메뉴 건너뛰기




Volumn 23, Issue 1, 2010, Pages 37-47

Site-specific protein adducts of 4-hydroxy-2(e)-nonenal in human THP-1 monocytic cells: Protein carbonylation is diminished by ascorbic acid

Author keywords

[No Author keywords available]

Indexed keywords

4 HYDROXYNONENAL; ALPHA ACTININ 4; ALPHA TUBULIN; ASCORBIC ACID; FRUCTOSE BISPHOSPHATE ALDOLASE; PHOSPHOGLYCERATE DEHYDROGENASE; VIMENTIN;

EID: 75149140183     PISSN: 0893228X     EISSN: 15205010     Source Type: Journal    
DOI: 10.1021/tx9002462     Document Type: Article
Times cited : (68)

References (55)
  • 1
    • 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.
    • (1991) Free Radical Biol. Med , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 2
    • 0037411282 scopus 로고    scopus 로고
    • 4-Hydroxy-2-nonenal: A product and mediator of oxidative stress
    • Uchida, K. (2003) 4-Hydroxy-2-nonenal: a product and mediator of oxidative stress. Prog. Lipid Res. 42, 318-343.
    • (2003) Prog. Lipid Res , vol.42 , pp. 318-343
    • Uchida, K.1
  • 3
    • 0345017021 scopus 로고    scopus 로고
    • Formation of trans-4-hydroxy-2-nonenal- and other enal-derived cyclic DNA adducts from omega-3 and omega-6 polyunsaturated fatty acids and their roles in DNA repair and human p53 gene mutation
    • Chung, F. L., Pan, J., Choudhury, S., Roy, R., Hu, W., and Tang, M. S. (2003) Formation of trans-4-hydroxy-2-nonenal- and other enal-derived cyclic DNA adducts from omega-3 and omega-6 polyunsaturated fatty acids and their roles in DNA repair and human p53 gene mutation. Mutat. Res. 531, 25-36.
    • (2003) Mutat. Res , vol.531 , pp. 25-36
    • Chung, F.L.1    Pan, J.2    Choudhury, S.3    Roy, R.4    Hu, W.5    Tang, M.S.6
  • 4
    • 0036905921 scopus 로고    scopus 로고
    • Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: Implications for neurodegeneration in Alzheimer's disease brain. A review
    • Butterfield, D. A. (2002) Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review. Free Radical Res. 36, 1307-1313.
    • (2002) Free Radical Res , vol.36 , pp. 1307-1313
    • Butterfield, D.A.1
  • 5
    • 60849109931 scopus 로고    scopus 로고
    • Hop proanthocyanidins induce apoptosis, protein carbonylation, and cytoskeleton disorganization in human colorectal adenocarcinoma cells via reactive oxygen species
    • Chung, W. G., Miranda, C. L., Stevens, J. F., and Maier, C. S. (2009) Hop proanthocyanidins induce apoptosis, protein carbonylation, and cytoskeleton disorganization in human colorectal adenocarcinoma cells via reactive oxygen species. Food Chem. Toxicol. 47, 827-836.
    • (2009) Food Chem. Toxicol , vol.47 , pp. 827-836
    • Chung, W.G.1    Miranda, C.L.2    Stevens, J.F.3    Maier, C.S.4
  • 6
    • 50949103793 scopus 로고    scopus 로고
    • The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal
    • Forman, H. J., Fukuto, J. M., Miller, T., Zhang, H., Rinna, A., and Levy, S. (2008) The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal. Arch. Biochem. Biophys. 477, 183-195.
    • (2008) Arch. Biochem. Biophys , vol.477 , pp. 183-195
    • Forman, H.J.1    Fukuto, J.M.2    Miller, T.3    Zhang, H.4    Rinna, A.5    Levy, S.6
  • 7
    • 33644514643 scopus 로고    scopus 로고
    • Endogenous reactive intermediates as modulators of cell signaling and cell death
    • West, J. D., and Marnett, L. J. (2006) Endogenous reactive intermediates as modulators of cell signaling and cell death. Chem. Res. Toxicol. 19, 173-194.
    • (2006) Chem. Res. Toxicol , vol.19 , pp. 173-194
    • West, J.D.1    Marnett, L.J.2
  • 9
    • 10044294918 scopus 로고    scopus 로고
    • Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal
    • Ferrington, D. A., and Kapphahn, R. J. (2004) Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal. FEBS Lett. 578, 217-223.
    • (2004) FEBS Lett , vol.578 , pp. 217-223
    • Ferrington, D.A.1    Kapphahn, R.J.2
  • 11
    • 33845390864 scopus 로고    scopus 로고
    • Protein adducts generated from products of lipid oxidation: Focus on HNE and one
    • 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.
    • (2006) Drug Metab. Rev , vol.38 , pp. 651-675
    • Sayre, L.M.1    Lin, D.2    Yuan, Q.3    Zhu, X.4    Tang, X.5
  • 12
    • 45249124663 scopus 로고    scopus 로고
    • 4-Hydroxynonenal: A membrane lipid oxidation product of medicinal interest
    • 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.
    • (2008) Med. Res. Rev , vol.28 , pp. 569-631
    • Poli, G.1    Schaur, R.J.2    Siems, W.G.3    Leonarduzzi, G.4
  • 14
    • 61349123614 scopus 로고    scopus 로고
    • The essential role of ERK in 4-oxo-2-nonenal-mediated cytotoxicity in SH-SY5Y human neuroblastoma cells
    • Lee, H. P., Zhu, X., Skidmore, S. C., Perry, G., Sayre, L. M., Smith, M. A., and Lee, H. G. (2009) The essential role of ERK in 4-oxo-2-nonenal-mediated cytotoxicity in SH-SY5Y human neuroblastoma cells. J. Neurochem. 108, 1434-1441.
    • (2009) J. Neurochem , vol.108 , pp. 1434-1441
    • Lee, H.P.1    Zhu, X.2    Skidmore, S.C.3    Perry, G.4    Sayre, L.M.5    Smith, M.A.6    Lee, H.G.7
  • 16
    • 34748907199 scopus 로고    scopus 로고
    • Carbonylation of mitochondrial proteins in Drosophila melanogaster during aging
    • Toroser, D., Orr, W. C., and Sohal, R. S. (2007) Carbonylation of mitochondrial proteins in Drosophila melanogaster during aging. Biochem. Biophys. Res. Commun. 363, 418-424.
    • (2007) Biochem. Biophys. Res. Commun , vol.363 , pp. 418-424
    • Toroser, D.1    Orr, W.C.2    Sohal, R.S.3
  • 17
    • 25644451257 scopus 로고    scopus 로고
    • Modification of heat shock protein 90 by 4-hydroxynonenal in a rat model of chronic alcoholic liver disease
    • Carbone, D. L., Doorn, J. A., Kiebler, Z., Ickes, B. R., and Petersen, D. R. (2005) Modification of heat shock protein 90 by 4-hydroxynonenal in a rat model of chronic alcoholic liver disease. J. Pharmacol. Exp. Ther. 315, 8-15.
    • (2005) J. Pharmacol. Exp. Ther , vol.315 , pp. 8-15
    • Carbone, D.L.1    Doorn, J.A.2    Kiebler, Z.3    Ickes, B.R.4    Petersen, D.R.5
  • 18
    • 23844442198 scopus 로고    scopus 로고
    • Cysteine modification by lipid peroxidation products inhibits protein disulfide isomerase
    • 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.
    • (2005) Chem. Res. Toxicol , vol.18 , pp. 1324-1331
    • Carbone, D.L.1    Doorn, J.A.2    Kiebler, Z.3    Petersen, D.R.4
  • 19
    • 33749457861 scopus 로고    scopus 로고
    • New role for an old probe: Affinity labeling of oxylipid protein conjugates by N′-aminooxymethylcarbonylhydrazino D-biotin
    • 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.
    • (2006) Anal. Chem , vol.78 , pp. 6847-6854
    • Chavez, J.1    Wu, J.2    Han, B.3    Chung, W.G.4    Maier, C.S.5
  • 21
    • 34248233116 scopus 로고    scopus 로고
    • Design, synthesis, and application of a hydrazide-functionalized isotope-coded affinity tag for the quantification of oxylipid-protein conjugates
    • 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.
    • (2007) Anal. Chem , vol.79 , pp. 3342-3354
    • Han, B.1    Stevens, J.F.2    Maier, C.S.3
  • 22
    • 17644362744 scopus 로고    scopus 로고
    • Affinity chromatographic selection of carbonylated proteins followed by identification of oxidation sites using tandem mass spectrometry
    • Mirzaei, H., and Regnier, F. (2005) Affinity chromatographic selection of carbonylated proteins followed by identification of oxidation sites using tandem mass spectrometry. Anal. Chem. 77, 2386-2392.
    • (2005) Anal. Chem , vol.77 , pp. 2386-2392
    • Mirzaei, H.1    Regnier, F.2
  • 23
    • 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
  • 24
    • 34249043563 scopus 로고    scopus 로고
    • Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry
    • 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.
    • (2007) Anal. Chem , vol.79 , pp. 3747-3756
    • Roe, M.R.1    Xie, H.2    Bandhakavi, S.3    Griffin, T.J.4
  • 25
    • 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
  • 26
    • 0026085408 scopus 로고
    • THP-1 cells form foam cells in response to coculture with lipoproteins but not platelets
    • Banka, C. L., Black, A. S., Dyer, C. A., and Curtiss, L. K. (1991) THP-1 cells form foam cells in response to coculture with lipoproteins but not platelets. J. Lipid Res. 32, 35-43.
    • (1991) J. Lipid Res , vol.32 , pp. 35-43
    • Banka, C.L.1    Black, A.S.2    Dyer, C.A.3    Curtiss, L.K.4
  • 27
    • 67649908957 scopus 로고    scopus 로고
    • Ascorbic acid promotes detoxification and elimination of 4-hydroxy-2(E)-nonenal in human monocytic THP-1 cells
    • Miranda, C. L., Reed, R. L., Kuiper, H. C., Alber, S., and Stevens, J. F. (2009) Ascorbic acid promotes detoxification and elimination of 4-hydroxy-2(E)-nonenal in human monocytic THP-1 cells. Chem. Res. Toxicol. 22, 863-874.
    • (2009) Chem. Res. Toxicol , vol.22 , pp. 863-874
    • Miranda, C.L.1    Reed, R.L.2    Kuiper, H.C.3    Alber, S.4    Stevens, J.F.5
  • 28
    • 41549164723 scopus 로고    scopus 로고
    • Detection of carbonyl-modified proteins in interfibrillar rat mitochondria using N′-aminooxymethylcarbonylhydrazino-D-biotin as an aldehyde/ketoreactive probe in combination with Western blot analysis and tandem mass spectrometry
    • 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/ketoreactive probe in combination with Western blot analysis and tandem mass spectrometry. Electrophoresis 29, 1317-1324.
    • (2008) Electrophoresis , vol.29 , pp. 1317-1324
    • Chung, W.G.1    Miranda, C.L.2    Maier, C.S.3
  • 29
    • 75149169949 scopus 로고    scopus 로고
    • Mass Spectrometry-Based Identification and Characterization of Oxylipid-Protein Conjugates
    • John Wiley & Sons, Inc, Hoboken, NJ; Unit 17.19
    • Chung, W. G., and Maier, C. S. (2008) Mass Spectrometry-Based Identification and Characterization of Oxylipid-Protein Conjugates, in Current Protocols in Toxicology; John Wiley & Sons, Inc., Hoboken, NJ; Unit 17.19.
    • (2008) Current Protocols in Toxicology
    • Chung, W.G.1    Maier, C.S.2
  • 30
    • 44449149681 scopus 로고    scopus 로고
    • Cell responses regulated by early reorganization of actin cytoskeleton
    • Papakonstanti, E. A., and Stournaras, C. (2008) Cell responses regulated by early reorganization of actin cytoskeleton. FEBS Lett. 582, 2120-2127.
    • (2008) FEBS Lett , vol.582 , pp. 2120-2127
    • Papakonstanti, E.A.1    Stournaras, C.2
  • 31
    • 0031443822 scopus 로고    scopus 로고
    • Apoptosis and necrosis in toxicology: A continuum or distinct modes of cell death?
    • Raffray, M., and Cohen, G. M. (1997) Apoptosis and necrosis in toxicology: a continuum or distinct modes of cell death? Pharmacol. Ther. 75, 153-177.
    • (1997) Pharmacol. Ther , vol.75 , pp. 153-177
    • Raffray, M.1    Cohen, G.M.2
  • 32
    • 0017651857 scopus 로고
    • Characterization of the mRNAs for alpha-, beta- and gamma-actin
    • Hunter, T., and Garrels, J. I. (1977) Characterization of the mRNAs for alpha-, beta- and gamma-actin. Cell 12, 767-781.
    • (1977) Cell , vol.12 , pp. 767-781
    • Hunter, T.1    Garrels, J.I.2
  • 34
    • 33845724468 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen species as signaling molecules regulating neutrophil function
    • Fialkow, L., Wang, Y., and Downey, G. P. (2007) Reactive oxygen and nitrogen species as signaling molecules regulating neutrophil function. Free Radical Biol. Med. 42, 153-164.
    • (2007) Free Radical Biol. Med , vol.42 , pp. 153-164
    • Fialkow, L.1    Wang, Y.2    Downey, G.P.3
  • 35
    • 58149170170 scopus 로고    scopus 로고
    • Coronin: The double-edged sword of actin dynamics
    • Gandhi, M., and Goode, B. L. (2008) Coronin: the double-edged sword of actin dynamics. Subcell. Biochem. 48, 72-87.
    • (2008) Subcell. Biochem , vol.48 , pp. 72-87
    • Gandhi, M.1    Goode, B.L.2
  • 36
    • 0029132690 scopus 로고
    • Sequence analysis and chromosomal localization of human Cap Z. Conserved residues within the actin-binding domain may link Cap Z to gelsolin/severin and profilin protein families
    • Barron-Casella, E. A., Torres, M. A., Scherer, S. W., Heng, H. H., Tsui, L. C., and Casella, J. F. (1995) Sequence analysis and chromosomal localization of human Cap Z. Conserved residues within the actin-binding domain may link Cap Z to gelsolin/severin and profilin protein families. J. Biol. Chem. 270, 21472-21479.
    • (1995) J. Biol. Chem , vol.270 , pp. 21472-21479
    • Barron-Casella, E.A.1    Torres, M.A.2    Scherer, S.W.3    Heng, H.H.4    Tsui, L.C.5    Casella, J.F.6
  • 37
    • 0034012322 scopus 로고    scopus 로고
    • Autophagic and apoptotic types of programmed cell death exhibit different fates of cytoskeletal filaments
    • Bursch, W., Hochegger, K., Torok, L., Marian, B., Ellinger, A., and Hermann, R. S. (2000) Autophagic and apoptotic types of programmed cell death exhibit different fates of cytoskeletal filaments. J. Cell Sci. 113 (Pt. 7), 1189-1198.
    • (2000) J. Cell Sci , vol.113 , Issue.PART. 7 , pp. 1189-1198
    • Bursch, W.1    Hochegger, K.2    Torok, L.3    Marian, B.4    Ellinger, A.5    Hermann, R.S.6
  • 40
    • 34548477636 scopus 로고    scopus 로고
    • Residue-specific adduction of tubulin by 4-hydroxynonenal and 4-oxononenal causes cross-linking and inhibits polymerization
    • Stewart, B. J., Doorn, J. A., and Petersen, D. R. (2007) Residue-specific adduction of tubulin by 4-hydroxynonenal and 4-oxononenal causes cross-linking and inhibits polymerization. Chem. Res. Toxicol. 20, 1111-1119.
    • (2007) Chem. Res. Toxicol , vol.20 , pp. 1111-1119
    • Stewart, B.J.1    Doorn, J.A.2    Petersen, D.R.3
  • 41
    • 0042861598 scopus 로고    scopus 로고
    • Proteomic changes in renal cancer and co-ordinate demonstration of both the glycolytic and mitochondrial aspects of the Warburg effect
    • Unwin, R. D., Craven, R. A., Harnden, P., Hanrahan, S., Totty, N., Knowles, M., Eardley, I., Selby, P. J., and Banks, R. E. (2003) Proteomic changes in renal cancer and co-ordinate demonstration of both the glycolytic and mitochondrial aspects of the Warburg effect. Proteomics 3, 1620-1632.
    • (2003) Proteomics , vol.3 , pp. 1620-1632
    • Unwin, R.D.1    Craven, R.A.2    Harnden, P.3    Hanrahan, S.4    Totty, N.5    Knowles, M.6    Eardley, I.7    Selby, P.J.8    Banks, R.E.9
  • 42
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional alpha-enolase: Its role in diseases
    • Pancholi, V. (2001) Multifunctional alpha-enolase: its role in diseases. Cell. Mol. Life Sci. 58, 902-920.
    • (2001) Cell. Mol. Life Sci , vol.58 , pp. 902-920
    • Pancholi, V.1
  • 43
    • 40849120274 scopus 로고    scopus 로고
    • Redox proteomic identification of 4-hydroxy-2-nonenal-modified brain proteins in amnestic mild cognitive impairment: Insight into the role of lipid peroxidation in the progression and pathogenesis of Alzheimer's disease
    • Reed, T., Perluigi, M., Sultana, R., Pierce, W. M., Klein, J. B., Turner, D. M., Coccia, R., Markesbery, W. R., and Butterfield, D. A. (2008) Redox proteomic identification of 4-hydroxy-2-nonenal-modified brain proteins in amnestic mild cognitive impairment: insight into the role of lipid peroxidation in the progression and pathogenesis of Alzheimer's disease. Neurobiol. Dis. 30, 107-120.
    • (2008) Neurobiol. Dis , vol.30 , pp. 107-120
    • Reed, T.1    Perluigi, M.2    Sultana, R.3    Pierce, W.M.4    Klein, J.B.5    Turner, D.M.6    Coccia, R.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 44
    • 33646144212 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: Insights into the development of Alzheimer's disease
    • Butterfield, D. A., Poon, H. F., St Clair, D., Keller, J. N., Pierce, W. M., Klein, J. B., and Markesbery, W. R. (2006) Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: insights into the development of Alzheimer's disease. Neurobiol. Dis. 22, 223-232.
    • (2006) Neurobiol. Dis , vol.22 , pp. 223-232
    • Butterfield, D.A.1    Poon, H.F.2    St Clair, D.3    Keller, J.N.4    Pierce, W.M.5    Klein, J.B.6    Markesbery, W.R.7
  • 45
    • 37749052671 scopus 로고    scopus 로고
    • Glycolitic enzymes are targets of oxidation in aged human frontal cortex and oxidative damage of these proteins is increased in progressive supranuclear palsy
    • Martinez, A., Dalfo, E., Muntane, G., and Ferrer, I. (2008) Glycolitic enzymes are targets of oxidation in aged human frontal cortex and oxidative damage of these proteins is increased in progressive supranuclear palsy. J. Neural. Transm. 115, 59-66.
    • (2008) J. Neural. Transm , vol.115 , pp. 59-66
    • Martinez, A.1    Dalfo, E.2    Muntane, G.3    Ferrer, I.4
  • 47
    • 0029975931 scopus 로고    scopus 로고
    • The molecular nature of the F-actin binding activity of aldolase revealed with site-directed mutants
    • Wang, J., Morris, A. J., Tolan, D. R., and Pagliaro, L. (1996) The molecular nature of the F-actin binding activity of aldolase revealed with site-directed mutants. J. Biol. Chem. 271, 6861-6865.
    • (1996) J. Biol. Chem , vol.271 , pp. 6861-6865
    • Wang, J.1    Morris, A.J.2    Tolan, D.R.3    Pagliaro, L.4
  • 48
    • 0031568822 scopus 로고    scopus 로고
    • A glycolytic enzyme binding domain on tubulin
    • Volker, K. W., and Knull, H. (1997) A glycolytic enzyme binding domain on tubulin. Arch. Biochem. Biophys. 338, 237-243.
    • (1997) Arch. Biochem. Biophys , vol.338 , pp. 237-243
    • Volker, K.W.1    Knull, H.2
  • 49
    • 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
  • 50
    • 0014288982 scopus 로고
    • The catalytic versatility of erythrocyte carbonic anhydrase. V. Kinetic studies of enzyme-catalyzed hydrations of aliphatic aldehydes
    • Pocker, Y., and Dickerson, D. G. (1968) The catalytic versatility of erythrocyte carbonic anhydrase. V. Kinetic studies of enzyme-catalyzed hydrations of aliphatic aldehydes. Biochemistry 7, 1995-2004.
    • (1968) Biochemistry , vol.7 , pp. 1995-2004
    • Pocker, Y.1    Dickerson, D.G.2
  • 51
    • 0031459806 scopus 로고    scopus 로고
    • Covalent attachment of 4-hydroxy-2-nonenal to erythrocyte proteins
    • Uchida, K., Hasui, Y., and Osawa, T. (1997) Covalent attachment of 4-hydroxy-2-nonenal to erythrocyte proteins. J. Biochem. 122, 1246-1251.
    • (1997) J. Biochem , vol.122 , pp. 1246-1251
    • Uchida, K.1    Hasui, Y.2    Osawa, T.3
  • 52
    • 57349185571 scopus 로고    scopus 로고
    • Carbonic anhydrase III and four-and-a-half LIM protein 1 are preferentially oxidized with muscle unloading
    • Chen, C. N., Ferrington, D. A., and Thompson, L. V. (2008) Carbonic anhydrase III and four-and-a-half LIM protein 1 are preferentially oxidized with muscle unloading. J. Appl. Physiol. 105, 1554-1561.
    • (2008) J. Appl. Physiol , vol.105 , pp. 1554-1561
    • Chen, C.N.1    Ferrington, D.A.2    Thompson, L.V.3
  • 53
    • 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., Pierce, W. M., Klein, J. B., Merchant, M., Markesbery, W. R., and Butterfield, D. A. (2006) 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 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    Pierce, W.M.5    Klein, J.B.6    Merchant, M.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 54
    • 38149060199 scopus 로고    scopus 로고
    • Rapid characterization of covalent modifications to rat brain mitochondrial proteins after ex vivo exposure to 4-hydroxy-2-nonenal by liquid chromatography-tandem mass spectrometry using data-dependent and neutral loss-driven MS3 acquisition
    • Stevens, S. M., Jr., Rauniyar, N., and Prokai, L. (2007) Rapid characterization of covalent modifications to rat brain mitochondrial proteins after ex vivo exposure to 4-hydroxy-2-nonenal by liquid chromatography-tandem mass spectrometry using data-dependent and neutral loss-driven MS3 acquisition. J. Mass Spectrom. 42, 1599-1605.
    • (2007) J. Mass Spectrom , vol.42 , pp. 1599-1605
    • Stevens Jr., S.M.1    Rauniyar, N.2    Prokai, L.3
  • 55
    • 0038820056 scopus 로고    scopus 로고
    • Oxidative post-translational modification of tryptophan residues in cardiac mitochondrial proteins
    • Taylor, S. W., Fahy, E., Murray, J., Capaldi, R. A., and Ghosh, S. S. (2003) Oxidative post-translational modification of tryptophan residues in cardiac mitochondrial proteins. J. Biol. Chem. 278, 19587-19590.
    • (2003) J. Biol. Chem , vol.278 , pp. 19587-19590
    • Taylor, S.W.1    Fahy, E.2    Murray, J.3    Capaldi, R.A.4    Ghosh, S.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.