Mechanisms of Cell Protection by Heme Oxygenase-1

Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics

Kerr, J. F. R., Wyllie, A. H., & Currie, A. R. (1972) · British Journal of Cancer · doi:10.1038/bjc.1972.33 · Cited by 15,980

Origin and physiological roles of inflammation

Medzhitov, R. (2008) · Nature · doi:10.1038/nature07201 · Cited by 6,618

The biochemistry of apoptosis

Hengartner, M. O. (2000) · Nature · doi:10.1038/35037710 · Cited by 5,779

Cleavage of BID by Caspase 8 Mediates the Mitochondrial Damage in the Fas Pathway of Apoptosis

Li, H., Zhu, H., Xu, C.-J., & Yuan, J. (1998) · Cell · doi:10.1016/s0092-8674(00)81590-1 · Cited by 4,445

Release of chromatin protein HMGB1 by necrotic cells triggers inflammation

Scaffidi, P., Misteli, T., & Bianchi, M. E. (2002) · Nature · doi:10.1038/nature00858 · Cited by 4,221

The Pathophysiology of Mitochondrial Cell Death

Green, D. R., & Kroemer, G. (2004) · Science · doi:10.1126/science.1099320 · Cited by 3,487

LXXIII.—Oxidation of tartaric acid in presence of iron

Fenton, H. J. H. (1894) · J. Chem. Soc., Trans. · doi:10.1039/ct8946500899 · Cited by 3,179

An Essential Role for NF-κB in Preventing TNF-α-Induced Cell Death

Beg, A. A., & Baltimore, D. (1996) · Science · doi:10.1126/science.274.5288.782 · Cited by 3,047

NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation.

Wang, C.-Y., Mayo, M., Korneluk, R., Goeddel, D., & Baldwin, A. (1998) · Science · doi:10.1126/science.281.5383.1680 · Cited by 2,950

Bilirubin Is an Antioxidant of Possible Physiological Importance

Stocker, R., Yamamoto, Y., McDonagh, A. F., Glazer, A. N., & Ames, B. N. (1987) · Science · doi:10.1126/science.3029864 · Cited by 2,948

Signalling pathways of the TNF superfamily: a double-edged sword

Aggarwal, B. B. (2003) · Nature Reviews Immunology · doi:10.1038/nri1184 · Cited by 2,793

Points of control in inflammation

Nathan, C. (2002) · Nature · doi:10.1038/nature01320 · Cited by 2,738

Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes

Micheau, O., & Tschopp, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00521-x · Cited by 2,738

The ferritins: molecular properties, iron storage function and cellular regulation

Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667

Integrating cell-signalling pathways with NF-κB and IKK function

Perkins, N. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2083 · Cited by 2,350

IκB: a Specific Inhibitor of the NF-κB Transcription Factor

Baeuerle, P. A., & Baltimore, D. (1988) · Science · doi:10.1126/science.3140380 · Cited by 2,154

Molecular mechanisms of caspase regulation during apoptosis

Riedl, S. J., & Shi, Y. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1496 · Cited by 1,933

The pathogenic basis of malaria

Miller, L. H., Baruch, D. I., Marsh, K., & Doumbo, O. K. (2002) · Nature · doi:10.1038/415673a · Cited by 1,804

The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase.

Tenhunen, R., Marver, H. S., & Schmid, R. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.61.2.748 · Cited by 1,803

Reactive Oxygen Species Promote TNFα-Induced Death and Sustained JNK Activation by Inhibiting MAP Kinase Phosphatases

Kamata, H., Honda, S.-I., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2004.12.041 · Cited by 1,792

Identification of the haemoglobin scavenger receptor

Kristiansen, M., Graversen, J. H., Jacobsen, C., Sonne, O., Hoffman, H.-J., Law, S. K. A., & Moestrup, S. K. (2001) · Nature · doi:10.1038/35051594 · Cited by 1,712

The Clinical Sequelae of Intravascular Hemolysis and Extracellular Plasma Hemoglobin

Rother, R. P., Bell, L. B., Hillmen, P., & Gladwin, M. T. (2005) · JAMA · doi:10.1001/jama.293.13.1653 · Cited by 1,565

Oxidation of tartaric acid in presence of iron

Fenton, H. J. H. (1894) · Journal of the Chemical Society (Resumed) · Cited by 1,498

Control of IκB-α Proteolysis by Site-Specific, Signal-Induced Phosphorylation

Brown, K., Gerstberger, S., Carlson, L., Franzoso, G., & Siebenlist, U. (1995) · Science · doi:10.1126/science.7878466 · Cited by 1,434

Mitogen-activated protein kinases in apoptosis regulation

Wada, T., & Penninger, J. M. (2004) · Oncogene · doi:10.1038/sj.onc.1207556 · Cited by 1,432

Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling

Rhee, S. G., Chae, H. Z., & Kim, K. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.02.026 · Cited by 1,409

Cell-free hemoglobin limits nitric oxide bioavailability in sickle-cell disease

Reiter, C. D., Wang, X., Tanus-Santos, J. E., Hogg, N., Cannon, R. O., Schechter, A. N., & Gladwin, M. T. (2002) · Nature Medicine · doi:10.1038/nm1202-799 · Cited by 1,330

Nrf2, a Cap'n'Collar Transcription Factor, Regulates Induction of the Heme Oxygenase-1 Gene

Alam, J., Stewart, D. P., Touchard, C. L., Boinapally, S., Choi, A. M. K., & Cook, J. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.37.26071 · Cited by 1,299

TUMOR NECROSIS FACTOR RECEPTOR AND Fas SIGNALING MECHANISMS

Wallach, D., Varfolomeev, E. E., Malinin, N. L., Goltsev, Y. V., Kovalenko, A. V., & Boldin, M. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.331 · Cited by 1,299

Reduced stress defense in heme oxygenase 1-deficient cells

Poss, K. D., & Tonegawa, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10925 · Cited by 1,294

Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway.Preprint

Chen, Z., Hagler, J., Palombella, V. J., Melandri, F. D., Scherer, D. C., Ballard, D. W., & Maniatis, T. (1995) · Genes & Development · doi:10.1101/gad.9.13.1586 · Cited by 1,270

Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency

Yachie, A., Niida, Y., Wada, T., Igarashi, N., Kaneda, H., Toma, T., Ohta, K., Kasahara, Y., & Koizumi, S. (1999) · Journal of Clinical Investigation · doi:10.1172/jci4165 · Cited by 1,256

Shaping the nuclear action of NF-κB

Chen, L., & Greene, W. C. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1368 · Cited by 1,248

Phosphorylation of NF-κB p65 by PKA Stimulates Transcriptional Activity by Promoting a Novel Bivalent Interaction with the Coactivator CBP/p300

Zhong, H., Voll, R. E., & Ghosh, S. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80066-0 · Cited by 1,210

Variation in the TNF-α promoter region associated with susceptibility to cerebral malaria

McGuire, W. L., Hill, A. V. S., Allsopp, C. E. M., Greenwood, B. M., & Kwiatkowski, D. P. (1994) · Nature · doi:10.1038/371508a0 · Cited by 1,166

Heme oxygenase-1: unleashing the protective properties of heme

Otterbein, L. E., Soares, M. P., Yamashita, K., & Bach, F. H. (2003) · Trends in Immunology · doi:10.1016/s1471-4906(03)00181-9 · Cited by 1,166

Heme Oxygenase-1: Function, Regulation, and Implication of a Novel Stress-Inducible Protein in Oxidant-Induced Lung Injury

Choi, A. M., & Alam, J. (1996) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.15.1.8679227 · Cited by 1,126

Pharmacological and Clinical Aspects of Heme Oxygenase

Abraham, N. G., & Kappas, A. (2008) · Pharmacological Reviews · doi:10.1124/pr.107.07104 · Cited by 1,115

Ferritin: a cytoprotective antioxidant strategem of endothelium.

Balla, G., Jacob, H., Balla, J., Rosenberg, M. E., Nath, K. A., Apple, F., Eaton, J. W., & Vercellotti, G. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37165-0 · Cited by 1,097

Cell-free hemoglobin limits nitric oxide bioavailability in sickle-cell disease

Reiter, C. D., Wang, X., Tanus-Santos, J. E., et al. (2002) · Nature Medicine · doi:10.1038/nm799 · Cited by 1,097

Indicators of Life-Threatening Malaria in African Children

Marsh, K., Forster, D., Waruiru, C., Mwangi, I., Winstanley, M., Marsh, V., Newton, C. R. J. C., Winstanley, P., Warn, P. A., Peshu, N. M., et al. (1995) · New England Journal of Medicine · doi:10.1056/nejm199505253322102 · Cited by 1,093

Biliverdin reductase: A major physiologic cytoprotectant

Barañano, D. E., Rao, M., Ferris, C. D., & Snyder, S. H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252626999 · Cited by 1,091

Rapid proteolysis of IκB-α is necessary for activation of transcription factor NF-κB

Henkel, T., Machleidt, T., Alkalay, I., Krönke, M., Ben‐Neriah, Y., & Baeuerle, P. A. (1993) · Nature · doi:10.1038/365182a0 · Cited by 1,085

Heme oxygenase-1 mediates the anti-inflammatory effect of interleukin-10 in mice

Lee, T.-S., & Chau, L.-Y. (2002) · Nature Medicine · doi:10.1038/nm0302-240 · Cited by 1,019

p16INK4a induces an age-dependent decline in islet regenerative potential

Krishnamurthy, J., Ramsey, M. R., Ligon, K. L., Torrice, C., Koh, A., Bonner-Weir, S., & Sharpless, N. E. (2006) · Nature · doi:10.1038/nature05092 · Cited by 1,003

Identification of a Molecular Signaling Network that Regulates a Cellular Necrotic Cell Death Pathway

Hitomi, J., Christofferson, D. E., Ng, A., Yao, J., Degterev, A., Xavier, R. J., & Yuan, J. (2008) · Cell · doi:10.1016/j.cell.2008.10.044 · Cited by 989

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

More than one way to die: apoptosis, necrosis and reactive oxygen damage

Fiers, W. C., Beyaert, R., Declercq, W., & Vandenabeele, P. (1999) · Oncogene · doi:10.1038/sj.onc.1203249 · Cited by 871

The lipocalin protein family: structural and sequence overview

Flower, D. R., North, A. C. T., & Sansom, C. E. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00148-5 · Cited by 868

Cleavage of the death domain kinase RIP by Caspase-8 prompts TNF-induced apoptosisPreprint

Lin, Y., Devin, A., Rodriguez, Y., & Liu, Z.-G. (1999) · Genes & Development · doi:10.1101/gad.13.19.2514 · Cited by 849

Identification of an Intestinal Heme Transporter

Shayeghi, M., Latunde-Dada, G. O., Oakhill, J. S., Laftah, A. H., Takeuchi, K., Halliday, N., Khan, Y., Warley, A., McCann, F. E., Hider, R. C., et al. (2005) · Cell · doi:10.1016/j.cell.2005.06.025 · Cited by 755

Tumor Necrosis Factor (Cachectin) as an Essential Mediator in Murine Cerebral Malaria

Grau, G. E., Fajardo, L. F., Piguet, P., Allet, B., Lambert, P., & VASSALLI, P. (1987) · Science · doi:10.1126/science.3306918 · Cited by 735

Necrosis, a well-orchestrated form of cell demise: Signalling cascades, important mediators and concomitant immune response

Festjens, N., Vanden Berghe, T., & Vandenabeele, P. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.06.014 · Cited by 710

The E3 Ubiquitin Ligase Itch Couples JNK Activation to TNFα-induced Cell Death by Inducing c-FLIPL Turnover

Chang, L., Kamata, H., Solinas, G., Luo, J.-L., Maeda, S., Venuprasad, K., Liu, Y.-C., & Karin, M. (2006) · Cell · doi:10.1016/j.cell.2006.01.021 · Cited by 706

Bilirubin, formed by activation of heme oxygenase-2, protects neurons against oxidative stress injury

Doré, S., Takahashi, M., Ferris, C. D., Hester, L. D., Guastella, D. B., & Snyder, S. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2445 · Cited by 699

The Stem Cell Marker Bcrp/ABCG2 Enhances Hypoxic Cell Survival through Interactions with Heme

Krishnamurthy, P. C., Ross, D. D., Nakanishi, T., Bailey-Dell, K., Zhou, S., Mercer, K. E., Sarkadi, B., Sorrentino, B. P., & Schuetz, J. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313599200 · Cited by 668

Ferritin heavy chain upregulation by NF-κB inhibits TNFα-induced apoptosis by suppressing reactive oxygen species

Pham, C. G., Bubici, C., Zazzeroni, F., Papa, S., Jones, J., Alvarez, K., Jayawardena, S., De Smaele, E., Cong, R., Beaumont, C., et al. (2004) · Cell · doi:10.1016/j.cell.2004.10.017 · Cited by 663

Hemoprotein Bach1 regulates enhancer availability of heme oxygenase‐1 gene

Sun, J., Hoshino, H., Takaku, K., Nakajima, O., Muto, A., Suzuki, H., Tashiro, S., Takahashi, S., Shibahara, S., Alam, J., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf516 · Cited by 637

Pro-oxidant and cytotoxic effects of circulating heme

Jeney, V., Balla, J., Yachie, A., Varga, Z., Vercellotti, G. M., Eaton, J. W., & Balla, G. (2002) · Blood · doi:10.1182/blood.v100.3.879 · Cited by 633

The endoplasmic reticulum stress response in immunity and autoimmunity

Todd, D. J., Lee, A., & Glimcher, L. H. (2008) · Nature reviews. Immunology · doi:10.1038/nri2359 · Cited by 621

Expression of heme oxygenase-1 can determine cardiac xenograft survival

Soares, M. P., Lin, Y., Anrather, J., Csizmadia, E., Takigami, K., Sato, K., Grey, S. T., Colvin, R. B., Choi, A. M. K., Poss, K. D., et al. (1998) · Nature Medicine · doi:10.1038/2063 · Cited by 613

Endothelial-cell heme uptake from heme proteins: induction of sensitization and desensitization to oxidant damage.

Balla, J., Jacob, H. S., Balla, G., Nath, K. A., Eaton, J. W., & Vercellotti, G. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.20.9285 · Cited by 596

Necroptosis: A Specialized Pathway of Programmed Necrosis

Galluzzi, L., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2008.12.004 · Cited by 561 · cited 1×

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

Both cIAP1 and cIAP2 regulate TNFα-mediated NF-κB activation

Mahoney, D. J., Cheung, H. H., Mrad, R. L., Plenchette, S., Simard, C., Enwere, E., Arora, V., Mak, T. W., Lacasse, E. C., Waring, J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711122105 · Cited by 540

Different Faces of the Heme-Heme Oxygenase System in Inflammation

Wagener, F. A. D. T. G., Volk, H., Willis, D., Abraham, N. G., Soares, M. P., Adema, G. J., & Figdor, C. G. (2003) · Pharmacological Reviews · doi:10.1124/pr.55.3.5 · Cited by 537

Heme mediates derepression of Maf recognition element through direct binding to transcription repressor Bach1

Ogawa, K., Sun, J., Taketani, S., Nakajima, O., Nishitani, C., Sassa, S., Hayashi, N., Yamamoto, M., Shibahara, S., Fujita, H., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.11.2835 · Cited by 532

Bilirubin and glutathione have complementary antioxidant and cytoprotective roles

Sedlak, T. W., Saleh, M., Higginson, D. S., Paul, B. D., Juluri, K. R., & Snyder, S. H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813132106 · Cited by 532

TNF-Induced Activation of the Nox1 NADPH Oxidase and Its Role in the Induction of Necrotic Cell Death

Kim, Y., Morgan, M. J., Choksi, S., & Liu, Z.-G. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.04.021 · Cited by 523

Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts.

Vile, G. F., Modak, S. B., Waltner, C., & Tyrrell, R. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.7.2607 · Cited by 517

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 513

Signaling by Gasotransmitters

Mustafa, A. K., Gadalla, M. M., & Snyder, S. H. (2009) · Science Signaling · doi:10.1126/scisignal.268re2 · Cited by 503

Hemoglobin Scavenger Receptor CD163 Mediates Interleukin-10 Release and Heme Oxygenase-1 Synthesis: Antiinflammatory Monocyte-Macrophage Responses In Vitro, in Resolving Skin Blisters In Vivo, and After Cardiopulmonary Bypass Surgery

Philippidis, P., Mason, J. C., Evans, B. J., Nadra, I., Taylor, K. M., Haskard, D. O., & Landis, R. C. (2004) · Circulation Research · doi:10.1161/01.res.0000109414.78907.f9 · Cited by 476

Identification of the receptor scavenging hemopexin-heme complexes

Hvidberg, V., Maniecki, M. B., Jacobsen, C., Højrup, P., Møller, H. J., & Moestrup, S. K. (2005) · Blood · doi:10.1182/blood-2005-03-1185 · Cited by 473

Heme Oxygenase-1 Modulates the Expression of Adhesion Molecules Associated with Endothelial Cell Activation

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

Carbon Monoxide Generated by Heme Oxygenase-1 Suppresses the Rejection of Mouse-to-Rat Cardiac Transplants

Sato, K., Balla, J., Otterbein, L. E., Smith, R. N., Brouard, S., Lin, Y., Csizmadia, E., Sévigny, J., Robson, S. C., Vercellotti, G. M., et al. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.6.4185 · Cited by 462

Carbon monoxide provides protection against hyperoxic lung injury

Otterbein, L. E., Mantell, L. L., & Choi, A. M. K. (1999) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1999.276.4.l688 · Cited by 439

CO AS A CELLULAR SIGNALING MOLECULE

Kim, H. P., Ryter, S. W., & Choi, A. M. K. (2005) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141053 · Cited by 429

Identification of a Human Heme Exporter that Is Essential for Erythropoiesis

Quigley, J. G., Yang, Z., Worthington, M., Phillips, J. D., Sabo, K. M., Sabath, D. E., Berg, C. L., Sassa, S., Wood, B. L., & Abkowitz, J. L. (2004) · Cell · doi:10.1016/j.cell.2004.08.014 · Cited by 423

Hemin: a possible physiological mediator of low density lipoprotein oxidation and endothelial injury.

Balla, G., Jacob, H. S., Eaton, J. W., Belcher, J. D., & Vercellotti, G. M. (1991) · Arteriosclerosis and Thrombosis A Journal of Vascular Biology · doi:10.1161/01.atv.11.6.1700 · Cited by 421

Heme Oxygenase-1 Protein Localizes to the Nucleus and Activates Transcription Factors Important in Oxidative Stress

Lin, Q., Weis, S., Yang, G., Weng, Y., Helston, R. M., Rish, K. R., Smith, A., Bordner, J., Polte, T., Gaunitz, F., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607954200 · Cited by 420

Hypoxia induces severe right ventricular dilatation and infarction in heme oxygenase-1 null mice

Yet, S., Perrella, M. A., Layne, M. D., Hsieh, C.-M., Maemura, K., Kobzik, L., Wiesel, P., Christou, H. A., Kourembanas, S., & Lee, M.-E. (1999) · Journal of Clinical Investigation · doi:10.1172/jci6163 · Cited by 407

A Heme Export Protein Is Required for Red Blood Cell Differentiation and Iron Homeostasis

Keel, S. B., Doty, R. T., Yang, Z., Quigley, J. G., Chen, J., Knoblaugh, S., Kingsley, P. D., De Domenico, I., Vaughn, M. B., Kaplan, J., et al. (2008) · Science · doi:10.1126/science.1151133 · Cited by 404

Paradoxical rescue from ischemic lung injury by inhaled carbon monoxide driven by derepression of fibrinolysis

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

Hemoglobin research and the origins of molecular medicine

Schechter, A. N. (2008) · Blood · doi:10.1182/blood-2008-04-078188 · Cited by 397

Haptoglobin, inflammation and disease

Quaye, I. K. (2008) · Transactions of the Royal Society of Tropical Medicine and Hygiene · doi:10.1016/j.trstmh.2008.04.010 · Cited by 388

Programmed cell death in Caenorhabditis elegans

Hengartner, M. O., & Horvitz, H. R. (1994) · Current Opinion in Genetics & Development · doi:10.1016/0959-437x(94)90076-f · Cited by 378

How Many Transcription Factors Does It Take to Turn On the Heme Oxygenase-1 Gene?

Alam, J., & Cook, J. L. (2006) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2006-0340tr · Cited by 378

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

The role of heme oxygenase-1 promoter polymorphisms in human disease

Exner, M., Minar, E., Wagner, O. F., & Schillinger, M. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.07.008 · Cited by 359

Identification of a mammalian mitochondrial porphyrin transporter

Krishnamurthy, P. C., Du, G., Fukuda, Y., Sun, D., Sampath, J., Mercer, K. E., Wang, J., Sosa‐Pineda, B., Murti, K. G., & Schuetz, J. D. (2006) · Nature · doi:10.1038/nature05125 · Cited by 358

ROLE OF ABCG2/BCRP IN BIOLOGY AND MEDICINE

Krishnamurthy, P., & Schuetz, J. D. (2005) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141238 · Cited by 357

Donor Toll-like receptor 4 contributes to ischemia and reperfusion injury following human kidney transplantation

Krüger, B., Krick, S., Dhillon, N. K., Lerner, S., Ames, S. A., Bromberg, J. S., Lin, M., Walsh, L., Vella, J. P., Fischereder, M., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810169106 · Cited by 355

Tumor necrosis factor's cytotoxic activity is signaled by the p55 TNF receptor

Tartaglia, L. A., Rothe, M., Hu, Y.-F., & Goeddel, D. V. (1993) · Cell · doi:10.1016/0092-8674(93)90222-c · Cited by 339

Structure-function analysis of the antioxidant properties of haptoglobin

Melamed‐Frank, M., Lache, O., Enav, B. I., Szafranek, T., Levy, N. S., Ricklis, R. M., & Levy, A. P. (2001) · Blood · doi:10.1182/blood.v98.13.3693 · Cited by 339

Disorders of red cell membrane

An, X., & Mohandas, N. (2008) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07091.x · Cited by 338

Heme Induces Ubiquitination and Degradation of the Transcription Factor Bach1

Zenke-Kawasaki, Y., Dohi, Y., Katoh, Y., Ikura, T., Ikura, M., Asahara, T., Tokunaga, F., Iwaï, K., & Igarashi, K. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02415-06 · Cited by 330

Heme oxygenase-1–derived carbon monoxide enhances the host defense response to microbial sepsis in mice

Chung, S. W., Liu, X., Macias, A. A., Baron, R. M., & Perrella, M. A. (2008) · Journal of Clinical Investigation · doi:10.1172/jci32730 · Cited by 324

Carbon monoxide signals via inhibition of cytochrome c oxidase and generation of mitochondrial reactive oxygen species

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

Haem homeostasis is regulated by the conserved and concerted functions of HRG-1 proteins

Rajagopal, A., Rao, A. U., Amigo, J., Tian, M., Upadhyay, S. K., Hall, C., Uhm, S., Mathew, M. K., Fleming, M. D., Paw, B. H., et al. (2008) · Nature · doi:10.1038/nature06934 · Cited by 316

The biochemistry of heme biosynthesis

Heinemann, I. U., Jahn, M., & Jahn, D. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.02.015 · Cited by 311

Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron.

Eisenstein, R. S., García-Mayol, D., Pettingell, W. H., & Munro, H. N. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.3.688 · Cited by 308

Heme Oxygenase-1-derived Carbon Monoxide Requires the Activation of Transcription Factor NF-κB to Protect Endothelial Cells from Tumor Necrosis Factor-α-mediated Apoptosis

Brouard, S., Berberat, P. O., Tobiasch, E., Seldon, M. P., Bach, F. H., & Soares, M. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108317200 · Cited by 306

Peroxiredoxins, Oxidative Stress, and Cell Proliferation

Immenschuh, S., & Baumgart‐Vogt, E. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.768 · Cited by 303

Regulation by Heme of Mitochondrial Protein Transport Through a Conserved Amino Acid Motif

Lathrop, J. T., & Timko, M. P. (1993) · Science · doi:10.1126/science.8424176 · Cited by 288

Stromal cell–derived factor 1 promotes angiogenesis via a heme oxygenase 1–dependent mechanism

Deshane, J. S., Chen, S., Caballero, S., Grochot‐Przeczek, A., Waś, H., Calzi, S. L., Lach, R., Hock, T., Chen, B., Hill‐Kapturczak, N., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20061609 · Cited by 284

Absence of heme oxygenase‐1 exacerbates atherosclerotic lesion formation and vascular remodeling

Yet, S., Layne, M. D., Liu, X., Chen, Y., Ith, B., Sibinga, N. E. S., & Perrella, M. A. (2003) · The FASEB Journal · doi:10.1096/fj.03-0187fje · Cited by 283

Carbon monoxide, reactive oxygen signaling, and oxidative stress

Piantadosi, C. A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.013 · Cited by 281

Hemoglobin and heme scavenging

Ascenzi, P., Bocedi, A., Visca, P., Altruda, F., Tolosano, E., Beringhelli, T., & Fasano, M. (2005) · IUBMB Life (International Union of Biochemistry and Molecular Biology: Life) · doi:10.1080/15216540500380871 · Cited by 280

Heme oxygenase-1 affords protection against noncerebral forms of severe malaria

Seixas, E., Gozzelino, R., Chora, Â., Ferreira, A., Silva, G., Larsen, R., Rebelo, S., Penido, C., Smith, N. R., Coutinho, A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903419106 · Cited by 275

Brain Injury After Intracerebral Hemorrhage: The Role of Thrombin and Iron

Hua, Y., Keep, R. F., Hoff, J. T., & Xi, G. (2007) · Stroke · doi:10.1161/01.str.0000247868.97078.10 · Cited by 273

Heme 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

Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains.

Baker, E. N., Paoli, M., Anderson, B. F., Baker, H. M., Morgan, W. T., & Smith, A. (1999) · Nature Structural Biology · doi:10.1038/13294 · Cited by 254

Nerve Growth Factor Protects against 6-Hydroxydopamine-induced Oxidative Stress by Increasing Expression of Heme Oxygenase-1 in a Phosphatidylinositol 3-Kinase-dependent Manner

Salinas, M., Díaz, R. G., Abraham, N. G., de Galarreta, C. M. R., & Cuadrado, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209164200 · Cited by 247

Dealing with iron: Common structural principles in proteins that transport iron and heme

Baker, H. M., Anderson, B. F., & Baker, E. N. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0637295100 · Cited by 243

Necrotic Death Pathway in FAS Receptor Signaling

Matsumura, H., Shimizu, Y., Ohsawa, Y., Kawahara, A., Uchiyama, Y., & Nagata, S. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.6.1247 · Cited by 242

Bilirubin

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

Red cell pyruvate kinase deficiency: molecular and clinical aspects

Zanella, A., Fermo, E., Bianchi, P. I., & Valentini, G. (2005) · British Journal of Haematology · doi:10.1111/j.1365-2141.2005.05527.x · Cited by 240

Hemolysis in Cardiac Surgery Patients Undergoing Cardiopulmonary Bypass: A Review in Search of a Treatment Algorithm

Vercaemst, L. (2008) · Journal of ExtraCorporeal Technology · doi:10.1051/ject/200840257 · Cited by 238

Heme oxygenase: Protective gene or Trojan horse

Platt, J. L., & Nath, K. A. (1998) · Nature Medicine · doi:10.1038/3947 · Cited by 236

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 236

Regulation of reactive oxygen species, DNA damage and c-Myc function by peroxiredoxin 1

Egler, R. A., Fernandes, E. R., Rothermund, K. D., Sereika, S. M., de Souza-Pinto, N. C., Jaruga, P., Dizdaroğlu, M., & Prochownik, E. V. (2005) · Oncogene · doi:10.1038/sj.onc.1208821 · Cited by 234

The effect of hemin on the synthesis of globin

Bruns, G. P., & London, I. M. (1965) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(65)90746-1 · Cited by 229

p38α Mitogen-activated Protein Kinase Sensitizes Cells to Apoptosis Induced by Different Stimuli

Porrás, A., Zuluaga, S., Black, E. V. I., Valladares, A., Alvarez, A. M., Ambrosino, C., Benito, M., & Nebreda, Á. R. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-08-0592 · Cited by 229

Hypoxia-inducible factor 1α stabilization by carbon monoxide results in cytoprotective preconditioning

Chin, 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

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

Biliverdin administration protects against endotoxin-induced acute lung injury in rats

Sarady, J. K., Liu, F., Gallo, D. J., Nakao, A., Overhaus, M., Öllinger, R., Choi, A. M. K., & Otterbein, L. E. (2005) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00458.2004 · Cited by 220

Identification of a Second Region Upstream of the Mouse Heme Oxygenase-1 Gene That Functions as a Basal Level and Inducer-dependent Transcription Enhancer

Alam, J., Camhi, S. L., & Choi, A. M. K. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.11977 · Cited by 217

Heme Oxygenase: Evolution, Structure, and Mechanism

Wilks, A. (2002) · Antioxidants and Redox Signaling · doi:10.1089/15230860260220102 · Cited by 213

Induction of Heme Oxygenase-1 Expression in Murine Macrophages Is Essential for the Anti-inflammatory Effect of Low Dose 15-Deoxy-Δ12,14-prostaglandin J2

Lee, T., Tsai, H.-L., & Chau, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300498200 · Cited by 212

Heme Oxygenase-1

Stocker, R., & Perrella, M. A. (2006) · Circulation · doi:10.1161/circulationaha.105.598698 · Cited by 210

Hemin: a possible physiological mediator of low density lipoprotein oxidation and endothelial injury.

GBalla, SJacob, H., WEaton, J., DBelcher, J., & MVercellotti, G. (1991) · Arteriosclerosis and Thrombosis A Journal of Vascular Biology · Cited by 209

Heavy chain ferritin acts as an anti‐apoptotic gene that protects livers from ischemia‐reperfusion injury

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

A central role for free heme in the pathogenesis of severe malaria: the missing link?

Ferreira, A., Balla, J., Jeney, V., Balla, G., & Soares, M. P. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0368-5 · Cited by 205

Myeloid heme oxygenase–1 regulates innate immunity and autoimmunity by modulating IFN-β production

Tzima, S., Victoratos, P., Kranidioti, K., Alexiou, M. V., & Kollias, G. A. (2009) · The Journal of Experimental Medicine · doi:10.1084/jem.20081582 · Cited by 204

Heme oxygenase‐1‐derived carbon monoxide protects hearts from transplant‐associated ischemia reperfusion injury

Akamatsu, 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

Bifunctional role for VEGF-induced heme oxygenase-1 in vivo: induction of angiogenesis and inhibition of leukocytic infiltration

Bussolati, B., Ahmed, A., Pemberton, H. N., Landis, R. C., Carlo, F. D., Haskard, D. O., & Mason, J. C. (2003) · Blood · doi:10.1182/blood-2003-06-1974 · Cited by 199

Carbon monoxide differentially modulates STAT1 and STAT3 and inhibits apoptosis via a phosphatidylinositol 3-kinase/Akt and p38 kinase-dependent STAT3 pathway during anoxia-reoxygenation injury

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

Endotoxin-Induced Mortality Is Related to Increased Oxidative Stress and End-Organ Dysfunction, Not Refractory Hypotension, in Heme Oxygenase-1–Deficient Mice

Wiesel, P., Patel, A. P., DiFonzo, N., Marria, P. B., Sim, C. U., Pellacani, A. U. E., Maemura, K., LeBlanc, B. W., Marino, K., Doerschuk, C. M., et al. (2000) · Circulation · doi:10.1161/01.cir.102.24.3015 · Cited by 191

Regulation of NF-κB RelA Phosphorylation and Transcriptional Activity by p21 and Protein Kinase Cζ in Primary Endothelial Cells

Anrather, J., Csizmadia, V., Soares, M. P., & Winkler, H. J. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13594 · Cited by 185

Hemolysis in cardiac surgery patients undergoing cardiopulmonary bypass: a review in search of a treatment algorithm.

Vercaemst, L. (2008) · PubMed · doi:10.1051/ject/200840257/pdf · Cited by 181

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

Pleiotropic functions of biliverdin reductase: cellular signaling and generation of cytoprotective and cytotoxic bilirubin

Kapitulnik, J., & Maines, M. D. (2009) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2008.12.003 · Cited by 178

Carbon Monoxide Induces Heme Oxygenase-1 via Activation of Protein Kinase R–Like Endoplasmic Reticulum Kinase and Inhibits Endothelial Cell Apoptosis Triggered by Endoplasmic Reticulum Stress

Kim, K. M., Pae, H., Zheng, M., Park, R., Kim, Y., & Chung, H. (2007) · Circulation Research · doi:10.1161/circresaha.107.154781 · Cited by 178

Randomized Trial of Volume Expansion with Albumin or Saline in Children with Severe Malaria: Preliminary Evidence of Albumin Benefit

Maitland, K., Pamba, A., English, M., Peshu, N. M., Marsh, K., Newton, C. R. J. C., & Levin, M. (2005) · Clinical Infectious Diseases · doi:10.1086/427505 · Cited by 174

Toll‐Like Receptor and Heme Oxygenase‐1 Signaling in Hepatic Ischemia/Reperfusion Injury

Shen, X., Ke, B., Zhai, Y., Gao, F., Busuttil, R. W., Cheng, G., & Kupiec‐Weglinski, J. W. (2005) · American Journal of Transplantation · doi:10.1111/j.1600-6143.2005.00932.x · Cited by 171

Microsatellite polymorphism in the human heme oxygenase-1 gene promoter and its application in association studies with Alzheimer and Parkinson disease

Kimpara, T., Takeda, A., Watanabe, K., Itoyama, Y., Ikawa, S., Watanabe, M., Arai, H., Sasaki, H., Higuchi, S., Okita, N., et al. (1997) · Human Genetics · doi:10.1007/s004390050480 · Cited by 169

Biliverdin Therapy Protects Rat Livers From Ischemia and Reperfusion Injury

Fondevila, C., Shen, X.-D., 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 167

Microsatellite polymorphism in heme oxygenase-1 gene promoter is associated with susceptibility to oxidant-induced apoptosis in lymphoblastoid cell lines

Hirai, H., Kubo, H., Yamaya, M., Nakayama, K., Numasaki, M., Kobayashi, S., Suzuki, S., Shibahara, S., & Sasaki, H. (2003) · Blood · doi:10.1182/blood-2002-12-3733 · Cited by 164

The antioxidant defense protein heme oxygenase 1 is a novel target for statins in endothelial cells

Grosser, N., Hemmerle, A., Berndt, G., Erdmann, K., Hinkelmann, U., Schürger, S., Wijayanti, N., Immenschuh, S., & Schröder, H. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.09.009 · Cited by 158

HEME OXYGENASE-1 OVEREXPRESSION PROTECTS RAT HEARTS FROM COLD ISCHEMIA/REPERFUSION INJURY VIA AN ANTIAPOPTOTIC PATHWAY1

Katori, M., Buelow, R., Ke, B., Ma, J., Coito, A. J., Iyer, S., Southard, D., Busuttil, R. W., & Kupiec‐Weglinski, J. W. (2002) · Transplantation · doi:10.1097/00007890-200201270-00023 · Cited by 157

Carbon Monoxide Orchestrates a Protective Response through PPARγ

Bilban, M., Bach, F. H., Otterbein, S. L., Ifedigbo, E., d’Avila, J. C., Esterbauer, H., Chin, B. Y., Usheva, A., Robson, S. C., Wagner, O. F., et al. (2006) · Immunity · doi:10.1016/j.immuni.2006.03.012 · Cited by 155

Isolation and characterization of the mouse heme oxygenase-1 gene. Distal 5' sequences are required for induction by heme or heavy metals.

Alam, J., Cai, J., & Smith, A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42211-3 · Cited by 152

Heme oxygenase-1 induction may explain the antioxidant profile of aspirin

Grosser, N., Abate, A., Oberle, S., Vreman, H. J., Dennery, P. A., Becker, J. C., Pohle, T., Seidman, D. S., & Schröder, H. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01504-3 · Cited by 151

Defective Recovery and Severe Renal Damage After Acute Hemolysis in Hemopexin-Deficient Mice

Tolosano, E., Hirsch, E., Patrucco, E., Camaschella, C., Navone, R., Silengo, L., & Altruda, F. (1999) · Blood · doi:10.1182/blood.v94.11.3906 · Cited by 149

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

Differentiation and erythropoietin receptor gene expression in human erythroid progenitor cells [see comments]

Wickrema, A., Krantz, S. B., Winkelmann, J., & Bondurant, M. C. (1992) · Blood · doi:10.1182/blood.v80.8.1940.1940 · Cited by 146

Kinetics of hemin distribution in plasma reveals its role in lipoprotein oxidation

Miller, Y. I., & Shaklai, N. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(99)00027-7 · Cited by 145

Purification, characterization, and cloning of a heme-binding protein (23 kDa) in rat liver cytosol

Iwahara, S.-I., Satoh, H., Song, D.-X., Webb, J., Burlingame, A. L., Nagae, Y., & Müller‐Eberhard, U. (1995) · Biochemistry · doi:10.1021/bi00041a017 · Cited by 140

Therapeutic Applications of Bilirubin and Biliverdin in Transplantation

Öllinger, R., Wang, H., Yamashita, K., Wegiel, B., Thomas, M. N., Margreiter, R., & Bach, F. H. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1807 · Cited by 140

Cloning of the cellular receptor for feline leukemia virus subgroup C (FeLV-C), a retrovirus that induces red cell aplasia

Quigley, J. G., Burns, C. C., Anderson, M. M., Lynch, E. D., Sabo, K. M., Overbaugh, J. M., & Abkowitz, J. L. (2000) · Blood · doi:10.1182/blood.v95.3.1093.003k01_1093_1099 · Cited by 139

Heme Oxygenase-1 Inhibits the Expression of Adhesion Molecules Associated with Endothelial Cell Activation via Inhibition of NF-κB RelA Phosphorylation at Serine 276

Seldon, M. P., Silva, G. P. D. L., Pejanovic, N., Larsen, R., Grégoire, I. P., Filipe, J. C.-R., Anrather, J., & Soares, M. P. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.11.7840 · Cited by 135

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

Hemin binding and oxidation of lipoproteins in serum: mechanisms and effect on the interaction of LDL with human macrophages

Camejo, G., Halberg, C., Manschik-Lundin, A., Hurt‐Camejo, E., Rosengren, B. E., Olsson, H., Hansson, G. I., Forsberg, G., & Ylhen, B. (1998) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)32564-5 · Cited by 134

Modulation of Endothelial Cell Apoptosis by Heme Oxygenase-1-Derived Carbon Monoxide

Soares, M. P., Usheva, A., Brouard, S., Berberat, P. O., Günther, L., Tobiasch, E., & Bach, F. H. (2002) · Antioxidants and Redox Signaling · doi:10.1089/152308602753666370 · Cited by 132

Biliverdin Reductase of Guinea Pig Liver

Singleton, J. W., & Laster, L. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97023-7 · Cited by 130

Upgrading the BCL-2 Network

Galonek, H. L., & Hardwick, J. M. (2006) · Nature Cell Biology · doi:10.1038/ncb1206-1317 · Cited by 128

Heme Oxygenase 1 Gene Transfer Prevents CD95/Fas Ligand-Mediated Apoptosis and Improves Liver Allograft Survival via Carbon Monoxide Signaling Pathway

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 127

The molecular biology of thrombotic microangiopathy

Tsai, H. (2006) · Kidney International · doi:10.1038/sj.ki.5001535 · Cited by 125

Processing of the lipocalin α1-microglobulin by hemoglobin induces heme-binding and heme-degradation properties

Allhorn, M., Berggård, T., Nordberg, J., Olsson, M. L., & Åkerström, B. (2002) · Blood · doi:10.1182/blood.v99.6.1894 · Cited by 124

Bach1, a heme‐dependent transcription factor, reveals presence of multiple heme binding sites with distinct coordination structure

Hira, S., Tomita, T., Matsui, T., Igarashi, K., & Ikeda‐Saito, M. (2007) · IUBMB Life · doi:10.1080/15216540701225941 · Cited by 118

Heme regulates hepatic 5-aminolevulinate synthase mRNA expression by decreasing mRNA half-life and not by altering its rate of transcription

Hamilton, J. W., Bement, W. J., Sinclair, P. R., Sinclair, J. F., Alcedo, J., & Wetterhahn, K. E. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90428-l · Cited by 114

Recent advances in mammalian haem transport

Latunde-Dada, G. O., Simpson, R. J., & McKie, A. T. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.01.005 · Cited by 113

Heme oxygenase‐1: a therapeutic amplification funnel

Bach, F. H. (2005) · The FASEB Journal · doi:10.1096/fj.04-3485cmt · Cited by 113

Induction of heme oxygenase-1 by hypoxia and free radicals in human dermal fibroblasts

Panchenko, M. V., Farber, H. W., & Korn, J. H. (2000) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2000.278.1.c92 · Cited by 113

Redox regulation of the transcriptional repressor Bach1

Ishikawa, M., Numazawa, S., & Yoshida, T. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.01.021 · Cited by 112

Volume Expansion with Albumin Compared to Gelofusine in Children with Severe Malaria: Results of a Controlled Trial

Akech, S., Gwer, S., Idro, R., Fegan, G., Eziefula, C., Newton, C. R. J. C., Levin, M., & Maitland, K. (2006) · PLoS Clinical Trials · doi:10.1371/journal.pctr.0010021 · Cited by 112

Protein kinase Akt/PKB phosphorylates heme oxygenase‐1 in vitro and in vivo

Salinas, M., Wang, J., de Sagarra, M. R., Martı́n, D., Rojo, A. I., Martı́n-Pérez, J., de Montellano, P. R. O., & Cuadrado, A. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.10.077 · Cited by 110

Rapamycin Induces Heme Oxygenase-1 in Human Pulmonary Vascular Cells

Visner, G. A., Lu, F., Zhou, H., Liu, J., Kazemfar, K., & Agarwal, A. (2003) · Circulation · doi:10.1161/01.cir.0000048191.75585.60 · Cited by 109

Heme oxygenase induction mediates the photoimmunoprotective activity of UVA radiation in the mouse

Reeve, V. E., & Tyrrell, R. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.9317 · Cited by 109

Hemin-induced necroptosis involves glutathione depletion in mouse astrocytes

Laird, M. D., Wakade, C. G., Alleyne, C. H., & Dhandapani, K. M. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.07.003 · Cited by 108

Differentiation and erythropoietin receptor gene expression in human erythroid progenitor cells [see comments]

Wickrema, A., Krantz, S. B., Winkelmann, J., et al. (1992) · Blood · doi:10.1182/blood.v80.8.1940.bloodjournal8081940 · Cited by 108

Limited Role for the Bilirubin-Biliverdin Redox Amplification Cycle in the Cellular Antioxidant Protection by Biliverdin Reductase

Maghzal, G. J., Leck, M.-C., Collinson, E. J., Li, C., & Stocker, R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.037119 · Cited by 106

Transfer of heme from heme-albumin to hemopexin

Morgan, W. T., Liem, H. H., Sutor, R. P., & Müller‐Eberhard, U. (1976) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(76)90387-1 · Cited by 106

Probucol Protects Against Smooth Muscle Cell Proliferation by Upregulating Heme Oxygenase-1

Deng, Y., Wu, B. J., Witting, P. K., & Stocker, R. (2004) · Circulation · doi:10.1161/01.cir.0000142610.10530.25 · Cited by 106

The ABC Transporter Abcg2/Bcrp: Role in Hypoxia Mediated Survival

Krishnamurthy, P. C., & Schuetz, J. D. (2005) · BioMetals · doi:10.1007/s10534-005-3709-7 · Cited by 104

The Antiapoptotic Effect of Heme Oxygenase-1 in Endothelial Cells Involves the Degradation of p38α MAPK Isoform

Silva, G. P. D. L., Cunha, A., Grégoire, I. P., Seldon, M. P., & Soares, M. P. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.3.1894 · Cited by 103

Heme-oxygenase-1-induced protection against hypoxia/reoxygenation is dependent on biliverdin reductase and its interaction with PI3K/Akt pathway

Pachori, A. S., Smith, A. M., McDonald, P. H., Zhang, L., Dzau, V. J., & Melo, L. G. (2007) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2007.08.003 · Cited by 103

Exchange of heme among hemoglobin molecules.

Bunn, H. F., & Jandl, J. H. (1966) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.56.3.974 · Cited by 103

Polymorphisms of TNF-enhancer and gene for FcγRIIa correlate with the severity of falciparum malaria in the ethnically diverse Indian population

Sinha, S., Mishra, S. K., Sharma, S., Patibandla, P. K., Mallick, P. K., Sharma, S. K., Mohanty, S., Pati, S. S., Mishra, S. K., Ramteke, B. K., et al. (2008) · Malaria Journal · doi:10.1186/1475-2875-7-13 · Cited by 100

Biliverdin protects against polymicrobial sepsis by modulating inflammatory mediators

Overhaus, M., Moore, B. A., Barbato, J. E., Behrendt, F. F., Doering, J. G., & Bauer, A. J. (2006) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00152.2005 · Cited by 100

From death receptor to reactive oxygen species and c‐Jun N‐terminal protein kinase: the receptor‐interacting protein 1 odyssey

Temkin, V., & Karin, M. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00560.x · Cited by 99

Protection of Human Vascular Smooth Muscle Cells From H 2 O 2 -Induced Apoptosis Through Functional Codependence Between HO-1 and AKT

Brunt, K. R., Fenrich, K. K., Kiani, G., Tse, M. Y., Pang, S. C.-N., Ward, C. A., & Melo, L. G. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000236204.37119.8d · Cited by 98

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

Long range interaction of cis‐DNA elements mediated by architectural transcription factor Bach1

Yoshida, C., Tokumasu, F., Hohmura, K. I., Bungert, J., Hayashi, N., Nagasawa, T., Engel, J. D., Yamamoto, M. P., Takeyasu, K., & Igarashi, K. (1999) · Genes to Cells · doi:10.1046/j.1365-2443.1999.00291.x · Cited by 96

Statin‐mediated cytoprotection of human vascular endothelial cells: a role for Kruppel‐like factor 2‐dependent induction of heme oxygenase‐1

ALI, F., Hamdulay, S., Kinderlerer, A. R., Boyle, J. J., Lidington, E. A., Yamaguchi, T., Soares, M. P., Haskard, D. O., RANDI, A. M., & Mason, J. C. (2007) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2007.02787.x · Cited by 92

Cellular Protection Mechanisms against Extracellular Heme

Eskew, J. D., Vanacore, R., Sung, L., Morales, P. J. C., & Smith, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.2.638 · Cited by 91

Heme Oxygenases in Pregnancy II: HO‐2 is Downregulated in Human Pathologic Pregnancies

Zenclussen, A. C., Lim, E., Knoeller, S., Knackstedt, M., Hertwig, K., Hagen, E. H., Klapp, B. F., & Arck, P. (2003) · American Journal of Reproductive Immunology · doi:10.1034/j.1600-0897.2003.00047.x · Cited by 91

cis-Acting Element-specific Transcriptional Activity of Differentially Phosphorylated Nuclear Factor-κB

Anrather, J., Racchumi, G., & Iadecola, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409344200 · Cited by 90

Modulation of oxidative stress as an anticancer strategy

Gorrini, C., Harris, I. S., & Mak, T. W. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4002 · Cited by 3,579

Oxidative Stress in Cancer

Hayes, J. D., Dinkova-Kostova, A. T., & Tew, K. D. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.06.001 · Cited by 2,654

Role of Nrf2/HO-1 system in development, oxidative stress response and diseases: an evolutionarily conserved mechanism

Łoboda, A., Damulewicz, M., Pyza, E., Józkowicz, A., & Dulak, J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2223-0 · Cited by 2,709

Transcriptional Regulation by Nrf2

Tonelli, C., Chio, I. I. C., & Tuveson, D. A. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7342 · Cited by 2,280

Disease Tolerance as a Defense Strategy

Medzhitov, R., Schneider, D. S., & Soares, M. P. (2012) · Science · doi:10.1126/science.1214935 · Cited by 1,718

Preface

(1969) · Annual Review of Pharmacology · doi:10.1146/annurev.pa.9.051606.100001

How I Am

Leake, C. D. (1976) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.16.040176.000245 · Cited by 4

Review of Reviews

Way, E. L. (1981) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.21.040181.003133 · Cited by 2

Host Biochemical Defense Mechanisms Against Prooxidants

Cotgreave, I. A. (1988) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.28.1.189 · Cited by 4

Reminiscences in Pharmacology: Auld Acquaintance Ne'er Forgot

Welch, A. D. (1985) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.25.040185.000245 · Cited by 3