Hydrogen peroxide in inflammation: Messenger, guide, and assassin

Methods in Enzymology , Vol

Colowick, S. P., Joshi, M. D., Jagannathan, & KAPLAN, N. O. (1966) · Cited by 26,137 · see citing works

Inflammation and cancer

Coussens, L. M., & Werb, Z. (2002) · Nature · doi:10.1038/nature01322 · Cited by 15,111 · see citing works

Dendritic cells and the control of immunity

Banchereau, J., & Steinman, R. M. (1998) · Nature · doi:10.1038/32588 · Cited by 14,244 · see citing works

Pattern Recognition Receptors and Inflammation

Takeuchi, O., & Akira, S. (2010) · Cell · doi:10.1016/j.cell.2010.01.022 · Cited by 8,895 · see citing works

Inflammation in atherosclerosis

Libby, P. (2002) · Nature · doi:10.1038/nature01323 · Cited by 8,315 · see citing works

The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology

Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989 · see citing works

Sterile inflammation: sensing and reacting to damage

Chen, G. Y., & Nuñez, G. (2010) · Nature Reviews Immunology · doi:10.1038/nri2873 · Cited by 3,051 · see citing works

Resolution of inflammation: the beginning programs the end

Serhan, C. N., & Savill, J. (2005) · Nature Immunology · doi:10.1038/ni1276 · Cited by 2,552 · see citing works

Myeloperoxidase: friend and foe

Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282 · see citing works

A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish

Niethammer, P., Grabher, C., Look, A. T., & Mitchison, T. J. (2009) · Nature · doi:10.1038/nature08119 · Cited by 1,541 · see citing works

Genetically encoded fluorescent indicator for intracellular hydrogen peroxide

Belousov, V. V., Fradkov, A. F., Lukyanov, K. A., Staroverov, D. B., Shakhbazov, K., Terskikh, A. V., & Lukyanov, S. (2006) · Nature Methods · doi:10.1038/nmeth866 · Cited by 1,260 · see citing works

Reactive oxygen species, cell signaling, and cell injury

Hensley, K., Robinson, K. A., Gabbita, S. P., Salsman, S., & Floyd, R. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00252-5 · Cited by 1,021 · see citing works

The interface between innate and adaptive immunity

Hoebe, K. H. N., Janssen, E. M., & Beutler, B. (2004) · Nature Immunology · doi:10.1038/ni1004-971 · Cited by 919 · see citing works

Reactive oxygen species prime Drosophila haematopoietic progenitors for differentiation

Owusu-Ansah, E., & Banerjee, U. (2009) · Nature · doi:10.1038/nature08313 · Cited by 742 · see citing works

Redox signaling in macrophages.

Forman, H., & Torres, M. (2001) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(01)00010-3 · Cited by 539 · see citing works

Oxidative Innate Immune Defenses by Nox/Duox Family NADPH Oxidases

Rada, B., & Leto, T. L. (2008) · KARGER eBooks · doi:10.1159/000136357 · Cited by 449 · see citing works

Lyn is a redox sensor that mediates leukocyte wound attraction in vivo

Yoo, S. K., Starnes, T. W., Deng, Q., & Anna Huttenlocher, A. (2011) · Nature · doi:10.1038/nature10632 · Cited by 442 · see citing works

Assembly of the phagocyte NADPH oxidase

Nauseef, W. M. (2004) · Histochemistry and Cell Biology · doi:10.1007/s00418-004-0679-8 · Cited by 427 · see citing works

Reactive Oxygen Species as Downstream Mediators of Angiogenic Signaling by Vascular Endothelial Growth Factor Receptor-2/KDR

Colavitti, R., Pani, G., Bedogni, B., Anzevino, R., Borrello, S., Waltenberger, J. L., & Galeotti, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107711200 · Cited by 384 · see citing works

Distinct mitochondrial retrograde signals control the G1-S cell cycle checkpoint

Owusu-Ansah, E., Yavari, A., Mandal, S., & Banerjee, U. K. (2008) · Nature Genetics · doi:10.1038/ng.2007.50 · Cited by 364 · see citing works

Redox signals in wound healing

Sen, C. K., & Roy, S. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.01.006 · Cited by 349 · see citing works

Molecular evolution of the reactive oxygen-generating NADPH oxidase (Nox/Duox) family of enzymes

Kawahara, T., Quinn, M. T., & Lambeth, J. D. (2007) · BMC Evolutionary Biology · doi:10.1186/1471-2148-7-109 · Cited by 336 · see citing works

Hydrogen peroxide stimulates macrophages and monocytes to actively release HMGB1

Tang, D., Shi, Y., Kang, R., Li, T., Xiao, W., Wang, H., & Xiao, X. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0806540 · Cited by 312 · see citing works

The NADPH Oxidase NOX4 Drives Cardiac Differentiation: Role in Regulating Cardiac Transcription Factors and MAP Kinase Activation

Li, J., Stouffs, M., Serrander, L., Bánfi, B., Bettiol, E., Charnay, Y., Steger, K., Krause, K., & Jaconi, M. E. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-06-0532 · Cited by 295 · see citing works

Role of hydrogen peroxide and oxidative stress in healing responses

Rojkind, M., Domı́nguez-Rosales, J. A., Nieto, N., & Greenwel, P. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/pl00012511 · Cited by 264 · see citing works

Glutathione S-Transferase p Elicits Protection against H2O2-induced Cell Death via Coordinated Regulation of Stress Kinases

Yin, Z., Ivanov, V. N., Habelhah, H., Tew, K. D., & Ronai, Z. A. (2000) · PubMed · doi:10.7916/d8571b9j · Cited by 264 · see citing works

Crucial role of the amino-terminal tyrosine residue 42 and the carboxyl-terminal PEST domain of IκBα in NF-κB activation by an oxidative stress

Schoonbroodt, S., Ferreira, V., Best-Belpomme, M., Boelaert, J. R., Legrand-Poels, S., Korner, M., & Piette, J. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.8.4292 · Cited by 263 · see citing works

Role of Nox Family NADPH Oxidases in Host Defense

Leto, T. L., & Geiszt, M. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1549 · Cited by 254 · see citing works

Plasma membrane repair and cellular damage control: The annexin survival kit

Draeger, A., Monastyrskaya, K., & Babiychuk, E. B. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2010.12.027 · Cited by 217 · see citing works

Activation of Dual Oxidases Duox1 and Duox2

Rigutto, S., Hoste, C., Grasberger, H., Milenkovic, M., Communi, D., Dumont, J. E., Corvilain, B., Miot, F., & De Deken, X. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806893200 · Cited by 213 · see citing works

Live Imaging of Innate Immune Cell Sensing of Transformed Cells in Zebrafish Larvae: Parallels between Tumor Initiation and Wound Inflammation

Feng, Y., Santoriello, C., Mione, M., Hurlstone, A. F. L., & Martin, P. B. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000562 · Cited by 200 · see citing works

Hydrogen peroxide induces DNA single- and double-strand breaks in thyroid cells and is therefore a potential mutagen for this organ

Driessens, N., Versteyhe, S., Ghaddhab, C., Burniat, A., Deken, X. D., SANDE, J. V., Dumont, J.-E., Miot, F., & Corvilain, B. (2009) · Endocrine Related Cancer · doi:10.1677/erc-09-0020 · Cited by 200 · see citing works

Prioritization of Competing Damage and Developmental Signals by Migrating Macrophages in the Drosophila Embryo

Moreira, S., Stramer, B. M., Evans, I. R., Wood, W., & Martin, P. B. (2010) · Current Biology · doi:10.1016/j.cub.2010.01.047 · Cited by 194 · see citing works

Redox Regulatory Mechanisms of Cellular Signal Transduction

Gabbita, S. P., Robinson, K. A., Stewart, C. A., Floyd, R. A., & Hensley, K. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1685 · Cited by 179 · see citing works

Extracellular matrix, junctional integrity and matrix metalloproteinase interactions in endothelial permeability regulation*

Alexander, J. S., & Elrod, J. W. (2002) · Journal of Anatomy · doi:10.1046/j.1469-7580.2002.00057.x · Cited by 179 · see citing works

Cellular distribution, metabolism and regulation of the xanthine oxidoreductase enzyme system

Pritsos, C. A. (2000) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(00)00203-9 · Cited by 167 · see citing works

Hydrogen peroxide-induced chemotaxis of mouse peritoneal neutrophils.

Klyubin, I. V., Kirpichnikova, K. M., & Gamaley, I. A. (1996) · PubMed · Cited by 137 · see citing works

Platelet-derived growth factor BB stimulates vasculogenesis of embryonic stem cell-derived endothelial cells by calcium-mediated generation of reactive oxygen species

Lange, S., Heger, J., Euler, G., Wartenberg, M., Piper, H. M., & Sauer, H. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn258 · Cited by 96 · see citing works

Contributions of Myeloperoxidase to Proinflammatory Events: More Than an Antimicrobial System

Nauseef, W. M. (2001) · International Journal of Hematology · doi:10.1007/bf02981994 · Cited by 69 · see citing works

Hydrogen peroxide activation of endothelial cell-associated MMPs during VCAM-1-dependent leukocyte migration.

Cook‐Mills, J. M. (2006) · PubMed · Cited by 53 · see citing works

Superoxide in the pulmonary circulation

Demiryürek, A. T. (1999) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(99)00041-8 · Cited by 44 · see citing works

In Vivo Real-Time Visualization of Leukocytes and Intracellular Hydrogen Peroxide Levels During a Zebrafish Acute Inflammation Assay

Pase, L. B., Nowell, C. J., & Lieschke, G. J. (2012) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-391856-7.00032-9 · Cited by 30 · see citing works

Chronic inflammation in asthma: a contest of persistence vs resolution

Hove, C. L. V., Maes, T., Joos, G., & Tournoy, K. G. (2008) · Allergy · doi:10.1111/j.1398-9995.2008.01772.x · Cited by 27 · see citing works

The Redox Code

Jones, D. P., & Sies, H. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2015.6247 · Cited by 647 · see citing works

Chemistry of Hydrogen Peroxide Formation and Elimination in Mammalian Cells, and Its Role in Various Pathologies

Andrés, C. M. C., Pérez de la Lastra, J. M., Juan, C. A., Plou, F. J., & Pérez-Lebeña, E. (2022) · Stresses · doi:10.3390/stresses2030019 · Cited by 218 · see citing works

The Role of Reactive Species on Innate Immunity

Andrés, C., Pérez de la Lastra, J., Juan, C., Plou, F., & Pérez-Lebeña, E. (2022) · Vaccines · doi:10.3390/vaccines10101735 · Cited by 142 · see citing works

Oxidative induction of pro-inflammatory cytokine formation by human monocyte-derived macrophages following exposure to manganese<i>in vitro</i>

Mokgobu, M. I., Cholo, M. C., Anderson, R., Steel, H. C., Motheo, M. P., Hlatshwayo, T. N., Tintinger, G. R., & Theron, A. J. (2015) · Journal of Immunotoxicology · doi:10.3109/1547691x.2014.902877 · Cited by 30 · see citing works

Model Organism Used in Biological Research: Drosophila Melanogaster

Pansuriya, V. N., & Gupta, A. (2022) · International Journal for Research in Applied Science and Engineering Technology · doi:10.22214/ijraset.2022.41335

Zebrafish as a model organism for nutrition and growth: towards comparative studies of nutritional genomics applied to aquacultured fishes

Ulloa, P. E., Iturra, P., Neira, R., & Araneda, C. (2011) · Reviews in Fish Biology and Fisheries · doi:10.1007/s11160-011-9203-0 · Cited by 124 · see citing works

The Time Is Right to Focus on Model Organism Metabolomes

Edison, A. S., Hall, R. D., Junot, C., Karp, P. D., Kurland, I. J., Mistrík, R., Reed, L. K., Saito, K., Salek, R. M., Steinbeck, C., et al. (2016) · Metabolites · doi:10.3390/metabo6010008 · Cited by 67 · see citing works

Interaction networks: Lessons from large‐scale studies in yeast

Cagney, G. (2009) · PROTEOMICS · doi:10.1002/pmic.200900177 · Cited by 10 · see citing works

Drosophila melanogaster: A Model Organism to Understand Biological Activities of Nanoparticles

Patra, B., Ghosh, P., & Das, S. P. (2020) · Springer eBooks · doi:10.1007/978-981-15-1702-0_10 · Cited by 3 · see citing works