Exploring the Biology of Lipid Peroxidation-Derived Protein Carbonylation
Open accessAbstract
The sustained overproduction of reactive oxygen and nitrogen species results in an imbalance of cellular prooxidant-antioxidant systems and is implicated in numerous disease states, including alcoholic liver disease, cancer, neurological disorders, inflammation, and cardiovascular disease. The accumulation of reactive aldehydes resulting from sustained oxidative stress and lipid peroxidation is an underlying factor in the development of these pathologies. Determining the biochemical factors that elicit cellular responses resulting from protein carbonylation remains a key element to developing therapeutic approaches and ameliorating disease pathologies. This review details our current understanding of the generation of reactive aldehydes via lipid peroxidation resulting in protein carbonylation, focusing on pathophysiologic factors associated with 4-hydroxynonenal-protein modification. Additionally, an overview of in vitro and in vivo model systems used to study the physiologic impact of protein carbonylation is presented. Finally, an update of the methods commonly used in characterizing protein modification by reactive aldehydes provides an overview of isolation techniques, mass spectrometry, and computational biology. It is apparent that research in this area employing state-of-the-art proteomics, mass spectrometry, and computational biology is rapidly evolving, yielding foundational knowledge concerning the molecular mechanisms of protein carbonylation and its relation to a spectrum of diseases associated with oxidative stress.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
After ethanol intake, AA, MDA, and 4-HNE adducts are produced rapidly in the hepatic centrilobular zone, sinusoids, and HSCs as well as on the hepatocyte surface; their amounts are markedly elevated in the early phase of ALD, suggesting a role in initial development and progression of ALD.
“After ethanol intake, AA, MDA, and 4-HNE adducts are produced rapidly in the hepatic centrilobular zone (zone III), sinusoids, and HSCs as well as on the hepatocyte surface in the liver.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [218]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Free radicals and antioxidants in normal physiological functions and human disease
Valko, M., Leibfritz, D., Moncol, J., Cronin, M. T. D., Mazur, M., & Telser, J. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.07.001 · Cited by 14,269 · see citing works
Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
Esterbauer, H., Schaur, R. J., & Zollner, H. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90192-6 · Cited by 6,672 · see citing works
The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide
Pryor, W. A., & Squadrito, G. L. (1995) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1995.268.5.l699 · Cited by 1,511 · see citing works
Radical-free biology of oxidative stress
Jones, D. P. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00283.2008 · Cited by 1,213 · see citing works
Lipid hydroperoxide generation, turnover, and effector action in biological systems
Girotti, A. W. (1998) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)32182-9 · Cited by 1,204 · see citing works
Butterfield, D. A., & Lauderback, C. M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00794-3 · Cited by 999 · see citing works
The oxidant stress hypothesis in Parkinson's disease: Evidence supporting it
Fahn, S., & Cohen, G. (1992) · Annals of Neurology · doi:10.1002/ana.410320616 · Cited by 927 · see citing works
Protein carbonylation, cellular dysfunction, and disease progression
Dalle‐Donne, I., Aldini, G., Carini, M., Colombo, R., Rossi, R., & Milzani, A. (2006) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2006.tb00407.x · Cited by 836 · see citing works
Profiling Enzyme Activities In Vivo Using Click Chemistry Methods
Speers, A. E., & Cravatt, B. F. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.03.012 · Cited by 774 · see citing works
Castegna, A., Aksenov, M., Aksenova, M., Thongboonkerd, V., Klein, J. B., Pierce, W. M., Booze, R., Markesbery, W. R., & Butterfield, D. A. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00914-0 · Cited by 581 · see citing works
Oxidative Stress and Covalent Modification of Protein with Bioactive Aldehydes
Grimsrud, P. A., Xie, H., Griffin, T. J., & Bernlohr, D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r700019200 · Cited by 570 · see citing works
The utility of ETD mass spectrometry in proteomic analysis
Mikesh, L. M., Ueberheide, B. M., Chi, A., Coon, J. J., Syka, J. E. P., Shabanowitz, J., & Hunt, D. F. (2006) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2006.10.003 · Cited by 535 · see citing works
Uchida, K., & Stadtman, E. R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53264-6 · Cited by 513 · see citing works
Protein oxidation in the brain in Alzheimer's disease
Aksenov, M. Y., Aksenova, M. V., Butterfield, D. A., Geddes, J. W., & Markesbery, W. R. (2001) · Neuroscience · doi:10.1016/s0306-4522(00)00580-7 · Cited by 503 · see citing works
4‐Hydroxynonenal: A membrane lipid oxidation product of medicinal interest
Poli, G., Schaur, R. J., Siems, W. G., & Leonarduzzi, G. (2007) · Medicinal Research Reviews · doi:10.1002/med.20117 · Cited by 434 · see citing works
Role of Nrf2 in the Regulation of CD36 and Stress Protein Expression in Murine Macrophages
Ishii, T., Itoh, K., Ruiz, E., Leake, D. S., Unoki‐Kubota, H., Yamamoto, M. P., & Mann, G. E. (2004) · Circulation Research · doi:10.1161/01.res.0000119171.44657.45 · Cited by 400 · see citing works
Reactions of 4-hydroxynonenal with proteins and cellular targets
Petersen, D. R., & Doorn, J. A. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.06.012 · Cited by 393 · see citing works
Self-citationOxidation of LDL by Myeloperoxidase and Reactive Nitrogen Species
Carr, A. C., McCall, M. R., & Frei, B. B. (2000) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.20.7.1716 · Cited by 392 · see citing works
Protein Adducts Generated from Products of Lipid Oxidation: Focus on HNE and ONE
Sayre, L. M., Lin, D., Yuan, Q., Zhu, X., & Tang, X. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600959508 · Cited by 364 · see citing works
Basic aspects of the biochemical reactivity of 4-hydroxynonenal
Schaur, R. J. (2003) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(03)00009-8 · Cited by 341 · see citing works
4-Hydroxynonenal and neurodegenerative diseases
Žarković, K. (2003) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(03)00024-4 · Cited by 315 · see citing works
Doorn, J. A., & Petersen, D. R. (2002) · Chemical Research in Toxicology · doi:10.1021/tx025590o · Cited by 297 · see citing works
Self-citationProteomic Identification of Carbonylated Proteins and Their Oxidation Sites
Madian, A. G., & Regnier, F. E. (2010) · Journal of Proteome Research · doi:10.1021/pr1002609 · Cited by 271 · see citing works
The Haber-Weiss cycle—70 years later: an alternative view
Liochev, S. I., & Fridovich, I. (2002) · Redox Report · doi:10.1179/135100002125000190 · Cited by 270 · see citing works
LoPachin, R. M., Gavin, T., Petersen, D. R., & Barber, D. S. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900147g · Cited by 263 · see citing works
Self-citationRukhsana Sultana, A., Marzia Perluigi, A., & Butterfield, D. A. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.2021 · Cited by 259 · see citing works
Protein Damage by Reactive Electrophiles: Targets and Consequences
Liebler, D. C. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700235t · Cited by 235 · see citing works
Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective
Møller, I. M., Rogowska-Wrzesińska, A., & Rao, R. S. P. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.05.004 · Cited by 233 · see citing works
Systems Analysis of Protein Modification and Cellular Responses Induced by Electrophile Stress
Jacobs, A. T., & Marnett, L. J. (2010) · Accounts of Chemical Research · doi:10.1021/ar900286y · Cited by 233 · see citing works
Vila, A., Tallman, K. A., Jacobs, A. T., Liebler, D. C., Porter, N. A., & Marnett, L. J. (2008) · Chemical Research in Toxicology · doi:10.1021/tx700347w · Cited by 192 · see citing works
Reed, T. T., Pierce, W. M., Markesbery, W. R., & Butterfield, D. A. (2009) · Brain Research · doi:10.1016/j.brainres.2009.04.009 · Cited by 190 · see citing works
The Oxidative Stress Metabolite 4-Hydroxynonenal Promotes Alzheimer Protofibril Formation
Siegel, S. J., Bieschke, J., Powers, E. T., & Kelly, J. W. (2007) · Biochemistry · doi:10.1021/bi061853s · Cited by 186 · see citing works
Protein Modification by Acrolein: Formation and Stability of Cysteine Adducts
Cai, J., Bhatnagar, A., & Pierce, W. M. J. (2009) · Chemical Research in Toxicology · doi:10.1021/tx800465m · Cited by 183 · see citing works
Tanito, M., Agbaga, M., & Anderson, R. E. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.018 · Cited by 174 · see citing works
Cysteine Modification by Lipid Peroxidation Products Inhibits Protein Disulfide Isomerase
Carbone, D. L., Doorn, J. A., Kiebler, Z., & Petersen, D. R. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050078z · Cited by 148 · see citing works
Self-citationGlobal Analysis of Protein Damage by the Lipid Electrophile 4-Hydroxy-2-nonenal
Codreanu, S. G., Zhang, B., Sobecki, S. M., Billheimer, D. D., & Liebler, D. C. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800070-mcp200 · Cited by 146 · see citing works
Rules Governing Selective Protein Carbonylation
Maisonneuve, E., Ducret, A., Khoueiry, P., Lignon, S., Longhi, S., Talla, E., & Dukan, S. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007269 · Cited by 145 · see citing works
Decreased complex II respiration and HNE-modified SDH subunit in diabetic heart
Lashin, O., Szweda, P. A., Szweda, L. I., & Romani, A. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.10.040 · Cited by 138 · see citing works
4-hydroxynonenal inhibits SIRT3 via thiol-specific modification
Fritz, K. S., Galligan, J. J., Smathers, R. L., Roede, J. R., Shearn, C. T., Reigan, P., & Petersen, D. R. (2011) · Chemical Research in Toxicology · doi:10.1021/tx100355a · Cited by 127 · see citing works
Self-citationButterfield, D. A., Reed, T. T., & Rukhsana Sultana, A. (2010) · Free Radical Research · doi:10.3109/10715762.2010.520014 · Cited by 123 · see citing works
Ishii, T., Tatsuda, E., Kumazawa, S., Nakayama, T., & Uchida, K. (2003) · Biochemistry · doi:10.1021/bi027172o · Cited by 118 · see citing works
Inhibition of Hsp72-Mediated Protein Refolding by 4-Hydroxy-2-nonenal
Carbone, D. L., Doorn, J. A., Kiebler, Z., Sampey, B. P., & Petersen, D. R. (2004) · Chemical Research in Toxicology · doi:10.1021/tx049838g · Cited by 116 · see citing works
Self-citationAldini, G., Gamberoni, L., Orioli, M., Beretta, G., Regazzoni, L., Facino, R. M., & Carini, M. (2006) · Journal of Mass Spectrometry · doi:10.1002/jms.1067 · Cited by 115 · see citing works
Aldini, G., Vistoli, G., Regazzoni, L., Gamberoni, L., Facino, R. M., Yamaguchi, S., Uchida, K., & Carini, M. (2008) · Chemical Research in Toxicology · doi:10.1021/tx700349r · Cited by 113 · see citing works
Soreghan, B. A., Yang, F. F., Thomas, S. N., Hsu, J. L., & Yang, A. J. (2003) · Pharmaceutical Research · doi:10.1023/b:pham.0000003366.25263.78 · Cited by 112 · see citing works
Comprehensive Comparison of Collision Induced Dissociation and Electron Transfer Dissociation
Molina, H., Matthiesen, R., Kandasamy, K., & Pandey, A. (2008) · Analytical Chemistry · doi:10.1021/ac8007785 · Cited by 106 · see citing works
Protein Carbonyl Formation in the Diaphragm
Barreiro, E., Gea, J., Falco, M. D., Kriazhev, L., James, S., & Hussain, S. N. A. (2004) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2004-0021oc · Cited by 105 · see citing works
Luo, J., Hill, B. G., Gu, Y., Cai, J., Srivastava, S., Bhatnagar, A., & Prabhu, S. D. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00284.2007 · Cited by 104 · see citing works
HNE increases HO-1 through activation of the ERK pathway in pulmonary epithelial cells
Iles, K. E., Dickinson, D. A., Wigley, A. F., Welty, N. E., Blank, V., & Forman, H. J. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.03.026 · Cited by 103 · see citing works
Kim, H., Tallman, K. A., Liebler, D. C., et al. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900121-mcp200 · Cited by 98 · see citing works
Roe, M. R., Xie, H., Bandhakavi, S., & Griffin, T. J. (2007) · Analytical Chemistry · doi:10.1021/ac0617971 · Cited by 93 · see citing works
Aldini, G., Dalle‐Donne, I., Vistoli, G., Facino, R. M., & Carini, M. (2005) · Journal of Mass Spectrometry · doi:10.1002/jms.872 · Cited by 83 · see citing works
Szapacs, M. E., Riggins, J. N., Zimmerman, L. J., et al. (2006) · Biochemistry · doi:10.1021/bi060535q · Cited by 83 · see citing works
Dalle‐Donne, I., Carini, M., Orioli, M., Vistoli, G., Regazzoni, L., Colombo, G., Rossi, R., Milzani, A., & Aldini, G. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.02.024 · Cited by 82 · see citing works
Structure-Toxicity Analysis of Type-2 Alkenes: In Vitro Neurotoxicity
LoPachin, R. M., Barber, D. S., Geohagen, B. C., Gavin, T., He, D., & Das, S. (2006) · Toxicological Sciences · doi:10.1093/toxsci/kfl127 · Cited by 81 · see citing works
Chavez, J. D., Wu, J., Han, B., Chung, W., & Maier, C. S. (2006) · Analytical Chemistry · doi:10.1021/ac0607257 · Cited by 80 · see citing works
Enrichment of Carbonylated Peptides Using Girard P Reagent and Strong Cation Exchange Chromatography
Mirzaei, H., & Regnier, F. E. (2005) · Analytical Chemistry · doi:10.1021/ac0514220 · Cited by 79 · see citing works
Liebler, D. C. (2002) · Environmental Health Perspectives · doi:10.1289/ehp.02110s113 · Cited by 77 · see citing works
Modification of Akt2 by 4-Hydroxynonenal Inhibits Insulin-Dependent Akt Signaling in HepG2 Cells
Shearn, C. T., Fritz, K. S., Reigan, P., & Petersen, D. R. (2011) · Biochemistry · doi:10.1021/bi200029w · Cited by 73 · see citing works
Self-citationDebra Boyd-kimball, A., Rukhsana Sultana, A., Abdul, H. M., & Butterfield, D. A. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20394 · Cited by 66 · see citing works
Sampey, B. P., Stewart, B. J., & Petersen, D. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610602200 · Cited by 64 · see citing works
Self-citationHan, B., Stevens, J. F., & Maier, C. S. (2007) · Analytical Chemistry · doi:10.1021/ac062262a · Cited by 63 · see citing works
Mirzaei, H., & Regnier, F. E. (2006) · Journal of Chromatography A · doi:10.1016/j.chroma.2006.08.096 · Cited by 56 · see citing works
Rauniyar, N., Stevens, S. M., Prókai-Tátrai, K., et al. (2008) · Analytical Chemistry · doi:10.1021/ac802015m · Cited by 56 · see citing works
Inverse correlation of protein oxidation and proteasome activity in liver and lung
Breusing, N., Arndt, J., Voß, P., Bresgen, N., Wiswedel, I., Gardemann, A., Siems, W., & Grune, T. (2009) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.09.004 · Cited by 52 · see citing works
Wakita, C., Maeshima, T., Yamazaki, A., Shibata, T., Ito, S., Akagawa, M., Ojika, M., Yodoi, J., & Uchida, K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.019927 · Cited by 50 · see citing works
Fenaille, F., Tabet, J., & Guy, P. A. (2002) · Analytical Chemistry · doi:10.1021/ac020443g · Cited by 50 · see citing works
Roede, J. R., Carbone, D. L., Doorn, J. A., Kirichenko, O. V., Reigan, P., & Petersen, D. R. (2008) · Chemical Research in Toxicology · doi:10.1021/tx800244u · Cited by 50 · see citing works
Self-citationOsna, N. A., White, R. L., Todero, S. L., et al. (2006) · Hepatology · doi:10.1002/hep.21442 · Cited by 48 · see citing works
Mirzaei, H., Baena, B., Barbas, C., & Regnier, F. E. (2008) · PROTEOMICS · doi:10.1002/pmic.200700363 · Cited by 47 · see citing works
Chung, W., Miranda, C. L., & Maier, C. S. (2008) · Electrophoresis · doi:10.1002/elps.200700606 · Cited by 41 · see citing works
Johnson, D. W. (2007) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.3175 · Cited by 40 · see citing works
Fleuranceau-Morel, P., Barrier, L., Fauconneau, B., Piriou, A., & Huguet, F. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00652-7 · Cited by 37 · see citing works
No effect of cigarette smoking dose on oxidized plasma proteins
Yeh, C., Barr, R. G., Powell, C. A., et al. (2007) · Environmental Research · doi:10.1016/j.envres.2007.09.008 · Cited by 36 · see citing works
Induction of COX-2 by acrolein in rat lung epithelial cells
Sarkar, P., & Hayes, B. E. (2007) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-007-9411-z · Cited by 33 · see citing works
Burcham, P. C., Raso, A., & Thompson, C. A. (2009) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2009.12.006 · Cited by 32 · see citing works
Gallagher, E. P., Huisden, C. M., & Gardner, J. L. (2007) · Toxicology in Vitro · doi:10.1016/j.tiv.2007.04.004 · Cited by 25 · see citing works
Lipid aldehyde-mediated cross-linking of apolipoprotein B-100 inhibits secretion from HepG2 cells
Stewart, B. J. R., Roede, J. R., Doorn, J. A., & Petersen, D. R. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.04.004 · Cited by 23 · see citing works
Self-citationWang, Q., Zhao, X., He, S., Liu, Y., An, M., & Ji, J. (2009) · Neurochemical Research · doi:10.1007/s11064-009-0023-8 · Cited by 22 · see citing works
A mass spectrometric analysis of 4‐hydroxy‐2‐(E)‐nonenal modificationof cytochrome c
Tang, X., Sayre, L. M., & Tochtrop, G. P. (2011) · Journal of Mass Spectrometry · doi:10.1002/jms.1890 · Cited by 22 · see citing works
Khan, R. N., Matharoo‐Ball, B., & Shaw, R. W. (2009) · Reproductive Sciences · doi:10.1177/1933719109348027 · Cited by 20 · see citing works
Proteomic profiling of rat lung epithelial cells induced by acrolein
Sarkar, P., & Hayes, B. E. (2009) · Life Sciences · doi:10.1016/j.lfs.2009.05.012 · Cited by 17 · see citing works
Rauniyar, N., Stevens, S. M., & Prókai, L. (2007) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-007-1534-2 · Cited by 16 · see citing works
Lin, C.-C., Su, T., & Wang, T. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900008h · Cited by 11 · see citing works
Pournamdari, M., Saadi, A., Ellis, E., Andrew, R., Walker, B. R., & Watson, D. G. (2008) · Analytica Chimica Acta · doi:10.1016/j.aca.2008.11.070 · Cited by 9 · see citing works
Identification and Characterization of Oxylipid‐Protein and Peptide Conjugates by Mass Spectrometry
Chung, W., & Maier, C. S. (2008) · Current Protocols in Toxicology · doi:10.1002/0471140856.tx1709s35 · Cited by 2 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- [1]Sies H Oxidative Stress II. Oxidants and Antioxidants 1991 London Academic Press
Cited by
Sorted by citations
Rungratanawanich, W., Qu, Y., Wang, X., Essa, M. M., & Song, B.-J. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00561-7 · Cited by 411 · see citing works
An overview of the chemistry and biology of reactive aldehydes
Fritz, K. S., & Petersen, D. R. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.06.025 · Cited by 237 · see citing works
Self-citationProtein Carbonylation in a Murine Model for Early Alcoholic Liver Disease
Galligan, J. J., Smathers, R. L., Fritz, K. S., Epperson, L. E., Hunter, L. E., & Petersen, D. R. (2012) · Chemical Research in Toxicology · doi:10.1021/tx300002q · Cited by 74 · see citing works
Self-citationRonis, M. J. J., Mercer, K. E., Gannon, B., Engi, B., Zimniak, P., Shearn, C. T., Orlicky, D. J., Albano, E., Badger, T. M., & Petersen, D. R. (2015) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00154.2014 · Cited by 27 · see citing works
Self-citation
- Authors
- Fritz, K. S., & Petersen, D. R.
- Affiliations
- University of Colorado Anschutz (US)
- Corresponding author
- Petersen, Dennis R.
- ORCID
- Fritz, Kristofer S.
- Venue
- Chemical Research in Toxicology
- Publisher
- American Chemical Society (ACS)
- Published
- 2011-08-18
- Volume
- 24
- Issue
- 9
- Pages
- 1411-1419
- ISSN
- 0893-228X (ISSN-L)
- 1520-5010
- PMC
- PMC3178011
- OpenAlex
- W2080280910
- Cited by
- 129
- References
- 86
- Citations by year
- 2026: 6 · 2025: 7 · 2024: 6 · 2023: 8 · 2022: 10 · 2021: 7 · 2020: 3 · 2019: 7 · 2018: 4 · 2017: 7 · 2016: 13 · 2015: 16 · 2014: 12 · 2013: 11 · 2012: 11
- FWCI
- 1.02
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Chemical Research in Toxicology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Alcohol Abuse and Alcoholism (R37AA009300)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK074487)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- lipid peroxidation, protein carbonylation, 4-hydroxynonenal, reactive aldehydes, oxidative stress, reactive oxygen species, protein modification, oxidative stress biomarkers, computational biology, pathogenesis
- MeSH terms
- Aldehydes, Animals, Humans, Proteins, Mass Spectrometry, Lipid Peroxidation, Computational Biology, Protein Carbonylation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
