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Volumn , Issue , 2010, Pages 173-197

Mass Spectrometric Strategies for Identification and Characterization of Carbonylated Peptides and Proteins

Author keywords

Advanced lipoxidation end products (ALEs); Carbonylated protein characterization in vitro section, conventional mass spectrometric approaches and peptide and protein detection; Carbonylation, irreversible, non enzymatic modification of proteins and change in activity or function; Mass spectrometric strategies, for identification and characterization of carbonylated peptides and proteins; Mass spectrometry strategies for protein oxidative modification identification; Method for immunoaffinity capture of DNPH derivatized HNE and MDA adducted tryptic peptides; Oxidative decomposition of polyunsaturated fatty acids (PUFAs) chain reactions leading to formation of RCS; Precursor ion scanning specific mass spectrometric detection methods, strategy in studying protein modifications; Protein carbonylation, by reactive carbonyl species (RCS) polyunsaturated fatty acid peroxidation; RCS characterization modified proteins in biological matrices

Indexed keywords


EID: 84886492809     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780813814438.ch11     Document Type: Chapter
Times cited : (3)

References (107)
  • 1
    • 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
    • Aldini G, Dalle-Donne I, Vistoli G, Maffei Facino R, 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 (7): 946-954.
    • (2005) J Mass Spectrom , vol.40 , Issue.7 , pp. 946-954
    • Aldini, G.1    Dalle-Donne, I.2    Vistoli, G.3    Maffei Facino, R.4    Carini, M.5
  • 2
    • 33750318889 scopus 로고    scopus 로고
    • Lipoxidation-derived reactive carbonyl species as potential drug targets in preventing protein carbonylation and related cellular dysfunction
    • Aldini G, Dalle-Donne I, Milzani A, Colombo R, Maffei Facino R, Carini M. 2006a. Lipoxidation-derived reactive carbonyl species as potential drug targets in preventing protein carbonylation and related cellular dysfunction. Chem Med Chem 1 (10): 1045-1058.
    • (2006) Chem Med Chem , vol.1 , Issue.10 , pp. 1045-1058
    • Aldini, G.1    Dalle-Donne, I.2    Milzani, A.3    Colombo, R.4    Maffei Facino, R.5    Carini, M.6
  • 3
    • 33749020292 scopus 로고    scopus 로고
    • Mass spectrometric characterization of covalent modification of human serum albumin by 4-hydroxy-trans-2-nonenal
    • Aldini G, Gamberoni L, Orioli M, Beretta G, Ragazzoni L, Maffei Facino R, Carini M. 2006b. Mass spectrometric characterization of covalent modification of human serum albumin by 4-hydroxy-trans-2-nonenal. J Mass Spectrom 41 (9): 1149-1161.
    • (2006) J Mass Spectrom , vol.41 , Issue.9 , pp. 1149-1161
    • Aldini, G.1    Gamberoni, L.2    Orioli, M.3    Beretta, G.4    Ragazzoni, L.5    Maffei Facino, R.6    Carini, M.7
  • 4
    • 35649008900 scopus 로고    scopus 로고
    • Intervention strategies to inhibit protein carbonylation by lipoxidation-derived reactive carbonyls
    • Aldini G, Dalle-Donne I, Maffei FR, Milzani Carini M. 2007a. Intervention strategies to inhibit protein carbonylation by lipoxidation-derived reactive carbonyls. Med Res Rev 27 (6): 817-868.
    • (2007) Med Res Rev , vol.27 , Issue.6 , pp. 817-868
    • Aldini, G.1    Dalle-Donne, I.2    Maffei, F.R.3    Milzani Carini, M.4
  • 5
    • 33947192876 scopus 로고    scopus 로고
    • Identification of actin as a 15-deoxy-Delta12,14-prostaglandin J2 target in neuroblastoma cells: mass spectrometric, computational, and functional approaches to investigate the effect on cytoskeletal derangement
    • Aldini G, Carini M, Vistoli G, Shibata T, Kusano Y, Gamberoni L, Dalle-Donne I, Milzani A, Uchida K. 2007b. Identification of actin as a 15-deoxy-Delta12,14-prostaglandin J2 target in neuroblastoma cells: mass spectrometric, computational, and functional approaches to investigate the effect on cytoskeletal derangement. Biochemistry 46 (10): 2707-2718.
    • (2007) Biochemistry , vol.46 , Issue.10 , pp. 2707-2718
    • Aldini, G.1    Carini, M.2    Vistoli, G.3    Shibata, T.4    Kusano, Y.5    Gamberoni, L.6    Dalle-Donne, I.7    Milzani, A.8    Uchida, K.9
  • 6
    • 33846806119 scopus 로고    scopus 로고
    • Alpha,beta-unsaturated aldehydes adducts to actin and albumin as potential biomarkers of carbonylation damage
    • Aldini G, Orioli M, Carini M. 2007c. Alpha,beta-unsaturated aldehydes adducts to actin and albumin as potential biomarkers of carbonylation damage. Redox Rep 12 (1): 20-25.
    • (2007) Redox Rep , vol.12 , Issue.1 , pp. 20-25
    • Aldini, G.1    Orioli, M.2    Carini, M.3
  • 7
    • 43149094897 scopus 로고    scopus 로고
    • Albumin is the main nucleophilic target of human plasma: a protective role against pro-atherogenic electrophilic reactive carbonyl species?
    • Aldini G, Vistoli G, Regazzoni L, Gamberoni L, Facino RM, Yamaguchi S, Uchida K, Carini M. 2008a. Albumin is the main nucleophilic target of human plasma: a protective role against pro-atherogenic electrophilic reactive carbonyl species? Chem Res Toxicol 21 (4): 824-835.
    • (2008) Chem Res Toxicol , 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
  • 8
    • 55249111076 scopus 로고    scopus 로고
    • A tandem MS precursor ion scan approach to identify variable covalent modification of albumin Cys34: a new tool for studying vascular carbonylation
    • Aldini G, Regazzoni L, Orioli M, Rimoldi I, Maffei Facino R, Carini M. 2008b. A tandem MS precursor ion scan approach to identify variable covalent modification of albumin Cys34: a new tool for studying vascular carbonylation. J Mass Spectrom 43 (11): 1470-1481.
    • (2008) J Mass Spectrom , vol.43 , Issue.11 , pp. 1470-1481
    • Aldini, G.1    Regazzoni, L.2    Orioli, M.3    Rimoldi, I.4    Maffei Facino, R.5    Carini, M.6
  • 9
    • 0842283942 scopus 로고    scopus 로고
    • Whole protein dissociation in a quadrupole ion trap: Identification of an a priori unknown modified protein
    • Amunugama R, Hogan JM, Newton KA, McLuckey SA. 2004. Whole protein dissociation in a quadrupole ion trap: Identification of an a priori unknown modified protein. Anal Chem 76 (3): 720-727.
    • (2004) Anal Chem , vol.76 , Issue.3 , pp. 720-727
    • Amunugama, R.1    Hogan, J.M.2    Newton, K.A.3    McLuckey, S.A.4
  • 12
    • 0030181297 scopus 로고    scopus 로고
    • Determination of the sites of 4-hydroxy-2-nonenal adduction to protein by electrospray tandem mass spectrometry
    • Bolgar MRS, Gaskell SJ. 1996. Determination of the sites of 4-hydroxy-2-nonenal adduction to protein by electrospray tandem mass spectrometry. Anal Chem 68 (14): 2325-2330.
    • (1996) Anal Chem , vol.68 , Issue.14 , pp. 2325-2330
    • Bolgar, M.R.S.1    Gaskell, S.J.2
  • 13
    • 14744304574 scopus 로고    scopus 로고
    • Proteomics by FTICR mass spectrometry: Top down and bottom up
    • Bogdanov B, Smith RD. 2005. Proteomics by FTICR mass spectrometry: Top down and bottom up. Mass Spectrom Rev 24 (2): 168-200.
    • (2005) Mass Spectrom Rev , vol.24 , Issue.2 , pp. 168-200
    • Bogdanov, B.1    Smith, R.D.2
  • 14
    • 25644451257 scopus 로고    scopus 로고
    • Modification of heat shock protein 90 by 4-hydroxynonenal in a rat model of chronic alcoholic liver disease
    • Carbone DL, Doorn JA, Kiebler Z, Ickes BR, Petersen DR. 2005a. Modification of heat shock protein 90 by 4-hydroxynonenal in a rat model of chronic alcoholic liver disease. J Pharmacol Exp Ther 315 (1): 8-15.
    • (2005) J Pharmacol Exp Ther , vol.315 , Issue.1 , pp. 8-15
    • Carbone, D.L.1    Doorn, J.A.2    Kiebler, Z.3    Ickes, B.R.4    Petersen, D.R.5
  • 15
    • 23844442198 scopus 로고    scopus 로고
    • Cysteine modification by lipid peroxidation products inhibits protein disulfide isomerase
    • Carbone DL, Doorn JA, Kiebler Z, Petersen DR. 2005b. Cysteine modification by lipid peroxidation products inhibits protein disulfide isomerase. Chem Res Toxicol 18 (8): 1324-1331.
    • (2005) Chem Res Toxicol , vol.18 , Issue.8 , pp. 1324-1331
    • Carbone, D.L.1    Doorn, J.A.2    Kiebler, Z.3    Petersen, D.R.4
  • 16
    • 3042596594 scopus 로고    scopus 로고
    • Mass spectrometry for detection of 4-hydroxy-trans -2-nonenal (HNE) adducts with peptides and proteins
    • Carini M, Aldini G, Maffei Facino R. 2004. Mass spectrometry for detection of 4-hydroxy-trans -2-nonenal (HNE) adducts with peptides and proteins. Mass Spectrom Rev 23 (4): 281-305.
    • (2004) Mass Spectrom Rev , vol.23 , Issue.4 , pp. 281-305
    • Carini, M.1    Aldini, G.2    Maffei Facino, R.3
  • 17
    • 33749003809 scopus 로고    scopus 로고
    • Sequestering agents of intermediate reactive aldehydes as inhibitors of advanced lipoxidation end-products (ALEs)
    • Dalle-Donne I, Scaloni A, Butterfield A. Eds. Hoboken: John Wiley and Sons Inc.
    • Carini M, Aldini G, Maffei Facino R. 2006. Sequestering agents of intermediate reactive aldehydes as inhibitors of advanced lipoxidation end-products (ALEs). In Redox Proteomics: from Protein Modifications to Cellular Dysfunction and Diseases, Dalle-Donne I, Scaloni A, Butterfield A. Eds. Hoboken: John Wiley and Sons Inc., pp. 887-929.
    • (2006) Redox Proteomics: from Protein Modifications to Cellular Dysfunction and Diseases , pp. 887-929
    • Carini, M.1    Aldini, G.2    Maffei Facino, R.3
  • 18
    • 33749457861 scopus 로고    scopus 로고
    • New role for an old probe: affinity labelling of oxylipid protein conjugates by N '-aminooxymethylcarbonylhydrazino D-biotin
    • Chavez J, Wu J, Han B, Chung WG, Maier CS. 2007. New role for an old probe: affinity labelling of oxylipid protein conjugates by N '-aminooxymethylcarbonylhydrazino D-biotin. Anal Chem 78 (19): 6847-6854.
    • (2007) Anal Chem , vol.78 , Issue.19 , pp. 6847-6854
    • Chavez, J.1    Wu, J.2    Han, B.3    Chung, W.G.4    Maier, C.S.5
  • 19
    • 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
    • Chung WG, Miranda CL, Maier CS. 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 (6): 1317-1324.
    • (2008) Electrophoresis , vol.29 , Issue.6 , pp. 1317-1324
    • Chung, W.G.1    Miranda, C.L.2    Maier, C.S.3
  • 24
    • 47249128563 scopus 로고    scopus 로고
    • Detection of catalase as a major protein target of the lipid peroxidation product 4-HNE and the lack of its genetic association as a risk factor in SLE
    • D'Souza A, Kurien BT, Rodgers R, Shenoi J, Kurono S, Matsumoto H, Hensley K, Nath SK, Scofield RH. 2008. Detection of catalase as a major protein target of the lipid peroxidation product 4-HNE and the lack of its genetic association as a risk factor in SLE. BMC Med Genet 9: 62.
    • (2008) BMC Med Genet , vol.9 , pp. 62
    • D'Souza, A.1    Kurien, B.T.2    Rodgers, R.3    Shenoi, J.4    Kurono, S.5    Matsumoto, H.6    Hensley, K.7    Nath, S.K.8    Scofield, R.H.9
  • 25
    • 35148864125 scopus 로고    scopus 로고
    • Active site modifications of the brain isoform of creatine kinase by 4-hydroxy-2-nonenal correlate with reduced enzyme activity: mapping of modified sites by Fourier transform-ion cyclotron resonance mass spectrometry
    • Eliuk SM, Renfrow MB, Shonsey EM, Barnes S, Kim H. 2007. Active site modifications of the brain isoform of creatine kinase by 4-hydroxy-2-nonenal correlate with reduced enzyme activity: mapping of modified sites by Fourier transform-ion cyclotron resonance mass spectrometry. Chem Res Toxicol 20 (9): 1260-1268.
    • (2007) Chem Res Toxicol , vol.20 , Issue.9 , pp. 1260-1268
    • Eliuk, S.M.1    Renfrow, M.B.2    Shonsey, E.M.3    Barnes, S.4    Kim, H.5
  • 26
    • 34648843445 scopus 로고    scopus 로고
    • Age-related macular degeneration and retinal protein modification by 4-hydroxy-2-nonenal
    • Ethen CM, Reilly C, Feng X, Olsen TW, Ferrington DA. 2007. Age-related macular degeneration and retinal protein modification by 4-hydroxy-2-nonenal. Invest Ophthalmol Vis Sci. 48 (8): 3469-3479.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , Issue.8 , pp. 3469-3479
    • Ethen, C.M.1    Reilly, C.2    Feng, X.3    Olsen, T.W.4    Ferrington, D.A.5
  • 27
    • 33244472848 scopus 로고    scopus 로고
    • Inhibition of thioredoxin and thioredoxin reductase by 4-hydroxy-2-nonenal in vitro and in vivo
    • Fang J, Holmgren A. 2006. Inhibition of thioredoxin and thioredoxin reductase by 4-hydroxy-2-nonenal in vitro and in vivo. J Am Chem Soc 128 (6): 1879-1885.
    • (2006) J Am Chem Soc , vol.128 , Issue.6 , pp. 1879-1885
    • Fang, J.1    Holmgren, A.2
  • 28
    • 33747770049 scopus 로고    scopus 로고
    • Inactivation of the proteasome by 4-hydroxy-2-nonenal is site specific and dependent on 20S proteasome subtypes
    • Farout L, Mary J, Vinh J, Szweda LI, Friguet B. 2006. Inactivation of the proteasome by 4-hydroxy-2-nonenal is site specific and dependent on 20S proteasome subtypes. Arch Biochem Biophys 453 (1): 135-142.
    • (2006) Arch Biochem Biophys , vol.453 , Issue.1 , pp. 135-142
    • Farout, L.1    Mary, J.2    Vinh, J.3    Szweda, L.I.4    Friguet, B.5
  • 29
    • 0346634902 scopus 로고    scopus 로고
    • Immunoaffinity purification and characterization of 4-hydroxy-2-nonenal-and malondialdehyde-modified peptides by electrospray ionization tandem mass spectrometry
    • Fenaille F, Tabet JC, Guy PA. 2002. Immunoaffinity purification and characterization of 4-hydroxy-2-nonenal-and malondialdehyde-modified peptides by electrospray ionization tandem mass spectrometry. Anal Chem 74 (24): 6298-6304.
    • (2002) Anal Chem , vol.74 , Issue.24 , pp. 6298-6304
    • Fenaille, F.1    Tabet, J.C.2    Guy, P.A.3
  • 30
    • 1242338830 scopus 로고    scopus 로고
    • Identification of 4-hydroxy-2-nonenal-modified peptides within unfractionated digests using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Fenaille F, Tabet JC, Guy PA. 2004a. Identification of 4-hydroxy-2-nonenal-modified peptides within unfractionated digests using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal Chem 76 (4): 867-873.
    • (2004) Anal Chem , vol.76 , Issue.4 , pp. 867-873
    • Fenaille, F.1    Tabet, J.C.2    Guy, P.A.3
  • 31
    • 0347419105 scopus 로고    scopus 로고
    • Study of peptides containing modified lysine residues by tandem mass spectrometry: precursor ion scanning of hexanal-modified peptides
    • Fenaille F, Tabet JC, Guy PA. 2004b. Study of peptides containing modified lysine residues by tandem mass spectrometry: precursor ion scanning of hexanal-modified peptides. Rapid Commun Mass Spectrom 18 (1): 67-76.
    • (2004) Rapid Commun Mass Spectrom , vol.18 , Issue.1 , pp. 67-76
    • Fenaille, F.1    Tabet, J.C.2    Guy, P.A.3
  • 32
    • 23844498767 scopus 로고    scopus 로고
    • Carbonylation of milk powder proteins as a consequence of processing conditions
    • Fenaille F, Parisod V, Tabet JC, Guy PA. 2005. Carbonylation of milk powder proteins as a consequence of processing conditions. Proteomics 5 (12): 3097-3104.
    • (2005) Proteomics , vol.5 , Issue.12 , pp. 3097-3104
    • Fenaille, F.1    Parisod, V.2    Tabet, J.C.3    Guy, P.A.4
  • 33
    • 10044294918 scopus 로고    scopus 로고
    • Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal
    • Ferrington DA, Kapphahn RJ. 2004. Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal. FEBS Lett 578 (3): 217-223.
    • (2004) FEBS Lett , vol.578 , Issue.3 , pp. 217-223
    • Ferrington, D.A.1    Kapphahn, R.J.2
  • 34
    • 33947396353 scopus 로고    scopus 로고
    • Standardized peptidome profiling of human urine by magnetic bead separation and matrix -assisted laser desorption/ionization time-of-flight mass spectrometry
    • Fiedler GM, Baumann S, Leichtle A, Oltmann A, Kase J, Thiery J, Ceglarek U. 2007. Standardized peptidome profiling of human urine by magnetic bead separation and matrix -assisted laser desorption/ionization time-of-flight mass spectrometry. Clin Chem 53 (3): 421-428.
    • (2007) Clin Chem , vol.53 , Issue.3 , pp. 421-428
    • Fiedler, G.M.1    Baumann, S.2    Leichtle, A.3    Oltmann, A.4    Kase, J.5    Thiery, J.6    Ceglarek, U.7
  • 35
    • 84934439766 scopus 로고    scopus 로고
    • Surface-enhanced laser desorption/ionization mass spectrometry for protein and Peptide profiling of body fluids
    • Gagnon A, Shi Q, Ye B. 2008. Surface-enhanced laser desorption/ionization mass spectrometry for protein and Peptide profiling of body fluids. Methods Mol Biol 441: 41-56.
    • (2008) Methods Mol Biol , vol.441 , pp. 41-56
    • Gagnon, A.1    Shi, Q.2    Ye, B.3
  • 36
    • 36348954964 scopus 로고    scopus 로고
    • Reactive aldehyde modification of thioredoxin-1 activates early steps of inflammation and cell adhesion
    • Go YM, Halvey PJ, Hansen JM, Reed M, Pohl J, Jones DP. 2007. Reactive aldehyde modification of thioredoxin-1 activates early steps of inflammation and cell adhesion. Am J Pathol 171 (5): 1670-1681.
    • (2007) Am J Pathol , vol.171 , Issue.5 , pp. 1670-1681
    • Go, Y.M.1    Halvey, P.J.2    Hansen, J.M.3    Reed, M.4    Pohl, J.5    Jones, D.P.6
  • 37
    • 34247361278 scopus 로고    scopus 로고
    • Carbonylation of adipose proteins in obesity and insulin resistance: identification of adipocyte fatty acid-binding protein as a cellular target of 4-hydroxynonenal
    • Grimsrud PA, Picklo MJ Sr, Griffin TJ, Bernlohr DA. 2007. Carbonylation of adipose proteins in obesity and insulin resistance: identification of adipocyte fatty acid-binding protein as a cellular target of 4-hydroxynonenal. Mol Cell Proteomics 6 (4): 624-637.
    • (2007) Mol Cell Proteomics , vol.6 , Issue.4 , pp. 624-637
    • Grimsrud, P.A.1    Picklo Sr, M.J.2    Griffin, T.J.3    Bernlohr, D.A.4
  • 38
    • 0034662907 scopus 로고    scopus 로고
    • Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology
    • Gygi SP, Corthals GL, Zhang Y, Rochon Y, Aebersold R. 2000. Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology. Proc Natl Acad Sci USA 97 (17): 9390-9395.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.17 , pp. 9390-9395
    • Gygi, S.P.1    Corthals, G.L.2    Zhang, Y.3    Rochon, Y.4    Aebersold, R.5
  • 39
    • 0037398266 scopus 로고    scopus 로고
    • Interfacing the orbitrap mass analyzer to an electrospray ion source
    • Hardman M, Makarov AA. 2003. Interfacing the orbitrap mass analyzer to an electrospray ion source. Anal Chem 75 (7): 1699-1705.
    • (2003) Anal Chem , vol.75 , Issue.7 , pp. 1699-1705
    • Hardman, M.1    Makarov, A.A.2
  • 44
    • 3242768438 scopus 로고    scopus 로고
    • Modification of Cytochrome c by 4-hydroxy-2-nonenal: evidence for histidine, lysine, and arginine-aldehyde adducts
    • Isom AL, Barnes S, Wilson L, Kirk M, Coward L, Darley-Usmar V. 2004. Modification of Cytochrome c by 4-hydroxy-2-nonenal: evidence for histidine, lysine, and arginine-aldehyde adducts. J Am Soc Mass Spectrom 15 (8): 1136-1147.
    • (2004) J Am Soc Mass Spectrom , vol.15 , Issue.8 , pp. 1136-1147
    • Isom, A.L.1    Barnes, S.2    Wilson, L.3    Kirk, M.4    Coward, L.5    Darley-Usmar, V.6
  • 45
    • 0035947678 scopus 로고    scopus 로고
    • IkappaB kinase, a molecular target for inhibition by 4-hydroxy-2-nonenal
    • Ji C, Kozak KR, Marnett LJ. 2001. IkappaB kinase, a molecular target for inhibition by 4-hydroxy-2-nonenal. J Biol Chem 276 (21): 18223-18228.
    • (2001) J Biol Chem , vol.276 , Issue.21 , pp. 18223-18228
    • Ji, C.1    Kozak, K.R.2    Marnett, L.J.3
  • 46
    • 43049093757 scopus 로고    scopus 로고
    • Aberrant molecular properties shared by familial Parkinson ' s disease-associated mutant UCH-L1 and carbonyl-modified UCH-L1
    • Kabuta T, Setsuie R, Mitsui T, Kinugawa A, Sakurai M, Aoki S, Uchida K, Wada K. 2008. Aberrant molecular properties shared by familial Parkinson ' s disease-associated mutant UCH-L1 and carbonyl-modified UCH-L1. Hum Mol Genet 17 (10): 1482-1496.
    • (2008) Hum Mol Genet , vol.17 , Issue.10 , pp. 1482-1496
    • Kabuta, T.1    Setsuie, R.2    Mitsui, T.3    Kinugawa, A.4    Sakurai, M.5    Aoki, S.6    Uchida, K.7    Wada, K.8
  • 47
    • 33947715680 scopus 로고    scopus 로고
    • Michael addition of acrolein to lysinyl and N-terminal residues of a model peptide: targets for cytoprotective hydrazino drugs
    • Kaminskas LM, Pyke SM, Burcham PC. 2007. Michael addition of acrolein to lysinyl and N-terminal residues of a model peptide: targets for cytoprotective hydrazino drugs. Rapid Commun Mass Spectrom. 21 (7): 1155-1164.
    • (2007) Rapid Commun Mass Spectrom. , vol.21 , Issue.7 , pp. 1155-1164
    • Kaminskas, L.M.1    Pyke, S.M.2    Burcham, P.C.3
  • 49
    • 2642520417 scopus 로고    scopus 로고
    • Top-down proteomics
    • Kelleher NL. 2004. Top-down proteomics. Anal Chem 76 (11): 197A -203A.
    • (2004) Anal Chem , vol.76 , Issue.11
    • Kelleher, N.L.1
  • 50
    • 35648936560 scopus 로고    scopus 로고
    • Use of SELDI-TOF mass spectrometry for identification of new biomarkers: potential and limitations
    • Kiehntopf M, Siegmund R, Deufel T. 2007. Use of SELDI-TOF mass spectrometry for identification of new biomarkers: potential and limitations. Clin Chem Lab Med 45 (11): 1435-1449.
    • (2007) Clin Chem Lab Med , vol.45 , Issue.11 , pp. 1435-1449
    • Kiehntopf, M.1    Siegmund, R.2    Deufel, T.3
  • 51
    • 33645958553 scopus 로고    scopus 로고
    • Proteomic analysis of nitrated and 4-hydroxy-2-nonenal-modified serum proteins during aging
    • Kim CH, Zou Y, Kim DH, Kim ND, Yu BP, Chung HY. 2006. Proteomic analysis of nitrated and 4-hydroxy-2-nonenal-modified serum proteins during aging. J Gerontol A Biol Sci Med Sci 61 (4): 332-338.
    • (2006) J Gerontol A Biol Sci Med Sci , vol.61 , Issue.4 , pp. 332-338
    • Kim, C.H.1    Zou, Y.2    Kim, D.H.3    Kim, N.D.4    Yu, B.P.5    Chung, H.Y.6
  • 52
    • 34547103281 scopus 로고    scopus 로고
    • Acrolein inhibits cytokine gene expression by alkylating cysteine and arginine residues in the NF-kappaB1 DNA binding domain
    • Lambert C, Li J, Jonscher K, Yang TC, Reigan P, Quintana M, Harvey J, Freed BM. 2007. Acrolein inhibits cytokine gene expression by alkylating cysteine and arginine residues in the NF-kappaB1 DNA binding domain. J Biol Chem 282 (27): 19666-75.
    • (2007) J Biol Chem , vol.282 , Issue.27 , pp. 19666-75
    • Lambert, C.1    Li, J.2    Jonscher, K.3    Yang, T.C.4    Reigan, P.5    Quintana, M.6    Harvey, J.7    Freed, B.M.8
  • 53
    • 58149090525 scopus 로고    scopus 로고
    • A novel 4-oxo-2(E)-nonenal-derived modification to angiotensin II: oxidative decarboxylation of N-terminal aspartic acid
    • Lee SH, Goto T, Oe T. 2008. A novel 4-oxo-2(E)-nonenal-derived modification to angiotensin II: oxidative decarboxylation of N-terminal aspartic acid. Chem Res Toxicol 21 (12): 2237-2244.
    • (2008) Chem Res Toxicol , vol.21 , Issue.12 , pp. 2237-2244
    • Lee, S.H.1    Goto, T.2    Oe, T.3
  • 54
    • 1642282736 scopus 로고    scopus 로고
    • Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products
    • Levonen AL, Landar A, Ramachandran A, Ceaser EK, Dickinson DA, Zanoni G, Morrow JD, Darley-Usmar VM. 2004. Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products. Biochem J 378 (Pt 2): 373-382.
    • (2004) Biochem J , vol.378 , Issue.2 PART , pp. 373-382
    • Levonen, A.L.1    Landar, A.2    Ramachandran, A.3    Ceaser, E.K.4    Dickinson, D.A.5    Zanoni, G.6    Morrow, J.D.7    Darley-Usmar, V.M.8
  • 55
    • 0041527152 scopus 로고    scopus 로고
    • Intact protein analysis by matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry
    • Lin M, Campbell JM, Mueller DR, Wirth U. 2003. Intact protein analysis by matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry. Rapid Commun Mass Spectrom 17 (16): 1809-1814.
    • (2003) Rapid Commun Mass Spectrom , vol.17 , Issue.16 , pp. 1809-1814
    • Lin, M.1    Campbell, J.M.2    Mueller, D.R.3    Wirth, U.4
  • 56
    • 0041408938 scopus 로고    scopus 로고
    • Electrostatic axially harmonic orbital trapping: A high-performance technique of mass analysis
    • Makarov A. 2000. Electrostatic axially harmonic orbital trapping: A high-performance technique of mass analysis. Anal Chem 72 (6): 1156-1162.
    • (2000) Anal Chem , vol.72 , Issue.6 , pp. 1156-1162
    • Makarov, A.1
  • 58
    • 14344257790 scopus 로고    scopus 로고
    • Detection and localization of protein modifications by high resolution tandem mass spectrometry
    • Meng F, Forbes AJ, Miller LM, Kelleher NL. 2005. Detection and localization of protein modifications by high resolution tandem mass spectrometry. Mass Spectrom Rev 24 (2): 126-134.
    • (2005) Mass Spectrom Rev , vol.24 , Issue.2 , pp. 126-134
    • Meng, F.1    Forbes, A.J.2    Miller, L.M.3    Kelleher, N.L.4
  • 59
    • 17644362744 scopus 로고    scopus 로고
    • Affinity chromatographyc selection of carbonylated proteins followed by identification of oxidation sites using tandem mass spectrometry
    • Mirzaei H, Regnier F. 2005. Affinity chromatographyc selection of carbonylated proteins followed by identification of oxidation sites using tandem mass spectrometry. Anal Chem 77 (8): 2386-2392.
    • (2005) Anal Chem , vol.77 , Issue.8 , pp. 2386-2392
    • Mirzaei, H.1    Regnier, F.2
  • 60
    • 32444449409 scopus 로고    scopus 로고
    • Enrichment of carbonylated peptides using Girard P Reagent and strong cation exchange chromatography
    • Mirzaei H, Regnier F. 2006a. Enrichment of carbonylated peptides using Girard P Reagent and strong cation exchange chromatography. Anal Chem 78 (3): 770-778.
    • (2006) Anal Chem , vol.78 , Issue.3 , pp. 770-778
    • Mirzaei, H.1    Regnier, F.2
  • 61
    • 33750350410 scopus 로고    scopus 로고
    • Identification and quantification of protein carbonylation using light and heavy isotope labeled Girard ' s P reagent
    • Mirzaei H, Regnier F. 2006b. Identification and quantification of protein carbonylation using light and heavy isotope labeled Girard ' s P reagent. J Chromatogr A 1134 (1-2): 122-133.
    • (2006) J Chromatogr A , vol.1134 , Issue.1-2 , pp. 122-133
    • Mirzaei, H.1    Regnier, F.2
  • 62
    • 33846025822 scopus 로고    scopus 로고
    • Identification of yeast oxidized proteins: Chromatographic top-down approach for identification of carbonylated, fragmented and cross-linked proteins in yeast
    • Mirzaei H, Regnier F. 2007. Identification of yeast oxidized proteins: Chromatographic top-down approach for identification of carbonylated, fragmented and cross-linked proteins in yeast. J Chromatogr A 1141 (1): 22-31.
    • (2007) J Chromatogr A , vol.1141 , Issue.1 , pp. 22-31
    • Mirzaei, H.1    Regnier, F.2
  • 63
    • 0033006380 scopus 로고    scopus 로고
    • The lipid peroxidation product 4-hydroxynonenal inhibits neurite outgrowth, disrupts neuronal microtubules, and modifies cellular tubulin
    • Neely MD, Sidell KR, Graham DG, Montine TJ. 1999. The lipid peroxidation product 4-hydroxynonenal inhibits neurite outgrowth, disrupts neuronal microtubules, and modifies cellular tubulin. J Neurochem 72 (6): 2323-2333.
    • (1999) J Neurochem , vol.72 , Issue.6 , pp. 2323-2333
    • Neely, M.D.1    Sidell, K.R.2    Graham, D.G.3    Montine, T.J.4
  • 64
    • 0036130033 scopus 로고    scopus 로고
    • Identification and sequencing analysis of intact proteins via collision-induced dissociation and quadrupole time-of-flight mass spectrometry
    • Nemeth-Cawley JF, Rouse JC. 2002. Identification and sequencing analysis of intact proteins via collision-induced dissociation and quadrupole time-of-flight mass spectrometry. J Mass Spectrom. 37 (3): 270-282.
    • (2002) J Mass Spectrom. , vol.37 , Issue.3 , pp. 270-282
    • Nemeth-Cawley, J.F.1    Rouse, J.C.2
  • 65
    • 34447575657 scopus 로고    scopus 로고
    • Analysis of modified apolipoprotein B-100 structures formed in oxidized low-density lipoprotein using LC-MS/MS
    • Obama T, Kato R, Masuda Y, Takahashi K, Aiuchi T, Itabe H. 2007. Analysis of modified apolipoprotein B-100 structures formed in oxidized low-density lipoprotein using LC-MS/MS. Proteomics 7 (13): 2132-2141.
    • (2007) Proteomics , vol.7 , Issue.13 , pp. 2132-2141
    • Obama, T.1    Kato, R.2    Masuda, Y.3    Takahashi, K.4    Aiuchi, T.5    Itabe, H.6
  • 66
    • 27644525132 scopus 로고    scopus 로고
    • LC-ESI-MS/MS determination of 4-hydroxy-trans-2-nonenal Michael adducts with cysteine and histidine-containing peptides as early markers of oxidative stress in excitable tissues
    • Orioli M, Aldini G, Beretta G, Maffei Facino R, Carini M. 2005. LC-ESI-MS/MS determination of 4-hydroxy-trans-2-nonenal Michael adducts with cysteine and histidine-containing peptides as early markers of oxidative stress in excitable tissues. J Chromatogr B Analyt Technol Biomed Life Sci 827 (1): 109-118.
    • (2005) J Chromatogr B Analyt Technol Biomed Life Sci , vol.827 , Issue.1 , pp. 109-118
    • Orioli, M.1    Aldini, G.2    Beretta, G.3    Maffei Facino, R.4    Carini, M.5
  • 67
    • 36849089644 scopus 로고    scopus 로고
    • HNE Michael adducts to histidine and histidine-containing peptides as biomarkers of lipid-derived carbonyl stress in urines: LC-MS/MS profiling in Zucker obese rats
    • Orioli M, Aldini G, Benfatto MC, Facino RM, Carini M. 2007. HNE Michael adducts to histidine and histidine-containing peptides as biomarkers of lipid-derived carbonyl stress in urines: LC-MS/MS profiling in Zucker obese rats. Anal Chem 79 (23): 9174-9184.
    • (2007) Anal Chem , vol.79 , Issue.23 , pp. 9174-9184
    • Orioli, M.1    Aldini, G.2    Benfatto, M.C.3    Facino, R.M.4    Carini, M.5
  • 68
    • 26944438195 scopus 로고    scopus 로고
    • Recent developments in the ion/ion chemistry of high-mass multiply-charged ions
    • Pitteri SJ, McLuckey SA. 2005. Recent developments in the ion/ion chemistry of high-mass multiply-charged ions. Mass Spectrom Rev 24 (6): 931-958.
    • (2005) Mass Spectrom Rev , vol.24 , Issue.6 , pp. 931-958
    • Pitteri, S.J.1    McLuckey, S.A.2
  • 69
    • 45249124663 scopus 로고    scopus 로고
    • 4-Hydroxynonenal: a membrane lipid oxidation product of medicinal interest
    • Poli G, Schaur RJ, Siems WG, Leonarduzzi G. 2008. 4-Hydroxynonenal: a membrane lipid oxidation product of medicinal interest. Med Res Rev 28 (4): 569-631.
    • (2008) Med Res Rev , vol.28 , Issue.4 , pp. 569-631
    • Poli, G.1    Schaur, R.J.2    Siems, W.G.3    Leonarduzzi, G.4
  • 70
    • 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
    • Rauniyar N, Stevens SM Jr, 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 (5): 1421-1428.
    • (2007) Anal Bioanal Chem , vol.389 , Issue.5 , pp. 1421-1428
    • Rauniyar, N.1    Stevens Jr., S.M.2    Prokai, L.3
  • 71
    • 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 MS(3) versus Neutral Loss-Driven Electron Capture Dissociation
    • Rauniyar N, Stevens SM, Prokai-Tatrai K, Prokai L. 2009. Characterization of 4-Hydroxy-2 -nonenal-modified Peptides by Liquid Chromatography-Tandem Mass Spectrometry using data-dependent acquisition: Neutral Loss-driven MS(3) versus Neutral Loss-Driven Electron Capture Dissociation. Anal Chem 81 (2): 782-789.
    • (2009) Anal Chem , vol.81 , Issue.2 , pp. 782-789
    • Rauniyar, N.1    Stevens, S.M.2    Prokai-Tatrai, K.3    Prokai, L.4
  • 72
    • 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 WM, Klein JB, Turner DM, Coccia R, Markesbery WR, Butterfield DA. 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 (1): 107-120.
    • (2008) Neurobiol Dis , vol.30 , Issue.1 , 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
  • 73
    • 0036315870 scopus 로고    scopus 로고
    • ' Top down' protein characterization via tandem mass spectrometry
    • Reid GE, McLuckey SA. 2002. ' Top down' protein characterization via tandem mass spectrometry. J Mass Spectrom 37 (7): 663-675.
    • (2002) J Mass Spectrom , vol.37 , Issue.7 , pp. 663-675
    • Reid, G.E.1    McLuckey, S.A.2
  • 74
    • 34249043563 scopus 로고    scopus 로고
    • Proteomic mapping of 4-hydroxynonenal protein modification sites by Solid-Phase Hydrazide chemistry and mass spectrometry
    • Roe MR, Xie H, Bandhakavi S, Griffin TJ. 2007 Proteomic mapping of 4-hydroxynonenal protein modification sites by Solid-Phase Hydrazide chemistry and mass spectrometry. Anal Chem 79 (10): 3747-3756.
    • (2007) Anal Chem , vol.79 , Issue.10 , pp. 3747-3756
    • Roe, M.R.1    Xie, H.2    Bandhakavi, S.3    Griffin, T.J.4
  • 75
    • 33847091274 scopus 로고    scopus 로고
    • 4-Hydroxy-2-nonenal adduction of extracellular signal-regulated kinase (Erk) and the inhibition of hepatocyte Erk -Est -Like Protein-1-Activating Protein-1 signal transduction
    • Sampey BP, Carbone DL, Doorn JA, Drechsel DA, Petersen DR. 2007. 4-Hydroxy-2-nonenal adduction of extracellular signal-regulated kinase (Erk) and the inhibition of hepatocyte Erk -Est -Like Protein-1-Activating Protein-1 signal transduction. Mol Pharmacol 71 (3): 871-883.
    • (2007) Mol Pharmacol , vol.71 , Issue.3 , pp. 871-883
    • Sampey, B.P.1    Carbone, D.L.2    Doorn, J.A.3    Drechsel, D.A.4    Petersen, D.R.5
  • 76
    • 0037427492 scopus 로고    scopus 로고
    • The effect of high -density lipoproteins on the formation of lipid/protein conjugates during in vitro oxidation of low-density lipoprotein
    • Sangvanich P, Mackness B, Gaskell SJ, Durrington P, Mackness M. 2003. The effect of high -density lipoproteins on the formation of lipid/protein conjugates during in vitro oxidation of low-density lipoprotein. Biochem Biophys Res Commun 300 (2): 501-506.
    • (2003) Biochem Biophys Res Commun , vol.300 , Issue.2 , pp. 501-506
    • Sangvanich, P.1    Mackness, B.2    Gaskell, S.J.3    Durrington, P.4    Mackness, M.5
  • 77
    • 33845390864 scopus 로고    scopus 로고
    • Protein adducts generated from products of lipid oxidation: focus on HNE and ONE
    • Sayre LM, Lin D, Yuan Q, Zhu X, Tang X. 2006. Protein adducts generated from products of lipid oxidation: focus on HNE and ONE. Drug Metab Rev 38 (4): 651-675.
    • (2006) Drug Metab Rev , vol.38 , Issue.4 , pp. 651-675
    • Sayre, L.M.1    Lin, D.2    Yuan, Q.3    Zhu, X.4    Tang, X.5
  • 78
    • 27744572151 scopus 로고    scopus 로고
    • Acrolein impairs ATP binding cassette transporter A1-dependent cholesterol export from cells through site-specific modification of apolipoprotein A-I
    • Shao B, Fu X, McDonald TO, Green PS, Uchida K, O'Brien KD, Oram JF, Heinecke JW. 2005a. Acrolein impairs ATP binding cassette transporter A1-dependent cholesterol export from cells through site-specific modification of apolipoprotein A-I. J Biol Chem 280 (43): 36386-96.
    • (2005) J Biol Chem , vol.280 , Issue.43 , pp. 36386-96
    • Shao, B.1    Fu, X.2    McDonald, T.O.3    Green, P.S.4    Uchida, K.5    O'Brien, K.D.6    Oram, J.F.7    Heinecke, J.W.8
  • 80
    • 33846949357 scopus 로고    scopus 로고
    • The oxidative stress metabolite 4-hydroxynonenal promotes Alzheimer protofibril formation
    • Siegel SJ, Bieschke J, Powers ET, Kelly JW. 2007. The oxidative stress metabolite 4-hydroxynonenal promotes Alzheimer protofibril formation. Biochemistry 46 (6): 1503-1510.
    • (2007) Biochemistry , vol.46 , Issue.6 , pp. 1503-1510
    • Siegel, S.J.1    Bieschke, J.2    Powers, E.T.3    Kelly, J.W.4
  • 81
    • 0042170296 scopus 로고    scopus 로고
    • Intracellular metabolism of 4-Hydroxynonenal
    • Siems W, Grune T. 2003. Intracellular metabolism of 4-Hydroxynonenal. Mol Aspects Med 24 (4-5): 167-175.
    • (2003) Mol Aspects Med , vol.24 , Issue.4-5 , pp. 167-175
    • Siems, W.1    Grune, T.2
  • 82
    • 0344084088 scopus 로고    scopus 로고
    • High-throughput proteomic-based identification of oxidatively induced protein carbonylation in mouse brain
    • Soreghan BA, Yang F, Thomas SN, Hsu J, Yang AJ. 2003. High-throughput proteomic-based identification of oxidatively induced protein carbonylation in mouse brain. Pharmac Res 20 (11): 1713-1720.
    • (2003) Pharmac Res , 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
  • 83
    • 34248545257 scopus 로고    scopus 로고
    • Applications of mass spectrometry for the structural characterization of recombinant protein pharmaceuticals
    • Srebalus Barnes CA, Lim A. 2007. Applications of mass spectrometry for the structural characterization of recombinant protein pharmaceuticals. Mass Spectrom Rev 26 (3): 370-388.
    • (2007) Mass Spectrom Rev , vol.26 , Issue.3 , pp. 370-388
    • Srebalus Barnes, C.A.1    Lim, A.2
  • 84
    • 84889453656 scopus 로고    scopus 로고
    • Chemical modification of proteins by reactive oxygen species
    • Dalle -Donne I, Scaloni A, Butterfield A, eds. Hoboken: John Wiley and Sons Inc.
    • Stadtman ER, Levine RL. 2006. Chemical modification of proteins by reactive oxygen species. In Redox Proteomics: from Protein Modifications to Cellular Dysfunction and Diseases, Dalle -Donne I, Scaloni A, Butterfield A, eds. Hoboken: John Wiley and Sons Inc., pp. 3-23.
    • (2006) Redox Proteomics: from Protein Modifications to Cellular Dysfunction and Diseases , pp. 3-23
    • Stadtman, E.R.1    Levine, R.L.2
  • 85
    • 0032161546 scopus 로고    scopus 로고
    • Simplification of product ion spectra derived from multiply charged parent ions via ion/ion chemistry
    • Stephenson JL Jr, McLuckey SA. 1998. Simplification of product ion spectra derived from multiply charged parent ions via ion/ion chemistry. Anal Chem 70 (17): 3533-3544.
    • (1998) Anal Chem , vol.70 , Issue.17 , pp. 3533-3544
    • Stephenson Jr., J.L.1    McLuckey, S.A.2
  • 86
    • 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 MS 3 acquisition
    • Stevens SM Jr, Rauniyar N, 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 MS 3 acquisition. J Mass Spectrom 42 (12): 1599-1605.
    • (2007) J Mass Spectrom , vol.42 , Issue.12 , pp. 1599-1605
    • Stevens Jr., S.M.1    Rauniyar, N.2    Prokai, L.3
  • 87
    • 38949113159 scopus 로고    scopus 로고
    • Acrolein: sources, metabolism, and biomolecular interactions relevant to human health and disease
    • Stevens JF, Maier CS. 2008. Acrolein: sources, metabolism, and biomolecular interactions relevant to human health and disease. Mol Nutr Food Res 52 (1): 7-25.
    • (2008) Mol Nutr Food Res , vol.52 , Issue.1 , pp. 7-25
    • Stevens, J.F.1    Maier, C.S.2
  • 88
    • 33748256154 scopus 로고    scopus 로고
    • Covalent adduction of human serum albumin by 4-hydroxy-2-nonenal: kinetic analysis of competing alkylation reactions
    • Szapacs ME, Riggins JN, Zimmerman LJ, Liebler DC. 2006. Covalent adduction of human serum albumin by 4-hydroxy-2-nonenal: kinetic analysis of competing alkylation reactions. Biochemistry 45 (35): 10521-10528.
    • (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
  • 89
    • 25644444455 scopus 로고    scopus 로고
    • A strategy for distinguishing modified peptides based on post -digestion 18 O labeling and mass spectrometry
    • Sun G, Anderson VE. 2005. A strategy for distinguishing modified peptides based on post -digestion 18 O labeling and mass spectrometry. Rapid Commun Mass Spectrom 19 (19): 2849-2856.
    • (2005) Rapid Commun Mass Spectrom , vol.19 , Issue.19 , pp. 2849-2856
    • Sun, G.1    Anderson, V.E.2
  • 91
    • 34447542267 scopus 로고    scopus 로고
    • Modification by acrolein, a component of tobacco smoke and age-related oxidative stress, mediates functional impairment of human apolipoprotein E
    • Tamamizu-Kato S, Wong JY, Jairam V, Uchida K, Raussens V, Kato H, Ruysschaert JM, Narayanaswami V. 2007. Modification by acrolein, a component of tobacco smoke and age-related oxidative stress, mediates functional impairment of human apolipoprotein E. Biochemistry 46 (28): 8392-8400.
    • (2007) Biochemistry , vol.46 , Issue.28 , pp. 8392-8400
    • Tamamizu-Kato, S.1    Wong, J.Y.2    Jairam, V.3    Uchida, K.4    Raussens, V.5    Kato, H.6    Ruysschaert, J.M.7    Narayanaswami, V.8
  • 92
    • 33751516438 scopus 로고    scopus 로고
    • Identification of 4-hydroxynonenal-modified retinal proteins induced by photooxidative stress prior to retinal degeneration
    • Tanito M, Haniu H, Elliott MH, Singh AK, Matsumoto H, Anderson RE. 2006. Identification of 4-hydroxynonenal-modified retinal proteins induced by photooxidative stress prior to retinal degeneration. Free Radic Biol Med 41 (12): 1847-1859.
    • (2006) Free Radic Biol Med , vol.41 , Issue.12 , pp. 1847-1859
    • Tanito, M.1    Haniu, H.2    Elliott, M.H.3    Singh, A.K.4    Matsumoto, H.5    Anderson, R.E.6
  • 95
    • 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 KA, Jacobs AT, Liebler DC, Porter NA, Marnett LJ. 2008. Identification of protein targets of 4-hydroxynonenal using click chemistry for ex vivo biotinylation of azido and alkynyl derivatives. Chem Res Toxicol 21 (2): 432-44.
    • (2008) Chem Res Toxicol , vol.21 , Issue.2 , 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
  • 96
    • 34250725999 scopus 로고    scopus 로고
    • Covalent adducts arising from the decomposition products of lipid hydroperoxides in the presence of cytochrome c
    • Williams MV, Wishnok JS, Tannenbaum SR. 2007. Covalent adducts arising from the decomposition products of lipid hydroperoxides in the presence of cytochrome c. Chem Res Toxicol 20 (5): 767-75.
    • (2007) Chem Res Toxicol , vol.20 , Issue.5 , pp. 767-775
    • Williams, M.V.1    Wishnok, J.S.2    Tannenbaum, S.R.3
  • 97
    • 0032190196 scopus 로고    scopus 로고
    • Identification of oxidized proteins based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, immunochemical detection, isoelectric focusing, and microsequencing
    • Yan LJ, Orr WC, Sohal RS. 1998. Identification of oxidized proteins based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, immunochemical detection, isoelectric focusing, and microsequencing. Anal Biochem 263 (1): 67-71.
    • (1998) Anal Biochem , vol.263 , Issue.1 , pp. 67-71
    • Yan, L.J.1    Orr, W.C.2    Sohal, R.S.3
  • 99
    • 0030950291 scopus 로고    scopus 로고
    • Oxidative modifications of apoB-100 by exposure of low density lipoproteins to HOCL in vitro
    • Yang CY, Gu ZW, Yang HX, Yang M, Gotto AM Jr, Smith CV. 1997b. Oxidative modifications of apoB-100 by exposure of low density lipoproteins to HOCL in vitro. Free Radic Biol Med 23 (1): 82-89.
    • (1997) Free Radic Biol Med , vol.23 , Issue.1 , pp. 82-89
    • Yang, C.Y.1    Gu, Z.W.2    Yang, H.X.3    Yang, M.4    Gotto Jr., A.M.5    Smith, C.V.6
  • 100
    • 0345148809 scopus 로고    scopus 로고
    • Selective modification of apoB-100 in the oxidation of low density lipoproteins by myeloperoxidase in vitro
    • Yang CY, Gu ZW, Yang M, Lin SN, Garcia-Prats AJ, Rogers LK, Welty SE, Smith CV. 1999a Selective modification of apoB-100 in the oxidation of low density lipoproteins by myeloperoxidase in vitro. J Lipid Res 40 (4): 686-698.
    • (1999) J Lipid Res , vol.40 , Issue.4 , pp. 686-698
    • Yang, C.Y.1    Gu, Z.W.2    Yang, M.3    Lin, S.N.4    Garcia-Prats, A.J.5    Rogers, L.K.6    Welty, S.E.7    Smith, C.V.8
  • 101
    • 0033619720 scopus 로고    scopus 로고
    • Identification of modified tryptophan residues in apolipoprotein B-100 derived from copper ion-oxidized low-density lipoprotein
    • Yang C, Gu ZW, Yang M, Lin SN, Siuzdak G, Smith CV. 1999b Identification of modified tryptophan residues in apolipoprotein B-100 derived from copper ion-oxidized low-density lipoprotein. Biochemistry 38 (48): 15903-15908.
    • (1999) Biochemistry , vol.38 , Issue.48 , pp. 15903-15908
    • Yang, C.1    Gu, Z.W.2    Yang, M.3    Lin, S.N.4    Siuzdak, G.5    Smith, C.V.6
  • 102
    • 0035199853 scopus 로고    scopus 로고
    • Selective oxidation in vitro by myeloperoxidase of the N-terminal amine in apolipoprotein B-100
    • Yang C, Wang J, Krutchinsky AN, Chait BT, Morrisett JD, Smith CV. 2001. Selective oxidation in vitro by myeloperoxidase of the N-terminal amine in apolipoprotein B-100. J Lipid Res 42 (11): 1891-1896.
    • (2001) J Lipid Res , vol.42 , Issue.11 , pp. 1891-1896
    • Yang, C.1    Wang, J.2    Krutchinsky, A.N.3    Chait, B.T.4    Morrisett, J.D.5    Smith, C.V.6
  • 103
    • 30744476222 scopus 로고    scopus 로고
    • Performance of a linear ion trap-orbitrap hybrid for peptide analysis
    • Yates JR, Cociorva D, Liao L, Zabrouskov V. 2006. Performance of a linear ion trap-orbitrap hybrid for peptide analysis. Anal Chem 78 (2): 493-500.
    • (2006) Anal Chem , vol.78 , Issue.2 , pp. 493-500
    • Yates, J.R.1    Cociorva, D.2    Liao, L.3    Zabrouskov, V.4
  • 104
    • 21344463592 scopus 로고    scopus 로고
    • Novel lipid hydroperoxide-derived hemoglobin histidine adducts as biomarkers of oxidative stress
    • Yocum AK, Oe T, Yergey AL, Blair IA. 2005. Novel lipid hydroperoxide-derived hemoglobin histidine adducts as biomarkers of oxidative stress. J Mass Spectrom 40 (6): 754-764.
    • (2005) J Mass Spectrom , vol.40 , Issue.6 , pp. 754-764
    • Yocum, A.K.1    Oe, T.2    Yergey, A.L.3    Blair, I.A.4
  • 105
    • 3042523891 scopus 로고    scopus 로고
    • Proteomic analysis of carbonylated proteins in two-dimensional gel electrophoresis using avidin-fluorescein affinity staining
    • Yoo BS, Regnier FE. 2004. Proteomic analysis of carbonylated proteins in two-dimensional gel electrophoresis using avidin-fluorescein affinity staining. Electrophoresis 25 (9): 1334-1341.
    • (2004) Electrophoresis , vol.25 , Issue.9 , pp. 1334-1341
    • Yoo, B.S.1    Regnier, F.E.2
  • 106
    • 33846853515 scopus 로고    scopus 로고
    • Chemical nature of stochastic generation of protein-based carbonyls: metal-catalyzed oxidation versus modification by products of lipid oxidation
    • Yuan Q, Zhu X, Sayre LM. 2007. Chemical nature of stochastic generation of protein-based carbonyls: metal-catalyzed oxidation versus modification by products of lipid oxidation. Chem Res Toxicol 20 (1): 129-139.
    • (2007) Chem Res Toxicol , vol.20 , Issue.1 , pp. 129-139
    • Yuan, Q.1    Zhu, X.2    Sayre, L.M.3
  • 107
    • 24944510341 scopus 로고    scopus 로고
    • Consecutive ion activation for top down mass spectrometry: Improved protein sequencing by nozzle-skimmer dissociation
    • Zhai H, Xuemei H, Breuker K, McLafferty FW. 2005. Consecutive ion activation for top down mass spectrometry: Improved protein sequencing by nozzle-skimmer dissociation. Anal Chem 77 (18): 5777-5784.
    • (2005) Anal Chem , vol.77 , Issue.18 , pp. 5777-5784
    • Zhai, H.1    Xuemei, H.2    Breuker, K.3    McLafferty, F.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.