Oxidation of the zinc-thiolate complex and uncoupling of endothelial nitric oxide synthase by peroxynitrite
Open accessAbstract
Nitric oxide (NO) is produced by NO synthase (NOS) in many cells and plays important roles in the neuronal, muscular, cardiovascular, and immune systems.In various disease conditions, all three types of NOS (neuronal, inducible, and endothelial) are reported to generate oxidants through unknown mechanisms.We present here the first evidence that peroxynitrite (ONOO -) releases zinc from the zinc-thiolate cluster of endothelial NOS (eNOS) and presumably forms disulfide bonds between the monomers.As a result, disruption of the otherwise SDS-resistant eNOS dimers occurs under reducing conditions.eNOS catalytic activity is exquisitely sensitive to ONOO -, which decreases NO synthesis and increases superoxide anion (O 2 .-)production by the enzyme.The reducing cofactor tetrahydrobiopterin is not oxidized, nor does it prevent oxidation of eNOS by the same low concentrations of OONO -.Furthermore, eNOS derived from endothelial cells exposed to elevated glucose produces more O 2 .-,and, like eNOS purified from diabetic LDL receptor-deficient mice, contains less zinc and fewer SDS-resistant dimers.Hence, eNOS exposure to oxidants including ONOO -causes increased enzymatic uncoupling and generation of O 2 .-indiabetes, contributing further to endothelial cell oxidant stress.Regulation of the zinc-thiolate center of NOS by ONOO -provides a novel mechanism for modulation of the enzyme function in disease.
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Mitochondrial hydrogen peroxide can oxidize the catalytic subunit of AMP kinase, leading to its autophosphorylation and activation to modulate metabolism.
“Mitochondrial hydrogen peroxide can oxidize the catalytic subunit of AMP kinase, leading to its autophosphorylation and subsequent activation to modulate metabolism within the cell (481, 1067).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [1067]
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Cites
Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly
Beckman, J. S., & Koppenol, W. H. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.271.5.c1424 · Cited by 5,513 · see citing works
Regulation of biosynthesis of nitric oxide.
Nathan, C., & Xie, Q. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36703-0 · Cited by 1,669 · see citing works
Superoxide generation by endothelial nitric oxide synthase: The influence of cofactors
Vásquez-Vivar, J., Kalyanaraman, B., Martásek, P., Hogg, N., Masters, B. S. S., Karoui, H., Tordo, P., & Pritchard, K. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9220 · Cited by 1,484 · see citing works
Nitric oxide synthase structure and mechanism
Marletta, M. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31375-9 · Cited by 1,341 · see citing works
Mechanisms Underlying Endothelial Dysfunction in Diabetes Mellitus
Hink, U., Li, H., Mollnau, H., Oelze, M., Matheis, E., Hartmann, M., Skatchkov, M. P., Thaiss, F., Stahl, R. A. K., Warnholtz, A., et al. (2001) · Circulation Research · doi:10.1161/01.res.88.2.e14 · Cited by 1,176 · see citing works
Nitric oxide synthases: which, where, how, and why?
Michel, T. M., & Féron, O. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119750 · Cited by 1,018 · see citing works
Oxidative Damage and Tyrosine Nitration from Peroxynitrite
Beckman, J. S. (1996) · Chemical Research in Toxicology · doi:10.1021/tx9501445 · Cited by 993 · see citing works
Pollock, J. S., Förstermann, U., Mitchell, J. A., Warner, T. D., Schmidt, H. H. H. W., Nakane, M., & Murad, F. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10480 · Cited by 979 · see citing works
Activation of molecular oxygen by flavins and flavoproteins.
Massey, V. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31664-2 · Cited by 818 · see citing works
Cosentino, F., Hishikawa, K., Katušić, Z. S., & Lüscher, T. F. (1997) · Circulation · doi:10.1161/01.cir.96.1.25 · Cited by 762 · see citing works
Laursen, J. B., Somers, M., Kurz, S., McCann, L., Warnholtz, A., Freeman, B. A., Tarpey, M., Fukai, T., & Harrison, D. G. (2001) · Circulation · doi:10.1161/01.cir.103.9.1282 · Cited by 721 · see citing works
Superoxide Generation from Endothelial Nitric-oxide Synthase
Xia, Y., Tsai, A.-L., Berka, V., & Zweier, J. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.25804 · Cited by 705 · see citing works
Superoxide and peroxynitrite generation from inducible nitric oxide synthase in macrophages
Xia, Y., & Zweier, J. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.13.6954 · Cited by 691 · see citing works
Tetranitromethane. A Reagent for the Nitration of Tyrosyl Residues in Proteins*
Sokolovsky, M., Riordan, J. F., & Vallée, B. L. (1966) · Biochemistry · doi:10.1021/bi00875a029 · Cited by 637 · see citing works
Crystal Structure of Constitutive Endothelial Nitric Oxide Synthase
Raman, C. S., Li, H., Pavel Martasek, E., Král, V., Masters, B. S. S., & Poulos, T. L. (1998) · Cell · doi:10.1016/s0092-8674(00)81718-3 · Cited by 621 · see citing works
Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide.
Castro, L., Rodriguez, M., & Radi, R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43894-x · Cited by 589 · see citing works
Thiolate ligands in metallothionein confer redox activity on zinc clusters
Maret, W., & Vallée, B. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3478 · Cited by 576 · see citing works
Control of zinc transfer between thionein, metallothionein, and zinc proteins
Jacob, C., Maret, W., & Vallée, B. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3489 · Cited by 465 · see citing works
Heitzer, T., Krohn, K., Albers, S., & Meinertz, T. (2000) · Diabetologia · doi:10.1007/s001250051551 · Cited by 427 · see citing works
Shinozaki, K., Kashiwagi, A., Nishio, Y., Okamura, T., Yoshida, Y., Masada, M., Toda, N., & Kikkawa, R. (1999) · Diabetes · doi:10.2337/diabetes.48.12.2437 · Cited by 329 · see citing works
Protection against peroxynitrite
Arteel, G. E., Briviba, K., & Sies, H. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00073-3 · Cited by 305 · see citing works
Zou, M., Martin, C., & Ullrich, V. (1997) · Biological Chemistry · doi:10.1515/bchm.1997.378.7.707 · Cited by 289 · see citing works
Self-citationZou, M.-H., Shi, C., & Cohen, R. A. (2002) · Diabetes · doi:10.2337/diabetes.51.1.198 · Cited by 262 · see citing works
Self-citationCrow, J. P., Beckman, J. S., & McCord, J. M. (1995) · Biochemistry · doi:10.1021/bi00011a008 · Cited by 244 · see citing works
Shinozaki, K., Nishio, Y., Okamura, T., Yoshida, Y., Maegawa, H., Kojima, H., Masada, M., Toda, N., Kikkawa, R., & Kashiwagi, A. (2000) · Circulation Research · doi:10.1161/01.res.87.7.566 · Cited by 242 · see citing works
Crystal Structures of Zinc-free and -bound Heme Domain of Human Inducible Nitric-oxide Synthase
Li, H., Raman, C. S., Glaser, C. B., Blasko, E., Young, T. A., Parkinson, J. F., Whitlow, M. D., & Poulos, T. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.21276 · Cited by 241 · see citing works
Zou, M., & Ullrich, V. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00160-3 · Cited by 231 · see citing works
Self-citationPieper, G. M. (1997) · Journal of Cardiovascular Pharmacology · doi:10.1097/00005344-199701000-00002 · Cited by 226 · see citing works
Knapp, L. T., & Klann, E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002043200 · Cited by 201 · see citing works
Bernier, S. G., Haldar, S. M., & Michel, T. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005116200 · Cited by 190 · see citing works
Vasquez-Vivar, J. M., Hogg, N., Pavel Martasek, E., Karoui, H., Pritchard, K. A., & Kalyanaraman, B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.38.26736 · Cited by 174 · see citing works
Role of peroxynitrite in altered fetal-placental vascular reactivity in diabetes or preeclampsia
Kossenjans, W., Eis, A., Sahay, R., Brockman, D. E., & Myatt, L. (2000) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2000.278.4.h1311 · Cited by 141 · see citing works
S17834, a New Inhibitor of Cell Adhesion and Atherosclerosis That Targets NADPH Oxidase
Cayatte, A. J., Rupin, A., Oliver-Krasinski, J. M., Maitland, K. A., Sansilvestri, P., Boussard, M.-F., Wierzbicki, M., Verbeuren, T. J., & Cohen, R. A. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq1001.096723 · Cited by 116 · see citing works
Self-citationRole of Bound Zinc in Dimer Stabilization but Not Enzyme Activity of Neuronal Nitric-oxide Synthase
Hemmens, B., Goessler, W., Schmidt, K., & Mayer, B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005976200 · Cited by 108 · see citing works
Zou, M., Jendral, M. J., & Ullrich, V. (1999) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0702434 · Cited by 93 · see citing works
Self-citationSuperoxide Dismutase Mimics Based on Iron in Vivo
NAGANO, T., Hirano, T., & Hirobe, M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60521-6 · Cited by 92 · see citing works
Involvement of the Reductase Domain of Neuronal Nitric Oxide Synthase in Superoxide Anion Production
Miller, R. T., Martásek, P., Roman, L. J., Nishimura, J. S., & Masters, B. S. S. (1997) · Biochemistry · doi:10.1021/bi972022c · Cited by 86 · see citing works
The C331A Mutant of Neuronal Nitric-Oxide Synthase Is Defective in Arginine Binding
Pavel Martasek, E., Miller, R. T., Liu, Q., Roman, L. J., Salerno, J. C., Migita, C. T., Raman, C. S., Gross, S. S., Ikeda‐Saito, M., & Masters, B. S. S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.34799 · Cited by 64 · see citing works
Leber, A., Hemmens, B., Klösch, B., Goessler, W., Raber, G., Mayer, B., & Schmidt, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.37658 · Cited by 63 · see citing works
Role of zinc in pulmonary endothelial cell response to oxidative stress.
Tang, Z.-L., Wasserloos, K., Croix, C. S. S., & Pitt, B. R. (2001) · American Journal of Physiology - Lung cellular and Molecular Physiology · doi:10.1152/ajplung.2001.281.1.l243 · Cited by 61 · see citing works
Zou, M., Daiber, A., Peterson, J. A., Shoun, H., & Ullrich, V. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1699 · Cited by 60 · see citing works
Self-citationPeroxynitrite inhibition of nitric oxide synthases
Pasquet, J. J. J. P., Zou, M., & Ullrich, V. (1996) · Biochimie · doi:10.1016/s0300-9084(97)82537-0 · Cited by 49 · see citing works
Self-citationInactivation of the Inducible Nitric Oxide Synthase by Peroxynitrite
Hühmer, A. F. R., Nishida, C. R., de Montellano, P. R. O., & Schöneich, C. (1997) · Chemical Research in Toxicology · doi:10.1021/tx960188t · Cited by 47 · see citing works
Peroxynitrite Reduction of Calmodulin Stimulation of Neuronal Nitric Oxide Synthase
Hühmer, A. F. R., Gerber, N. C., de Montellano, P. R. O., & Schöneich, C. (1996) · Chemical Research in Toxicology · doi:10.1021/tx950152l · Cited by 41 · see citing works
Zinc Content of Escherichia coli-expressed Constitutive Isoforms of Nitric-oxide Synthase
Miller, R. T., Pavel Martasek, E., Raman, C. S., & Masters, B. S. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.21.14537 · Cited by 38 · see citing works
A new decoration for nitric oxide synthase – a Zn(Cys)4 site
Ludwig, M. L., & Marletta, M. A. (1999) · Structure · doi:10.1016/s0969-2126(99)80047-1 · Cited by 28 · see citing works
Hepatoprotective Effect of Fe-TPEN on Carbon Tetrachloride Induced Liver Injury in Rats.
Moon, J., Su-Kyung, P. A. R. K., & Nagano, T. (1998) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.21.284 · Cited by 11 · see citing works
Kinetics of CO and NO Ligation with the Cys331 → Ala Mutant of Neuronal Nitric-oxide Synthase
Scheele, J. S., Bruner, E. L., Żemojtel, T., Pavel Martasek, E., Roman, L. J., Masters, B. S. S., Sharma, V. S., & Magde, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007461200 · Cited by 11 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390 · see citing works
Role of Oxidative Modifications in Atherosclerosis
Stocker, R., & Keaney, J. F. (2004) · Physiological Reviews · doi:10.1152/physrev.00047.2003 · Cited by 2,611 · see citing works
Endothelial Nitric Oxide Synthase in Vascular Disease: From Marvel to Menace
Förstermann, U., & Münzel, T. (2006) · Circulation · doi:10.1161/circulationaha.105.602532 · Cited by 1,957 · see citing works
Mészáros, B., Erdős, G., & Dosztányi, Z. (2018) · Nucleic Acids Res. · doi:10.1093/nar/gky384 · Cited by 1,376 · see citing works
Incalza, M. A., D’Oria, R., Natalicchio, A., Perrini, S., Laviola, L., & Giorgino, F. (2017) · Vascular Pharmacology · doi:10.1016/j.vph.2017.05.005 · Cited by 1,375 · see citing works
Myeloperoxidase and Cardiovascular Disease
Nicholls, S. J., & Hazen, S. L. (2005) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000163262.83456.6d · Cited by 803 · see citing works
Role of Oxidative Stress in Cardiac Hypertrophy and Remodeling
Takimoto, E., & Kass, D. A. (2006) · Hypertension · doi:10.1161/01.hyp.0000254415.31362.a7 · Cited by 772 · see citing works
Ceriello, A. (2003) · Diabetes Care · doi:10.2337/diacare.26.5.1589 · Cited by 734 · see citing works
Interactions of Peroxynitrite, Tetrahydrobiopterin, Ascorbic Acid, and Thiols
Kuzkaya, N., Weissmann, N., Harrison, D. G., & Dikalov, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302227200 · Cited by 692 · see citing works
Mikkelsen, R. B., & Wardman, P. (2003) · Oncogene · doi:10.1038/sj.onc.1206663 · Cited by 591 · see citing works
Endothelial dysfunction in diabetes mellitus: Molecular mechanisms and clinical implications
Tabit, C. E., Chung, W. B., Hamburg, N. M., & Vita, J. A. (2010) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-010-9134-4 · Cited by 584 · see citing works
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works
NADPH oxidases and oxidase crosstalk in cardiovascular diseases: novel therapeutic targets
Zhang, Y., Murugesan, P., Huang, K., & Cai, H. “. (2019) · Nature Reviews Cardiology · doi:10.1038/s41569-019-0260-8 · Cited by 546 · see citing works
Regulation of Endothelial Nitric Oxide Synthase by Tetrahydrobiopterin in Vascular Disease
Alp, N. J., & Channon, K. M. (2003) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000110785.96039.f6 · Cited by 524 · see citing works
Oxidative stress and endothelial dysfunction in hypertension
Schulz, E., Gori, T., & Münzel, T. F. (2011) · Hypertension Research · doi:10.1038/hr.2011.39 · Cited by 503 · see citing works
Oxidative stress and nitric oxide deficiency in the kidney: a critical link to hypertension?
Wilcox, C. S. (2005) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00250.2005 · Cited by 479 · see citing works
Activation of the AMP-activated Protein Kinase by the Anti-diabetic Drug Metformin in Vivo
Zou, M., Kirkpatrick, S. S., Davis, B. J., Nelson, J. S., Wiles, W. G., Schlattner, U., Neumann, D., Brownlee, M., Freeman, M. B., & Goldman, M. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404421200 · Cited by 471 · see citing works
Self-citationRetractedDavis, B. J., Xie, Z., Viollet, B., & Zou, M. (2006) · Diabetes · doi:10.2337/diabetes.55.02.06.db05-1064 · Cited by 467 · see citing works
Self-citationVascular protection: superoxide dismutase isoforms in the vessel wall.
Faraci, F., & Didion, S. (2004) · Arteriosclerosis, Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000133604.20182.cf · Cited by 528 · see citing works
Dysfunction of Endothelial Nitric Oxide Synthase and Atherosclerosis
Kawashima, S., & Yokoyama, M. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000125114.88079.96 · Cited by 455 · see citing works
Takimoto, E., Champion, H. C., Li, M., Ren, S. V., Rodríguez, E. R., Tavazzi, B., Lazzarino, G., Paolocci, N., Gabrielson, K. L., Wang, Y., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci21968 · Cited by 446 · see citing works
Sydow, K., & Münzel, T. F. (2003) · Atherosclerosis Supplements · doi:10.1016/s1567-5688(03)00033-3 · Cited by 431 · see citing works
Thum, T., Fraccarollo, D., Schultheiß, M., Froese, S., Galuppo, P., Widder, J. D., Tsikas, D., Ertl, G., & Bauersachs, J. K. (2007) · Diabetes · doi:10.2337/db06-0699 · Cited by 411 · see citing works
Münzel, T. F., Daiber, A., Ullrich, V., & Mülsch, A. (2005) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000168896.64927.bb · Cited by 409 · see citing works
Kellner, M., Noonepalle, S. K. R., Lü, Q., Srivastava, A., Zemskov, E. A., & Black, S. M. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-63245-2_8 · Cited by 411 · see citing works
Pathophysiology, diagnosis and prognostic implications of endothelial dysfunction
Münzel, T. F., Sinning, C., Post, F., Warnholtz, A., & Schulz, E. (2008) · Annals of Medicine · doi:10.1080/07853890701854702 · Cited by 399 · see citing works
Vitamin D and Endothelial Function
Kim, D., Meza, C., Clarke, H. E., Kim, J., & Hickner, R. C. (2020) · Nutrients · doi:10.3390/nu12020575 · Cited by 382 · see citing works
Endothelium‐mediated control of vascular tone: COX‐1 and COX‐2 products
Félétou, M., Huang, Y., & Vanhoutte, P. M. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01276.x · Cited by 372 · see citing works
eNOS uncoupling and endothelial dysfunction in aged vessels
Yang, Y., Huang, A., Kaley, G., & Sun, D. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00230.2009 · Cited by 370 · see citing works
Schulze, P. C., Yoshioka, J., Takahashi, T., He, Z., King, G. L., & Lee, R. T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400549200 · Cited by 369 · see citing works
Serum Myeloperoxidase Levels Independently Predict Endothelial Dysfunction in Humans
Vita, J. A., Brennan, M., Gokce, N., Mann, S. A., Goormastic, M., Shishehbor, M. H., Penn, M. S., Keaney, J. F., & Hazen, S. L. (2004) · Circulation · doi:10.1161/01.cir.0000140262.20831.8f · Cited by 366 · see citing works
Molecular Insights and Therapeutic Targets for Diabetic Endothelial Dysfunction
Xu, J., & Zou, M. (2009) · Circulation · doi:10.1161/circulationaha.108.835223 · Cited by 348 · see citing works
Self-citationDaiber, A. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.01.032 · Cited by 347 · see citing works
Pharmacological inhibition of AMP-activated protein kinase provides neuroprotection in stroke
McCullough, L. D., Zeng, Z., Li, H., Landree, L. E., McFadden, J., & Ronnett, G. V. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409985200 · Cited by 333 · see citing works
Vascular endothelial dysfunction, a major mediator in diabetic cardiomyopathy
Knapp, M., Tu, X., & Wu, R. (2018) · Acta Pharmacologica Sinica · doi:10.1038/s41401-018-0042-6 · Cited by 329 · see citing works
Endothelial Dysfunction: Is There a Hyperglycemia-Induced Imbalance of NOX and NOS?
Meza, C. A., La Favor, J. D., Kim, D.-H., & Hickner, R. C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153775 · Cited by 323 · see citing works
Münzel, T., Feil, R., Mülsch, A., Lohmann, S. M., Hofmann, F., & Walter, U. (2003) · Circulation · doi:10.1161/01.cir.0000094403.78467.c3 · Cited by 316 · see citing works
Biochemical basis and metabolic interplay of redox regulation
Zhang, L., Wang, X., Cueto, R., Effi, C., Zhang, Y., Tan, H., Qin, X., Ji, Y., Yang, X., & Wang, H. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101284 · Cited by 308 · see citing works
Daiber, A., Xia, N., Steven, S., Oelze, M. W., Hanf, A., Kröller‐Schön, S., Münzel, T. F., & Li, H. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20010187 · Cited by 311 · see citing works
The SGLT2 inhibitor empagliflozin improves the primary diabetic complications in ZDF rats
Steven, S., Oelze, M. W., Hanf, A., Kröller‐Schön, S., Kashani, F., Roohani, S., Welschof, P., Kopp, M., Gödtel‐Armbrust, U., Xia, N., et al. (2017) · Redox Biology · doi:10.1016/j.redox.2017.06.009 · Cited by 299 · see citing works
d’Uscio, L. V., Milstien, S., Richardson, D. M., Smith, L., & Katušić, Z. S. (2003) · Circulation Research · doi:10.1161/01.res.0000049166.33035.62 · Cited by 297 · see citing works
ROS and RNS signalling: adaptive redox switches through oxidative/nitrosative protein modifications
Moldogazieva, N. T., Mokhosoev, I. M., Feldman, N. B., & Lutsenko, S. V. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1457217 · Cited by 291 · see citing works
Varga, Z. V., Giricz, Z., Liaudet, L., Haskó, G., Ferdinandy, P., & Pacher, P. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.06.030 · Cited by 288 · see citing works
Role of oxidative stress and nitric oxide in atherothrombosis
Lubos, E. (2008) · Frontiers in bioscience · doi:10.2741/3084 · Cited by 290 · see citing works
Zinc and Regulation of Inflammatory Cytokines: Implications for Cardiometabolic Disease
Foster, M. J., & Samman, S. (2012) · Nutrients · doi:10.3390/nu4070676 · Cited by 281 · see citing works
Sun, Y., Lu, Y., Saredy, J., Wang, X., Drummer, C., Shao, Y., Saaoud, F., Xu, K., Liu, M., Yang, W. Y., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101696 · Cited by 283 · see citing works
Peroxynitrite and Vascular Endothelial Dysfunction in Diabetes Mellitus
Zou, M., Cohen, R. A., & Ullrich, V. (2004) · Endothelium · doi:10.1080/10623320490482619 · Cited by 270 · see citing works
Self-citationRavi, K., Brennan, L., Levic, S., Ross, P. A., & Black, S. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0300464101 · Cited by 263 · see citing works
Mitochondrial ROS Formation in the Pathogenesis of Diabetic Cardiomyopathy
Kaludercic, N., & Lisa, F. D. (2020) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2020.00012 · Cited by 264 · see citing works
Mikhed, Y., Daiber, A., & Steven, S. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160715918 · Cited by 257 · see citing works
Receptor for Advanced-Glycation End Products: Key Modulator of Myocardial Ischemic Injury
Bucciarelli, L. G., Kaneko, M., Ananthakrishnan, R., Harja, E., Lee, L. K., Hwang, Y. C., Lerner, S., Bakr, S., Li, Q., Lu, Y., et al. (2006) · Circulation · doi:10.1161/circulationaha.105.575993 · Cited by 256 · see citing works
Jaimes, E. A., DeMaster, E. G., Tian, R.-X., & Raij, L. R. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000127083.88549.58 · Cited by 248 · see citing works
Barua, R. S., Ambrose, J. A., Srivastava, S. K., DeVoe, M. C., & Eales‐Reynolds, L. (2003) · Circulation · doi:10.1161/01.cir.0000066691.52789.be · Cited by 246 · see citing works
AMP-activated protein kinase, stress responses and cardiovascular diseases
Wang, S., Song, P., & Zou, M. (2012) · Clinical Science · doi:10.1042/cs20110625 · Cited by 243 · see citing works
Self-citationZinc-Binding Cysteines: Diverse Functions and Structural Motifs
Pace, N., & Weerapana, E. (2014) · Biomolecules · doi:10.3390/biom4020419 · Cited by 241 · see citing works
Mechanisms and consequences of endothelial nitric oxide synthase dysfunction in hypertension
Li, Q., Youn, J.-Y., & Cai, H. “. (2015) · Journal of Hypertension · doi:10.1097/hjh.0000000000000587 · Cited by 237 · see citing works
Endothelial Arginase II: A Novel Target for the Treatment of Atherosclerosis
Ryoo, S., Gupta, G., Benjo, A., Lim, H. K., Camara, A., Sikka, G., Lim, H. K., Sohi, J., Santhanam, L., Soucy, K., et al. (2008) · Circulation Research · doi:10.1161/circresaha.107.169573 · Cited by 236 · see citing works
The redox biology of redox-inert zinc ions
Maret, W. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.01.006 · Cited by 237 · see citing works
Zhang, Q., Holland, W. L., Wilson, L. J., Tanner, J. M., Kearns, D., Cahoon, J. M., Pettey, D., Losee, J. T., Duncan, B., Gale, D. C., et al. (2012) · Diabetes · doi:10.2337/db11-1399 · Cited by 236 · see citing works
Vascular NADPH oxidases as drug targets for novel antioxidant strategies
Guzik, T. J., & Harrison, D. G. (2006) · Drug Discovery Today · doi:10.1016/j.drudis.2006.04.003 · Cited by 234 · see citing works
ABCG1 and HDL protect against endothelial dysfunction in mice fed a high-cholesterol diet
Terasaka, N., Yu, S., Yvan‐Charvet, L., Wang, N., Mzhavia, N., Langlois, R., Pagler, T. A., Li, R., Welch, C. L., Goldberg, I. J., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci35470 · Cited by 232 · see citing works
Redox signaling in cardiovascular health and disease
Madamanchi, N. R., & Runge, M. S. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.04.001 · Cited by 223 · see citing works
Mechanisms Involved in the Aging-Induced Vascular Dysfunction
Fuente, M. E. A. D. L., Angulo, J., Fernán, S. E., Peiró, C., Sánchez‐Ferrer, C. F., & Rodríguez‐Mañas, L. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00132 · Cited by 226 · see citing works
Endothelial dysfunction in aged humans is related with oxidative stress and vascular inflammation
Rodríguez‐Mañas, L., El‐Assar, M., Vallejo, S., Bonnardeaux, P. L.-D., Solı́s, J., Torregrossa, R. P., Montes, M., Nevado, J. B., Castro, M., Gómez‐Guerrero, C., et al. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00466.x · Cited by 225 · see citing works
van Golen, R. F., van Gulik, T. M., & Heger, M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.01.013 · Cited by 221 · see citing works
Wang, J., Song, Y., Elsherif, L., Song, Z., Zhou, G., Prabhu, S. D., Saari, J. T., & Cai, L. (2006) · Circulation · doi:10.1161/circulationaha.105.537894 · Cited by 222 · see citing works
Srinivasan, S. R., Hatley, M., Bolick, D. T., Palmer, L. A., Edelstein, D., Brownlee, M., & Hedrick, C. C. (2004) · Diabetologia · doi:10.1007/s00125-004-1525-1 · Cited by 216 · see citing works
Oxidative risk for atherothrombotic cardiovascular disease
Leopold, J. A., & Loscalzo, J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.09.009 · Cited by 216 · see citing works
Crabtree, M. J., Smith, C. L., Lam, G., Goligorsky, M. S., & Gross, S. S. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00823.2007 · Cited by 213 · see citing works
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Wang, M., Li, Y., Li, S., & Lv, J. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.851941 · Cited by 210 · see citing works
Oxidative Stress and Antioxidant Treatment in Diabetes
Scott, J. A., & King, G. L. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1331.020 · Cited by 206 · see citing works
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Li, H., Xia, N., Hasselwander, S., & Daiber, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092155 · Cited by 204 · see citing works
El‐Remessy, A. B., Behzadian, M. A., Abou-Mohamed, G., Franklin, T., Caldwell, R. W., & Caldwell, R. B. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64332-5 · Cited by 203 · see citing works
Mechanisms for the role of tetrahydrobiopterin in endothelial function and vascular disease
Schmidt, T. S., & Alp, N. J. (2007) · Clinical Science · doi:10.1042/cs20070108 · Cited by 195 · see citing works
Channon, K. M. (2004) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2004.10.003 · Cited by 196 · see citing works
The superoxide radical switch in the biology of nitric oxide and peroxynitrite
Piacenza, L., Zeida, A., Trujillo, M., & Radí, R. (2022) · Physiological Reviews · doi:10.1152/physrev.00005.2022 · Cited by 204 · see citing works
Zou, M., Hou, X., Shi, C., Nagata, D., Walsh, K., & Cohen, R. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204512200 · Cited by 189 · see citing works
Self-citationNew insights on oxidative stress in the artery wall
STOCKER, R., & KEANEY, J. F. (2005) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2005.01370.x · Cited by 188 · see citing works
Zinc Metabolism and Metallothioneins
Baltacı, A. K., Yüce, K., & Moğulkoç, R. (2017) · Biological Trace Element Research · doi:10.1007/s12011-017-1119-7 · Cited by 187 · see citing works
Li, H., Witte, K. K., August, M., Brausch, I., Gödtel‐Armbrust, U., Habermeier, A., Closs, E. I., Oelze, M., Münzel, T. F., & Förstermann, U. (2006) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2006.01.071 · Cited by 179 · see citing works
Tsuchiya, K., Tanaka, J., Yu, S., Welch, C. L., DePinho, R. A., Tabas, I. A., Tall, A. R., Goldberg, I. J., & Accili, D. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.01.018 · Cited by 179 · see citing works
Proatherosclerotic Mechanisms Involving Protein Kinase C in Diabetes and Insulin Resistance
Rask‐Madsen, C., & King, G. L. (2005) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000155325.41507.e0 · Cited by 176 · see citing works
Post-translational regulation of endothelial nitric oxide synthase in vascular endothelium
Qian, J., & Fulton, D. J. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00347 · Cited by 176 · see citing works
Trace minerals intake: Risks and benefits for cardiovascular health
Mohammadifard, N., Humphries, K. H., Gotay, C. C., Mena‐Sánchez, G., Salas‐Salvadó, J., Esmaillzadeh, A., Ignaszewski, A. P., & Sarrafzadegan, N. (2017) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2017.1406332 · Cited by 169 · see citing works
Reduced release of nitric oxide to shear stress in mesenteric arteries of aged rats
Sun, D., Huang, A., Yan, E. H., Wu, Z., Yan, C., Kaminski, P. M., Oury, T. D., Wolin, M. S., & Kaley, G. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00854.2003 · Cited by 167 · see citing works
Daiber, A., & Chłopicki, S. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.02.026 · Cited by 169 · see citing works
Zou, M., Hou, X., Shi, C., Kirkpatick, S., Liu, F., Goldman, M. H., & Cohen, R. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300215200 · Cited by 167 · see citing works
Self-citationRetractedZinc homeostasis in the metabolic syndrome and diabetes
Miao, X., Sun, W., Fu, Y., Miao, L., & Cai, L. (2013) · Frontiers of Medicine · doi:10.1007/s11684-013-0251-9 · Cited by 165 · see citing works
Salvemini, D., Kim, S. F., & Mollace, V. (2013) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00355.2012 · Cited by 165 · see citing works
Xie, Z., Zhang, J., Wu, J., Viollet, B., & Zou, M. (2008) · Diabetes · doi:10.2337/db08-0610 · Cited by 163 · see citing works
Self-citationRetractedMechanisms of H2O2-induced oxidative stress in endothelial cells
Coyle, C. H., Martínez, L. J., Coleman, M. C., Spitz, D. R., Weintraub, N. L., & Kader, K. N. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.02.017 · Cited by 160 · see citing works
Rajapakse, A. G., Yepuri, G., Carvas, J. M., Stein, S. M. A., Matter, C. M., Scerri, I., Ruffieux, J., Montani, J., Ming, X., & Yang, Z. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019237 · Cited by 161 · see citing works
Campos, A. C. E., Molognoni, F., de Melo, F. H. M., Galdieri, L. C., Carneiro, C. R. W., D’Almeida, V., Correa, M., & Jasiulionis, M. G. (2007) · Neoplasia · doi:10.1593/neo.07712 · Cited by 160 · see citing works
Recent novel approaches to limit oxidative stress and inflammation in diabetic complications
Pickering, R. J., Rosado, C. J., Sharma, A., Buksh, S., Tate, M., & de Haan, J. B. (2018) · Clinical & Translational Immunology · doi:10.1002/cti2.1016 · Cited by 164 · see citing works
Massion, P. B., & Balligand, J. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2002.025973 · Cited by 159 · see citing works
Nitric oxide synthase uncoupling: A therapeutic target in cardiovascular diseases
Roe, N. D., & Ren, J. T. (2012) · Vascular Pharmacology · doi:10.1016/j.vph.2012.02.004 · Cited by 157 · see citing works
Hemnes, A. R., Zaiman, A., & Champion, H. C. (2007) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00245.2007 · Cited by 156 · see citing works
Haemoglobin scavenging in intracranial bleeding: biology and clinical implications
Bulters, D. O., Gaastra, B., Zolnourian, A. H., Alexander, S. A., Ren, D., Blackburn, S., Borsody, M. K., Doré, S., Galea, J. P., Iihara, K., et al. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0020-0 · Cited by 157 · see citing works
Pathogenetic role of eNOS uncoupling in cardiopulmonary disorders
Gielis, J. F., Lin, J. Y., Wingler, K., Schil, P. E. V., Schmidt, H. H. H. W., & Moens, A. L. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.018 · Cited by 155 · see citing works
- Authors
- Zou, M.-H., Shi, C., & Cohen, R. A.
- Affiliations
- Boston University (US)
- Corresponding author
- Zou, Ming-Hui
- Venue
- Journal of Clinical Investigation
- Published
- 2002-03-15
- Volume
- 109
- Issue
- 6
- Pages
- 817-826
- ISSN
- 0021-9738 (ISSN-L)
- OpenAlex
- W4254181710
- Cited by
- 494
- References
- 48
- Citations by year
- 2026: 1 · 2025: 10 · 2024: 7 · 2023: 12 · 2022: 19 · 2021: 12 · 2020: 17 · 2019: 15 · 2018: 19 · 2017: 23 · 2016: 15 · 2015: 22 · 2014: 22 · 2013: 22 · 2012: 29
- FWCI
- 17.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- Funders
- American Heart Association
- National Institutes of Health (PO1 HL)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- peroxynitrite, endothelial nitric oxide synthase, superoxide production, tetrahydrobiopterin, disulfide bonds, oxidative stress, diabetes mellitus, endothelial cells, nitric oxide production
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