Carbon monoxide, reactive oxygen signaling, and oxidative stress
Open accessAbstract
The ubiquitous gas, carbon monoxide (CO), is of substantial biological importance, but apart from its affinity for reduced transition metals, particularly heme-iron, it is surprisingly nonreactive-as is the ferrous-carbonyl-in living systems. CO does form strong complexes with heme proteins for which molecular O2 is the preferred ligand and to which are attributed diverse physiological, adaptive, and toxic effects. Lately, it has become apparent that both exogenous and endogenous CO produced by heme oxygenase engender a prooxidant milieu in aerobic mammalian cells which initiates signaling related to reactive oxygen species (ROS) generation. ROS signaling contingent on CO can be segregated by CO concentration-time effects on cellular function, by the location of heme proteins, e.g., mitochondrial or nonmitochondrial sites, or by specific oxidation-reduction (redox) reactions. The fundamental responses to CO involve overt physiological regulatory events, such as activation of redox-sensitive transcription factors or stress-activated kinases, which institute compensatory expression of antioxidant enzymes and other adaptations to oxidative stress. In contrast, responses originating from highly elevated or protracted CO exposures tend to be nonspecific, produce untoward biological oxidations, and interfere with homeostasis. This brief overview provides a conceptual framework for understanding CO biology in terms of this physiological-pathological hierarchy.
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NO functions in mammalian systems extend beyond vascular signaling and are relevant in all organ systems, including neuronal signaling and host defense.
“The functions of NO in mammalian systems extend beyond vascular signaling and are relevant in all organ systems, including but not limited to neuronal signaling, and host defense”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [738]
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3 retracted
Suliman, H. B., Carraway, M. S., Ali, A. S., Reynolds, C. M., Welty‐Wolf, K. E., & Piantadosi, C. A. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32967 · Cited by 255 · see citing works
Self-citationRetractedRETRACTED: A new activating role for CO in cardiac mitochondrial biogenesis
Suliman, H. B., Carraway, M. S., Tatro, L. G., & Piantadosi, C. A. (2006) · Journal of Cell Science · doi:10.1242/jcs.03318 · Cited by 210 · see citing works
Self-citationRetractedWang, X., Wang, Y., Kim, H. P., Nakahira, K., Ryter, S. W., & Choi, A. M. K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607610200 · Cited by 192 · see citing works
RetractedWu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139 · see citing works
THE HEME OXYGENASE SYSTEM:A Regulator of Second Messenger Gases
Maines, M. D. (1997) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.37.1.517 · Cited by 2,489 · see citing works
Carbon monoxide has anti-inflammatory effects involving the mitogen-activated protein kinase pathway
Otterbein, L. E., Bach, F. H., Alam, J., Soares, M., Tao Lu, H., Wysk, M., Davis, R. J., Flavell, R. A., & Choi, A. M. K. (2000) · Nature Medicine · doi:10.1038/74680 · Cited by 2,153 · see citing works
Chandel, N. S., McClintock, D. S., Feliciano, C. E., Wood, T. M., Melendez, J. A., Rodriguez, A. M., & Schumacker, P. T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001914200 · Cited by 2,000 · see citing works
Carbon Monoxide: a Putative Neural Messenger
Verma, A. M., Hirsch, D. B., Glatt, C. E., Ronnett, G. V., & Snyder, S. H. (1993) · Science · doi:10.1126/science.7678352 · Cited by 1,563 · see citing works
Tenhunen, R., Marver, H. S., & Schmid, R. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63477-5 · Cited by 1,357 · see citing works
Transcriptional regulatory circuits controlling mitochondrial biogenesis and function
Kelly, D. P., & Scarpulla, R. C. (2004) · Genes & Development · doi:10.1101/gad.1177604 · Cited by 1,243 · see citing works
Mitochondrial biogenesis in mammals: the role of endogenous nitric oxide
Nisoli, E., Clementi, E., Paolucci, C., Cozzi, V., Tonello, C., Sciorati, C., Bracale, R., Valerio, A., Francolini, M., Moncada, S., et al. (2003) · Science · doi:10.1126/science.1079368 · Cited by 1,243 · see citing works
Reversible Inactivation of the Tumor Suppressor PTEN by H2O2
Lee, S.-R., Yang, K., Kwon, J., Lee, C., Jeong, W., & Rhee, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111899200 · Cited by 1,061 · see citing works
Carbon Monoxide Generated by Heme Oxygenase 1 Suppresses Endothelial Cell Apoptosis
Brouard, S., Otterbein, L. E., Anrather, J., Tobiasch, E., Bach, F. H., Choi, A. M. K., & Soares, M. P. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.7.1015 · Cited by 984 · see citing works
The heme synthesis and degradation pathways: role in oxidant sensitivity
Ryter, S. W., & Tyrrell, R. M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00223-3 · Cited by 822 · see citing works
Virbasius, J. V., & Scarpulla, R. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.4.1309 · Cited by 819 · see citing works
Redox regulation of PI 3‐kinase signalling via inactivation of PTEN
Leslie, N. R., Bennett, D., Lindsay, Y. E., Stewart, H., Gray, A., & Downes, C. P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg513 · Cited by 614 · see citing works
Trumpower, B. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38410-8 · Cited by 596 · see citing works
Heme oxygenase-1 and carbon monoxide suppress the pathogenesis of experimental cerebral malaria
Pamplona, A., Ferreira, A., Balla, J., Jeney, V., Balla, G., Epiphanio, S., Chora, Â., Rodrigues, C. D., Gregoire, I. P., Cunha-Rodrigues, M., et al. (2007) · Nature Medicine · doi:10.1038/nm1586 · Cited by 560 · see citing works
Nitric oxide and iron proteins
Cooper, C. E. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00021-3 · Cited by 510 · see citing works
Haem oxygenase-1 prevents cell death by regulating cellular iron
Ferris, C. D., Jaffrey, S. R., Sawa, A., Takahashi, M., Brady, S. D., Barrow, R. K., Tysoe, S. A., Wolosker, H., Barañano, D. E., Doré, S., et al. (1999) · Nature Cell Biology · doi:10.1038/11072 · Cited by 509 · see citing works
Regulation of Nox and Duox enzymatic activity and expression
Lambeth, J. D., Kawahara, T., & Diebold, B. A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.028 · Cited by 498 · see citing works
Mechanism of p38 MAP kinase activation in vivoPreprint
Brancho, D., Tanaka, N., Jaeschke, A., Ventura, J., Kelkar, N., Tanaka, Y., Kyuuma, M., Takeshita, T., Flavell, R. A., & Davis, R. J. (2003) · Genes & Development · doi:10.1101/gad.1107303 · Cited by 490 · see citing works
Brüne, B., & Ullrich, V. (1987) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)13029-0 · Cited by 472 · see citing works
Furchgott, R. F., & Jothianandan, D. (2008) · Blood Vessels · doi:10.1159/000158843 · Cited by 471 · see citing works
Soares, M. P., Seldon, M. P., Grégoire, I. P., Vassilevskaia, T. D., Berberat, P. O., Yu, J. H., Tsui, T., & Bach, F. H. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.6.3553 · Cited by 464 · see citing works
Hemoxygenase-2 Is an Oxygen Sensor for a Calcium-Sensitive Potassium Channel
Williams, S. E. J., Wootton, P., Mason, H. S., Bould, J., Iles, D., Riccardi, D., Peers, C., & Kemp, P. J. (2004) · Science · doi:10.1126/science.1105010 · Cited by 458 · see citing works
Dewilde, S., Kiger, L., Burmester, T., Hankeln, T., Baudin‐Creuza, V., Aerts, T., Marden, M. C., Caubergs, R. J., & Moens, L. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106438200 · Cited by 453 · see citing works
NPAS2: A Gas-Responsive Transcription Factor
Dioum, E. M., Rutter, J. P., Tuckerman, J. R., Gonzalez, G., Gilles‐Gonzalez, M., & McKnight, S. L. (2002) · Science · doi:10.1126/science.1078456 · Cited by 432 · see citing works
Heme Oxygenase-1 Modulates Early Inflammatory Responses
Kapturczak, M., Wasserfall, C. H., Brusko, T. M., Campbell‐Thompson, M., Ellis, T. M., Atkinson, M. A., & Agarwal, A. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63365-2 · Cited by 417 · see citing works
Fujita, T., Toda, K., Karimova, A., Yan, S., Naka, Y., Yet, S., & Pinsky, D. J. (2001) · Nature Medicine · doi:10.1038/87929 · Cited by 399 · see citing works
Suppression of Inflammatory Cytokine Production by Carbon Monoxide Involves the JNK Pathway and AP-1
Morse, D., Pischke, S. E., Zhou, Z., Davis, R. J., Flavell, R. A., Loop, T., Otterbein, S. L., Otterbein, L. E., & Choi, A. M. K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302942200 · Cited by 373 · see citing works
Heme oxygenase and the cardiovascular–renal system
Abraham, N. G., & Kappas, A. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.03.010 · Cited by 356 · see citing works
Nakahira, K., Kim, H. P., Geng, X. H., Nakao, A., Wang, X., Murase, N., Drain, P. F., Wang, X., Sasidhar, M., Nabel, E. G., et al. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20060845 · Cited by 356 · see citing works
Carbon Monoxide Controls the Proliferation of Hypoxic Vascular Smooth Muscle Cells
Morita, T., Mitsialis, S. A., Koike, H., Liu, Y., & Kourembanas, S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.32804 · Cited by 332 · see citing works
Durante, W., Kroll, M. H., Christodoulides, N., Peyton, K. J., & Schafer, A. I. (1997) · Circulation Research · doi:10.1161/01.res.80.4.557 · Cited by 329 · see citing works
Heme-based sensors: defining characteristics, recent developments, and regulatory hypotheses
Gilles‐Gonzalez, M., & GONZALEZ, G. (2004) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2004.11.006 · Cited by 328 · see citing works
Zuckerbraun, B. S., Chin, B. Y., Bilban, M., d'Avila, J. D. C., Rao, J., Billiar, T. R., & Otterbein, L. E. (2007) · The FASEB Journal · doi:10.1096/fj.06-6644com · Cited by 323 · see citing works
Mitochondrial oxidative stress after carbon monoxide hypoxia in the rat brain.
Zhang, J., & Piantadosi, C. A. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115980 · Cited by 320 · see citing works
Self-citationTanaka, H., Matsumura, I., Ezoe, S., Satoh, Y., Sakamaki, T., Albanese, C., Machii, T., Pestell, R. G., & Kanakura, Y. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00522-1 · Cited by 289 · see citing works
Inhibition of Hypoxia-inducible Factor 1 Activation by Carbon Monoxide and Nitric Oxide
Huang, E. L., Willmore, W. G., Gu, J., Goldberg, M. A., & Bunn, H. F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.9038 · Cited by 287 · see citing works
Siow, R. C. M. (1999) · Cardiovascular Research · doi:10.1016/s0008-6363(98)00278-8 · Cited by 274 · see citing works
Foresti, R., & Motterlini, R. (1999) · Free Radical Research · doi:10.1080/10715769900301031 · Cited by 271 · see citing works
The Stoichiometry and Absorption Spectra of Components a and a3 in Cytochrome c Oxidase*
Vanneste, W. H. (1966) · Biochemistry · doi:10.1021/bi00867a005 · Cited by 265 · see citing works
The Drosophila Nuclear Receptor E75 Contains Heme and Is Gas Responsive
Reinking, J., Lam, M. M. S., Pardee, K., Sampson, H. M., Liu, S., Yang, P., Williams, S. P., White, W. L., Lajoie, G., Edwards, A. M., et al. (2005) · Cell · doi:10.1016/j.cell.2005.07.005 · Cited by 260 · see citing works
Mitochondrial Transcription Factor A Induction by Redox Activation of Nuclear Respiratory Factor 1
Piantadosi, C. A., & Suliman, H. B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508805200 · Cited by 254 · see citing works
Self-citationMitochondrial H2O2 Regulates the Angiogenic Phenotype via PTEN Oxidation
Connor, K. M., Subbaram, S., Regan, K. J., Nelson, K. K., Mazurkiewicz, J. E., Bartholomew, P. J., Aplin, A. E., Tai, Y.-T., Aguirre-Ghiso, J., Flores, S. C., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410690200 · Cited by 251 · see citing works
Taillé, C., El-Benna, J., Lanone, S., Boczkowski, J., & Motterlini, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503512200 · Cited by 246 · see citing works
Vascular Smooth Muscle Cell Heme Oxygenases Generate Guanylyl Cyclase–Stimulatory Carbon Monoxide
Christodoulides, N., Durante, W., Kroll, M. H., & Schafer, A. I. (1995) · Circulation · doi:10.1161/01.cir.91.9.2306 · Cited by 244 · see citing works
Apoptosis and Delayed Neuronal Damage after Carbon Monoxide Poisoning in the Rat
Piantadosi, C. A., Zhang, J., Levin, E. D., Folz, R. J., & Schmechel, D. E. (1997) · Experimental Neurology · doi:10.1006/exnr.1997.6584 · Cited by 243 · see citing works
Self-citationChin, B. Y., Jiang, G., Wegiel, B., Wang, H. J., MacDonald, T. Y., Zhang, X., Gallo, D. J., Cszimadia, E., Bach, F. H., Lee, P. J., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609611104 · Cited by 228 · see citing works
Liu, Y., Christou, H. A., Morita, T., Laughner, E., Semenza, G. L., & Kourembanas, S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.24.15257 · Cited by 220 · see citing works
Carbon Monoxide Protects against Liver Failure through Nitric Oxide–induced Heme Oxygenase 1
Zuckerbraun, B. S., Billiar, T. R., Otterbein, S. L., Kim, P. K. M., Liu, F., Choi, A. M. K., Bach, F. H., & Otterbein, L. E. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20031003 · Cited by 220 · see citing works
Heme Is a Carbon Monoxide Receptor for Large-Conductance Ca 2+ -Activated K + Channels
Jaggar, J. H., Li, A., Parfenova, H., Liu, J., Umstot, E. S., Dopico, A. M., & Leffler, C. W. (2005) · Circulation Research · doi:10.1161/01.res.0000186180.47148.7b · Cited by 218 · see citing works
Biological Chemistry of Carbon Monoxide
Piantadosi, C. A. (2002) · Antioxidants and Redox Signaling · doi:10.1089/152308602753666316 · Cited by 201 · see citing works
Self-citationAkamatsu, Y., Haga, M., Tyagi, S., Yamashita, K., Graça-Souza, A. V., Öllinger, R., Czismadia, E., May, G. A., Ifedigbo, E., Otterbein, L. E., et al. (2004) · The FASEB Journal · doi:10.1096/fj.03-0921fje · Cited by 201 · see citing works
Heme oxygenase activity as measured by carbon monoxide production
Vreman, H. J., & Stevenson, D. K. (1988) · Analytical Biochemistry · doi:10.1016/0003-2697(88)90006-1 · Cited by 200 · see citing works
Zhang, X., Shan, P., Alam, J., Fu, X.-Y., & Lee, P. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m408092200 · Cited by 198 · see citing works
Fang, J. Q., Akaike, T., & Maeda, H. (2004) · APOPTOSIS · doi:10.1023/b:appt.0000012119.83734.4e · Cited by 192 · see citing works
Adaptive responses and apoptosis in endothelial cells exposed to carbon monoxide
Thom, S. R., Fisher, D., Xu, Y., Notarfrancesco, K., & Ischiropoulos, H. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.3.1305 · Cited by 192 · see citing works
Estabrook, R. W., Cooper, D. Y., & Rosenthal, O. (1963) · PubMed · Cited by 184 · see citing works
Vallone, B., Nienhaus, K., Matthes, A., Brunori, M., & Nienhaus, G. U. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407633101 · Cited by 184 · see citing works
Carbon monoxide inhibits apoptosis in vascular smooth muscle cells
Liu, X. (2002) · Cardiovascular Research · doi:10.1016/s0008-6363(02)00410-8 · Cited by 182 · see citing works
Fago, A., Hundahl, C. A., Dewilde, S., Gilany, K., Moens, L. J., & Weber, R. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407126200 · Cited by 181 · see citing works
CO–metal interaction: vital signaling from a lethal gas
Boczkowski, J., Poderoso, J. J., & Motterlini, R. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.09.001 · Cited by 181 · see citing works
Activation of soluble guanylate cyclase by carbon monoxide and inhibition by superoxide anion
Brüne, B., SCHMIDT, K., & Ullrich, V. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19276.x · Cited by 181 · see citing works
Zhang, H. J., Zhao, W., Venkataraman, S., Robbins, M. E. C., Buettner, G. R., Kregel, K. C., & Oberley, L. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109801200 · Cited by 179 · see citing works
Mitochondrial Biogenesis Restores Oxidative Metabolism during Staphylococcus aureus Sepsis
Haden, D. W., Suliman, H. B., Carraway, M. S., Welty‐Wolf, K. E., Ali, A. S., Shitara, H., Yonekawa, H., & Piantadosi, C. A. (2007) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200701-161oc · Cited by 177 · see citing works
Self-citationFunction of cytochrome P-450 of microsomes.
Omura, T., Sato, R., COOPER, D. Y., Rosenthal, O., & Estabrook, R. W. (1965) · PubMed · Cited by 175 · see citing works
Vascular Endothelial Cells Generate Peroxynitrite in Response to Carbon Monoxide Exposure
Thom, S. R., Xu, Y., & Ischiropoulos, H. (1997) · Chemical Research in Toxicology · doi:10.1021/tx970041h · Cited by 173 · see citing works
Acquired resistance to acute oxidative stress. Possible role of heme oxygenase and ferritin.
Vogt, B. A., Alam, J., Croatt, A. J., Vercellotti, G. M., & Nath, K. A. (1995) · PubMed · Cited by 168 · see citing works
Wikström, M. K. F., Harmon, H. J., Ingledew, W. J., & Chance, B. (1976) · FEBS Letters · doi:10.1016/0014-5793(76)80127-5 · Cited by 164 · see citing works
Mechanisms of carbon monoxide toxicity
Coburn, R. F. (1979) · Preventive Medicine · doi:10.1016/0091-7435(79)90008-2 · Cited by 156 · see citing works
Peyton, K. J., Reyna, S. V., Chapman, G. B., Ensenat, D., Liu, X., Wang, H., Schafer, A. I., & Durante, W. (2002) · Blood · doi:10.1182/blood.v99.12.4443 · Cited by 156 · see citing works
Fujimoto, H., Ohno, M., Ayabe, S., Kobayashi, H., Ishizaka, N., Kimura, H., Yoshida, K.-I., & Nagai, R. (2004) · Arteriosclerosis, Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000142364.85911.0e · Cited by 153 · see citing works
Heme Inhibits Human Neutrophil Apoptosis: Involvement of Phosphoinositide 3-Kinase, MAPK, and NF-κB
Arruda, M. A., Rossi, A. G., de Freitas, M. S., Barja‐Fidalgo, C., & Graça-Souza, A. V. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.3.2023 · Cited by 147 · see citing works
Carbon Monoxide: Innovative Anti-inflammatory Properties of an Age-Old Gas Molecule
Otterbein, L. E. (2002) · Antioxidants and Redox Signaling · doi:10.1089/152308602753666361 · Cited by 147 · see citing works
In vivo binding of carbon monoxide to cytochrome c oxidase in rat brain
Brown, S. D., & Piantadosi, C. A. (1990) · Journal of Applied Physiology · doi:10.1152/jappl.1990.68.2.604 · Cited by 146 · see citing works
Self-citationThe Heme Oxygenase System: Update 2005
Maines, M. D. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1761 · Cited by 146 · see citing works
A kinetic description of ligand binding to sperm whale myoglobin.
Gibson, Q. H., Olson, J. S., McKinnie, R. E., & Rohlfs, R. J. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67514-3 · Cited by 144 · see citing works
Carbon monoxide attenuates aeroallergen-induced inflammation in mice
Chapman, J. T., Otterbein, L. E., Elias, J. A., & Choi, A. M. K. (2001) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2001.281.1.l209 · Cited by 144 · see citing works
Liu, X., Chapman, G. B., Wang, H., & Durante, W. (2002) · Circulation · doi:10.1161/hc0102.101369 · Cited by 142 · see citing works
Endoplasmic Reticulum Stress Stimulates Heme Oxygenase-1 Gene Expression in Vascular Smooth Muscle
Liu, X., Peyton, K. J., Ensenat, D., Wang, H., Schafer, A. I., Alam, J., & Durante, W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410413200 · Cited by 139 · see citing works
Ramos, K. S., Lin, H., & McGrath, J. J. (1989) · Biochemical Pharmacology · doi:10.1016/0006-2952(89)90347-x · Cited by 138 · see citing works
Ricchetti, G., Williams, L. M., & Foxwell, B. M. J. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0104046 · Cited by 134 · see citing works
Inhibition of cellular respiration by endogenously produced carbon monoxide
D’Amico, G., Lam, F., Hagen, T., & Moncada, S. (2006) · Journal of Cell Science · doi:10.1242/jcs.02914 · Cited by 132 · see citing works
Carbon Monoxide Signaling in Promoting Angiogenesis in Human Microvessel Endothelial Cells
Volti, G. L., Sacerdoti, D., Sangras, B., Vanella, A., Mezentsev, A., Scapagnini, G., Falck, J. R., & Abraham, N. G. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.704 · Cited by 124 · see citing works
The Heme Environment of Mouse Neuroglobin
Couture, M., Burmester, T., Hankeln, T., & Rousseau, D. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103907200 · Cited by 123 · see citing works
Calabrese, V., Stella, A. M. G., Butterfield, D. A., & Scapagnini, G. (2004) · Antioxidants and Redox Signaling · doi:10.1089/ars.2004.6.895 · Cited by 117 · see citing works
Chen, K., Thomas, S. R., Albano, A., Murphy, M. P., & Keaney, J. F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404859200 · Cited by 116 · see citing works
Kim, H. P., Wang, X. B., Nakao, A., Kim, S. I., Murase, N., Choi, M. E., Ryter, S. W., & Choi, A. M. K. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501345102 · Cited by 114 · see citing works
Carbon Monoxide Suppresses Bleomycin-Induced Lung Fibrosis
Zhou, Z., Song, R., Fattman, C. L., Greenhill, S. R., Alber, S. M., Oury, T. D., Choi, A. M. K., & Morse, D. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62229-8 · Cited by 110 · see citing works
Li, M., Jang, J.-H., Na, H., Cha, Y., & Surh, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701916200 · Cited by 109 · see citing works
Roberts, G. P., Youn, H., & Kerby, R. L. (2004) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.68.3.453-473.2004 · Cited by 106 · see citing works
Vreman, H. J., Wong, R. J., Sanesi, C. A., Dennery, P. A., & Stevenson, D. K. (1998) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-76-12-1057 · Cited by 103 · see citing works
Stopped-Flow Analysis of CO and NO Binding to Inducible Nitric Oxide Synthase
Abu‐Soud, H. M., Wu, C., Ghosh, D. K., & Stuehr, D. J. (1998) · Biochemistry · doi:10.1021/bi972398q · Cited by 103 · see citing works
L-arginine and calmodulin regulation of the heme iron reactivity in neuronal nitric oxide synthase.
Matsuoka, A., Stuehr, D. J., Olson, J. S., Clark, P., & Ikeda‐Saito, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31996-8 · Cited by 99 · see citing works
CooA, a paradigm for gas sensing regulatory proteins
ROBERTS, G., Kerby, R. L., Youn, H., & CONRAD, M. (2004) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2004.10.032 · Cited by 99 · see citing works
CARBON MONOXIDE BONDING IN HEMEPROTEINS *
Caughey, W. S. (1970) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1970.tb49781.x · Cited by 99 · see citing works
Measurement of Endogenous Carbon Monoxide Formation in Biological Systems
Marks, G. S., Vreman, H. J., McLaughlin, B. E., Brien, J. F., & Nakatsu, K. (2002) · Antioxidants and Redox Signaling · doi:10.1089/152308602753666325 · Cited by 98 · see citing works
Ligand Selectivity of Soluble Guanylyl Cyclase
Martin, E., Berka, V., Bogatenkova, E., Murad, F., & Tsai, A.-L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601078200 · Cited by 97 · see citing works
The formation of carbon monoxide during peroxidation of microsomal lipids
Wolff, D. G., & Bidlack, W. R. (1976) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(76)90199-6 · Cited by 96 · see citing works
Lutter, R., van Schaik, M. L., van Zwieten, R., Wever, R., Roos, D., & Hamers, M. N. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89544-8 · Cited by 94 · see citing works
Carbon monoxide mediates heme oxygenase 1 induction via Nrf2 activation in hepatoma cells
Lee, B.-S., Heo, J., Kim, Y., Shim, S. M., Pae, H., Kim, Y., & Chung, H. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.03.058 · Cited by 89 · see citing works
Myoglobin O2 tension determined from measurement of carboxymyoglobin in skeletal muscle
Coburn, R. F., & Mayers, L. (1971) · American Journal of Physiology-Legacy Content · doi:10.1152/ajplegacy.1971.220.1.66 · Cited by 87 · see citing works
Recent advances in heme-protein sensors
Chan, M. K. (2001) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00193-9 · Cited by 81 · see citing works
Carbon monoxide, oxidative stress, and mitochondrial permeability pore transition
Piantadosi, C. A., Carraway, M. S., & Suliman, H. B. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.11.020 · Cited by 80 · see citing works
Self-citationVreman, H. J., Wong, R. J., Sanesi, C. A., et al. (1998) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y98-126 · Cited by 79 · see citing works
Nelson, K. K., Subbaram, S., Connor, K. M., Dasgupta, J., Ha, X.-F., Meng, T., Tonks, N. K., & Melendez, J. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601820200 · Cited by 78 · see citing works
Brüne, B., Mohr, S., & Meßmer, U. K. (1995) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/bfb0048263 · Cited by 76 · see citing works
Andrew, C. R., Green, E. L., Lawson, D. M., & Eady, R. R. (2001) · Biochemistry · doi:10.1021/bi0023652 · Cited by 75 · see citing works
Carbon Monoxide Promotes Fas/CD95-induced Apoptosis in Jurkat Cells
Song, R., Zhou, Z., Kim, P. K. M., Shapiro, R. A., Liu, F., Ferran, C. J., Choi, A. M. K., & Otterbein, L. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406105200 · Cited by 72 · see citing works
NO Synthase Isozymes Have Distinct Substrate Binding Sites
Fan, B., Wang, J., Stuehr, D. J., & Rousseau, D. L. (1997) · Biochemistry · doi:10.1021/bi9715369 · Cited by 72 · see citing works
Nitric oxide priming protects nitric oxide-mediated apoptosis via HEME OXYGENASE-1 induction
Choi, B., Pae, H., & Chung, H. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00064-9 · Cited by 71 · see citing works
CARBON MONOXIDE ACTUATES O2-LIMITED HEME DEGRADATION IN THE RAT BRAIN
Cronje, F. J., Carraway, M. S., Freiberger, J. J., Suliman, H. B., & Piantadosi, C. A. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.08.022 · Cited by 71 · see citing works
Self-citationWijayanti, N., Huber, S., Samoylenko, A., Kietzmann, T., & Immenschuh, S. (2004) · Antioxidants and Redox Signaling · doi:10.1089/ars.2004.6.802 · Cited by 71 · see citing works
Role of endothelial carbon monoxide in attenuated vasoreactivity following chronic hypoxia
Caudill, T. K., Resta, T. C., Kanagy, N. L., & Walker, B. R. (1998) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1998.275.4.r1025 · Cited by 69 · see citing works
Production of Hydroxyl Radical in the Hippocampus After CO Hypoxia or Hypoxic Hypoxia in the Rat
Piantadosi, C. A., Zhang, J., & It, D. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00423-6 · Cited by 68 · see citing works
Self-citationSawai, H., Makino, M., Mizutani, Y., Ohta, T., Sugimoto, H., Uno, T., Kawada, N., Yoshizato, K., Kitagawa, T., & Shiro, Y. (2005) · Biochemistry · doi:10.1021/bi050997o · Cited by 68 · see citing works
REACTIONS OF OXYGEN WITH HEMOGLOBIN, CYTOCHROME C OXIDASE AND OTHER HEMEPROTEINS*
Caughey, W. S., Barlow, C., Maxwell, J. C., Volpe, J. A., & Wallace, W. J. (1975) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1975.tb41517.x · Cited by 62 · see citing works
Tron, K., Samoylenko, A., Musikowski, G., Kobe, F., Immenschuh, S., Schaper, F., Ramadori, G. P., & Kietzmann, T. (2006) · Journal of Hepatology · doi:10.1016/j.jhep.2005.12.019 · Cited by 50 · see citing works
Vreman, H. J., Wong, R. J., Stevenson, D. K., Smialek, J. E., Fowler, D. R., Li, L., Vigorito, R. D., & Zielke, H. R. (2006) · Journal of Forensic Sciences · doi:10.1111/j.1556-4029.2006.00212.x · Cited by 47 · see citing works
Peroxynitrite-mediated inactivation of heme oxygenases
Kinobe, R. T., Ji, Y., & Nakatsu, K. (2004) · BMC Pharmacology · doi:10.1186/1471-2210-4-26 · Cited by 46 · see citing works
Oxygenation of carbon monoxide by bovine heart cytochrome c oxidase
Young, L. J., & Caughey, W. S. (1986) · Biochemistry · doi:10.1021/bi00349a022 · Cited by 41 · see citing works
Human Biliverdin Reductase, a Previously Unknown Activator of Protein Kinase C βII
Maines, M. D., Miralem, T., Lerner‐Marmarosh, N., Shen, J. Y., & Gibbs, P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m513427200 · Cited by 41 · see citing works
STEVENSON, T. H., Gutiérrez, A., ALDERTON, W. K., Lian, L., & Scrutton, N. S. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3580201 · Cited by 41 · see citing works
Pulmonary Vascular Stress from Carbon Monoxide
Thom, S. R., Ohnishi, S. T., Fisher, D., Xu, Y., & Ischiropoulos, H. (1999) · Toxicology and Applied Pharmacology · doi:10.1006/taap.1998.8553 · Cited by 40 · see citing works
Carbon monoxide promotes hypoxic pulmonary vascular remodeling
Carraway, M. S., Ghio, A. J., Suliman, H. B., Carter, J. D., Whorton, A. R., & Piantadosi, C. A. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00211.2001 · Cited by 40 · see citing works
Self-citationMechanism of oxidative stress from low levels of carbon monoxide.
Thom, & Ischiropoulos, H. (1997) · PubMed · Cited by 38 · see citing works
Carbon monoxide-cytochrome interactions in the brain of the fluorocarbon-perfused rat
Piantadosi, C. A., Sylvia, A. L., Saltzman, H. A., & Jöbsis-VanderVliet, F. F. (1985) · Journal of Applied Physiology · doi:10.1152/jappl.1985.58.2.665 · Cited by 38 · see citing works
Self-citationHalogenated methanes: metabolism and toxicity.
Ahmed, A. A. E., Kubic, V. L., Stevens, J. L., & Anders, M. W. (1980) · PubMed · Cited by 35 · see citing works
Arias‐Díaz, J. (1995) · Archives of Surgery · doi:10.1001/archsurg.1995.01430120041006 · Cited by 32 · see citing works
Differences in brain cytochrome responses to carbon monoxide and cyanide in vivo
Piantadosi, C. A., Sylvia, A. L., & Jöbsis-VanderVliet, F. F. (1987) · Journal of Applied Physiology · doi:10.1152/jappl.1987.62.3.1277 · Cited by 31 · see citing works
Self-citationEARLY STUDIES OF CO PRODUCTION
Sjöstrand, T. (1970) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1970.tb49767.x · Cited by 25 · see citing works
Light Pulse‐Induced Heme and Iron‐Associated Transcripts in Mouse Brain: A Microarray Analysis
Ben‐Shlomo, R., Akhtar, R. A., Collins, B. H., Judah, D. J., Davies, R., & Kyriacou, C. P. (2005) · Chronobiology International · doi:10.1081/cbi-200062353 · Cited by 25 · see citing works
Fenn, W. O. (1970) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1970.tb49772.x · Cited by 24 · see citing works
Correlation of carbon monoxide and bilirubin production by tissue homogenates
Vreman, H. J., Stevenson, D. K., Henton, D. H., & Rosenthal, P. J. (1988) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/0378-4347(88)80134-8 · Cited by 23 · see citing works
Sato, H., Nomura, S., Sagami, I., Ito, O., Daff, S. N., & Shimizu, T. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00699-1 · Cited by 21 · see citing works
Carbon Monoxide Reversibly Alters Iron Homeostasis and Respiratory Epithelial Cell Function
Ghio, A. J., Stonehuerner, J. G., Dailey, L. A., Richards, J. H., Madden, M. D., Deng, Z., Nguyen, N.-B., Callaghan, K. D., Yang, F., & Piantadosi, C. A. (2008) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2007-0179oc · Cited by 19 · see citing works
Self-citationNisimoto, Y., Otsuka-Murakami, H., & Iwata, S. (1994) · Biochemical Journal · doi:10.1042/bj2970585 · Cited by 16 · see citing works
Żemojtel, T., Scheele, J. S., Pavel Martasek, E., Masters, B. S. S., Sharma, V. S., & Magde, D. (2003) · Biochemistry · doi:10.1021/bi026886w · Cited by 15 · see citing works
Roy, A., Baby, S. M., Wilson, D. F., & Lahiri, S. (2007) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00882.2006 · Cited by 9 · see citing works
Bengea, S., Araki, Y., Ito, O., Igarashi, J., Sagami, I., & Shimizu, T. (2004) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2004.04.009 · Cited by 7 · see citing works
Reactivity of photoreduced cytochrome aa3 complexes with molecular oxygen
Nicholls, P. J., & Chanady, G. A. (1981) · Biochemical Journal · doi:10.1042/bj1940713 · Cited by 6 · see citing works
Kinetics of ligand binding of cytochrome oxidases: a comparative study
Basu, A., Yin, M. R., Waterland, R. A., & Chance, B. (1994) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(94)90235-6 · Cited by 4 · see citing works
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The therapeutic potential of carbon monoxide
Motterlini, R., & Otterbein, L. E. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3228 · Cited by 1,643 · see citing works
Mechanisms of Cell Protection by Heme Oxygenase-1
Gozzelino, R., Jeney, V., & Soares, M. P. (2010) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.010909.105600 · Cited by 1,241 · see citing works
Calabrese, V., Cornelius, C., Dinkova‐Kostova, A. T., Calabrese, E. J., & Mattson, M. P. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3074 · Cited by 803 · 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
Developing drug molecules for therapy with carbon monoxide
Romão, C. C., Blättler, W. A., Seixas, J. D., & Bernardes, G. J. L. (2012) · Chemical Society Reviews · doi:10.1039/c2cs15317c · Cited by 524 · see citing works
Li, H., Kim, H., Xu, F., Han, J., Yao, Q., Wang, J., Pu, K., Peng, X., & Yoon, J. (2022) · Chemical Society Reviews · doi:10.1039/d1cs00307k · Cited by 512 · see citing works
Kohli, S. K., Khanna, K., Bhardwaj, R., Allah, E. F. A., Ahmad, P., & Corpas, F. J. (2019) · Antioxidants · doi:10.3390/antiox8120641 · Cited by 449 · see citing works
Survival in Critical Illness Is Associated with Early Activation of Mitochondrial Biogenesis
Carré, J. E., Orban, J., Re, L., Felsmann, K., Iffert, W., Bauer, M. W., Suliman, H. B., Piantadosi, C. A., Mayhew, T. M., Breen, P., et al. (2010) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201003-0326oc · Cited by 437 · see citing works
Self-citationCellular stress responses, hormetic phytochemicals and vitagenes in aging and longevity
Calabrese, V., Cornelius, C., Dinkova‐Kostova, A. T., Iavicoli, I., Paola, R. D., Koverech, A., Cuzzocrea, S., Rizzarelli, E., & Calabrese, E. J. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.11.002 · Cited by 420 · see citing works
Carbon monoxide – physiology, detection and controlled release
Heinemann, S. H., Hoshi, T., Westerhausen, M., & Schiller, A. (2014) · Chemical Communications · doi:10.1039/c3cc49196j · Cited by 389 · see citing works
Mitochondrial Quality Control as a Therapeutic Target
Suliman, H. B., & Piantadosi, C. A. (2015) · Pharmacological Reviews · doi:10.1124/pr.115.011502 · Cited by 265 · see citing works
Self-citationHeme oxygenase-1: from biology to therapeutic potential
Soares, M. P., & Bach, F. H. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.12.004 · Cited by 257 · see citing works
Xie, Y., Xu, S. B., Han, B., Wu, M., Yuan, X., Han, Y., Gu, Q., Xu, D., Yang, Q., & Shen, W. (2011) · The Plant Journal · doi:10.1111/j.1365-313x.2011.04488.x · Cited by 257 · see citing works
Chemical sensing of neurotransmitters
Pradhan, T., Jung, H. S., Jang, J. H., Kim, T. W., Kang, C., & Kim, J. S. (2014) · Chemical Society Reviews · doi:10.1039/c3cs60477b · Cited by 254 · see citing works
Wang, K., Li, Y., Wang, X., Zhang, Z., Cao, L., Fan, X., Wan, B., Liu, F., Zhang, X., He, Z., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38601-7 · Cited by 254 · see citing works
Novel lead structures and activation mechanisms for CO ‐releasing molecules ( CORMs )
Schatzschneider, U. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12688 · Cited by 251 · see citing works
Human myeloperoxidase in innate and acquired immunity
Arnhold, J., & Flemmig, J. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.04.008 · Cited by 251 · see citing works
CORM-3 Reactivity toward Proteins: The Crystal Structure of a Ru(II) Dicarbonyl−Lysozyme Complex
Santos‐Silva, T., Mukhopadhyay, A., Seixas, J. D., Bernardes, G. J. L., Romão, C. C., & Romão, M. J. (2011) · Journal of the American Chemical Society · doi:10.1021/ja108820s · Cited by 216 · see citing works
Smart Hydrogels – Synthetic Stimuli-Responsive Antitumor Drug Release Systems
Kasiński, A., Zielińska–Pisklak, M., Olędzka, E., & Sobczak, M. (2020) · International Journal of Nanomedicine · doi:10.2147/ijn.s248987 · Cited by 212 · see citing works
Liu, C., Yin, P., Chen, R., Meng, X., Wang, L., Niu, Y., Lin, Z., Liu, Y., Liu, J., Qi, J., et al. (2018) · The Lancet Planetary Health · doi:10.1016/s2542-5196(17)30181-x · Cited by 206 · see citing works
Iacono, L. L., Boczkowski, J., Zini, R., Salouage, I., Berdeaux, A., Motterlini, R., & Morin, D. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.02.033 · Cited by 160 · see citing works
du Plessis, S. S., Hagenaar, K., & Lampiao, F. (2010) · Andrologia · doi:10.1111/j.1439-0272.2009.00964.x · Cited by 155 · see citing works
Emergency Hospital Admissions for Cardiovascular Diseases and Ambient Levels of Carbon Monoxide
Bell, M. L., Peng, R. D., Dominici, F., & Samet, J. M. (2009) · Circulation · doi:10.1161/circulationaha.109.851113 · Cited by 147 · see citing works
Carbon monoxide: Mechanisms of action and potential clinical implications
Rochette, L., Cottin, Y., Zeller, M., & Vergely, C. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.09.007 · Cited by 145 · see citing works
Ashrafi, I., Kohram, H., & Farrokhi‐Ardabili, F. (2013) · Animal Reproduction Science · doi:10.1016/j.anireprosci.2013.03.016 · Cited by 141 · see citing works
Mitochondrial quality surveillance as a therapeutic target in myocardial infarction
Zhu, H., Toan, S., Mui, D., & Zhou, H. (2020) · Acta Physiologica · doi:10.1111/apha.13590 · Cited by 142 · see citing works
Innamorato, N. G., Jaźwa, A., Rojo, A. I., García, C., Fernández‐Ruíz, J., Grochot‐Przeczek, A., Stachurska, A., Józkowicz, A., Dulak, J., & Cuadrado, A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011838 · Cited by 138 · see citing works
Calabrese, V., Cornelius, C., Stella, A. M. G., & Calabrese, E. J. (2010) · Neurochemical Research · doi:10.1007/s11064-010-0307-z · Cited by 134 · see citing works
Barone, E., Di Domenico, F., Mancuso, C., & Butterfield, D. A. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.09.018 · Cited by 127 · see citing works
Surh, Y., Kundu, J. K., Li, M., Na, H., & Cha, Y. (2009) · Archives of Pharmacal Research · doi:10.1007/s12272-009-1807-8 · Cited by 121 · see citing works
Mitochondria: Redox Metabolism and Dysfunction
Kang, J., & Pervaiz, S. (2012) · Biochemistry Research International · doi:10.1155/2012/896751 · Cited by 121 · see citing works
Heme Cytotoxicity and the Pathogenesis of Immune-Mediated Inflammatory Diseases
Larsen, R., Gouveia, Z. L., Soares, M. P., & Gozzelino, R. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00077 · Cited by 112 · see citing works
Photoactive metal carbonyl complexes as potential agents for targeted CO delivery
Gonzales, M. A., & Mascharak, P. K. (2013) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2013.10.015 · Cited by 110 · see citing works
Dördelmann, G., Meinhardt, T., Sowik, T., Krueger, A., & Schatzschneider, U. (2012) · Chemical Communications · doi:10.1039/c2cc36491c · Cited by 105 · see citing works
Chen, Z., Liu, N., Tang, H., Gao, X., Zhang, Y., Kan, H., Deng, F., Zhao, B., Zeng, X., Sun, Y., et al. (2022) · Indoor Air · doi:10.1111/ina.13170 · Cited by 103 · see citing works
Dunn, L., Kong, S. M. Y., Tumanov, S., Chen, W., Cantley, J., Ayer, A., Maghzal, G. J., Midwinter, R. G., Chan, K. H., Ng, M., et al. (2020) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.120.315393 · Cited by 99 · see citing works
Immunoregulatory effects of HO-1: how does it work?
Soares, M. P., Marguti, I., Cunha, A., & Larsen, R. (2009) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2009.05.008 · Cited by 97 · see citing works
The Heme Oxygenase/Biliverdin Reductase Pathway in Drug Research and Development
Mancuso, C., & Barone, E. (2009) · Current Drug Metabolism · doi:10.2174/138920009789375405 · Cited by 99 · see citing works
Olsson, M. G., Allhorn, M., Bülow, L., Hansson, S. R., Ley, D., Olsson, M. L., Schmidtchen, A., & Åkerström, B. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4282 · Cited by 96 · see citing works
Endogenous carbon monoxide production in disease
Oesterling, E. (2010) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2010.07.011 · Cited by 96 · see citing works
Myeloperoxidase Inhibitors as Potential Drugs
Pašti, T. D. L., Leskovac, A. R., & Vasić, V. (2015) · Current Drug Metabolism · doi:10.2174/138920021603150812120640 · Cited by 95 · see citing works
Tang, S. N., Tong, Q., Xia, D., Xu, M., Xu, M., Zhu, A., Shen, W., & Lee, H. K. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b00255 · Cited by 93 · see citing works
Zhao, Y., Hu, J., Tan, Z., Liu, T., Zeng, W., Li, X., Huang, C., Wang, S., Huang, Z., & Ma, W. (2019) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2019.02.333 · Cited by 92 · see citing works
Carbon monoxide, skeletal muscle oxidative stress, and mitochondrial biogenesis in humans
Rhodes, M. A., Carraway, M. S., Piantadosi, C. A., Reynolds, C. M., Cherry, A. D., Wester, T. E., Natoli, M. J., Massey, E. W., Moon, R. E., & Suliman, H. B. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00164.2009 · Cited by 90 · see citing works
Self-citationWaterpipe (shisha, hookah) smoking, oxidative stress and hidden disease potential
Badran, M., & Laher, I. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101455 · Cited by 84 · see citing works
Belcher, J. D., Vineyard, J. V., Bruzzone, C. M., Chen, C., Beckman, J. D., Nguyen, J., Steer, C. J., & Vercellotti, G. M. (2010) · Journal of Molecular Medicine · doi:10.1007/s00109-010-0613-6 · Cited by 84 · see citing works
Bose, J., Xie, Y., Shen, W., & Shabala, S. N. (2013) · Journal of Experimental Botany · doi:10.1093/jxb/ers343 · Cited by 84 · see citing works
Bischof, C., Joshi, T., Dimri, A., Spiccia, L., & Schatzschneider, U. (2013) · Inorganic Chemistry · doi:10.1021/ic400746n · Cited by 83 · see citing works
Enhancement of tolerance of Indian mustard (Brassica juncea) to mercury by carbon monoxide
Meng, D. K., Chen, J., & Yang, Z. M. (2010) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2010.12.062 · Cited by 81 · see citing works
Chakraborty, I., Carrington, S. J., Hauser, J. L., Oliver, S. R. J., & Mascharak, P. K. (2015) · Chemistry of Materials · doi:10.1021/acs.chemmater.5b03859 · Cited by 78 · see citing works
Zheng, G., Zhan, Y., Wang, H., Luo, Z., Zheng, F., Zhou, Y., Wu, Y., Wang, S., Wu, Y., Xiang, G., et al. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2018.12.059 · Cited by 76 · see citing works
Carbon monoxide: A vital signalling molecule and potent toxin in the myocardium
Peers, C., & Steele, D. S. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.05.013 · Cited by 74 · see citing works
Mitochondrial complex III: An essential component of universal oxygen sensing machinery?
Chandel, N. S. (2010) · Respiratory Physiology & Neurobiology · doi:10.1016/j.resp.2010.08.004 · Cited by 75 · see citing works
Emerging Roles of Carbonyl Sulfide in Chemical Biology: Sulfide Transporter or Gasotransmitter?
Steiger, A. K., Zhao, Y., & Pluth, M. D. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7119 · Cited by 74 · see citing works
Steiner, S., Czerwiński, J., Comte, P., Popovicheva, O., Kireeva, Е., Müller, L. L., Heeb, N. V., Mayer, A. C. R., Petri‐Fink, A., & Rothen‐Rutishauser, B. (2013) · Atmospheric Environment · doi:10.1016/j.atmosenv.2013.08.059 · Cited by 73 · see citing works
Towards Improved Therapeutic CORMs: Understanding the Reactivity of CORM-3 with Proteins
Santos‐Silva, T., Mukhopadhyay, A., Seixas, J. D., Bernardes, G. J. L., Romão, C. C., & Romão, M. J. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711796504583 · Cited by 73 · see citing works
Carbon monoxide promotes root hair development in tomato
Guo, K., KONG, W. W., & Yang, Z. M. (2009) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2009.01986.x · Cited by 73 · see citing works
Mitochondrial dysfunction and biogenesis: do ICU patients die from mitochondrial failure?
Kozlov, A. V., Bahrami, S., Calzia, E., Dungel, P., Gille, L., Kuznetsov, A. V., & Troppmair, J. (2011) · Annals of Intensive Care · doi:10.1186/2110-5820-1-41 · Cited by 73 · see citing works
Smoking and COVID-19: A Scoping Review
Haddad, C., Malhab, S. B., Sacre, H., & Salameh, P. (2021) · Tobacco Use Insights · doi:10.1177/1179173x21994612 · Cited by 72 · see citing works
Bauer, N., Yuan, Z., Yang, X., & Wang, B. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115642 · Cited by 71 · see citing works
Cyclo(His-Pro) exerts anti-inflammatory effects by modulating NF-κB and Nrf2 signalling
Minelli, A., Grottelli, S., Mierla, A. L., Pinnen, F., Cacciatore, I., & Bellezza, I. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.12.006 · Cited by 71 · see citing works
Yuan, Z., Cruz, L. K. D. L., Yang, X., & Wang, B. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000564 · Cited by 70 · see citing works
Nañagas, K., Penfound, S., & Kao, L. W. (2022) · Emergency Medicine Clinics of North America · doi:10.1016/j.emc.2022.01.005 · Cited by 72 · see citing works
Diverse mechanisms underlying the regulation of ion channels by carbon monoxide
Peers, C., Boyle, J. P., Scragg, J. L., Dallas, M. L., Al‐Owais, M. M., Hettiarachichi, N. T., Elíes, J., Johnson, E., Gamper, N. L., & Steele, D. S. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12760 · Cited by 69 · see citing works
Interaction between HY1 and H2O2 in auxin-induced lateral root formation in Arabidopsis
Ma, F., Wang, L., Li, J., Samma, M. K., Xie, Y., Wang, R., Wang, J., Zhang, J., & Shen, W. (2013) · Plant Molecular Biology · doi:10.1007/s11103-013-0168-3 · Cited by 68 · see citing works
The Carbon Monoxide Releasing Molecule CORM-2 Attenuates Pseudomonas aeruginosa Biofilm Formation
Murray, T. S., Okegbe, C., Gao, Y., Kazmierczak, B. I., Motterlini, R., Dietrich, L. E. P., & Bruscia, E. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035499 · Cited by 67 · see citing works
Lin, S., Wei, D., Sun, Y., Chen, K., Yang, L., Liu, B., Huang, Q., Paoliello, M. M. B., Li, H., & Wu, S. (2020) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2020.111035 · Cited by 62 · see citing works
Ye, W., Zheng, Q., Liu, Z. P., & Yang, Z. Y. (2011) · Plant and Cell Physiology · doi:10.1093/pcp/pcr102 · Cited by 61 · see citing works
Parallel evolution of Nitric Oxide signaling: Diversity of synthesis and memory pathways
Moroz, L. L. (2011) · Frontiers in bioscience · doi:10.2741/3837 · Cited by 59 · see citing works
CO metabolism, sensing, and signaling
Gullotta, F., di Masi, A., Coletta, M., & Ascenzi, P. (2011) · BioFactors · doi:10.1002/biof.192 · Cited by 60 · see citing works
Olas, B. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.08.005 · Cited by 60 · see citing works
Cheung, I. M. Y., McGhee, C. N. J., & Sherwin, T. (2013) · Clinical and Experimental Optometry · doi:10.1111/cxo.12025 · Cited by 57 · see citing works
Effects of serum bilirubin on atherosclerotic processes
Kang, S. J., Lee, C., & Kružliak, P. (2014) · Annals of Medicine · doi:10.3109/07853890.2014.895588 · Cited by 57 · see citing works
Pun, P. B. L., Lu, J., Kan, E. M., & Moochhala, S. (2009) · Mitochondrion · doi:10.1016/j.mito.2009.12.142 · Cited by 56 · see citing works
Zhang, S., Yu, Y., Xiao, C., Wang, X., & Tian, Y. (2013) · LWT · doi:10.1016/j.lwt.2013.04.001 · Cited by 56 · see citing works
Mizuguchi, S., Stephen, J., Bihari, R., Markovic, N., Suehiro, S., Capretta, A. A., Potter, R. F., & Cepinskas, G. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00305.2009 · Cited by 56 · see citing works
Yang, C., Jeong, S., Ku, S., Lee, K., & Park, M. H. (2018) · Journal of Controlled Release · doi:10.1016/j.jconrel.2018.04.025 · Cited by 53 · see citing works
Yang, B., Su, M.-M., Xue, Y., He, Z., Xu, C., & Zhu, H. (2018) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2018.08.138 · Cited by 52 · see citing works
Fujita, K., Yamafuji, M., Nakabeppu, Y., & Noda, M. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/324256 · Cited by 51 · see citing works
Pinto, M. N., & Mascharak, P. K. (2020) · Journal of Photochemistry and Photobiology C Photochemistry Reviews · doi:10.1016/j.jphotochemrev.2020.100341 · Cited by 51 · see citing works
Redox and catalase-like activities of four widely used carbon monoxide releasing molecules (CO-RMs)
Yuan, Z., Yang, X., & Wang, B. (2021) · Chemical Science · doi:10.1039/d1sc03832j · Cited by 49 · see citing works
The role of carbon monoxide signaling in the responses of plants to abiotic stresses
He, H., & He, L. (2014) · Nitric Oxide · doi:10.1016/j.niox.2014.08.011 · Cited by 49 · see citing works
Inhaled carbon monoxide reduces leukocytosis in a murine model of sickle cell disease
Beckman, J. D., Belcher, J. D., Vineyard, J. V., Chen, C., Nguyen, J., Nwaneri, M. O., O’Sullivan, M. G., Gulbahce, E. H., Hebbel, R. P., & Vercellotti, G. M. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00327.2009 · Cited by 49 · see citing works
Heme oxygenase-nitric oxide crosstalk-mediated iron homeostasis in plants under oxidative stress
Singh, N., & Bhatla, S. C. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.02.034 · Cited by 49 · see citing works
Lee, L., Kaizu, T., Toyokawa, H., Zhang, M., Ross, M., Stolz, D. B., Huang, C., Gandhi, C. R., Geller, D. A., & Murase, N. (2011) · Liver Transplantation · doi:10.1002/lt.22415 · Cited by 48 · see citing works
Carbon monoxide pollution aggravates ischemic heart failure through oxidative stress pathway
Reboul, C., Boissière, J., André, L., Meyer, G., Bideaux, P., Fouret, G., Feillet‐Coudray, C., Obert, P., Lacampagne, A., Thireau, J., et al. (2017) · Scientific Reports · doi:10.1038/srep39715 · Cited by 48 · see citing works
The Role of Cyclo(His-Pro) in Neurodegeneration
Grottelli, S., Ferrari, I., Pietrini, G., Peirce, M. J., Minelli, A., & Bellezza, I. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17081332 · Cited by 47 · see citing works
Kang, J. S., Han, M. H., Kim, G., Kim, C., Kim, B. G., Hwang, H. J., & Choi, Y. H. (2014) · Nutrients · doi:10.3390/nu6125667 · Cited by 46 · see citing works
Biological Stimuli-responsive Polymer Systems: Design, Construction and Controlled Self-assembly
Xu, M., Liu, R., & Yan, Q. (2017) · Chinese Journal of Polymer Science · doi:10.1007/s10118-018-2080-4 · Cited by 46 · see citing works
Neurobehavioral Consequences of Traffic-Related Air Pollution
Salvi, A., & Salim, S. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01232 · Cited by 46 · see citing works
Retracted: Cyclo(His‐Pro) up‐regulates heme oxygenase 1 via activation of Nrf2‐ARE signalling
Minelli, A., Conte, C., Grottelli, S., Bellezza, I., Emiliani, C., & Bolaños, J. P. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06376.x · Cited by 45 · see citing works
RetractedThe role of decorin in cardiovascular diseases: more than just a decoration
Vu, T. T., Marquez, J. C., Long, L. T., Nguyen, A. T. T., Kim, H. K., & Han, J. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1516285 · Cited by 44 · see citing works
Plasma biomarkers in carbon monoxide poisoning
Thom, S. R., Bhopale, V. M., Milovanova, T. M., Hardy, K. R., Logue, C. J., Lambert, D. S., Troxel, A. B., Ballard, K., & Eisinger, D. P. (2010) · Clinical Toxicology · doi:10.3109/15563650903468209 · Cited by 43 · see citing works
Rose, J. J., Bocian, K. A., Xu, Q., Wang, L., DeMartino, A. W., Chen, X., Corey, C. G., Guimarães, D. A., Azarov, I., Huang, X. N., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010593 · Cited by 43 · see citing works
Gram, M., Anderson, U. D., Johansson, M. E., Anneli, E.-H., Larsson, I., Jälmby, M., Hansson, S. R., & Åkerström, B. (2015) · PLoS ONE · doi:10.1371/journal.pone.0138111 · Cited by 42 · see citing works
ZmHO-1, a maize haem oxygenase-1 gene, plays a role in determining lateral root development
Han, B., Xu, S. B., Xie, Y., Huang, J., Wang, L., Zheng, Y., Zhang, C., Sun, Y., Shen, W., & Xie, G. (2011) · Plant Science · doi:10.1016/j.plantsci.2011.12.012 · Cited by 42 · see citing works
Cremers, N. A. J., Lundvig, D. M. S., van Dalen, S. C. M., Schelbergen, R. F. P., van Lent, P., Szarek, W. A., Regan, R. F., Carels, C. E. L., & Wagener, F. A. D. T. G. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151017974 · Cited by 41 · see citing works
Pinto, M. N., Chakraborty, I., Sandoval, C., & Mascharak, P. K. (2017) · Journal of Controlled Release · doi:10.1016/j.jconrel.2017.08.039 · Cited by 41 · see citing works
Müllebner, A., Dorighello, G. G., Kozlov, A. V., & Duvigneau, J. C. (2018) · Frontiers in Medicine · doi:10.3389/fmed.2017.00252 · Cited by 41 · see citing works
Mitochondrial Biogenesis: Regulation By Endogenous Gases During Inflammation and Organ Stress
Suliman, H. B., & Piantadosi, C. A. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666140306095717 · Cited by 40 · see citing works
Self-citation
- Authors
- Piantadosi, C. A.
- Affiliations
- Duke University (US)
- Corresponding author
- Piantadosi, Claude A.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2008-09
- Volume
- 45
- Issue
- 5
- Pages
- 562-569
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC2570053
- OpenAlex
- W2087826558
- Cited by
- 281
- References
- 145
- Citations by year
- 2026: 11 · 2025: 10 · 2024: 15 · 2023: 13 · 2022: 19 · 2021: 16 · 2020: 21 · 2019: 8 · 2018: 16 · 2017: 13 · 2016: 7 · 2015: 11 · 2014: 17 · 2013: 16 · 2012: 16
- FWCI
- 1.83
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL090679)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- carbon monoxide, reactive oxygen species, oxidative stress, heme proteins, heme oxygenase, pro-oxidant activity, redox signaling, stress-activated kinases, redox-sensitive transcription factors, antioxidant enzymes, co-toxicity
- MeSH terms
- Adaptation, Biological, Animals, Carbon Monoxide, Hemeproteins, Humans, Signal Transduction, Reactive Oxygen Species, Oxidative Stress
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