The DOI matches its Crossref record; 716 of the 716 references it cites were found in a registry or an index.
Heme Oxygenase-1/Carbon Monoxide: From Basic Science to Therapeutic Applications
Abstract
The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO). In recent years, endogenously produced CO has been shown to possess intriguing signaling properties affecting numerous critical cellular functions including but not limited to inflammation, cellular proliferation, and apoptotic cell death. The era of gaseous molecules in biomedical research and human diseases initiated with the discovery that the endothelial cell-derived relaxing factor was identical to the gaseous molecule nitric oxide (NO). The discovery that endogenously produced gaseous molecules such as NO and now CO can impart potent physiological and biological effector functions truly represented a paradigm shift and unraveled new avenues of intense investigations. This review covers the molecular and biochemical characterization of HOs, with a discussion on the mechanisms of signal transduction and gene regulation that mediate the induction of HO-1 by environmental stress. Furthermore, the current understanding of the functional significance of HO shall be discussed from the perspective of each of the metabolic by-products, with a special emphasis on CO. Finally, this presentation aspires to lay a foundation for potential future clinical applications of these systems.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
2 retracted
Items 201–400 of 716
Motohashi, H. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.15.2953 · Cited by 281
Absence of heme oxygenase‐1 exacerbates atherosclerotic lesion formation and vascular remodeling
Yet, S.-F., Layne, M. D., Liu, X., Chen, Y.-H., Ith, B., Sibinga, N. E. S., & Perrella, M. A. (2003) · The FASEB Journal · doi:10.1096/fj.03-0187fje · Cited by 280
Drummond, G. S., & Kappas, A. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.10.6466 · Cited by 279
Kohchi, T., Mukougawa, K., Frankenberg, N., Masuda, M., Yokota, A., & Lagarias, J. C. (2001) · The Plant Cell · doi:10.1105/tpc.13.2.425 · Cited by 278
Ma, K. (2000) · PubMed · Cited by 276
Kang, K. W., Lee, S. J., Park, J. W., & Kim, S. G. (2002) · Molecular Pharmacology · doi:10.1124/mol.62.5.1001 · Cited by 274
Siow, R. (1999) · Cardiovascular Research · doi:10.1016/s0008-6363(98)00278-8 · Cited by 272
UNSATURATED LIPIDE OXIDATION CATALYZED BY HEMATIN COMPOUNDS
Tappel, A. L. (1955) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65938-1 · Cited by 269
Li, N., Venkatesan, M. I., Miguel, A., Kaplan, R., Gujuluva, C., Alam, J., & Nel, A. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.6.3393 · Cited by 267
Self-citationENDOGENOUS CARBON MONOXIDE PRODUCTION IN MAN*
Coburn, R. F., Blakemore, W. S., & Forster, R. E. (1963) · Journal of Clinical Investigation · doi:10.1172/jci104802 · Cited by 264
Reversal of long-term potentiation by inhibitors of haem oxygenase
Stevens, C. F., & Wang, Y. (1993) · Nature · doi:10.1038/364147a0 · Cited by 262
Tenhunen, R., Ross, M. E., Marver, H. S., & Schmid, R. (1970) · Biochemistry · doi:10.1021/bi00804a016 · Cited by 262
Bach1 Functions as a Hypoxia-inducible Repressor for the Heme Oxygenase-1 Gene in Human Cells
Kitamuro, T., Takahashi, K., Ogawa, K., Udono-Fujimori, R., Takeda, K., Furuyama, K., Nakayama, M., Sun, J., Fujita, H., Hida, W., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209939200 · Cited by 262
Ewing, J. F., & Maines, M. D. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.12.5364 · Cited by 261
Maines, M. D., & Kappas, A. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.11.4293 · Cited by 261
Chen, C., Pung, D., Leong, V., Hebbar, V., Shen, G., Nair, S., Li, W., & Tony Kong, A.-N. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.07.021 · Cited by 260
Pileggi, A., Molano, R. D., Berney, T., Cattan, P., Vizzardelli, C., Oliver, R., Fraker, C., Ricordi, C., Pastori, R. L., Bach, F. H., et al. (2001) · Diabetes · doi:10.2337/diabetes.50.9.1983 · Cited by 260
Trakshel, G. M., Kutty, R. K., & Maines, M. D. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67358-2 · Cited by 259
Carbon monoxide-mediated brain lipid peroxidation in the rat
Thom, S. R. (1990) · Journal of Applied Physiology · doi:10.1152/jappl.1990.68.3.997 · Cited by 258
The clinical toxicology of carbon monoxide
Gorman, D., Drewry, A., Huang, Y. L., & Sames, C. (2003) · Toxicology · doi:10.1016/s0300-483x(03)00005-2 · Cited by 258
Induction of heme oxygenase-1 gene expression by lipopolysaccharide is mediated by AP-1 activation.
Camhi, S. L., Alam, J., Otterbein, L., Sylvester, S. L., & Choi, A. M. (1995) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.13.4.7546768 · Cited by 257
Self-citationTurkseven, S., Kruger, A., Mingone, C. J., Kaminski, P., Inaba, M., Rodella, L. F., Ikehara, S., Wolin, M. S., & Abraham, N. G. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00024.2005 · Cited by 256
Heme Oxygenase: Clinical Applications and Functions
Maines, M. D. (1992) · Medical Entomology and Zoology · Cited by 256
Expression of heme oxygenase-1 in atherosclerotic lesions.
Wang, L.-J., Lee, T., Lee, F.-Y., Pai, R., & Chau, L. (1998) · Europe PMC (PubMed Central) · Cited by 254
Mechanism of Sodium Arsenite-mediated Induction of Heme Oxygenase-1 in Hepatoma Cells
Elbirt, K. K., Whitmarsh, A. J., Davis, R. J., & Bonkovsky, H. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.15.8922 · Cited by 254
Schacter, B. A., Nelson, E. B., Marver, H. S., & Masters, B. S. S. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45183-1 · Cited by 253
Wilks, A., & Ortiz de Montellano, P. R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41536-0 · Cited by 253
Carbon monoxide induces vasodilation and nitric oxide release but suppresses endothelial NOS
Thorup, C., Jones, C. L., Gross, S. S., Moore, L. C., & Goligorsky, M. S. (1999) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.1999.277.6.f882 · Cited by 251
Salinas, M., Diaz, R., Abraham, N. G., Ruiz de Galarreta, C. M., & Cuadrado, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209164200 · Cited by 247
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 247
Taillé, C., El-Benna, J., Lanone, S., Boczkowski, J., & Motterlini, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503512200 · Cited by 246
The enzymic reduction and kinetics of oxidation of cytochrome b.245 of neutrophils
Cross, A. R., Higson, F. K., Jones, O. T. G., Harper, A. M., & Segal, A. W. (1982) · Biochemical Journal · doi:10.1042/bj2040479 · Cited by 246
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 245
Carbon Monoxide: An Endogenous Modulator of the Nitric Oxide–Cyclic GMP Signaling System
Ingi, T., Cheng, J., & Ronnett, G. V. (1996) · Neuron · doi:10.1016/s0896-6273(00)80103-8 · Cited by 244
Bilirubin From Heme Oxygenase-1 Attenuates Vascular Endothelial Activation and Dysfunction
Kawamura, K., Ishikawa, K., Wada, Y., Kimura, S., Matsumoto, H., Kohro, T., Itabe, H., Kodama, T., & Maruyama, Y. (2005) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000148405.18071.6a · Cited by 244
Heme oxygenase–1 deficiency: The first autopsy case
Kawashima, A., Oda, Y., Yachie, A., Koizumi, S., & Nakanishi, I. (2002) · Human Pathology · doi:10.1053/hupa.2002.30217 · Cited by 244
Heme Oxygenase-1: Redox Regulation of a Stress Protein in Lung and Cell Culture Models
Ryter, S. W., & Choi, A. M. K. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.80 · Cited by 243
Self-citationBilirubin: A Natural Inhibitor of Vascular Smooth Muscle Cell Proliferation
Öllinger, R., Bilban, M., Erat, A., Froio, A., McDaid, J., Tyagi, S., Csizmadia, E., Graça-Souza, A. V., Liloia, A., Soares, M. P., et al. (2005) · Circulation · doi:10.1161/circulationaha.104.528802 · Cited by 241
Heme regulates gene expression by triggering Crm1‐dependent nuclear export of Bach1
Suzuki, H., Tashiro, S., Hira, S., Sun, J., Yamazaki, C., Zenke, Y., Ikeda‐Saito, M., Yoshida, M., & Igarashi, K. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600248 · Cited by 240
Kapitulnik, J. (2004) · Molecular Pharmacology · doi:10.1124/mol.104.002832 · Cited by 239
The story so far: molecular regulation of the heme oxygenase-1 gene in renal injury
Sikorski, E. M., Hock, T., Hill-Kapturczak, N., & Agarwal, A. (2004) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00297.2003 · Cited by 238
Heme oxygenase expression in human central nervous system disorders
Schipper, H. M. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.09.015 · Cited by 237
Targeted gene deletion of heme oxygenase 2 reveals neural role for carbon monoxide
Zakhary, R., Poss, K. D., Jaffrey, S. R., Ferris, C. D., Tonegawa, S., & Snyder, S. H. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14848 · Cited by 236
Schmitt, M. P. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.3.838-845.1997 · Cited by 234
The physiological significance of heme oxygenase
Abraham, N. G., Lin, J. H.-C., Schwartzman, M. L., Levere, R. D., & Shibahara, S. (1988) · International Journal of Biochemistry · doi:10.1016/0020-711x(88)90093-6 · Cited by 234
Serum bilirubin and risk of ischemic heart disease in middle-aged British men
Breimer, L. H., Wannamethee, G., Ebrahim, S., & Shaper, A. G. (1995) · Clinical Chemistry · doi:10.1093/clinchem/41.10.1504 · Cited by 229
The direct effect of carbon monoxide on K Ca channels in vascular smooth muscle cells
Wang, R., Wu, L., & Wang, Z. (1997) · Pfl�gers Archiv European Journal of Physiology · doi:10.1007/s004240050398 · Cited by 228
Amersi, F., Shen, X.-D., Anselmo, D., Melinek, J., Iyer, S., Southard, D. J., Katori, M., Volk, H.-D., Busuttil, R. W., Buelow, R., et al. (2002) · Hepatology · doi:10.1053/jhep.2002.32467 · Cited by 228
Hayashi, S., Omata, Y., Sakamoto, H., Higashimoto, Y., Hara, T., Sagara, Y., & Noguchi, M. (2004) · Gene · doi:10.1016/j.gene.2004.04.002 · Cited by 227
Transcriptional Activation of the Heme Oxygenase Gene by Heme and Cadmium in Mouse Hepatoma Cells
Alam, J., Shibahara, S., & Smith, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83358-0 · Cited by 226
Self-citationKeyse, S. M., Applegate, L. A., Tromvoukis, Y., & Tyrrell, R. M. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.9.4967 · Cited by 226
Nakao, A., Neto, J. S., Kanno, S., Stolz, D. B., Kimizuka, K., Liu, F., Bach, F. H., Billiar, T. R., Choi, A. M., Otterbein, L. E., et al. (2005) · American Journal of Transplantation · doi:10.1111/j.1600-6143.2004.00695.x · Cited by 226
Self-citationSeptic shock. Hemodynamics and pathogenesis.
Parker, M. M., & Parrillo, J. E. (1984) · PubMed · Cited by 225
Maines, M., & Kappas, A. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41402-6 · Cited by 224
Endogenous Formation of Carbon Monoxide in Man Under Normal and Pathological Conditions
Sjöstrand, T. (1949) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.3109/00365514909069943 · Cited by 223
Song, R., Kubo, M., Morse, D., Zhou, Z., Zhang, X., Dauber, J. H., Fabisiak, J., Alber, S. M., Watkins, S. C., Zuckerbraun, B. S., et al. (2003) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63646-2 · Cited by 222
Self-citationRatliff, M., Zhu, W., Deshmukh, R., Wilks, A., & Stojiljkovic, I. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.21.6394-6403.2001 · Cited by 221
Meffert, M. K., Haley, J. E., Schuman, E. M., Schulman, H., & Madison, D. V. (1994) · Neuron · doi:10.1016/0896-6273(94)90060-4 · Cited by 221
Administration of a CO-releasing molecule at the time of reperfusion reduces infarct size in vivo
Guo, Y., Stein, A. B., Wu, W.-J., Tan, W., Zhu, X., Li, Q.-H., Dawn, B., Motterlini, R., & Bolli, R. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00971.2003 · Cited by 221
The mechanism of heme oxygenase
Ortiz de Montellano, P. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)00079-4 · Cited by 221
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 219
Self-citationKeyse, S. M., & Tyrrell, R. M. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47869-6 · Cited by 218
Alam, J., Camhi, S., & Choi, A. M. K. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.11977 · Cited by 217
Self-citationInduction of four proteins in chick embryo cells by sodium arsenite.
Johnston, D., Oppermann, H., Jackson, J., & Levinson, W. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43671-x · Cited by 215
Tanaka, T., & Knox, W. E. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98149-4 · Cited by 214
Lautier, D., Luscher, P., & Tyrrell, R. M. (1992) · Carcinogenesis · doi:10.1093/carcin/13.2.227 · Cited by 213
Oxygen toxicity and iron accumulation in the lungs of mice lacking heme oxygenase-2.
Dennery, P. A., Spitz, D. R., Yang, G., Tatarov, A., Lee, C. S., Shegog, M. L., & Poss, K. D. (1998) · Journal of Clinical Investigation · doi:10.1172/jci448 · Cited by 212
Katoh, Y., Iida, K., Kang, M.-I., Kobayashi, A., Mizukami, M., Tong, K. I., McMahon, M., Hayes, J. D., Itoh, K., & Yamamoto, M. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.10.012 · Cited by 212
Bilirubin inhibits iNOS expression and NO production in response to endotoxin in rats
Wang, W. W., Smith, D. L. H., & Zucker, S. D. (2004) · Hepatology · doi:10.1002/hep.20334 · Cited by 212
Lee, T.-S., Tsai, H.-L., & Chau, L.-Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300498200 · Cited by 211
Weaver, L. K. (1999) · Critical Care Clinics · doi:10.1016/s0749-0704(05)70056-7 · Cited by 211
Interaction of bilirubin and biliverdin with reactive nitrogen species
Kaur, H., Hughes, M. N., Green, C. J., Naughton, P., Foresti, R., & Motterlini, R. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00420-4 · Cited by 209
Peroxynitrite induces haem oxygenase-1 in vascular endothelial cells: a link to apoptosis
Foresti, R., Sarathchandra, P., Clark, J., Green, C. J., & Motterlini, R. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3390729 · Cited by 209
Basis of guanylate cyclase activation by carbon monoxide.
Kharitonov, V. G., Sharma, V. S., Pilz, R. B., Magde, D., & Koesling, D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.7.2568 · Cited by 207
Berberat, P. O., Katori, M., Kaczmarek, E., Anselmo, D., Lassman, C., Ke, B., Shen, X., Busuttil, R. W., Yamashita, K., Csizmadia, E., et al. (2003) · The FASEB Journal · doi:10.1096/fj.03-0229fje · Cited by 207
Nucleotide sequence and organization of the rat heme oxygenase gene.
Müller, R. M., Taguchi, H., & Shibahara, S. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48315-9 · Cited by 204
Expression and Characterization of a Heme Oxygenase (Hmu O) fromCorynebacterium diphtheriae
Wilks, A., & Schmitt, M. P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.2.837 · Cited by 204
Christou, H., Morita, T., Hsieh, C.-M., Koike, H., Arkonac, B., Perrella, M. A., & Kourembanas, S. (2000) · Circulation Research · doi:10.1161/01.res.86.12.1224 · Cited by 204
Modak, S. B., & Tyrrell, R. M. (1993) · PubMed · Cited by 204
Heme Oxygenase: Evolution, Structure, and Mechanism
Wilks, A. (2002) · Antioxidants & Redox Signaling · doi:10.1089/15230860260220102 · Cited by 204
Carbon monoxide and the nervous system
Raub, J. A., & Benignus, V. A. (2002) · Neuroscience & Biobehavioral Reviews · doi:10.1016/s0149-7634(03)00002-2 · Cited by 201
Zhang, X., Shan, P., Sasidhar, M., Chupp, G. L., Flavell, R. A., Choi, A. M. K., & Lee, P. J. (2003) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2002-0156oc · Cited by 201
Self-citationXue, L., Farrugia, G., Miller, S. M., Ferris, C. D., Snyder, S. H., & Szurszewski, J. H. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.4.1851 · Cited by 200
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
Caveolae compartmentalization of heme oxygenase‐1 in endothelial cells
Kim, H. P., Wang, X., Galbiati, F., Ryter, S. W., & Choi, A. M. K. (2004) · The FASEB Journal · doi:10.1096/fj.03-1391com · Cited by 196
Self-citationEwing, J. F., Haber, S. N., & Maines, M. D. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb09373.x · Cited by 195
Inamdar, N. M., Ahn, Y. I., & Alam, J. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0637 · Cited by 194
Self-citationShibahara, S., Yoshizawa, M., Suzuki, H., Takeda, K., Meguro, K., & Endo, K. (1993) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a124028 · Cited by 193
Carbon monoxide: a role in carotid body chemoreception.
Prabhakar, N. R., Dinerman, J. L., Agani, F. H., & Snyder, S. H. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.6.1994 · Cited by 193
Alam, J., & Den, Z. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36696-7 · Cited by 192
Self-citationSinglet Molecular Oxygen (1O2): A Possible Effector of Eukaryotic Gene Expression
Ryter, S. W., & Tyrrell, R. M. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00461-9 · Cited by 192
Self-citationAdaptive responses and apoptosis in endothelial cells exposed to carbon monoxide
Thom, S. R., Fisher, D., Xu, Y. A., Notarfrancesco, K., & Ischiropoulos, H. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.3.1305 · Cited by 192
A Heme Oxygenase Product, Presumably Carbon Monoxide, Mediates a Vasodepressor Function in Rats
Johnson, R. A., Lavesa, M., Askari, B., Abraham, N. G., & Nasjletti, A. (1995) · Hypertension · doi:10.1161/01.hyp.25.2.166 · Cited by 192
Krönke, G., Bochkov, V. N., Huber, J., Gruber, F., Blüml, S., Fürnkranz, A., Kadl, A., Binder, B. R., & Leitinger, N. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304103200 · Cited by 190
Purification and properties of heme oxygenase from pig spleen microsomes.
Yoshida, T., & Kikuchi, G. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34707-5 · Cited by 189
Heme Oxygenase-1: Molecular Mechanisms of Gene Expression in Oxygen-Related Stress
Ryter, S. W., & Choi, A. M. K. (2002) · Antioxidants & Redox Signaling · doi:10.1089/15230860260220120 · Cited by 187
Self-citationEwing, J. F., & Maines, M. D. (1992) · Molecular and Cellular Neuroscience · doi:10.1016/1044-7431(92)90068-d · Cited by 187
Zhu, W., Wilks, A., & Stojiljkovic, I. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.23.6783-6790.2000 · Cited by 186
Potential Mechanism by Which Resveratrol, a Red Wine Constituent, Protects Neurons
ZHUANG, H., KIM, Y., KOEHLER, R. C., & DORÉ, S. (2003) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2003.tb07534.x · Cited by 186
Molinari, E., Gilman, M., & Natesan, S. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6439 · Cited by 185
Otterbein, L. E., Otterbein, S. L., Ifedigbo, E., Liu, F., Morse, D. E., Fearns, C., Ulevitch, R. J., Knickelbein, R., Flavell, R. A., & Choi, A. M. (2003) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63610-3 · Cited by 184
Self-citationKaide, J.-I., Zhang, F., Wei, Y., Jiang, H., Yu, C., Wang, W., Balazy, M., Abraham, N. G., & Nasjletti, A. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11218 · Cited by 184
McCoubrey, W. K., Huang, T. J., & Maines, M. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.19.12568 · Cited by 183
Takahashi, M., Doré, S., Ferris, C. D., Tomita, T., Sawa, A., Wolosker, H., Borchelt, D. R., Iwatsubo, T., Kim, S.-H., Thinakaran, G., et al. (2000) · Neuron · doi:10.1016/s0896-6273(00)00125-2 · Cited by 183
Protective effect of heme oxygenase induction in ischemic acute renal failure
Shimizu, H., Takahashi, T., Suzuki, T., Yamasaki, A., Fujiwara, T., Odaka, Y., Hirakawa, M., Fujita, H., & Akagi, R. (2000) · Critical Care Medicine · doi:10.1097/00003246-200003000-00033 · Cited by 183
Overexpression of Heme Oxygenase in Neuronal Cells, the Possible Interaction with Tau
Takeda, A., Perry, G., Abraham, N. G., Dwyer, B. E., Kutty, R. K., Laitinen, J. T., Petersen, R. B., & Smith, M. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5395 · Cited by 183
Kietzmann, T., Samoylenko, A., & Immenschuh, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m203929200 · Cited by 182
McCoubrey, W. K., Ewing, J. F., & Maines, M. D. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90481-b · Cited by 182
Terry, C. M., Clikeman, J. A., Hoidal, J. R., & Callahan, K. S. (1998) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1998.274.3.h883 · Cited by 182
Biliverdin, a natural product of heme catabolism, induces tolerance to cardiac allografts
Yamashita, K., McDaid, J., Öllinger, R., Tsui, T., Berberat, P. O., Usheva, A., Csizmadia, E., Smith, R. N., Soares, M. P., & Bach, F. H. (2004) · The FASEB Journal · doi:10.1096/fj.03-0839fje · Cited by 180
Pathways of cell signaling in hyperoxia
Lee, P. J., & Choi, A. M. K. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00279-x · Cited by 180
Self-citationGlutathione Depletion Induces Heme Oxygenase‐1 (HSP32) mRNA and Protein in Rat Brain
Ewing, J. F., & Maines, M. D. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03315.x · Cited by 178
Regulation of heme oxygenase-1 gene expression in vascular smooth muscle cells by nitric oxide
Hartsfield, C. L., Alam, J., Cook, J. L., & Choi, A. M. K. (1997) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1997.273.5.l980 · Cited by 177
Self-citationBilirubin attenuates radical‐mediated damage to serum albumin
Neužil, J., & Stocker, R. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80353-v · Cited by 176
Mechanism of heme degradation by heme oxygenase
Yoshida, T., & Migita, C. T. (2000) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(00)00156-2 · Cited by 175
National Asthma Education Program
Lenfant, C., & Hurd, S. S. (1990) · Chest · doi:10.1378/chest.98.1.226 · Cited by 174
Cytochrome P-450 heme and the regulation of hepatic heme oxygenase activity
Bissell, D. M., & Hammaker, L. E. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90144-2 · Cited by 172
Zhang, X., Shan, P., Alam, J., Davis, R. J., Flavell, R. A., & Lee, P. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301858200 · Cited by 171
Self-citationExner, M., Schillinger, M., Minar, E., Mlekusch, W., Schlerka, G., Haumer, M., Mannhalter, C., & Wagner, O. (2001) · Journal of Endovascular Therapy · doi:10.1177/152660280100800501 · Cited by 171
Cadmium Induces Nuclear Export of Bach1, a Transcriptional Repressor of Heme Oxygenase-1 Gene
Suzuki, H., Tashiro, S., Sun, J., Doi, H., Satomi, S., & Igarashi, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306764200 · Cited by 170
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
Self-citationHippocampal long-term potentiation is normal in heme oxygenase-2 mutant mice
Poss, K. D., Thomas, M. J., Ebralidze, A. K., O'Dell, T. J., & Tonegawa, S. (1995) · Neuron · doi:10.1016/0896-6273(95)90177-9 · Cited by 168
Liu, Z.-M., Chen, G. G., Ng, E. K., Leung, W.-K., Sung, J. J., & Chung, S. S. (2004) · Oncogene · doi:10.1038/sj.onc.1207173 · Cited by 167
Heme activates the heme oxygenase-1 gene in renal epithelial cells by stabilizing Nrf2
Alam, J., Killeen, E., Gong, P., Naquin, R., Hu, B., Stewart, D., Ingelfinger, J. R., & Nath, K. A. (2003) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00376.2002 · Cited by 167
Self-citationSardana, M. K., & Kappas, A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.8.2464 · Cited by 167
Biliverdin Therapy Protects Rat Livers From Ischemia and Reperfusion Injury
Fondevila, C., Shen, X., Tsuchiyashi, S., Yamashita, K., Csizmadia, E., Lassman, C., Busuttil, R. W., Kupiec–Weglinski, J. W., & Bach, F. H. (2004) · Hepatology · doi:10.1002/hep.20480 · Cited by 166
Antioxidant Gene Polymorphisms and Susceptibility to a Rapid Decline in Lung Function in Smokers
He, J.-Q., Ruan, J., Connett, J. E., Anthonisen, N. R., Paré, P. D., & Sandford, A. J. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2111059 · Cited by 166
NO and CO as second messengers in oxygen sensing in the carotid body
Prabhakar, N. R. (1999) · Respiration Physiology · doi:10.1016/s0034-5687(99)00019-5 · Cited by 164
The human 32‐kDa stress protein induced by exposure to arsenite and cadmium ions is heme oxygenase
Taketani, S., Kohno, H., Yoshinaga, T., & Tokunaga, R. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)80215-7 · Cited by 164
Muramoto, T., Tsurui, N., Terry, M. J., Yokota, A., & Kohchi, T. (2002) · Plant Physiology · doi:10.1104/pp.008128 · Cited by 164
Yoshida, T., & Kikuchi, G. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34708-7 · Cited by 163
Tulis, D. A., Durante, W., Liu, X., Evans, A. J., Peyton, K. J., & Schafer, A. I. (2001) · Circulation · doi:10.1161/hc4701.099585 · Cited by 162
Jaggar, J. H., Leffler, C. W., Cheranov, S. Y., Tcheranova, D., E, S., & Cheng, X. (2002) · Circulation Research · doi:10.1161/01.res.0000036900.76780.95 · Cited by 161
Pitfalls using metalloporphyrins in carbon monoxide research
Grundemar, L., & Ny, L. (1997) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(97)01065-1 · Cited by 159
Unconjugated Bilirubin Inhibits VCAM-1-Mediated Transendothelial Leukocyte Migration
Keshavan, P., Deem, T. L., Schwemberger, S. J., Babcock, G. F., Cook-Mills, J. M., & Zucker, S. D. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.6.3709 · Cited by 159
Carbon monoxide and cerebral microvascular tone in newborn pigs
Leffler, C. W., Nasjletti, A., Yu, C., Johnson, R. A., Fedinec, A. L., & Walker, N. (1999) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1999.276.5.h1641 · Cited by 158
Kaneda, H., Ohno, M., Taguchi, J., Togo, M., Hashimoto, H., Ogasawara, K., Aizawa, T., Ishizaka, N., & Nagai, R. (2002) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000033515.96747.6f · Cited by 158
Adin, C. A., Croker, B. P., & Agarwal, A. (2004) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00215.2004 · Cited by 157
Erdoğan, D., Güllü, H., Yıldırım, E., Tok, D., Kırbaş, İ., Çiftçi, Ö., Baycan, S., & Müderrisoğlu, H. (2005) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2005.05.011 · Cited by 156
Mechanisms of carbon monoxide toxicity
Coburn, R. F. (1979) · Preventive Medicine · doi:10.1016/0091-7435(79)90008-2 · Cited by 156
Yoshinaga, T., Sassa, S., & Kappas, A. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34449-1 · Cited by 155
Gene expression profiles of heme oxygenase isoforms in the rat brain
Scapagnini, G., D’Agata, V., Calabrese, V., Pascale, A., Colombrita, C., Alkon, D. L., & Cavallaro, S. (2002) · Brain Research · doi:10.1016/s0006-8993(02)03338-3 · Cited by 155
Sabaawy, H. E., Zhang, F., Nguyen, X., Elhosseiny, A. A., Nasjletti, A., Schwartzman, M. L., Dennery, P. A., Kappas, A., & Abraham, N. G. (2001) · Hypertension · doi:10.1161/01.hyp.38.2.210 · Cited by 155
Shibahara, S. (2003) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.200.167 · Cited by 154
Juan, S., Cheng, T., Lin, H., Chu, Y.-L., & Lee, W. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.09.015 · Cited by 153
Carbon Monoxide as an Endogenous Modulator of Hepatic Vascular Perfusion
Suematsu, M., Kashiwagi, S., Sano, T., Goda, N., Shinoda, Y., & Ishimura, Y. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.2811 · Cited by 153
Cantoni, L., Rossi, C., Rizzardini, M., Gadina, M., & Ghezzi, P. (1991) · Biochemical Journal · doi:10.1042/bj2790891 · Cited by 153
Alam, J., Cai, J., & Smith, A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42211-3 · Cited by 152
Self-citationNitric oxide stimulates Nrf2 nuclear translocation in vascular endothelium
Buckley, B. J., Marshall, Z. M., & Whorton, A. R. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01308-1 · Cited by 152
Angiotensin II induces apoptosis in renal proximal tubular cells
Bhaskaran, M. C., Reddy, K., Radhakrishanan, N., Franki, N., Ding, G., & Singhal, P. C. (2003) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00246.2002 · Cited by 152
THE FORMATION OF BILIRUBIN FROM HEMOGLOBIN IN VIVO*
Ostrow, J. D., Jandi, J. H., & Schmid, R. (1962) · Journal of Clinical Investigation · doi:10.1172/jci104620 · Cited by 150
Regulation of Heme Oxygenase-1 by Redox Signals Involving Nitric Oxide
Motterlini, R., Green, C. J., & Foresti, R. (2002) · Antioxidants and Redox Signaling · doi:10.1089/15230860260220111 · Cited by 150
Potential role of conjugated bilirubin and copper in the metabolism of lipid peroxides in bile.
Stocker, R., & Ames, B. N. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.22.8130 · Cited by 149
Inhaled Carbon Monoxide Confers Antiinflammatory Effects against Ventilator-induced Lung Injury
Dolinay, T., Szilasi, M., Liu, M., & Choi, A. M. K. (2004) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200401-023oc · Cited by 146
Self-citationBrain heme oxygenase isoenzymes and nitric oxide synthase are co-localized in select neurons
Vincent, S. R., Das, S., & Maines, M. D. (1994) · Neuroscience · doi:10.1016/0306-4522(94)90018-3 · Cited by 146
In vivo ozone exposure induces antioxidant/stress-related responses in murine lung and skin
Valacchi, G., Pagnin, E., Corbacho, A. M., Olano-Martin, E., Davis, P. A., Packer, L., & Cross, C. E. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.12.005 · Cited by 146
Aizawa, T., Ishizaka, N., Taguchi, J., Nagai, R., Mori, I., Tang, S., Ingelfinger, J. R., & Ohno, M. (2000) · Hypertension · doi:10.1161/01.hyp.35.3.800 · Cited by 146
Bakken, A. F., Thaler, M., & Schmid, R. (1972) · Journal of Clinical Investigation · doi:10.1172/jci106841 · Cited by 145
Absence of Heme Oxygenase-1 Exacerbates Myocardial Ischemia/Reperfusion Injury in Diabetic Mice
Liu, X., Wei, J., Peng, D. H., Layne, M. D., & Yet, S. (2005) · Diabetes · doi:10.2337/diabetes.54.3.778 · Cited by 145
Wu, R., Skaar, E. P., Zhang, R., Joachimiak, G., Gornicki, P., Schneewind, O., & Joachimiak, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409526200 · Cited by 144
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
Self-citationRotenberg, M. O., & Maines, M. D. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39141-0 · Cited by 143
New Developments in the Regulation of Heme Metabolism and Their Implications
Maines, M. D., & Snyder, R. (1984) · Critical Reviews in Toxicology · doi:10.3109/10408448409021604 · Cited by 143
Rizzardini, M., Terao, M., Falciani, F., & Cantoni, L. (1993) · Biochemical Journal · doi:10.1042/bj2900343 · Cited by 143
Carbon Monoxide Neurotransmission Activated by CK2 Phosphorylation of Heme Oxygenase-2
Boehning, D. F., Moon, C., Sharma, S., Hurt, K. J., Hester, L. D., Ronnett, G. V., Shugar, D., & Snyder, S. H. (2003) · Neuron · doi:10.1016/s0896-6273(03)00596-8 · Cited by 142
Wagener, F. A. D. T. G., da Silva, J.-L., Farley, T., de Witte, T., Kappas, A., & Abraham, N. G. (1999) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)35116-x · Cited by 142
Gong, P., Hu, B., Stewart, D., Ellerbe, M., Figueroa, Y. G., Blank, V., Beckman, B. S., & Alam, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103658200 · Cited by 141
Self-citationEndoplasmic 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 141
Self-citationDavis, S. J., Bhoo, S. H., Durski, A. M., Walker, J. M., & Vierstra, R. D. (2001) · PLANT PHYSIOLOGY · doi:10.1104/pp.126.2.656 · Cited by 140
Heme oxygenase-1 and carbon monoxide in pulmonary medicine
Slebos, D., Ryter, S. W., & Choi, A. M. K. (2003) · Respiratory Research · doi:10.1186/1465-9921-4-7 · Cited by 140
Self-citationHaemin uptake and use as an iron source by Candida albicans: role of CaHMX1-encoded haem oxygenase
Santos, R., Buisson, N., Knight, S., Dancis, A., Camadro, J.-M., & Lesuisse, E. (2003) · Microbiology · doi:10.1099/mic.0.26108-0 · Cited by 139
Bilirubin Ameliorates Bleomycin-Induced Pulmonary Fibrosis in Rats
WANG, H.-D., Yamaya, M., Okinaga, S., JIA, Y.-X., Kamanaka, M., Takahashi, H., GUO, L.-Y., Ohrui, T., & Sasaki, H. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.165.3.2003149 · Cited by 139
Gong, P., Stewart, D., Hu, B., Li, N., Cook, J. L., Nel, A. E., & Alam, J. (2002) · Antioxidants and Redox Signaling · doi:10.1089/152308602753666307 · Cited by 139
Self-citationSarady, J. K., Otterbein, S. L., Liu, F., Otterbein, L. E., & Choi, A. M. K. (2002) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.4816 · Cited by 139
Self-citationRamos, K. S., Lin, H., & McGrath, J. J. (1989) · Biochemical Pharmacology · doi:10.1016/0006-2952(89)90347-x · Cited by 138
Structural organization of the human heme oxygenase gene and the function of its promoter
Shibahara, S., Sato, M., Müller, R., & Yoshida, T. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb14583.x · Cited by 138
Ricchetti, G., Williams, L. M., & Foxwell, B. M. J. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0104046 · Cited by 138
Wang, X., Ryter, S. W., Dai, C., Tang, Z.-L., Watkins, S. C., Yin, X.-M., Song, R., & Choi, A. M. K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301624200 · Cited by 136
Self-citationCaltabiano, M. M., Koestler, T. P., Poste, G. H., & GREIG, R. G. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69316-0 · Cited by 136
A Mammalian Iron ATPase Induced by Iron
Barañano, D. E., Wolosker, H., Bae, B.-I., Barrow, R. K., Snyder, S. H., & Ferris, C. D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.20.15166 · Cited by 134
Regulation of human heme oxygenase-1 gene expression under thermal stress
Okinaga, S., Takahashi, K., Takeda, K., Yoshizawa, M., Fujita, H., Sasaki, H., & Shibahara, S. (1996) · Blood · doi:10.1182/blood.v87.12.5074.bloodjournal87125074 · Cited by 133
Filippo, C. D., Marfella, R., Cuzzocrea, S., Piegari, E., Petronella, P., Giugliano, D., Rossi, F., & D’Amico, M. (2005) · Diabetes · doi:10.2337/diabetes.54.3.803 · Cited by 132
Takeda, K., Ishizawa, S., Sato, M. N., Yoshida, T., & Shibahara, S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31724-6 · Cited by 131
Nitric Oxide-inducible Expression of Heme Oxygenase-1 in Human Cells
Bouton, C., & Demple, B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.42.32688 · Cited by 131
Terry, C. M., Clikeman, J. A., Hoidal, J. R., & Callahan, K. S. (1999) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1999.276.5.h1493 · Cited by 131
Camhi, S. L., Alam, J., Wiegand, G. W., Chin, B. Y., & Choi, A. M. K. (1998) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.18.2.2910 · Cited by 131
Self-citationHawkins, R. D., Zhuo, M., & Arancio, O. (1994) · Journal of Neurobiology · doi:10.1002/neu.480250607 · Cited by 130
McDonagh, A. F. (1990) · Clinics in Perinatology · doi:10.1016/s0095-5108(18)30572-4 · Cited by 130
Angiotensin II–Induced Hypertension Increases Heme Oxygenase-1 Expression in Rat Aorta
Ishizaka, N., León, H. D., Laursen, J. B., Fukui, T., Wilcox, J. N., Keulenaer, G. W. D., Griendling, K. K., & Alexander, R. W. (1997) · Circulation · doi:10.1161/01.cir.96.6.1923 · Cited by 129
Administration of a CO-releasing molecule induces late preconditioning against myocardial infarction
STEIN, A., Guo, Y., TAN, W., Wu, W., ZHU, X., Li, Q. H., Luo, C., DAWN, B., Johnson, T., Motterlini, R., et al. (2004) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2004.10.006 · Cited by 129
Ewing, J. F., Vulapalli, R., & Maines, M. D. (1994) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)22706-9 · Cited by 129
Ke, B., Buelow, R., Shen, X., Melinek, J., Amersi, F. F., Gao, F., Ritter, T., Volk, H., Busuttil, R. W., & Kupiec‐Weglinski, J. W. (2002) · Human Gene Therapy · doi:10.1089/104303402320138970 · Cited by 128
Iron loading of endothelial cells augments oxidant damage.
Balla, G., Vercellotti, G. M., Eaton, J. W., & Jacob, H. S. (1990) · PubMed · Cited by 127
Alam, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31496-5 · Cited by 127
Self-citationTHE ENZYMATIC DEGRADATION OF HEMOGLOBIN TO BILE PIGMENTS BY MACROPHAGES
Pimstone, N. R., Tenhunen, R., Seitz, P. T., Marver, H. S., & Schmid, R. (1971) · The Journal of Experimental Medicine · doi:10.1084/jem.133.6.1264 · Cited by 127
Yoshida, T., Noguchi, M., & Kikuchi, G. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85506-0 · Cited by 127
Raju, V. S., McCoubrey, W. K., & Maines, M. D. (1997) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(96)00183-2 · Cited by 126
Carbon monoxide relaxes ileal smooth muscle through activation of guanylate cyclase
UTZ, J., & Ullrich, V. (1991) · Biochemical Pharmacology · doi:10.1016/0006-2952(91)90658-r · Cited by 126
Suttner, D. M., Sridhar, K. J., Lee, C. S., Tomura, T., Hansen, T. N., & Dennery, P. A. (1999) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1999.276.3.l443 · Cited by 126
Kataoka, K., Handa, H., & Nishizawa, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105383200 · Cited by 125
Cited by
Oxidative Stress: An Essential Factor in the Pathogenesis of Gastrointestinal Mucosal Diseases
Bhattacharyya, A., Chattopadhyay, R., Mitra, S., & Crowe, S. E. (2014) · Physiological Reviews · doi:10.1152/physrev.00040.2012 · Cited by 2,484
The therapeutic potential of carbon monoxide
Motterlini, R., & Otterbein, L. E. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3228 · Cited by 1,638
Application of Metal Coordination Chemistry To Explore and Manipulate Cell Biology
Haas, K. L., & Franz, K. J. (2009) · Chemical Reviews · doi:10.1021/cr900134a · Cited by 984
Carbon monoxide intoxication: An updated review
Prockop, L. D., & Chichkova, R. I. (2007) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2007.06.037 · Cited by 730
Kalogeris, T., Baines, C. P., Krenz, M., & Korthuis, R. J. (2016) · Comprehensive Physiology · doi:10.1002/cphy.c160006 · Cited by 718
Metadata
- Authors
- Ryter, S. W., Alam, J., & Choi, A. M. K.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2006-04
- Volume
- 86
- Issue
- 2
- Pages
- 583-650
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2005904261
- Cited by
- 2,307
- References
- 716
- FWCI
- 6.74
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.