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Volumn 24, Issue 9, 2011, Pages 1411-1419

Exploring the biology of lipid peroxidation-derived protein carbonylation

Author keywords

[No Author keywords available]

Indexed keywords

4 HYDROXYNONENAL; ALDEHYDE DERIVATIVE; ELECTROPHILE; NUCLEOPHILE;

EID: 80052998418     PISSN: 0893228X     EISSN: 15205010     Source Type: Journal    
DOI: 10.1021/tx200169n     Document Type: Review
Times cited : (105)

References (88)
  • 1
    • 0042449072 scopus 로고
    • Oxidative Stress II
    • Academic Press, London.
    • Sies, H. (1991) Oxidative Stress II. Oxidants and Antioxidants, Academic Press, London.
    • (1991) Oxidants and Antioxidants
    • Sies, H.1
  • 3
    • 80053041158 scopus 로고    scopus 로고
    • Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective
    • not supplied.
    • Moller, I. M., Rogowska-Wrzesinska, A., and Rao, R. S. Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective. J. Proteomics 2011, not supplied.
    • (2011) J. Proteomics
    • Moller, I.M.1    Rogowska-Wrzesinska, A.2    Rao, R.S.3
  • 4
    • 77955455232 scopus 로고    scopus 로고
    • Proteomic identification of carbonylated proteins and their oxidation sites
    • Madian, A. G. and Regnier, F. E. (2010) Proteomic identification of carbonylated proteins and their oxidation sites J. Proteome Res. 9, 3766-3780
    • (2010) J. Proteome Res. , vol.9 , pp. 3766-3780
    • Madian, A.G.1    Regnier, F.E.2
  • 5
    • 55149107716 scopus 로고    scopus 로고
    • Radical-free biology of oxidative stress
    • Jones, D. P. (2008) Radical-free biology of oxidative stress Am. J. Physiol. Cell Physiol. 295, C849-868
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295 , pp. 849-868
    • Jones, D.P.1
  • 6
    • 0038275597 scopus 로고    scopus 로고
    • Free radicals and alcohol-induced liver injury
    • In (Sherman, V. P. a. R. W. Ed.) pp, Taylor and Francis, London.
    • Albano, E. (2002) Free radicals and alcohol-induced liver injury. In Ethanol and the Liver (Sherman, V. P. a. R. W., Ed.) pp 153-190, Taylor and Francis, London.
    • (2002) Ethanol and the Liver , pp. 153-190
    • Albano, E.1
  • 7
    • 0036211994 scopus 로고    scopus 로고
    • The Haber-Weiss cycle - 70 years later: An alternative view [1]
    • DOI 10.1179/135100002125000190
    • Liochev, S. I. and Fridovich, I. (2002) The Haber-Weiss cycle-70 years later: An alternative view Redox Rep. 7, 55-57; author reply 59-60 (Pubitemid 34285109)
    • (2002) Redox Report , vol.7 , Issue.1 , pp. 55-57
    • Liochev, S.I.1    Fridovich, I.2
  • 9
    • 0029037495 scopus 로고
    • The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide
    • Pryor, W. A. and Squadrito, G. L. (1995) The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide Am. J. Physiol. 268, L699-L722
    • (1995) Am. J. Physiol. , vol.268
    • Pryor, W.A.1    Squadrito, G.L.2
  • 10
    • 0033927959 scopus 로고    scopus 로고
    • Oxidation of LDL by myeloperoxidase and reactive nitrogen species: Reaction pathways and antioxidant protection
    • Carr, A. C., McCall, M. R., and Frei, B. (2000) Oxidation of LDL by myeloperoxidase and reactive nitrogen species: Reaction pathways and antioxidant protection Arterioscler., Thromb., Vasc. Biol. 20, 1716-1723 (Pubitemid 30470585)
    • (2000) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.20 , Issue.7 , pp. 1716-1723
    • Carr, A.C.1    McCall, M.R.2    Frei, B.3
  • 11
    • 23844442198 scopus 로고    scopus 로고
    • Cysteine modification by lipid peroxidation products inhibits protein disulfide isomerase
    • DOI 10.1021/tx050078z
    • Carbone, D. L., Doorn, J. A., Kiebler, Z., and Petersen, D. R. (2005) Cysteine modification by lipid peroxidation products inhibits protein disulfide isomerase Chem. Res. Toxicol. 18, 1324-1331 (Pubitemid 41174583)
    • (2005) Chemical Research in Toxicology , vol.18 , Issue.8 , pp. 1324-1331
    • Carbone, D.L.1    Doorn, J.A.2    Kiebler, Z.3    Petersen, D.R.4
  • 13
    • 33644637265 scopus 로고    scopus 로고
    • Decreased complex II respiration and HNE-modified SDH subunit in diabetic heart
    • DOI 10.1016/j.freeradbiomed.2005.10.040, PII S0891584905006350
    • Lashin, O. M., Szweda, P. A., Szweda, L. I., and Romani, A. M. (2006) Decreased complex II respiration and HNE-modified SDH subunit in diabetic heart Free Radical Biol. Med. 40, 886-896 (Pubitemid 43327322)
    • (2006) Free Radical Biology and Medicine , vol.40 , Issue.5 , pp. 886-896
    • Lashin, O.M.1    Szweda, P.A.2    Szweda, L.I.3    Romani, A.M.P.4
  • 14
    • 36849019121 scopus 로고    scopus 로고
    • Mechanisms of acrolein-induced myocardial dysfunction: Implications for environmental and endogenous aldehyde exposure
    • Luo, J., Hill, B. G., Gu, Y., Cai, J., Srivastava, S., Bhatnagar, A., and Prabhu, S. D. (2007) Mechanisms of acrolein-induced myocardial dysfunction: Implications for environmental and endogenous aldehyde exposure Am. J. Physiol. Heart Circ. Physiol. 293, H3673-3684
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.293 , pp. 3673-3684
    • Luo, J.1    Hill, B.G.2    Gu, Y.3    Cai, J.4    Srivastava, S.5    Bhatnagar, A.6    Prabhu, S.D.7
  • 15
    • 0031821531 scopus 로고    scopus 로고
    • Lipid hydroperoxide generation, turnover, and effector action in biological systems
    • Girotti, A. W. (1998) Lipid hydroperoxide generation, turnover, and effector action in biological systems J. Lipid Res. 39, 1529-1542 (Pubitemid 28377917)
    • (1998) Journal of Lipid Research , vol.39 , Issue.8 , pp. 1529-1542
    • Girotti, A.W.1
  • 16
    • 4444314070 scopus 로고    scopus 로고
    • Reactions of 4-hydroxynonenal with proteins and cellular targets
    • DOI 10.1016/j.freeradbiomed.2004.06.012, PII S0891584904004666
    • Petersen, D. R. and Doorn, J. A. (2004) Reactions of 4-hydroxynonenal with proteins and cellular targets Free Radical Biol. Med. 37, 937-945 (Pubitemid 39164576)
    • (2004) Free Radical Biology and Medicine , vol.37 , Issue.7 , pp. 937-945
    • Petersen, D.R.1    Doorn, J.A.2
  • 17
    • 34248591499 scopus 로고    scopus 로고
    • Upregulation of thioredoxin system via Nrf2-antioxidant responsive element pathway in adaptive-retinal neuroprotection in vivo and in vitro
    • DOI 10.1016/j.freeradbiomed.2007.03.018, PII S0891584907002146
    • Tanito, M., Agbaga, M. P., and Anderson, R. E. (2007) Upregulation of thioredoxin system via Nrf2-antioxidant responsive element pathway in adaptive-retinal neuroprotection in vivo and in vitro Free Radical Biol. Med. 42, 1838-1850 (Pubitemid 46754760)
    • (2007) Free Radical Biology and Medicine , vol.42 , Issue.12 , pp. 1838-1850
    • Tanito, M.1    Agbaga, M.-P.2    Anderson, R.E.3
  • 18
    • 1642396537 scopus 로고    scopus 로고
    • Role of Nrf2 in the Regulation of CD36 and Stress Protein Expression in Murine Macrophages: Activation by Oxidatively Modified LDL and 4-Hydroxynonenal
    • DOI 10.1161/01.RES.0000119171.44657.45
    • Ishii, T., Itoh, K., Ruiz, E., Leake, D. S., Unoki, H., Yamamoto, M., and Mann, G. E. (2004) Role of Nrf2 in the regulation of CD36 and stress protein expression in murine macrophages: Activation by oxidatively modified LDL and 4-hydroxynonenal Circ. Res. 94, 609-616 (Pubitemid 38387743)
    • (2004) Circulation Research , vol.94 , Issue.5 , pp. 609-616
    • Ishii, T.1    Itoh, K.2    Ruiz, E.3    Leake, D.S.4    Unoki, H.5    Yamamoto, M.6    Mann, G.E.7
  • 19
    • 21344473623 scopus 로고    scopus 로고
    • HNE increases HO-1 through activation of the ERK pathway in pulmonary epithelial cells
    • DOI 10.1016/j.freeradbiomed.2005.03.026, PII S0891584905001681
    • Iles, K. E., Dickinson, D. A., Wigley, A. F., Welty, N. E., Blank, V., and Forman, H. J. (2005) HNE increases HO-1 through activation of the ERK pathway in pulmonary epithelial cells Free Radical Biol. Med. 39, 355-364 (Pubitemid 40910192)
    • (2005) Free Radical Biology and Medicine , vol.39 , Issue.3 , pp. 355-364
    • Iles, K.E.1    Dickinson, D.A.2    Wigley, A.F.3    Welty, N.E.4    Blank, V.5    Forman, H.J.6
  • 20
    • 0032733640 scopus 로고    scopus 로고
    • Origin of 4-hydroxynonenal incubation-induced inhibition of dopamine transporter and Na+/K+ adenosine triphosphate in rat striatal synaptosomes
    • Fleuranceau-Morel, P., Barrier, L., Fauconneau, B., Piriou, A., and Huguet, F. (1999) Origin of 4-hydroxynonenal incubation-induced inhibition of dopamine transporter and Na+/K+ adenosine triphosphate in rat striatal synaptosomes Neurosci. Lett. 277, 91-94
    • (1999) Neurosci. Lett. , vol.277 , pp. 91-94
    • Fleuranceau-Morel, P.1    Barrier, L.2    Fauconneau, B.3    Piriou, A.4    Huguet, F.5
  • 21
    • 0036591849 scopus 로고    scopus 로고
    • Lipid peroxidation and protein oxidation in Alzheimer's disease brain: Potential causes and consequences involving amyloid β-peptide-associated free radical oxidative stress
    • DOI 10.1016/S0891-5849(02)00794-3, PII S0891584902007943
    • Butterfield, D. A. and Lauderback, C. M. (2002) Lipid peroxidation and protein oxidation in Alzheimer's disease brain: Potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress Free Radical Biol. Med. 32, 1050-1060 (Pubitemid 34603342)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.11 , pp. 1050-1060
    • Butterfield D.Allan1    Lauderback, C.M.2
  • 22
    • 33846949357 scopus 로고    scopus 로고
    • The oxidative stress metabolite 4-hydroxynonenal promotes Alzheimer protofibril formation
    • Siegel, S. J., Bieschke, J., Powers, E. T., and Kelly, J. W. (2007) The oxidative stress metabolite 4-hydroxynonenal promotes Alzheimer protofibril formation Biochemistry (Moscow) 46, 1503-1510
    • (2007) Biochemistry (Moscow) , vol.46 , pp. 1503-1510
    • Siegel, S.J.1    Bieschke, J.2    Powers, E.T.3    Kelly, J.W.4
  • 23
    • 33947644871 scopus 로고    scopus 로고
    • Protein oxidation and lipid peroxidation in brain of subjects with Alzheimer's disease: Insights into mechanism of neurodegeneration from redox proteomics
    • Sultana, R., Perluigi, M., and Butterfield, D. A. (2006) Protein oxidation and lipid peroxidation in brain of subjects with Alzheimer's disease: Insights into mechanism of neurodegeneration from redox proteomics Antioxid. Redox Signaling 8, 2021-2037 (Pubitemid 46499264)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.11-12 , pp. 2021-2037
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 24
    • 67349279818 scopus 로고    scopus 로고
    • Proteomic identification of HNE-bound proteins in early Alzheimer disease: Insights into the role of lipid peroxidation in the progression of AD
    • Reed, T. T., Pierce, W. M., Markesbery, W. R., and Butterfield, D. A. (2009) Proteomic identification of HNE-bound proteins in early Alzheimer disease: Insights into the role of lipid peroxidation in the progression of AD Brain Res. 1274, 66-76
    • (2009) Brain Res. , vol.1274 , pp. 66-76
    • Reed, T.T.1    Pierce, W.M.2    Markesbery, W.R.3    Butterfield, D.A.4
  • 25
    • 0026484388 scopus 로고
    • The oxidant stress hypothesis in Parkinson's disease: Evidence supporting it
    • Fahn, S. and Cohen, G. (1992) The oxidant stress hypothesis in Parkinson's disease: Evidence supporting it Ann. Neurol. 32, 804-812
    • (1992) Ann. Neurol. , vol.32 , pp. 804-812
    • Fahn, S.1    Cohen, G.2
  • 26
    • 0043172468 scopus 로고    scopus 로고
    • 4-Hydroxynonenal and neurodegenerative diseases
    • DOI 10.1016/S0098-2997(03)00024-4
    • Zarkovic, K. (2003) 4-hydroxynonenal and neurodegenerative diseases Mol. Aspects Med. 24, 293-303 (Pubitemid 36945029)
    • (2003) Molecular Aspects of Medicine , vol.24 , Issue.4-5 , pp. 293-303
    • Zarkovic, K.1
  • 27
    • 45249124663 scopus 로고    scopus 로고
    • 4-Hydroxynonenal: A membrane lipid oxidation product of medicinal interest
    • DOI 10.1002/med.20117
    • Poli, G., Schaur, R. J., Siems, W. G., and Leonarduzzi, G. (2008) 4-Hydroxynonenal: A membrane lipid oxidation product of medicinal interest Med. Res. Rev. 28, 569-631 (Pubitemid 351842143)
    • (2008) Medicinal Research Reviews , vol.28 , Issue.4 , pp. 569-631
    • Poli, G.1    Schaur, R.J.2    Siems, W.G.3    Leonarduzzi, G.4
  • 29
    • 79955830382 scopus 로고    scopus 로고
    • Modification of Akt2 by 4-hydroxynonenal inhibits insulin-dependent Akt signaling in HepG2 cells
    • Shearn, C. T., Fritz, K. S., Reigan, P., and Petersen, D. R. (2011) Modification of Akt2 by 4-hydroxynonenal inhibits insulin-dependent Akt signaling in HepG2 cells Biochemistry (Moscow) 50, 3984-3996
    • (2011) Biochemistry (Moscow) , vol.50 , pp. 3984-3996
    • Shearn, C.T.1    Fritz, K.S.2    Reigan, P.3    Petersen, D.R.4
  • 30
    • 70349492687 scopus 로고    scopus 로고
    • Molecular mechanisms of 4-hydroxy-2-nonenal and acrolein toxicity: Nucleophilic targets and adduct formation
    • LoPachin, R. M., Gavin, T., Petersen, D. R., and Barber, D. S. (2009) Molecular mechanisms of 4-hydroxy-2-nonenal and acrolein toxicity: Nucleophilic targets and adduct formation Chem. Res. Toxicol. 22, 1499-1508
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 1499-1508
    • Lopachin, R.M.1    Gavin, T.2    Petersen, D.R.3    Barber, D.S.4
  • 31
    • 43149094897 scopus 로고    scopus 로고
    • Albumin is the main nucleophilic target of human plasma: A protective role against pro-atherogenic electrophilic reactive carbonyl species?
    • DOI 10.1021/tx700349r
    • Aldini, G., Vistoli, G., Regazzoni, L., Gamberoni, L., Facino, R. M., Yamaguchi, S., Uchida, K., and Carini, M. (2008) Albumin is the main nucleophilic target of human plasma: A protective role against pro-atherogenic electrophilic reactive carbonyl species? Chem. Res. Toxicol. 21, 824-835 (Pubitemid 351644560)
    • (2008) Chemical Research in Toxicology , vol.21 , Issue.4 , pp. 824-835
    • Aldini, G.1    Vistoli, G.2    Regazzoni, L.3    Gamberoni, L.4    Facino, R.M.5    Yamaguchi, S.6    Uchida, K.7    Carini, M.8
  • 32
    • 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
    • DOI 10.1021/bi027172o
    • Ishii, T., Tatsuda, E., Kumazawa, S., Nakayama, T., and Uchida, K. (2003) Molecular basis of enzyme inactivation by an endogenous electrophile 4-hydroxy-2-nonenal: Identification of modification sites in glyceraldehyde-3-phosphate dehydrogenase Biochemistry (Moscow) 42, 3474-3480 (Pubitemid 36368641)
    • (2003) Biochemistry , vol.42 , Issue.12 , pp. 3474-3480
    • Ishii, T.1    Tatsuda, E.2    Kumazawa, S.3    Nakayama, T.4    Uchida, K.5
  • 33
    • 66049159838 scopus 로고    scopus 로고
    • Protein modification by acrolein: Formation and stability of cysteine adducts
    • Cai, J., Bhatnagar, A., and Pierce, W. M., Jr. (2009) Protein modification by acrolein: Formation and stability of cysteine adducts Chem. Res. Toxicol. 22, 708-716
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 708-716
    • Cai, J.1    Bhatnagar, A.2    Pierce Jr., W.M.3
  • 34
    • 33845606362 scopus 로고    scopus 로고
    • Structure-toxicity analysis of Type-2 Alkenes: In vitro neurotoxicity
    • DOI 10.1093/toxsci/kfl127
    • Lopachin, R. M., Barber, D. S., Geohagen, B. C., Gavin, T., He, D., and Das, S. (2007) Structure-toxicity analysis of type-2 alkenes: In vitro neurotoxicity Toxicol. Sci. 95, 136-146 (Pubitemid 44942784)
    • (2007) Toxicological Sciences , vol.95 , Issue.1 , pp. 136-146
    • LoPachin, R.M.1    Barber, D.S.2    Geohagen, B.C.3    Gavin, T.4    He, D.5    Das, S.6
  • 35
    • 0036852609 scopus 로고    scopus 로고
    • Covalent modification of amino acid nucleophiles by the lipid peroxidation products 4-hydroxy-2-nonenal and 4-oxo-2-nonenal
    • DOI 10.1021/tx025590o
    • Doorn, J. A. and Petersen, D. R. (2002) Covalent modification of amino acid nucleophiles by the lipid peroxidation products 4-hydroxy-2-nonenal and 4-oxo-2-nonenal Chem. Res. Toxicol. 15, 1445-1450 (Pubitemid 35364906)
    • (2002) Chemical Research in Toxicology , vol.15 , Issue.11 , pp. 1445-1450
    • Doorn, J.A.1    Petersen, D.R.2
  • 36
    • 23244458797 scopus 로고    scopus 로고
    • Covalent modification of actin by 4-hydroxy-trans-2-nonenal (HNE): LC-ESI-MS/MS evidence for Cys374 Michael adduction
    • DOI 10.1002/jms.872
    • Aldini, G., Dalle-Donne, I., Vistoli, G., Maffei Facino, R., and Carini, M. (2005) Covalent modification of actin by 4-hydroxy-trans-2-nonenal (HNE): LC-ESI-MS/MS evidence for Cys374 Michael adduction J. Mass Spectrom. 40, 946-954 (Pubitemid 41098081)
    • (2005) Journal of Mass Spectrometry , vol.40 , Issue.7 , pp. 946-954
    • Aldini, G.1    Dalle-Donne, I.2    Vistoli, G.3    Facino, R.M.4    Carini, M.5
  • 37
    • 58149096024 scopus 로고    scopus 로고
    • In Vitro and in Silico Characterization of Peroxiredoxin 6 Modified by 4-Hydroxynonenal and 4-Oxononenal
    • Roede, J. R., Carbone, D. L., Doorn, J. A., Kirichenko, O. V., Reigan, P., and Petersen, D. R. (2008) In Vitro and in Silico Characterization of Peroxiredoxin 6 Modified by 4-Hydroxynonenal and 4-Oxononenal Chem. Res. Toxicol. 21, 2289-2299
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 2289-2299
    • Roede, J.R.1    Carbone, D.L.2    Doorn, J.A.3    Kirichenko, O.V.4    Reigan, P.5    Petersen, D.R.6
  • 38
    • 33748256154 scopus 로고    scopus 로고
    • Covalent adduction of human serum albumin by 4-hydroxy-2-nonenal: Kinetic analysis of competing alkylation reactions
    • DOI 10.1021/bi060535q
    • Szapacs, M. E., Riggins, J. N., Zimmerman, L. J., and Liebler, D. C. (2006) Covalent adduction of human serum albumin by 4-hydroxy-2-nonenal: Kinetic analysis of competing alkylation reactions Biochemistry (Moscow) 45, 10521-10528 (Pubitemid 44320468)
    • (2006) Biochemistry , vol.45 , Issue.35 , pp. 10521-10528
    • Szapacs, M.E.1    Riggins, J.N.2    Zimmerman, L.J.3    Liebler, D.C.4
  • 39
    • 0035857738 scopus 로고    scopus 로고
    • Protein oxidation in the brain in Alzheimer's disease
    • DOI 10.1016/S0306-4522(00)00580-7, PII S0306452200005807
    • Aksenov, M. Y., Aksenova, M. V., Butterfield, D. A., Geddes, J. W., and Markesbery, W. R. (2001) Protein oxidation in the brain in Alzheimer's disease Neuroscience 103, 373-383 (Pubitemid 32201924)
    • (2001) Neuroscience , vol.103 , Issue.2 , pp. 373-383
    • Aksenov, M.Y.1    Aksenova, M.V.2    Butterfield, D.A.3    Geddes, J.W.4    Markesbery, W.R.5
  • 40
    • 16444379174 scopus 로고    scopus 로고
    • γ-glutamylcysteine ethyl ester-induced up-regulation of glutathione protects neurons against Aβ(1-42)-mediated oxidative stress and neurotoxicity: Implications for Alzheimer's disease
    • DOI 10.1002/jnr.20394
    • Boyd-Kimball, D., Sultana, R., Abdul, H. M., and Butterfield, D. A. (2005) Gamma-glutamylcysteine ethyl ester-induced up-regulation of glutathione protects neurons against Abeta(1-42)-mediated oxidative stress and neurotoxicity: Implications for Alzheimer's disease J. Neurosci. Res. 79, 700-706 (Pubitemid 40476449)
    • (2005) Journal of Neuroscience Research , vol.79 , Issue.5 , pp. 700-706
    • Boyd-Kimball, D.1    Sultana, R.2    Mohmmad Abdul, H.3    Butterfield, D.A.4
  • 41
    • 0037101889 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I: Creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1
    • DOI 10.1016/S0891-5849(02)00914-0, PII S0891584902009140
    • Castegna, A., Aksenov, M., Aksenova, M., Thongboonkerd, V., Klein, J. B., Pierce, W. M., Booze, R., Markesbery, W. R., and Butterfield, D. A. (2002) Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I: Creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1 Free Radical Biol. Med. 33, 562-571 (Pubitemid 34874977)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.4 , pp. 562-571
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3    Thongboonkerd, V.4    Klein, J.B.5    Pierce, W.M.6    Booze, R.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 43
    • 33749020292 scopus 로고    scopus 로고
    • Mass spectrometric characterization of covalent modification of human serum albumin by 4-hydroxy-trans-2-nonenal
    • DOI 10.1002/jms.1067
    • Aldini, G., Gamberoni, L., Orioli, M., Beretta, G., Regazzoni, L., Maffei Facino, R., and Carini, M. (2006) Mass spectrometric characterization of covalent modification of human serum albumin by 4-hydroxy-trans-2-nonenal J. Mass Spectrom. 41, 1149-1161 (Pubitemid 44454168)
    • (2006) Journal of Mass Spectrometry , vol.41 , Issue.9 , pp. 1149-1161
    • Aldini, G.1    Gamberoni, L.2    Orioli, M.3    Beretta, G.4    Regazzoni, L.5    Facino, R.M.6    Carini, M.7
  • 45
    • 67651007592 scopus 로고    scopus 로고
    • Protein carbonylation in THP-1 cells induced by cigarette smoke extract via a copper-catalyzed pathway
    • Lin, C. C., Su, T. H., and Wang, T. S. (2009) Protein carbonylation in THP-1 cells induced by cigarette smoke extract via a copper-catalyzed pathway Chem. Res. Toxicol. 22, 1232-1238
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 1232-1238
    • Lin, C.C.1    Su, T.H.2    Wang, T.S.3
  • 46
    • 33846421564 scopus 로고    scopus 로고
    • Ethanol-induced oxidative stress suppresses generation of peptides for antigen presentation by hepatoma cells
    • DOI 10.1002/hep.21442
    • Osna, N. A., White, R. L., Todero, S., McVicker, B. L., Thiele, G. M., Clemens, D. L., Tuma, D. J., and Donohue, T. M., Jr. (2007) Ethanol-induced oxidative stress suppresses generation of peptides for antigen presentation by hepatoma cells Hepatology 45, 53-61 (Pubitemid 46144364)
    • (2007) Hepatology , vol.45 , Issue.1 , pp. 53-61
    • Osna, N.A.1    White, R.L.2    Todero, S.3    Mc Vicker, B.L.4    Thiele, G.M.5    Clemens, D.L.6    Tuma, D.J.7    Donohue Jr., T.M.8
  • 47
    • 74149087665 scopus 로고    scopus 로고
    • Toxicity of smoke extracts towards A549 lung cells: Role of acrolein and suppression by carbonyl scavengers
    • Burcham, P. C., Raso, A., and Thompson, C. A. (2010) Toxicity of smoke extracts towards A549 lung cells: Role of acrolein and suppression by carbonyl scavengers Chem.-Biol. Interact. 183, 416-424
    • (2010) Chem.-Biol. Interact. , vol.183 , pp. 416-424
    • Burcham, P.C.1    Raso, A.2    Thompson, C.A.3
  • 48
    • 34250193289 scopus 로고    scopus 로고
    • Induction of COX-2 by acrolein in rat lung epithelial cells
    • DOI 10.1007/s11010-007-9411-z
    • Sarkar, P. and Hayes, B. E. (2007) Induction of COX-2 by acrolein in rat lung epithelial cells Mol. Cell. Biochem. 301, 191-199 (Pubitemid 46895160)
    • (2007) Molecular and Cellular Biochemistry , vol.301 , Issue.1-2 , pp. 191-199
    • Sarkar, P.1    Hayes, B.E.2
  • 49
    • 67650239323 scopus 로고    scopus 로고
    • Lipid aldehyde-mediated cross-linking of apolipoprotein B-100 inhibits secretion from HepG2 cells
    • Stewart, B. J., Roede, J. R., Doorn, J. A., and Petersen, D. R. (2009) Lipid aldehyde-mediated cross-linking of apolipoprotein B-100 inhibits secretion from HepG2 cells Biochim. Biophys. Acta 1791, 772-780
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 772-780
    • Stewart, B.J.1    Roede, J.R.2    Doorn, J.A.3    Petersen, D.R.4
  • 50
    • 36048944481 scopus 로고    scopus 로고
    • Transfection of HepG2 cells with hGSTA4 provides protection against 4-hydroxynonenal-mediated oxidative injury
    • DOI 10.1016/j.tiv.2007.04.004, PII S0887233307001452
    • Gallagher, E. P., Huisden, C. M., and Gardner, J. L. (2007) Transfection of HepG2 cells with hGSTA4 provides protection against 4-hydroxynonenal-mediated oxidative injury Toxicol. in Vitro 21, 1365-1372 (Pubitemid 350086851)
    • (2007) Toxicology in Vitro , vol.21 , Issue.8 , pp. 1365-1372
    • Gallagher, E.P.1    Huisden, C.M.2    Gardner, J.L.3
  • 51
    • 67649814628 scopus 로고    scopus 로고
    • Proteomic profiling of rat lung epithelial cells induced by acrolein
    • Sarkar, P. and Hayes, B. E. (2009) Proteomic profiling of rat lung epithelial cells induced by acrolein Life Sci. 85, 188-195
    • (2009) Life Sci. , vol.85 , pp. 188-195
    • Sarkar, P.1    Hayes, B.E.2
  • 52
    • 78650147789 scopus 로고    scopus 로고
    • Roles of 3-nitrotyrosine- and 4-hydroxynonenal-modified brain proteins in the progression and pathogenesis of Alzheimer's disease
    • Butterfield, D. A., Reed, T., and Sultana, R. (2011) Roles of 3-nitrotyrosine- and 4-hydroxynonenal-modified brain proteins in the progression and pathogenesis of Alzheimer's disease Free Radical Res. 45, 59-72
    • (2011) Free Radical Res. , vol.45 , pp. 59-72
    • Butterfield, D.A.1    Reed, T.2    Sultana, R.3
  • 53
    • 41549164723 scopus 로고    scopus 로고
    • Detection of carbonyl-modified proteins in interfibrillar rat mitochondria using N′-aminooxymethylcarbonylhydrazino-D-biotin as an aldehyde/keto-reactive probe in combination with Western blot analysis and tandem mass spectrometry
    • DOI 10.1002/elps.200700606
    • Chung, W. G., Miranda, C. L., and Maier, C. S. (2008) Detection of carbonyl-modified proteins in interfibrillar rat mitochondria using N′-aminooxymethylcarbonylhydrazino-D-biotin as an aldehyde/keto-reactive probe in combination with Western blot analysis and tandem mass spectrometry Electrophoresis 29, 1317-1324 (Pubitemid 351461085)
    • (2008) Electrophoresis , vol.29 , Issue.6 , pp. 1317-1324
    • Chung, W.-G.1    Miranda, C.L.2    Maier, C.S.3
  • 54
    • 33847329229 scopus 로고    scopus 로고
    • Ethanol-induced modulation of hepatocellular extracellular signal-regulated kinase-1/2 activity via 4-hydroxynonenal
    • DOI 10.1074/jbc.M610602200
    • Sampey, B. P., Stewart, B. J., and Petersen, D. R. (2007) Ethanol-induced modulation of hepatocellular extracellular signal-regulated kinase-1/2 activity via 4-hydroxynonenal J. Biol. Chem. 282, 1925-1937 (Pubitemid 47076723)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.3 , pp. 1925-1937
    • Sampey, B.P.1    Stewart, B.J.2    Petersen, D.R.3
  • 56
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer, H., Schaur, R. J., and Zollner, H. (1991) Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes Free Radical Biol. Med. 11, 81-128 (Pubitemid 121003917)
    • (1991) Free Radical Biology and Medicine , vol.11 , Issue.1 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 57
    • 52049088770 scopus 로고    scopus 로고
    • Oxidative stress and covalent modification of protein with bioactive aldehydes
    • Grimsrud, P. A., Xie, H., Griffin, T. J., and Bernlohr, D. A. (2008) Oxidative stress and covalent modification of protein with bioactive aldehydes J. Biol. Chem. 283, 21837-21841
    • (2008) J. Biol. Chem. , vol.283 , pp. 21837-21841
    • Grimsrud, P.A.1    Xie, H.2    Griffin, T.J.3    Bernlohr, D.A.4
  • 58
    • 33845390864 scopus 로고    scopus 로고
    • Protein adducts generated from products of lipid oxidation: Focus on HNE and ONE
    • DOI 10.1080/03602530600959508, PII X078211547323X23
    • Sayre, L. M., Lin, D., Yuan, Q., Zhu, X., and Tang, X. (2006) Protein adducts generated from products of lipid oxidation: Focus on HNE and one Drug Metab. Rev. 38, 651-675 (Pubitemid 44903261)
    • (2006) Drug Metabolism Reviews , vol.38 , Issue.4 , pp. 651-675
    • Sayre, L.M.1    Lin, D.2    Yuan, Q.3    Zhu, X.4    Tang, X.5
  • 59
    • 0027480753 scopus 로고
    • Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase. A possible involvement of intra- and intermolecular cross- linking reaction
    • Uchida, K. and Stadtman, E. R. (1993) Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase. A possible involvement of intra- and intermolecular cross-linking reaction J. Biol. Chem. 268, 6388-6393 (Pubitemid 23099334)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.9 , pp. 6388-6393
    • Uchida, K.1    Stadtman, E.R.2
  • 60
    • 0043172509 scopus 로고    scopus 로고
    • Basic aspects of the biochemical reactivity of 4-hydroxynonenal
    • DOI 10.1016/S0098-2997(03)00009-8
    • Schaur, R. J. (2003) Basic aspects of the biochemical reactivity of 4-hydroxynonenal Mol. Aspects Med. 24, 149-159 (Pubitemid 36945015)
    • (2003) Molecular Aspects of Medicine , vol.24 , Issue.4-5 , pp. 149-159
    • Schaur, R.J.1
  • 61
    • 79952550111 scopus 로고    scopus 로고
    • A mass spectrometric analysis of 4-hydroxy-2-(E)-nonenal modification of cytochrome c
    • Tang, X., Sayre, L. M., and Tochtrop, G. P. (2011) A mass spectrometric analysis of 4-hydroxy-2-(E)-nonenal modification of cytochrome c J. Mass Spectrom. 46, 290-297
    • (2011) J. Mass Spectrom. , vol.46 , pp. 290-297
    • Tang, X.1    Sayre, L.M.2    Tochtrop, G.P.3
  • 62
    • 77449148487 scopus 로고    scopus 로고
    • Antioxidant enzyme expression, lipid peroxidation, and protein oxidation in human myometrium with parturition
    • Khan, R. N., Matharoo-Ball, B., and Shaw, R. W. (2010) Antioxidant enzyme expression, lipid peroxidation, and protein oxidation in human myometrium with parturition Reprod. Sci. 17, 78-84
    • (2010) Reprod. Sci. , vol.17 , pp. 78-84
    • Khan, R.N.1    Matharoo-Ball, B.2    Shaw, R.W.3
  • 63
    • 0346634902 scopus 로고    scopus 로고
    • Immunoaffinity purification and characterization of 4-hydroxy-2-nonenal- and malondialdehyde-modified peptides by electrospray ionization tandem mass spectrometry
    • DOI 10.1021/ac020443g
    • Fenaille, F., Tabet, J. C., and Guy, P. A. (2002) Immunoaffinity purification and characterization of 4-hydroxy-2-nonenal- and malondialdehyde-modified peptides by electrospray ionization tandem mass spectrometry Anal. Chem. 74, 6298-6304 (Pubitemid 36025176)
    • (2002) Analytical Chemistry , vol.74 , Issue.24 , pp. 6298-6304
    • Fenaille, F.1    Tabet, J.-C.2    Guy, P.A.3
  • 64
    • 34249043563 scopus 로고    scopus 로고
    • Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry
    • DOI 10.1021/ac0617971
    • Roe, M. R., Xie, H., Bandhakavi, S., and Griffin, T. J. (2007) Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry Anal. Chem. 79, 3747-3756 (Pubitemid 46799071)
    • (2007) Analytical Chemistry , vol.79 , Issue.10 , pp. 3747-3756
    • Roe, M.R.1    Xie, H.2    Bandhakavi, S.3    Griffin, T.J.4
  • 65
    • 0344084088 scopus 로고    scopus 로고
    • High-Throughput Proteomic-Based Identification of Oxidatively Induced Protein Carbonylation in Mouse Brain
    • DOI 10.1023/B:PHAM.0000003366.25263.78
    • Soreghan, B. A., Yang, F., Thomas, S. N., Hsu, J., and Yang, A. J. (2003) High-throughput proteomic-based identification of oxidatively induced protein carbonylation in mouse brain Pharm. Res. 20, 1713-1720 (Pubitemid 37449442)
    • (2003) Pharmaceutical Research , vol.20 , Issue.11 , pp. 1713-1720
    • Soreghan, B.A.1    Yang, F.2    Thomas, S.N.3    Hsu, J.4    Yang, A.J.5
  • 66
    • 33749457861 scopus 로고    scopus 로고
    • New role for an old probe: Affinity labeling of oxylipid protein conjugates by N′-aminooxymethylcarbonylhydrazino D-biotin
    • DOI 10.1021/ac0607257
    • Chavez, J., Wu, J., Han, B., Chung, W. G., and Maier, C. S. (2006) New role for an old probe: affinity labeling of oxylipid protein conjugates by N′-aminooxymethylcarbonylhydrazino d-biotin Anal. Chem. 78, 6847-6854 (Pubitemid 44522535)
    • (2006) Analytical Chemistry , vol.78 , Issue.19 , pp. 6847-6854
    • Chavez, J.1    Wu, J.2    Han, B.3    Chung, W.-G.4    Maier, C.S.5
  • 67
    • 76849104804 scopus 로고    scopus 로고
    • Differential proteomics analysis of specific carbonylated proteins in the temporal cortex of aged rats: The deterioration of antioxidant system
    • Wang, Q., Zhao, X., He, S., Liu, Y., An, M., and Ji, J. (2010) Differential proteomics analysis of specific carbonylated proteins in the temporal cortex of aged rats: The deterioration of antioxidant system Neurochem. Res. 35, 13-21
    • (2010) Neurochem. Res. , vol.35 , pp. 13-21
    • Wang, Q.1    Zhao, X.2    He, S.3    Liu, Y.4    An, M.5    Ji, J.6
  • 69
    • 42049099009 scopus 로고    scopus 로고
    • Identification of oxidized proteins in rat plasma using avidin chromatography and tandem mass spectrometry
    • DOI 10.1002/pmic.200700363
    • Mirzaei, H., Baena, B., Barbas, C., and Regnier, F. (2008) Identification of oxidized proteins in rat plasma using avidin chromatography and tandem mass spectrometry Proteomics 8, 1516-1527 (Pubitemid 351518558)
    • (2008) Proteomics , vol.8 , Issue.7 , pp. 1516-1527
    • Mirzaei, H.1    Baena, B.2    Barbas, C.3    Regnier, F.E.4
  • 70
    • 34248233116 scopus 로고    scopus 로고
    • Design, synthesis, and application of a hydrazide-functionalized isotope-coded affinity tag for the quantification of oxylipid-protein conjugates
    • DOI 10.1021/ac062262a
    • Han, B., Stevens, J. F., and Maier, C. S. (2007) Design, synthesis, and application of a hydrazide-functionalized isotope-coded affinity tag for the quantification of oxylipid-protein conjugates Anal. Chem. 79, 3342-3354 (Pubitemid 46717165)
    • (2007) Analytical Chemistry , vol.79 , Issue.9 , pp. 3342-3354
    • Han, B.1    Stevens, J.F.2    Maier, C.S.3
  • 73
    • 34548658592 scopus 로고    scopus 로고
    • A modified Girard derivatizing reagent for universal profiling and trace analysis of aldehydes and ketones by electrospray ionization tandem mass spectrometry
    • DOI 10.1002/rcm.3175
    • Johnson, D. W. (2007) A modified Girard derivatizing reagent for universal profiling and trace analysis of aldehydes and ketones by electrospray ionization tandem mass spectrometry Rapid Commun. Mass Spectrom. 21, 2926-2932 (Pubitemid 47401428)
    • (2007) Rapid Communications in Mass Spectrometry , vol.21 , Issue.18 , pp. 2926-2932
    • Johnson, D.W.1
  • 74
    • 32444449409 scopus 로고    scopus 로고
    • Enrichment of carbonylated peptides using Girard P reagent and strong cation exchange chromatography
    • DOI 10.1021/ac0514220
    • Mirzaei, H. and Regnier, F. (2006) Enrichment of carbonylated peptides using Girard P reagent and strong cation exchange chromatography Anal. Chem. 78, 770-778 (Pubitemid 43228584)
    • (2006) Analytical Chemistry , vol.78 , Issue.3 , pp. 770-778
    • Mirzaei, H.1    Regnier, F.2
  • 75
    • 33750350410 scopus 로고    scopus 로고
    • Identification and quantification of protein carbonylation using light and heavy isotope labeled Girard's P reagent
    • DOI 10.1016/j.chroma.2006.08.096, PII S0021967306016797
    • Mirzaei, H. and Regnier, F. (2006) Identification and quantification of protein carbonylation using light and heavy isotope labeled Girard's P reagent J Chromatogr. A 1134, 122-133 (Pubitemid 44633939)
    • (2006) Journal of Chromatography A , vol.1134 , Issue.1-2 , pp. 122-133
    • Mirzaei, H.1    Regnier, F.2
  • 76
    • 1942522084 scopus 로고    scopus 로고
    • Profiling enzyme activities in vivo using click chemistry methods
    • DOI 10.1016/j.chembiol.2004.03.012, PII S1074552104000961
    • Speers, A. E. and Cravatt, B. F. (2004) Profiling enzyme activities in vivo using click chemistry methods Chem. Biol. 11, 535-546 (Pubitemid 38511759)
    • (2004) Chemistry and Biology , vol.11 , Issue.4 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2
  • 77
    • 41649118986 scopus 로고    scopus 로고
    • Identification of protein targets of 4-hydroxynonenal using click chemistry for ex vivo biotinylation of azido and alkynyl derivatives
    • Vila, A., Tallman, K. A., Jacobs, A. T., Liebler, D. C., Porter, N. A., and Marnett, L. J. (2008) Identification of protein targets of 4-hydroxynonenal using click chemistry for ex vivo biotinylation of azido and alkynyl derivatives Chem. Res. Toxicol. 21, 432-444
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 432-444
    • Vila, A.1    Tallman, K.A.2    Jacobs, A.T.3    Liebler, D.C.4    Porter, N.A.5    Marnett, L.J.6
  • 78
    • 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. Mol
    • Kim, H. Y., Tallman, K. A., Liebler, D. C., and Porter, N. A. (2009) An azido-biotin reagent for use in the isolation of protein adducts of lipid-derived electrophiles by streptavidin catch and photorelease. Mol Cell. Proteomics 8, 2080-2089
    • (2009) Cell. Proteomics , vol.8 , pp. 2080-2089
    • Kim, H.Y.1    Tallman, K.A.2    Liebler, D.C.3    Porter, N.A.4
  • 79
    • 80052972191 scopus 로고    scopus 로고
    • Identification and Characterization of Oxylipid-Protein and Peptide Conjugates by Mass Spectrometry
    • Maier, W. C. a. C. (2008) Identification and Characterization of Oxylipid-Protein and Peptide Conjugates by Mass Spectrometry Curr. Protoc. Toxicol. 35, 17.19.11-17.19.19
    • (2008) Curr. Protoc. Toxicol. , vol.35 , pp. 171911-171919
    • Maier A. C W, C.1
  • 80
    • 0036182039 scopus 로고    scopus 로고
    • Proteomic approaches to characterize protein modifications: New tools to study the effects of environmental exposures
    • Liebler, D. C. (2002) Proteomic approaches to characterize protein modifications: new tools to study the effects of environmental exposures. Environ Health Perspect. 110 (Suppl. 1) 3-9 (Pubitemid 34163089)
    • (2002) Environmental Health Perspectives , vol.110 , Issue.SUPPL. 1 , pp. 3-9
    • Liebler, D.C.1
  • 81
    • 38949089246 scopus 로고    scopus 로고
    • Protein damage by reactive electrophiles: Targets and consequences
    • DOI 10.1021/tx700235t
    • Liebler, D. C. (2008) Protein damage by reactive electrophiles: targets and consequences Chem. Res. Toxicol. 21, 117-128 (Pubitemid 351219713)
    • (2008) Chemical Research in Toxicology , vol.21 , Issue.1 , pp. 117-128
    • Liebler, D.C.1
  • 82
    • 58249128642 scopus 로고    scopus 로고
    • Development of a derivatisation method for the analysis of aldehyde modified amino acid residues in proteins by Fourier transform mass spectrometry
    • Pournamdari, M., Saadi, A., Ellis, E., Andrew, R., Walker, B., and Watson, D. G. (2009) Development of a derivatisation method for the analysis of aldehyde modified amino acid residues in proteins by Fourier transform mass spectrometry Anal. Chim. Acta 633, 216-222
    • (2009) Anal. Chim. Acta , vol.633 , pp. 216-222
    • Pournamdari, M.1    Saadi, A.2    Ellis, E.3    Andrew, R.4    Walker, B.5    Watson, D.G.6
  • 83
    • 46849098407 scopus 로고    scopus 로고
    • Comprehensive comparison of collision induced dissociation and electron transfer dissociation
    • DOI 10.1021/ac8007785
    • Molina, H., Matthiesen, R., Kandasamy, K., and Pandey, A. (2008) Comprehensive comparison of collision induced dissociation and electron transfer dissociation Anal. Chem. 80, 4825-4835 (Pubitemid 351956289)
    • (2008) Analytical Chemistry , vol.80 , Issue.13 , pp. 4825-4835
    • Molina, H.1    Matthiesen, R.2    Kandasamy, K.3    Pandey, A.4
  • 84
    • 35649012000 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometry of covalent adducts of proteins and 4-hydroxy-2-nonenal, a reactive end-product of lipid peroxidation
    • DOI 10.1007/s00216-007-1534-2, Ultrahigh Resolution Mass Spectrometry
    • Rauniyar, N., Stevens, S. M., Jr., and Prokai, L. (2007) Fourier transform ion cyclotron resonance mass spectrometry of covalent adducts of proteins and 4-hydroxy-2-nonenal, a reactive end-product of lipid peroxidation Anal. Bioanal. Chem. 389, 1421-1428 (Pubitemid 350023666)
    • (2007) Analytical and Bioanalytical Chemistry , vol.389 , Issue.5 , pp. 1421-1428
    • Rauniyar, N.1    Stevens Jr., S.M.2    Prokai, L.3
  • 85
    • 60549083972 scopus 로고    scopus 로고
    • Characterization of 4-hydroxy-2-nonenal-modified peptides by liquid chromatography-tandem mass spectrometry using data-dependent acquisition: Neutral loss-driven MS3 versus neutral loss-driven electron capture dissociation
    • Rauniyar, N., Stevens, S. M., Prokai-Tatrai, K., and Prokai, L. (2009) Characterization of 4-hydroxy-2-nonenal-modified peptides by liquid chromatography-tandem mass spectrometry using data-dependent acquisition: Neutral loss-driven MS3 versus neutral loss-driven electron capture dissociation Anal. Chem. 81, 782-789
    • (2009) Anal. Chem. , vol.81 , pp. 782-789
    • Rauniyar, N.1    Stevens, S.M.2    Prokai-Tatrai, K.3    Prokai, L.4
  • 87
    • 70350357221 scopus 로고    scopus 로고
    • Stereochemical configuration of 4-hydroxy-2-nonenal-cysteine adducts and their stereoselective formation in a redox-regulated protein
    • Wakita, C., Maeshima, T., Yamazaki, A., Shibata, T., Ito, S., Akagawa, M., Ojika, M., Yodoi, J., and Uchida, K. (2009) Stereochemical configuration of 4-hydroxy-2-nonenal-cysteine adducts and their stereoselective formation in a redox-regulated protein J. Biol. Chem. 284, 28810-28822
    • (2009) J. Biol. Chem. , vol.284 , pp. 28810-28822
    • Wakita, C.1    Maeshima, T.2    Yamazaki, A.3    Shibata, T.4    Ito, S.5    Akagawa, M.6    Ojika, M.7    Yodoi, J.8    Uchida, K.9
  • 88
    • 77952650680 scopus 로고    scopus 로고
    • Systems analysis of protein modification and cellular responses induced by electrophile stress
    • Jacobs, A. T. and Marnett, L. J. (2010) Systems analysis of protein modification and cellular responses induced by electrophile stress Acc. Chem. Res. 43, 673-683
    • (2010) Acc. Chem. Res. , vol.43 , pp. 673-683
    • Jacobs, A.T.1    Marnett, L.J.2


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