutase in the central nervous system: insight into the mechanism of chemobrain
    • Tangpong, J., Cole, M. P., Sultana, R., Estus, S. et al., Adriamycin-mediated nitration of manganese superoxide dismutase in the central nervous system: insight into the mechanism of chemobrain. J. Neurochem. 2007, 100, 191-201.
    • (2007) J. Neurochem. , vol.100 , pp. 191-201
    • Tangpong, J.1    Cole, M.P.2    Sultana, R.3    Estus, S.4
  • 145
    • 0035370748 scopus 로고    scopus 로고
    • Do white cells matter in white matter damage?
    • Dammann, O., Durum, S., Leviton, A., Do white cells matter in white matter damage? Trends Neurosci. 2001, 24, 320-324.
    • (2001) Trends Neurosci. , vol.24 , pp. 320-324
    • Dammann, O.1    Durum, S.2    Leviton, A.3
  • 146
    • 84864809901 scopus 로고    scopus 로고
    • JNK signaling is the shared pathway linking neuroinflammation, blood-brain barrier disruption, and oligodendroglial apoptosis in the white matter injury of the immature brain
    • Wang, L. W., Tu, Y. F., Huang, C. C., Ho, C. J., JNK signaling is the shared pathway linking neuroinflammation, blood-brain barrier disruption, and oligodendroglial apoptosis in the white matter injury of the immature brain. J. Neuroinflammation 2012, 9, 175.
    • (2012) J. Neuroinflammation , vol.9 , pp. 175
    • Wang, L.W.1    Tu, Y.F.2    Huang, C.C.3    Ho, C.J.4
  • 147
    • 33846005877 scopus 로고    scopus 로고
    • TNFalpha and TNF receptor 1 expression in the mixed neuronal-glial cultures of hippocampal dentate gyrus exposed to glutamate or trimethyltin
    • Figiel, I., Dzwonek, K., TNFalpha and TNF receptor 1 expression in the mixed neuronal-glial cultures of hippocampal dentate gyrus exposed to glutamate or trimethyltin. Brain Res. 2007, 1131, 17-28.
    • (2007) Brain Res. , vol.1131 , pp. 17-28
    • Figiel, I.1    Dzwonek, K.2
  • 148
    • 0030996264 scopus 로고    scopus 로고
    • Differential expression, cytokine modulation, and specific functions of type-1 and type-2 tumor necrosis factor receptors in rat glia
    • Dopp, J. M., Mackenzie-Graham, A., Otero, G. C., Merrill, J. E., Differential expression, cytokine modulation, and specific functions of type-1 and type-2 tumor necrosis factor receptors in rat glia. J. Neuroimmunol. 1997, 75, 104-112.
    • (1997) J. Neuroimmunol. , vol.75 , pp. 104-112
    • Dopp, J.M.1    Mackenzie-Graham, A.2    Otero, G.C.3    Merrill, J.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.