Cited by 294Antioxidant Activity and Oxidative StressRedox biology and oxidative stressParaoxonase enzyme and polymorphisms

The DOI matches its Crossref record; 33 of the 35 references it cites were found in a registry or an index.

Quantification of malondialdehyde and 4-hydroxynonenal adducts to lysine residues in native and oxidized human low-density lipoprotein

Open access

REQUENA, Jesús R., FU, Min Xin, AHMED, Mahtab U., JENKINS, Alicia J., LYONS, Timothy J., BAYNES, John W., THORPE, Suzanne R.·1997·Biochemical Journal

DOI 10.1042/bj3220317PMC PMC1218194

Open this paper in CoChat — free account Open PDF

Abstract

Malondialdehyde (MDA) and 4-hydroxynonenal (HNE) are major end-products of oxidation of polyunsaturated fatty acids, and are frequently measured as indicators of lipid peroxidation and oxidative stress in vivo. MDA forms Schiff-base adducts with lysine residues and cross-links proteins in vitro; HNE also reacts with lysines, primarily via a Michael addition reaction. We have developed methods using NaBH4 reduction to stabilize these adducts to conditions used for acid hydrolysis of protein, and have prepared reduced forms of lysine-MDA [3-(Nε-lysino)propan-1-ol (LM)], the lysine-MDA-lysine iminopropene cross-link [1,3-di(Nε-lysino)propane (LML)] and lysine-HNE [3-(Nε-lysino)-4-hydroxynonan-1-ol (LHNE)]. Gas chromatography/MS assays have been developed for quantification of the reduced compounds in protein. RNase incubated with MDA or HNE was used as a model for quantification of the adducts by gas chromatography/MS. There was excellent agreement between measurement of MDA bound to RNase as LM and LML, and as thiobarbituric acid-MDA adducts measured by HPLC; these adducts accounted for 70Ő80% of total lysine loss during the reaction with MDA. LM and LML (0.002Ő0.12mmol/mol of lysine) were also found in freshly isolated low-density lipoprotein (LDL) from healthy subjects. LHNE was measured in RNase treated with HNE, but was not detectable in native LDL. LM, LML and LHNE increased in concert with the formation of conjugated dienes during the copper-catalysed oxidation of LDL, but accounted for modification of < 1% of lysine residues in oxidized LDL. These results are the first report of direct chemical measurement of MDA and HNE adducts to lysine residues in LDL. LM, LML and LHNE should be useful as biomarkers of lipid peroxidative modification of protein and of oxidative stress in vitro and in vivo.

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

Crossref · 10.1042/bj3220317

Cites

33 of 33 references verified0 citation errors · 0 not checkable

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 316,394
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
Malondialdehyde and thiobarbituric acid-reactivity as diagnostic indices of lipid peroxidation and peroxidative tissue injury
Janero, D. R. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90131-2 · Cited by 2,735
Role of oxidized low density lipoprotein in atherogenesis.
Witztum, J. L., & Steinberg, D. H. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115499 · Cited by 2,675
The role of lipid peroxidation and antioxidants in oxidative modification of LDL
Esterbauer, H., Gebicki, J. M., Puhl, H., & Jürgens, G. (1992) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(92)90181-f · Cited by 2,307
Evidence for the presence of oxidatively modified low density lipoprotein in atherosclerotic lesions of rabbit and man.
Ylä‐Herttuala, S., Palinski, W., Rosenfeld, M. E., Parthasarathy, S., Carew, T. E., Butler, S. S., Witztum, J. L., & Steinberg, D. H. (1989) · Journal of Clinical Investigation · doi:10.1172/jci114271 · Cited by 1,877
Autoantibody against oxidised LDL and progression of carotid atherosclerosis
Salonen, J. T., Korpela, H., Salonen, R., Nyyssönen, K., Ylä‐Herttuala, S., Yamamoto, R., Butler, S., Palinski, W., & Witztum, J. L. (1992) · The Lancet · doi:10.1016/0140-6736(92)90926-t · Cited by 1,311
The Advanced Glycation End Product, N∊-(Carboxymethyl)lysine, Is a Product of both Lipid Peroxidation and Glycoxidation Reactions
Fu, M.-X., Requena, J. R., Jenkins, A. J., Lyons, T. J., Baynes, J. W., & Thorpe, S. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.17.9982 · Cited by 822
Self-citation
Oxidation of human low density lipoprotein results in derivatization of lysine residues of apolipoprotein B by lipid peroxide decomposition products.
Steinbrecher, U. P. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61395-x · Cited by 618
Antisera and monoclonal antibodies specific for epitopes generated during oxidative modification of low density lipoprotein.
Palinski, W., Ylä‐Herttuala, S., Rosenfeld, M. E., Butler, S. W., Socher, S. S., Parthasarathy, S., Curtiss, L. K., & Witztum, J. L. (1990) · Arteriosclerosis An Official Journal of the American Heart Association Inc · doi:10.1161/01.atv.10.3.325 · Cited by 616

Flagged first, then by citations

Show all 35 references

2 of the 35 references couldn’t be matched to a known paper.

Research works printed but not linked: 2

Fruebis, J., Parthasarathy, S. and Steinberg, D. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 10588-10592
Sell, D. R. and Monnier, V. M. (1989) in Physiology of Aging (Masero, E. J., ed.), pp. 235-305, Oxford University Press, New York

Sorted by citations

Items 101–200 of 294

A Clinical Trial about a Food Supplement Containing α-Lipoic Acid on Oxidative Stress Markers in Type 2 Diabetic Patients
Derosa, G., D’Angelo, A., Romano, D., & Maffioli, P. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17111802 · Cited by 72
Lipid peroxidation and decomposition — Conflicting roles in plaque vulnerability and stability
Parthasarathy, S., Litvinov, D. Y., Selvarajan, K., & Garelnabi, M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2008.03.002 · Cited by 71
Aldose Reductase Protects Against Early Atherosclerotic Lesion Formation in Apolipoprotein E-Null Mice
Srivastava, S., Vladykovskaya, E. N., Barski, O. A., Spite, M. R., Kaiserová, K., Petrash, J. M., Chung, S. S. M., Hunt, G., Dawn, B., & Bhatnagar, A. (2009) · Circulation Research · doi:10.1161/circresaha.109.200568 · Cited by 71
Detoxification of cytotoxic α,β‐unsaturated aldehydes by carnosine: characterization of conjugated adducts by electrospray ionization tandem mass spectrometry and detection by liquid chromatography/mass spectrometry in rat skeletal muscle
Aldini, G., Granata, P., & Carini, M. (2002) · Journal of Mass Spectrometry · doi:10.1002/jms.381 · Cited by 71
Oxidized LDLs as Signaling Molecules
Zingg, J.-M., Vlad, A., & Ricciarelli, R. (2021) · Antioxidants · doi:10.3390/antiox10081184 · Cited by 80
The role of immune and inflammatory processes in the development of macrovascular disease in diabetes
Lopes-Virella, M. F. (2003) · Frontiers in bioscience · doi:10.2741/1141 · Cited by 71
Protein and lipid oxidative damage and complex I content are lower in the brain of budgerigar and canaries than in mice. Relation to aging rate
Pamplona, R., Portero‐Otín, M., Sanz, A., Ayala, V., Vasileva, E., & Barja, G. (2005) · AGE · doi:10.1007/s11357-005-4562-x · Cited by 70
Effect of ageing and caloric restriction on specific markers of protein oxidative damage and membrane peroxidizability in rat liver mitochondria
Lambert, A. J., Portero‐Otín, M., Pamplona, R., & Merry, B. J. (2004) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2004.06.002 · Cited by 69
Modification of Casein by the Lipid Oxidation Product Malondialdehyde
Adams, A., KIMPE, N. D., & van Boekel, M. A. J. S. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf072385b · Cited by 69
Comparison of taurine, GABA, Glu, and Asp as scavengers of malondialdehyde in vitro and in vivo
Deng, Y., Wang, W., Yu, P., Xi, Z., Xu, L., Li, X., & He, N. (2013) · Nanoscale Research Letters · doi:10.1186/1556-276x-8-190 · Cited by 71
Modification of the longevity-related degree of fatty acid unsaturation modulates oxidative damage to proteins and mitochondrial DNA in liver and brain
Pamplona, R., Portero‐Otín, M., Sanz, A., Requena, J. R., & Barja, G. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.01.006 · Cited by 69
Self-citation
Identification of biochemical pathways for the metabolism of oxidized low-density lipoprotein derived aldehyde-4-hydroxy trans-2-nonenal in vascular smooth muscle cells
Srivastava, S. (2001) · Atherosclerosis · doi:10.1016/s0021-9150(01)00454-3 · Cited by 69
Protein Cross-Links: Universal Isolation and Characterization by Isotopic Derivatization and Electrospray Ionization Mass Spectrometry
Chen, X., Chen, Y. H., & Anderson, V. E. (1999) · Analytical Biochemistry · doi:10.1006/abio.1999.4243 · Cited by 69
Mechanisms of oxidative modification of low density lipoproteins under conditions of oxidative and carbonyl stress
Lankin, V. Z., Tikhaze, A. K., Kapelko, V. I., Сергеевна, Ш. Г., Шумаев, К. Б., Panasenko, O. M., Георгиевна, К. Г., & Belenkov, Y. N. (2007) · Biochemistry (Moscow) · doi:10.1134/s0006297907100069 · Cited by 67
Effect of insulin and growth hormone on rat heart and liver oxidative stress in control and caloric restricted animals
Sanz, A., Gredilla, R., Pamplona, R., Portero‐Otín, M., Vara, E., Tresguerres, J. A. F., & Barja, G. (2005) · Biogerontology · doi:10.1007/s10522-004-7380-0 · Cited by 66
Diabetes impairs the enzymatic disposal of 4-hydroxynonenal in rat liver
Traverso, N., Menini, S., Odetti, P. R., Pronzato, M. A., Cottalasso, D., & Marinari, U. M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00811-5 · Cited by 65
Histochemical visualization of oxidant stress
Frank, J., Alfonso Pompella, C., & Biesalski, H. K. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00395-6 · Cited by 63
Enzyme-linked immunosorbent assay for 4-hydroxynonenal–histidine conjugates
Borović, S., Rabuzin, F., Waeg, G., & Žarković, N. (2006) · Free Radical Research · doi:10.1080/10715760600693422 · Cited by 65
Contribution of mass spectrometry to assess quality of milk‐based products
Guy, P. A., & Fenaille, F. (2005) · Mass Spectrometry Reviews · doi:10.1002/mas.20074 · Cited by 64
Immunochemical Characterization of Purified Human Oxidized Low-Density Lipoprotein Antibodies
Virella, G., Koskinen, S., Krings, G., Onorato, J. M., Thorpe, S. R., & Lopes-Virella, M. F. (2000) · Clinical Immunology · doi:10.1006/clim.2000.4857 · Cited by 63
Self-citation
Supplementation with carnosine decreases plasma triglycerides and modulates atherosclerotic plaque composition in diabetic apo E−/− mice
Brown, B. E., Kim, C. H. J., Torpy, F. R., Bursill, C. A., McRobb, L. S., Heather, A. K., Davies, M. J., & van Reyk, D. M. (2013) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2013.11.068 · Cited by 62
Chemical modification of muscle protein in diabetes
Alt, N., Carson, J. A., Alderson, N. L., Wang, Y., Nagai, R., Henle, T., Thorpe, S. R., & Baynes, J. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.03.012 · Cited by 62
Self-citation
Inhibition of the oxidative metabolism of 3,4-dihydroxyphenylacetaldehyde, a reactive intermediate of dopamine metabolism, by 4-hydroxy-2-nonenal
Florang, V. R., Rees, J., Brogden, N. K., Anderson, D. G., Hurley, T. D., & Doorn, J. A. (2006) · NeuroToxicology · doi:10.1016/j.neuro.2006.07.018 · Cited by 63
Protein methionine content and MDA-lysine adducts are inversely related to maximum life span in the heart of mammals
Ruiz, M. C., Ayala, V., Portero‐Otín, M., Requena, J. R., Barja, G., & Pamplona, R. (2005) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2005.04.005 · Cited by 61
Self-citation
Lipoprotein Autoantibodies
Virella, G., & Lopes-Virella, M. F. (2003) · Clinical and Vaccine Immunology · doi:10.1128/cdli.10.4.499-505.2003 · Cited by 58
A ribozyme with michaelase activity
Eisenführ, A., Arora, P. S., Sengle, G., Takaoka, L. R., Nowick, J. S., & Famulok, M. (2003) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(02)00311-5 · Cited by 58
Aging Increases N epsilon -(Carboxymethyl)lysine and Caloric Restriction Decreases N epsilon -(Carboxyethyl)lysine and N epsilon -(Malondialdehyde)lysine in Rat Heart Mitochondrial Proteins
Pamplona, R., Portero‐Otín, M., Bellmunt, M. J., Gredilla, R., & Barja, G. (2002) · Free Radical Research · doi:10.1080/10715760210165 · Cited by 58
New Perspective of GABA as an Inhibitor of Formation of Advanced Lipoxidation End-Products: It's Interaction with Malondiadehyde
Deng, Y., Xu, L., Zeng, X., Li, Z., Qin, B., & He, N. (2010) · Journal of Biomedical Nanotechnology · doi:10.1166/jbn.2010.1130 · Cited by 57
Geometrical trans Lipid Isomers: A New Target for Lipidomics
Ferreri, C., & Chatgilialoglu, C. (2005) · ChemBioChem · doi:10.1002/cbic.200500109 · Cited by 57
The initiation of free radical peroxidation of low-density lipoproteins by glucose and its metabolite methylglyoxal: a common molecular mechanism of vascular wall injure in atherosclerosis and diabetes
Lankin, V. Z., Георгиевна, К. Г., Tikhaze, A. K., Шумаев, К. Б., Kumskova, E. M., & Viigimaa, M. (2014) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-014-2131-2 · Cited by 55
Definition of the immunogenic forms of modified human LDL recognized by human autoantibodies and by rabbit hyperimmune antibodies
Virella, G., Thorpe, S. R., Alderson, N. L., Derrick, M. B., Chassereau, C. N., Rhett, J. M., & Lopes-Virella, M. F. (2004) · Journal of Lipid Research · doi:10.1194/jlr.m400095-jlr200 · Cited by 55
Self-citation
Human and rat brain lipofuscin proteome
Ottis, P., Koppe, K., Onisko, B., Dynin, I. C., Arzberger, T., Kretzschmar, H. A., Requena, J. R., Silva, C. J., Huston, J. P., & Korth, C. (2012) · PROTEOMICS · doi:10.1002/pmic.201100668 · Cited by 55
Self-citation
Glycated LDL increases monocyte CC chemokine receptor 2 expression and monocyte chemoattractant protein-1-mediated chemotaxis
Isoda, K., Folco, E. J. E., Marwali, M. R., Ohsuzu, F., & Libby, P. (2008) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2007.10.035 · Cited by 53
Effect of the degree of fatty acid unsaturation of rat heart mitochondria on their rates of H2O2 production and lipid and protein oxidative damage
Herrero, A., Portero‐Otín, M., Bellmunt, M. J., Pamplona, R., & Barja, G. (2001) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(01)00214-7 · Cited by 53
Thyroid status modulates glycoxidative and lipoxidative modification of tissue proteins
Pamplona, R., Portero‐Otín, M., Ruiz, C., Bellmunt, M. J., Requena, J. R., Thorpe, S. R., Baynes, J., Romero, M., Lopez‐Torres, M., & Barja, G. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00135-5 · Cited by 53
Self-citation
Proinflammatory effects of malondialdehyde in lymphocytes
Raghavan, S., Subramaniyam, G., & Shanmugam, N. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.1211617 · Cited by 50
Oxidative modifications of protein structures
Naskalski, J. W., & Bartosz, G. (2001) · Advances in clinical chemistry · doi:10.1016/s0065-2423(01)35017-5 · Cited by 50
Efficient algal lipid extraction via photocatalysis and its conversion to biofuel
Shwetharani, R., & Balakrishna, R. G. (2016) · Applied Energy · doi:10.1016/j.apenergy.2016.01.087 · Cited by 49
Mass spectrometry of fatty aldehydes
Berdyshev, E. V. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.08.018 · Cited by 48
Oxidative Fragmentation of Hydroxy Octadecadienoates Generates Biologically Active γ-Hydroxyalkenals
Sun, M., & Salomon, R. G. (2004) · Journal of the American Chemical Society · doi:10.1021/ja038756w · Cited by 48
Formation of Lipid-Protein Adducts in Low-Density Lipoprotein by Fluxes of Peroxynitrite and Its Inhibition by Nitric Oxide
Trostchansky, A., Batthyány, C., Botti, H., Radí, R., Denicola, A., & Rubbo, H. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2583 · Cited by 46
Detection of lipofuscin‐like fluorophore in oxidized human low‐density lipoprotein
Itakura, K., Oya‐Ito, T., Osawa, T., Yamada, S., Toyokuni, S., Shibata, N., Kobayashi, M., & Uchida, K. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01539-8 · Cited by 44
Chemical modification of proteins during peroxidation of phospholipids
Januszewski, A. S., Alderson, N. L., Jenkins, A. J., Thorpe, S. R., & Baynes, J. (2005) · Journal of Lipid Research · doi:10.1194/jlr.m400442-jlr200 · Cited by 42
Self-citation
Study of peptides containing modified lysine residues by tandem mass spectrometry: precursor ion scanning of hexanal‐modified peptides
Fenaille, F., Tabet, J., & Guy, P. A. (2003) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.1283 · Cited by 42
Polyphenol rich oil palm leaves extract reduce hyperglycaemia and lipid oxidation in STZ-rats
Tan, R. T. R., Mohammed, S., Fard, S. G., Mustapha, N. M., Goh, Y. M., & Manap, M. Y. A. (2011) · Universiti Putra Malaysia Institutional Repository (Universiti Putra Malaysia) · Cited by 41
Formation of Nε-(Carboxymethyl)lysine and Loss of Lysine in Casein Glucose−Fatty Acid Model Systems
Lima, M., Assar, S. H., & Ames, J. M. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf903562c · Cited by 41
Solid Phase Extraction and Liquid Chromatography−Tandem Mass Spectrometry for the Evaluation of 4-Hydroxy-2-nonenal in Pork Products
Zanardi, E., Jagersma, C. G., Ghidini, S., & Chizzolini, R. (2002) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf020201h · Cited by 41
Iron Chelators with Topoisomerase-Inhibitory Activity and Their Anticancer Applications
Rao, V. A. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4877 · Cited by 41
Aldehyde adducts generated during lipid peroxidation modification of proteins
Uchida, K. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1036052 · Cited by 40
Protein nonenzymatic modifications and proteasome activity in skeletal muscle from the short-lived rat and long-lived pigeon
Portero‐Otín, M., Requena, J. R., Bellmunt, M. J., Ayala, V., & Pamplona, R. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.08.001 · Cited by 40
Self-citation
U-101033E (2,4-diaminopyrrolopyrimidine), a potent inhibitor of membrane lipid peroxidation as assessed by the production of 4-hydroxynonenal, malondialdehyde, and 4-hydroxynonenal– protein adducts
Rohn, T. T., Nelson, L. K., Waeg, G., & Quinn, M. T. (1998) · Biochemical Pharmacology · doi:10.1016/s0006-2952(98)00266-4 · Cited by 40
Lipofuscin-like fluorophores originated from malondialdehyde
Uchida, K. (2006) · Free Radical Research · doi:10.1080/10715760600902302 · Cited by 39
New developments in the isoprostane pathway: identification of novel highly reactive γ‐ketoaldehydes (isolevuglandins) and characterization of their protein adducts
Roberts, L. J., Salomon, R. G., Morrow, J. D., & Brame, C. J. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.10.1157 · Cited by 39
Identification and quantification of Nɛ-(Hexanoyl)lysine in human urine by liquid chromatography/tandem mass spectrometry
Kato, Y., Yoshida, A., Naito, M., Kawai, Y., Tsuji, K., Kitamura, M., Kitamoto, N., & Osawa, T. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.09.007 · Cited by 38
Fish oil and 3-thia fatty acid have additive effects on lipid metabolism but antagonistic effects on oxidative damage when fed to rats for 50 weeks
Vigerust, N. F., Cacabelos, D., Burri, L., Berge, K., Wergedahl, H., Christensen, B. J., Portero‐Otín, M., Viste, A., Pamplona, R., Berge, R. K., et al. (2012) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2011.08.006 · Cited by 37
Method To Characterize and Monitor Covalent Interactions of Flavor Compounds with β‑Lactoglobulin Using Mass Spectrometry and Proteomics
Anantharamkrishnan, V., & Reineccius, G. A. (2020) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b07978 · Cited by 37
Development of Capture Assays for Different Modifications of Human Low-Density Lipoprotein
Virella, G., Derrick, M. B., Pate, V., Chassereau, C. N., Thorpe, S. R., & Lopes-Virella, M. F. (2005) · Clinical and Vaccine Immunology · doi:10.1128/cdli.12.1.68-75.2005 · Cited by 36
Self-citation
Effect of Malondialdehyde on the Digestibility of Beef Myofibrillar Protein: Potential Mechanisms from Structure to Modification Site
Yin, Y., Zhou, L., Cai, J., Feng, F., Xing, L., & Zhang, W. (2022) · Foods · doi:10.3390/foods11152176 · Cited by 35
Oxidized Low Density Lipoproteins-Do We Know Enough About Them?
Jiang, X., Yang, Z., Chandrakala, A. N., Pressley, D., & Parthasarathy, S. (2011) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-011-6326-4 · Cited by 35
Effect of graded corticosterone treatment on aging-related markers of oxidative stress in rat liver mitochondria
Caro, P., Gómez, J., Sanz, A., Portero‐Otín, M., Pamplona, R., & Barja, G. (2006) · Biogerontology · doi:10.1007/s10522-006-9026-x · Cited by 35
Skin beautification with oral non-hydrolized versions of carnosine and carcinine: Effective therapeutic management and cosmetic skincare solutions against oxidative glycation and free-radical production as a causal mechanism of diabetic complications and skin aging
Babizhayev, M. A., Deyev, A. I., Savel'yeva, E. L., Lankin, V. Z., & Yegorov, Y. E. (2011) · Journal of Dermatological Treatment · doi:10.3109/09546634.2010.521812 · Cited by 35
Irreversible Inhibition of Plasma Membrane (Ca2++ Mg2+)-ATPase and Ca2+Transport by 4-OH-2,3-trans-Nonenal
McConnell, E. J., Bittelmeyer, A. M., & Raess, B. U. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0976 · Cited by 35
Nε-(carboxymethyl)lysine (CML) as a Biomarker of Oxidative Stress in Long-Lived Tissue Proteins
Shaw, J., Baynes, J., & Thorpe, S. R. (2003) · Humana Press eBooks · doi:10.1385/1-59259-173-6:129 · Cited by 34
Self-citation
Determination of malondialdehyde in biological fluids by high-performance liquid chromatography using rhodamine B hydrazide as the derivatization reagent
Li, P., Ding, G., Deng, Y., Punyapitak, D., Li, D., & Cao, Y. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.06.032 · Cited by 33
Effects of oxidised linoleic acid on the formation of Nε‐carboxymethyl‐lysine and Nε‐carboxyethyl‐lysine in Maillard reaction system
Yu, L., He, Z., Zeng, M., Zheng, Z., He, J., Wang, M., & Chen, J. (2015) · International Journal of Food Science & Technology · doi:10.1111/ijfs.13016 · Cited by 33
Decreased IL-7 Responsiveness Is Related to Oxidative Stress in HIV Disease
Kalinowska, M., Bazdar, D. A., Lederman, M. M., Funderburg, N., & Sieg, S. F. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058764 · Cited by 32
Effect of reactive oxygen and carbonyl species on crucial cellular antioxidant enzymes
Lesgards, J., Gauthier, C., Iovanna, J., Vidal, N., Dolla, A. R., & Stocker, P. (2011) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.12.028 · Cited by 32
Superoxide formation as a result of interaction of L-lysine with dicarbonyl compounds and its possible mechanism
Шумаев, К. Б., Gubkina, S. A., Kumskova, E. M., Сергеевна, Ш. Г., Ruuge, E. K., & Lankin, V. Z. (2009) · Biochemistry (Moscow) · doi:10.1134/s0006297909040154 · Cited by 32
Effects of UVR and UVR-induced Cytokines on Production of Extracellular Matrix Proteins and Proteases by Dermal Fibroblasts Cultured in Collagen Gels¶
Kossodo, S. C., Wong, W., Simon, G., & Kochevar, I. E. (2004) · Photochemistry and Photobiology · doi:10.1562/0031-8655(2004)79 · Cited by 6
Mass spectrometric quantification of amino acid oxidation products identifies oxidative mechanisms of diabetic end-organ damage
Vivekanandan‐Giri, A., Wang, J. H., Byun, J., & Pennathur, S. (2008) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-008-9093-1 · Cited by 30
Oxidative injury in multiple sclerosis cerebellar grey matter
Kemp, K. C., Redondo, J., Hares, K. M., Rice, C. M., Scolding, N. J., & Wilkins, A. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.027 · Cited by 29
Effects of dietary canola, olive, and linolenic acid enriched olive oils on plasma lipids, lipid peroxidation and lipoprotein lipase activity in rats
Hwalla, N. C., Antoniades, K., & Habbal, Z. (1999) · Nutrition Research · doi:10.1016/s0271-5317(99)00025-1 · Cited by 29
Oxidized proteins and their contribution to redox homeostasis
Martı́nez-Sánchez, G., Giuliani, A., Pérez-Davison, G., & León, O. S. (2005) · Redox Report · doi:10.1179/135100005x57382 · Cited by 28
Inhibition of Glycosylation Processes: the Reaction between Pyridoxamine and Glucose
Adrover, M., Vilanova, B., Muñoz, F., & Donoso, J. (2005) · Chemistry & Biodiversity · doi:10.1002/cbdv.200590074 · Cited by 28
An Experimentally Robust Model of Monomeric Apolipoprotein A-I Created from a Chimera of Two X-ray Structures and Molecular Dynamics Simulations
Segrest, J. P., Jones, M. K., Shao, B., & Heinecke, J. W. (2014) · Biochemistry · doi:10.1021/bi501111j · Cited by 27
AICAR Protects Vascular Endothelial Cells from Oxidative Injury Induced by the Long-Term Palmitate Excess
Samsonov, M. V., Podkuychenko, N. V., Khapchaev, A. Y., Efremov, E. E., Yanushevskaya, E. V., Vlasik, T. N., Lankin, V. Z., Stafeev, I., Skulachev, M. V., Шестакова, М. В., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010211 · Cited by 29
Excessive Lipid Peroxidation in Uterine Epithelium Causes Implantation Failure and Pregnancy Loss
Lu, Y., Shao, Y., Cui, W., Jia, Z., Zhang, Q., Zhao, Q., Chen, Z., Yan, J., Chu, B., & Yuan, J. (2023) · Advanced Science · doi:10.1002/advs.202302887 · Cited by 29
Macrophages actively accumulate malonyldialdehyde-modified but not enzymatically oxidized low density lipoprotein
Lankin, V. Z., Tikhaze, A. K., & Kumskova, E. M. (2012) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-012-1247-5 · Cited by 27
Free malondialdehyde determination in rat brain tissue by capillary zone electrophoresis: evaluation of two protein removal procedures
Claeson, K., Åberg, F. O., & Karlberg, B. (2000) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(00)00030-x · Cited by 27
Dietary cholesterol enhances osmoregulation, antioxidant defenses and immune response of Litopenaeus vannamei to alleviate the macromolecular damage induced by salinity stress
Su, C., Li, J., Zhang, M., Pan, L., Wang, Y., Ding, Y., Chen, Z., & Lu, M. (2022) · Aquaculture · doi:10.1016/j.aquaculture.2022.738861 · Cited by 26
Circulating antibodies recognizing malondialdehyde-modified proteins in healthy subjects
Vay, D., Parodi, M., Rolla, R., Mottaran, E., Vidali, M., Bellomo, G., & Albano, E. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00469-x · Cited by 26
Lipid Peroxidation Has Major Impact on Malondialdehyde-Derived but Only Minor Influence on Glyoxal and Methylglyoxal-Derived Protein Modifications in Carbohydrate-Rich Foods
Eggen, M. D., Merboth, P., Neukirchner, H., & Glomb, M. A. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c04052 · Cited by 24
Lipid nitration and formation of lipid-protein adducts: biological insights
Trostchansky, A., & Rubbo, H. (2006) · Amino Acids · doi:10.1007/s00726-006-0426-7 · Cited by 24
Polyunsaturated fatty acids acutely suppress antibodies to malondialdehyde-modified lipoproteins in patients with vascular disease
Gradek, W. Q., Harris, M. T., Yahia, N., Davis, W. W., Le, N., & Brown, W. V. (2004) · The American Journal of Cardiology · doi:10.1016/j.amjcard.2003.12.028 · Cited by 24
Overexpression of Interleukin-8 Promotes the Progression of Fatty Liver to Nonalcoholic Steatohepatitis in Mice
Cho, Y. E., Kim, Y. S., Kim, S.-J., Lee, H., & Hwang, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015489 · Cited by 24
Analysis of Interactions of Brevetoxin-B and Human Serum Albumin by Liquid Chromatography/Mass Spectrometry
Wang, Z., & Ramsdell, J. S. (2010) · Chemical Research in Toxicology · doi:10.1021/tx1002854 · Cited by 23
Site-specific Effects of Peptide Lipidation on β-Amyloid Aggregation and Cytotoxicity
Qahwash, I. M., Boire, A. A., Lanning, J. D., Krausz, T. N., Pytel, P., & Meredith, S. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702146200 · Cited by 22
Exceptionally old mice are highly resistant to lipoxidation-derived molecular damage
Arranz, L., Naudí, A., la Fuente, M. D., & Pamplona, R. (2012) · AGE · doi:10.1007/s11357-012-9391-0 · Cited by 23
Evidence That Malondialdehyde-Derived Aminoenimine Is Not a Fluorescent Age Pigment
Itakura, K., & Uchida, K. (2001) · Chemical Research in Toxicology · doi:10.1021/tx010055u · Cited by 23
Protein conjugated with aldehydes derived from lipid peroxidation as an independent parameter of the carbonyl stress in the kidney damage
Medina-Navarro, R., Nieto-Aguilar, R., & Alvares-Aguilar, C. (2011) · Lipids in Health and Disease · doi:10.1186/1476-511x-10-201 · Cited by 22
New Functions of Glucosamine as a Scavenger of the Lipid Peroxidation Product Malondialdehyde
Fang, C., Peng, M., Li, G., Tian, J., & Yin, D. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700059b · Cited by 22
Formation of N-(hexanoyl)ethanolamine, a novel phosphatidylethanolamine adduct, during the oxidation of erythrocyte membrane and low-density lipoprotein
Tsuji, K., Kawai, Y., Kato, Y., & Osawa, T. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01038-6 · Cited by 22
Synthesis of a Novel Radical Trapping and Carbonyl Group Trapping Anti-AGE Agent: A Pyridoxamine Analogue for Inhibiting Advanced Glycation (AGE) and Lipoxidation (ALE) End Products
Culbertson, S. M., Enright, G. D., & Ingold, K. U. (2003) · Organic Letters · doi:10.1021/ol0348147 · Cited by 22
Changes in serum levels of MDA and MMP-9 after UPF in patients with OSAS
Vuralkan, E., Mutlu, M., Firat, I. H., Yardım-Akaydin, S., Sağıt, M., Akın, İ., Salihoğlu, E. M., & Ardiç, S. (2013) · European Archives of Oto-Rhino-Laryngology · doi:10.1007/s00405-013-2821-5 · Cited by 21
Reaction Mechanism of Covalent Modification of Phosphatidylethanolamine Lipids by Reactive Aldehydes 4-Hydroxy-2-nonenal and 4-Oxo-2-nonenal
Vazdar, K., Vojta, D., Margetić, D., & Vazdar, M. (2017) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.6b00443 · Cited by 21
Detection of acrolein?lysine adducts in plasma low-density lipoprotein and in aorta of cyclophosphamide-administered rats
Arikketh, D., Niranjali, S., & Devaraj, H. (2004) · Archives of Toxicology · doi:10.1007/s00204-004-0556-1 · Cited by 21
Improved method for the immunological detection of malondialdehyde-modified low-density lipoproteins in human serum
Kitano, S., Kanno, T., Maekawa, M., Sakurabayashi, I., Kotani, K., Hisatomi, H., Hibi, N., Kubono, K., & Harada, S. (2004) · Analytica Chimica Acta · doi:10.1016/j.aca.2003.12.040 · Cited by 21
HNE‐dependent molecular damage in diabetic nephropathy and its possible prevention by N‐acetyl‐cysteine and oxerutin
Furfaro, A. L., Menini, S., Patriarca, S., Pesce, C. M., Odetti, P. R., Cottalasso, D., Marinari, U. M., Pronzato, M. A., & Traverso, N. (2005) · BioFactors · doi:10.1002/biof.5520240134 · Cited by 21
Mitochondrial Dysfunction and Oxidative and Endoplasmic Reticulum Stress in Argyrophilic Grain Disease
Ilieva, E. V., Kichev, A., Naudí, A., Ferrer, I., Pamplona, R., & Portero‐Otín, M. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31820f8765 · Cited by 20
Differential distribution of 4-hydroxynonenal adducts to sulfur and nitrogen residues in blood proteins as revealed using Raney nickel and gas chromatography–mass spectrometry
Lesgards, J., Frayne, I. R., Comte, B., Busseuil, D., Rhéaume, É., Tardif, J., & Rosiers, C. D. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.08.002 · Cited by 20

Authors: REQUENA, J. R., FU, M. X., AHMED, M. U., JENKINS, A. J., LYONS, T. J., BAYNES, J. W., & THORPE, S. R.
Affiliations: University of South Carolina (US)
Medical University of South Carolina (US)
ORCID: JENKINS, Alicia J.
LYONS, Timothy J.
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 1997-02-15
Volume: 322
Issue: 1
Pages: 317-325
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj3220317
PMC: PMC1218194
OpenAlex: W1843398852
Cited by: 293
References: 35
Citations by year: 2026: 4 · 2025: 3 · 2024: 3 · 2023: 13 · 2022: 7 · 2021: 6 · 2020: 7 · 2019: 2 · 2018: 5 · 2017: 9 · 2016: 6 · 2015: 5 · 2014: 7 · 2013: 11 · 2012: 14
FWCI: 10.07
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Scholar Commons (University of South Carolina) (submittedVersion)
Research Portal (Queen's University Belfast) (submittedVersion)
Funders: National Institutes of Health (5r01ag011472-04)
National Institute on Aging (AG-11472)
National Eye Institute (5R29 EY10697, R29EY010697)
Topics: Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Paraoxonase enzyme and polymorphisms
Keywords: malondialdehyde, 4-hydroxynonenal, lipid peroxidation, lysine adducts, low-density lipoprotein, protein oxidation, Schiff base adducts, Michael addition, sodium borohydride reduction, oxidative stress biomarkers, conjugated dienes, protein cross-linking
MeSH terms: Aldehydes, Amino Acids, Collagen, Copper, Crystallins, Drug Stability, Humans, Lipoproteins, LDL, Lysine, Malondialdehyde, Gas Chromatography-Mass Spectrometry, Oxidation-Reduction, Ribonucleases, Schiff Bases, Skin, Lipid Peroxidation

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

Quantification of malondialdehyde and 4-hydroxynonenal adducts to lysine residues in native and oxidized human low-density lipoprotein

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks