The Plasma Membrane: A Platform for Intra- and Intercellular Redox Signaling
Open accessAbstract
Membranes are of outmost importance to allow for specific signal transduction due to their ability to localize, amplify, and direct signals. However, due to the double-edged nature of reactive oxygen species (ROS)—toxic at high concentrations but essential signal molecules—subcellular localization of ROS-producing systems to the plasma membrane has been traditionally regarded as a protective strategy to defend cells from unwanted side-effects. Nevertheless, specialized regions, such as lipid rafts and caveolae, house and regulate the activated/inhibited states of important ROS-producing systems and concentrate redox targets, demonstrating that plasma membrane functions may go beyond acting as a securing lipid barrier. This is nicely evinced by nicotinamide adenine dinucleotide phosphate (NADPH)-oxidases (NOX), enzymes whose primary function is to generate ROS and which have been shown to reside in specific lipid compartments. In addition, membrane-inserted bidirectional H2O2-transporters modulate their conductance precisely during the passage of the molecules through the lipid bilayer, ensuring time-scaled delivery of the signal. This review aims to summarize current evidence supporting the role of the plasma membrane as an organizing center that serves as a platform for redox signal transmission, particularly NOX-driven, providing specificity at the same time that limits undesirable oxidative damage in case of malfunction. As an example of malfunction, we explore several pathological situations in which an inflammatory component is present, such as inflammatory bowel disease and neurodegenerative disorders, to illustrate how dysregulation of plasma-membrane-localized redox signaling impacts normal cell physiology.
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NOX2 is predominantly expressed in phagocytes and produces a relatively large amount of superoxide in order to kill bacteria within phagosomes in an inflamed area.
“NOX2 is predominantly expressed in phagocytes and produces a relatively large amount of superoxide in order to kill bacteria within phagosomes in an inflamed area [33,34], Figure 13.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [34]
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Functional rafts in cell membranes
Simons, K., & Ikonen, E. (1997) · Nature · doi:10.1038/42408 · Cited by 9,757 · cited 1× · see citing works
“Thus, as result of an asymmetrical distribution of specific lipids, membranes are further organized in lipid rafts (LRs), defined by being detergent-insoluble sphingolipid- and cholesterol-rich domains [65].”
BackgroundThe Fluid Mosaic Model of the Structure of Cell Membranes
Singer, S. J., & Nicolson, G. L. (1972) · Science · doi:10.1126/science.175.4023.720 · Cited by 9,158 · see citing works
Free Radicals in Biology and Medicine
Halliwell, B., & Gutteridge, J. M. C. (2015) · doi:10.1093/acprof:oso/9780198717478.001.0001 · Cited by 8,990 · see citing works
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · 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
Lipid rafts and signal transduction
Simons, K., & Toomre, D. K. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35036052 · Cited by 6,252 · see citing works
AKT/PKB signaling: navigating downstream
Manning, B. D., & Cantley, L. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.009 · Cited by 6,115 · see citing works
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587 · see citing works
Evidence for the Formation of Symmetric and Asymmetric DLPC-DAPC Lipid Bilayer Domains
Ritter, M., Schmidt, S., Jakab, M., Paulmichl, M., & Henderson, R. M. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350122 · Cited by 3,923 · see citing works
ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
D'Autréaux, B., & Toledano, M. B. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2256 · Cited by 3,642 · see citing works
The Treatment-Naive Microbiome in New-Onset Crohn’s Disease
Gevers, D., Kugathasan, S., Denson, L. A., Vázquez-Baeza, Y., Van Treuren, W., Ren, B., Schwager, E., Knights, D., Song, S. J., Yassour, M., et al. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.02.005 · Cited by 3,220 · see citing works
Srimaroeng, C., Cecile, J. P., Walden, R., & Pritchard, J. B. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350077 · Cited by 2,989 · see citing works
Nitric oxide synthases: Roles, tolls, and controls
Nathan, C., & Xie, Q. W. (1994) · Cell · doi:10.1016/0092-8674(94)90266-6 · Cited by 2,920 · see citing works
Abraham, C., & Cho, J. H. (2009) · New England Journal of Medicine · doi:10.1056/nejmra0804647 · Cited by 2,712 · see citing works
Reconciling the chemistry and biology of reactive oxygen species
Winterbourn, C. C. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.85 · Cited by 2,504 · see citing works
Liang, S. C., Tan, X.-Y., Luxenberg, D. P., Karim, R., Dunussi-Joannopoulos, K., Collins, M., & Fouser, L. A. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20061308 · Cited by 2,330 · see citing works
Imlay, J. A. (2003) · Annual Review of Microbiology · doi:10.1146/annurev.micro.57.030502.090938 · Cited by 2,201 · see citing works
Protein S-nitrosylation: Purview and parameters
Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1569 · Cited by 2,153 · see citing works
Sies, H. (2017) · Redox Biology · doi:10.1016/j.redox.2016.12.035 · Cited by 2,148 · see citing works
Cellular mechanisms and physiological consequences of redox-dependent signalling
Holmström, K. M., & Finkel, T. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3801 · Cited by 2,093 · see citing works
Stem cells, self-renewal, and differentiation in the intestinal epithelium.
van der Flier, L. G., & Clevers, H. (2009) · Annual Review of Physiology · doi:10.1146/annurev.physiol.010908.163145 · Cited by 1,859 · see citing works
Chronic Granulomatous Disease: Report on a National Registry of 368 Patients
Winkelstein, J. A., Marino, M. C., Johnston, R. B., Boyle, J., Curnutte, J., Gallin, J. I., Malech, H. L., Holland, S. M., Ochs, H., Quie, P., et al. (2000) · Medicine · doi:10.1097/00005792-200005000-00003 · Cited by 1,728 · see citing works
Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation
Balla, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00028.2012 · Cited by 1,638 · see citing works
Hydrogen peroxide sensing and signaling
Veal, E. A., Day, A. M., & Morgan, B. A. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.016 · Cited by 1,604 · see citing works
Loss of Caveolae, Vascular Dysfunction, and Pulmonary Defects in Caveolin-1 Gene-Disrupted Mice
Dráb, M., Verkade, P., Elger, M., Kasper, M. E., Löhn, M., Lauterbach, B., Menne, J., Lindschau, C., Mende, F., Luft, F. C., et al. (2001) · Science · doi:10.1126/science.1062688 · Cited by 1,555 · see citing works
ALS: A Disease of Motor Neurons and Their Nonneuronal Neighbors
Boillée, S., Velde, C. V., & Cleveland, D. W. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.018 · Cited by 1,426 · see citing works
Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling
Wood, Z. A., Poole, L. B., & Karplus, P. A. (2003) · Science · doi:10.1126/science.1080405 · Cited by 1,369 · see citing works
Specific Aquaporins Facilitate the Diffusion of Hydrogen Peroxide across Membranes
Bienert, G. P., Møller, A. L. B., Kristiansen, K. A., Schulz, A., Møller, I. M., Schjoerring, J. K., & Jahn, T. P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603761200 · Cited by 1,311 · see citing works
Zhang, W., Wang, T., Pei, Z., Miller, D. S., Wu, X., Block, M. L., Wilson, B., Zhang, W., Zhou, Y., Hong, J.-S., et al. (2005) · The FASEB Journal · doi:10.1096/fj.04-2751com · Cited by 1,265 · see citing works
Thiol chemistry and specificity in redox signaling
Winterbourn, C. C., & Hampton, M. B. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.004 · Cited by 1,226 · see citing works
Wu, D. C., Jackson-Lewis, V., Vila, M., Tieu, K., Teismann, P., Vadseth, C., Choi, D.-K., Ischiropoulos, H., & Przedborski, S. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-05-01763.2002 · Cited by 1,183 · see citing works
Membrane transport of hydrogen peroxide
Bienert, G. P., Schjoerring, J. K., & Jahn, T. P. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.02.015 · Cited by 1,079 · see citing works
The basics of thiols and cysteines in redox biology and chemistry
Poole, L. B. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.013 · Cited by 1,031 · see citing works
Nitric oxide synthases: which, where, how, and why?
Michel, T. M., & Féron, O. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119750 · Cited by 1,018 · see citing works
Control of EGF Receptor Signaling by Clathrin-Mediated Endocytosis
Vieira, A. V., Lamaze, C., & Schmid, S. L. (1996) · Science · doi:10.1126/science.274.5295.2086 · Cited by 998 · see citing works
Savina, A., Jancic, C. C., Hugues, S., Guermonprez, P., Vargas, P., Moura, I. C., Lennon‐Duménil, A., Seabra, M. C., Raposo, G., & Amigorena, S. (2006) · Cell · doi:10.1016/j.cell.2006.05.035 · Cited by 896 · see citing works
Reactive Oxygen Species and Neutrophil Function
Winterbourn, C. C., Kettle, A. J., & Hampton, M. B. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014442 · Cited by 885 · see citing works
Mitochondrial proton and electron leaks
Jastroch, M., Divakaruni, A. S., Mookerjee, S., Treberg, J. R., & Brand, M. D. (2010) · Essays in Biochemistry · doi:10.1042/bse0470053 · Cited by 829 · see citing works
A Direct Role for Dual Oxidase in Drosophila Gut Immunity
Ha, E.-M., Oh, C.-T., Bae, Y. S., & Lee, W. (2005) · Science · doi:10.1126/science.1117311 · Cited by 824 · see citing works
Intracellular Ca2+ Sensing: Its Role in Calcium Homeostasis and Signaling
Bagur, R., & Hajnóczky, G. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.028 · Cited by 815 · see citing works
Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
Winterbourn, C. C., & Metodiewa, D. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00051-9 · Cited by 799 · see citing works
Superoxide is the major reactive oxygen species regulating autophagy
Chen, Y., Azad, M. B., & Gibson, S. B. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.49 · Cited by 796 · see citing works
Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis
Henchcliffe, C., & Beal, M. F. (2008) · Nature Clinical Practice Neurology · doi:10.1038/ncpneuro0924 · Cited by 786 · see citing works
Aquaporin-facilitated transmembrane diffusion of hydrogen peroxide
Bienert, G. P., & Chaumont, F. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.09.017 · Cited by 736 · see citing works
Role of Metabolic H2O2 Generation
Sies, H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.544635 · Cited by 734 · see citing works
Sumimoto, H. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06488.x · Cited by 718 · see citing works
Redox signaling: hydrogen peroxide as intracellular messenger
Rhee, S. G. (1999) · Experimental & Molecular Medicine · doi:10.1038/emm.1999.9 · Cited by 701 · see citing works
Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling
Miller, E. W., Dickinson, B. C., & Chang, C. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1005776107 · Cited by 688 · see citing works
Myeloperoxidase: a front-line defender against phagocytosed microorganisms
Klebanoff, S. J., Kettle, A. J., Rosen, H., Winterbourn, C. C., & Nauseef, W. M. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0712349 · Cited by 679 · see citing works
Nox enzymes, ROS, and chronic disease: An example of antagonistic pleiotropy
Lambeth, J. D. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.027 · Cited by 677 · see citing works
Chronic Granulomatous Disease: The European Experience
van den Berg, J. M., van Koppen, E., Åhlin, A., Belohradsky, B. H., Bernatowska, E. A., Corbeel, L., Español, T., Fischer, A., Kurenko-Deptuch, M., Mouy, R., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005234 · Cited by 675 · see citing works
Cloning of Two Human Thyroid cDNAs Encoding New Members of the NADPH Oxidase Family
Deken, X. D., Wang, D., Many, M., Costagliola, S., Libert, F., Vassart, G., Dumont, J. E., & Miot, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000916200 · Cited by 639 · see citing works
Kwon, J., Lee, S.-R., Yang, K.-S., Ahn, Y., Kim, Y. J., Stadtman, E. R., & Rhee, S. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407396101 · Cited by 631 · see citing works
Hofmann, B., Hecht, H., & Flohé, L. (2002) · Biological Chemistry · doi:10.1515/bc.2002.040 · Cited by 620 · see citing works
Woo, H. A., Yim, S. H., Shin, D. H., Kang, D., Yu, D., & Rhee, S. G. (2010) · Cell · doi:10.1016/j.cell.2010.01.009 · Cited by 613 · see citing works
Protein Sulfenic Acids in Redox Signaling
Poole, L. B., Karplus, P. A., & Claiborne, A. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121735 · Cited by 595 · see citing works
Distinct Subcellular Localizations of Nox1 and Nox4 in Vascular Smooth Muscle Cells
Hilenski, L. L., Clempus, R. E., Quinn, M. T., Lambeth, J. D., & Griendling, K. K. (2004) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000112024.13727.2c · Cited by 573 · see citing works
Phosphoinositide Recognition Domains
Lemmon, M. A. (2003) · Traffic · doi:10.1034/j.1600-0854.2004.00071.x · Cited by 564 · see citing works
Parton, R. G. (1996) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(96)80033-0 · Cited by 551 · see citing works
Regulation of Endothelial Nitric Oxide Synthase: Location, Location, Location
Shaul, P. W. (2002) · Annual Review of Physiology · doi:10.1146/annurev.physiol.64.081501.155952 · Cited by 541 · see citing works
NADPH oxidase is the primary source of superoxide induced by NMDA receptor activation
Brennan, A. M., Suh, S. W., Won, S. J., Narasimhan, P., Kauppinen, T. M., Lee, H., Edling, Y., Chan, P. H., & Swanson, R. A. (2009) · Nature Neuroscience · doi:10.1038/nn.2334 · Cited by 538 · see citing works
Ca2+/calmodulin-dependent formation of hydrogen peroxide by brain nitric oxide synthase
Heinzel, B., John, M., Klatt, P., Böhme, E., & Mayer, B. (1992) · Biochemical Journal · doi:10.1042/bj2810627 · Cited by 530 · see citing works
Pediatric Crohn disease patients exhibit specific ileal transcriptome and microbiome signature
Haberman, Y., Tickle, T. L., Dexheimer, P. J., Kim, M., Tang, D., Karns, R. A., Baldassano, R. N., Noe, J. D., Rosh, J. R., Markowitz, J. F., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci75436 · Cited by 521 · see citing works
Fischer, M. T., Sharma, R., Lim, J. L., Haider, L., Frischer, J. M., Drexhage, J., Mahad, D., Bradl, M., van Horssen, J., & Lassmann, H. (2012) · Brain · doi:10.1093/brain/aws012 · Cited by 507 · see citing works
A Cell Surface Receptor Complex for Fibrillar β-Amyloid Mediates Microglial Activation
Bamberger, M. E., Harris, M. E., McDonald, D. R., Husemann, J., & Landreth, G. E. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-07-02665.2003 · Cited by 501 · see citing works
Nox enzymes and new thinking on reactive oxygen: A double-edged sword revisited
Lambeth, J. D., & Neish, A. S. (2014) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012513-104651 · Cited by 495 · see citing works
THE RELATIONSHIP OF EPINEPHRINE AND GLUCAGON TO LIVER PHOSPHORYLASE
Rall, T. W., Sutherland, E. W., & Berthet, J. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65045-8 · Cited by 493 · see citing works
Reactive oxygen generated by Nox1 triggers the angiogenic switch
Arbiser, J. L., Petros, J. A., Klafter, R., Govindajaran, B., McLaughlin, E. R., Brown, L. F., Cohen, C., Moses, M. A., Kilroy, S. M., Arnold, R. S., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.022630199 · Cited by 489 · see citing works
Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation
Ambruso, D. R., Knall, C., Abell, A. N., Panepinto, J. A., Kurkchubasche, A. G., Thurman, G. W., Gonzalez-Aller, C., Hiester, A. A., deBoer, M., Harbeck, R. J., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.080074897 · Cited by 480 · see citing works
NOX Enzymes in the Central Nervous System: From Signaling to Disease
Sorce, S., & Krause, K. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2578 · Cited by 472 · see citing works
Beers, D. R., Henkel-Tigges, J., Zhao, W., Wang, J., & Appel, S. H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807419105 · Cited by 468 · see citing works
Purification of a Novel Flavoprotein Involved in the Thyroid NADPH Oxidase
Dupuy, C., Ohayon, R., Valent, A., Noël‐Hudson, M., Dème, D., & Virion, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37265 · Cited by 464 · see citing works
The Biological Chemistry of Hydrogen Peroxide
Winterbourn, C. C. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-405881-1.00001-x · Cited by 459 · 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
Kleinschnitz, C., Grund, H., Wingler, K., Armitage, M. E., Jones, E., Mittal, M., Barit, D., Schwarz, T., Geis, C., Kraft, P., et al. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000479 · Cited by 447 · see citing works
Sulfenic acid chemistry, detection and cellular lifetime
Gupta, V., & Carroll, K. S. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.05.040 · Cited by 427 · 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
THE REGULATION AND PHARMACOLOGY OF ENDOTHELIAL NITRIC OXIDE SYNTHASE
Dudzinski, D. M., Igarashi, J., Greif, D. M., & Michel, T. M. (2005) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121844 · Cited by 425 · see citing works
Byrne, J., Grieve, D., Bendall, J. K., Li, J., Gove, C. D., Lambeth, J. D., Cave, A. C., & Shah, A. M. (2003) · Circulation Research · doi:10.1161/01.res.0000099504.30207.f5 · Cited by 411 · see citing works
Oxygen Reduction by Nitric-oxide Synthases
Stuehr, D. J., Pou, S., & Rosen, G. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100011200 · Cited by 400 · see citing works
Autocrine, paracrine and juxtacrine signaling by EGFR ligands
Singh, A. B., & Harris, R. C. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2005.03.026 · Cited by 400 · see citing works
Peskin, A. V., Low, F. M., Paton, L. N., Maghzal, G. J., Hampton, M. B., & Winterbourn, C. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700339200 · Cited by 393 · see citing works
Shenoy-Scaria, A. M., Dietzen, D. J., Kwong, J., Link, D. C., & Lublin, D. M. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.2.353 · Cited by 391 · see citing works
Reactive oxygen species signaling in vascular smooth muscle cells
Clempus, R. E., & Griendling, K. K. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.02.033 · Cited by 358 · see citing works
Phosphorylation of Caveolin by Src Tyrosine Kinases
Li, S. C., Seitz, R. S., & Lisanti, M. P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.7.3863 · Cited by 353 · see citing works
Holland, S. M. (2012) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2012.11.002 · Cited by 350 · see citing works
Go, Y., Chandler, J. D., & Jones, D. P. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.03.022 · Cited by 343 · see citing works
Copper, zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide.
Yim, M. B., Chock, P. B., & Stadtman, E. R. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.13.5006 · Cited by 341 · see citing works
Caveolin-1 regulates cell polarization and directional migration through Src kinase and Rho GTPases
Grande-García, A., Echarri, A., de Rooij, J., Alderson, N. B., Waterman, C. M., Valdivielso, J. M., & del Pozo, M. Á. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200701006 · Cited by 340 · see citing works
Current molecular models for NADPH oxidase regulation by Rac GTPase
Bokoch, G. M., & Diebold, B. A. (2002) · Blood · doi:10.1182/blood-2002-04-1149 · Cited by 336 · see citing works
Williams, D., Tao, W., Yang, F., Kim, C., Gu, Y., Mansfield, P. J., Levine, J. E., Petryniak, B., Derrow, C. W., Harris, C., et al. (2000) · PubMed · Cited by 334 · see citing works
Identification of the Maturation Factor for Dual Oxidase
Grasberger, H., & Refetoff, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600095200 · Cited by 333 · see citing works
Park, L., Zhou, P., Pitstick, R., Capone, C., Anrather, J., Norris, E. H., Younkin, L., Younkin, S., Carlson, G., McEwen, B. S., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711568105 · Cited by 332 · see citing works
NADPH oxidase controls phagosomal pH and antigen cross-presentation in human dendritic cells
Mantegazza, A. R., Savina, A., Vermeulen, M., Pérez, L., Geffner, J., Hermine, O., Rosenzweig, S. D., Faure, F., & Amigorena, S. (2008) · Blood · doi:10.1182/blood-2008-01-134791 · Cited by 329 · see citing works
β-Amyloid Activates the O⨪2 Forming NADPH Oxidase in Microglia, Monocytes, and Neutrophils
Della Bianca, V., Dusi, S., Bianchini, E., Dal Prà, I., & Rossi, F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.22.15493 · Cited by 324 · see citing works
Michel, J. B., Féron, O., Sase, K., Prabhakar, P., & Michel, T. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.41.25907 · Cited by 323 · see citing works
Mechanisms of inflammatory neurodegeneration: iNOS and NADPH oxidase
Brown, G. C. (2007) · Biochemical Society Transactions · doi:10.1042/bst0351119 · Cited by 315 · see citing works
Montezano, A. C. I., & Touyz, R. M. (2011) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/j.1742-7843.2011.00785.x · Cited by 309 · see citing works
The Redox Biochemistry of Protein Sulfenylation and Sulfinylation
Conte, M. L., & Carroll, K. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.467738 · Cited by 305 · see citing works
Bouloumié, A., Bauersachs, J. K., Linz, W., Schölkens, B. A., Wiemer, G., Fleming, I., & Busse, R. (1997) · Hypertension · doi:10.1161/01.hyp.30.4.934 · Cited by 304 · see citing works
Inflammatory Bowel Disease: Mechanisms, Redox Considerations, and Therapeutic Targets
Biasi, F., Leonarduzzi, G., Oteiza, P. I., & Poli, G. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4530 · Cited by 301 · see citing works
Plant plasma membrane water channels conduct the signalling molecule H2O2
Dynowski, M., Schaaf, G., Loqué, D., Morán, Ó., & Ludewig, U. (2008) · Biochemical Journal · doi:10.1042/bj20080287 · Cited by 299 · see citing works
Wang, Y., Pennock, S., Chen, X., & Wang, Z. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.20.7279-7290.2002 · Cited by 296 · see citing works
Qin, L., Liu, Y., Cooper, C. L., Liu, B., Wilson, B. C., & Hong, J. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01210.x · Cited by 290 · see citing works
The CoQH2/CoQ Ratio Serves as a Sensor of Respiratory Chain Efficiency
Guarás, A., Perales‐Clemente, E., Calvo, E., Acín‐Pérez, R., Loureiro, M., Pujol, C., Martínez-Carrascoso, I., Núñez, E., Garcia-Marques, F. J., Hernández, M., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.03.009 · Cited by 290 · see citing works
Factors Affecting Protein Thiol Reactivity and Specificity in Peroxide Reduction
Ferrer‐Sueta, G., Manta, B., Botti, H., Radí, R., Trujillo, M., & Denicola, A. (2011) · Chemical Research in Toxicology · doi:10.1021/tx100413v · Cited by 286 · see citing works
Shelat, P. B., Chalimoniuk, M., Wang, J., Strosznajder, J. B., Lee, J. C., Sun, A. Y., Simonyi, Á., & Sun, G. Y. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05347.x · Cited by 283 · see citing works
New Insights on <i>NOX</i> Enzymes in the Central Nervous System
Nayernia, Z., Jaquet, V., & Krause, K.-H. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5703 · Cited by 279 · see citing works
The superoxide‐producing NAD(P)H oxidase Nox4 in the nucleus of human vascular endothelial cells
Kuroda, J., Nakagawa, K., Yamasaki, T., Nakamura, K., Takeya, R., Kuribayashi, F., Imajoh‐Ohmi, S., Igarashi, K., Shibata, Y., Sueishi, K., et al. (2005) · Genes to Cells · doi:10.1111/j.1365-2443.2005.00907.x · Cited by 275 · see citing works
Vestibular defects in head-tilt mice result from mutations in Nox3 , encoding an NADPH oxidasePreprint
Paffenholz, R., Bergstrom, R. A., Pasutto, F., Wabnitz, P., Munroe, R. J., Jagla, W., Heinzmann, U., Marquardt, A., Bareiss, A., Laufs, J., et al. (2004) · Genes & Development · doi:10.1101/gad.1172504 · Cited by 269 · see citing works
Extracellular superoxide dismutase
Nozik‐Grayck, E., Suliman, H. B., & Piantadosi, C. A. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.06.012 · Cited by 269 · see citing works
Regulation and termination of NADPH oxidase activity
DeCoursey, T. E., & Ligeti, E. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5177-1 · Cited by 268 · see citing works
Hematologically Important Mutations: X-Linked Chronic Granulomatous Disease—An Update
Heyworth, P. G., Curnutte, J. T., Rae, J., Noack, D., & Cross, A. R. (1997) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.1997.0163 · Cited by 266 · see citing works
Effects of membrane lipids on ion channel structure and function
Tillman, T. S., & Cascio, M. (2003) · Cell Biochemistry and Biophysics · doi:10.1385/cbb:38:2:161 · Cited by 265 · see citing works
Boursiac, Y., Boudet, J., Postaire, O., Luu, D., Tournaire‐Roux, C., & Maurel, C. (2008) · The Plant Journal · doi:10.1111/j.1365-313x.2008.03594.x · Cited by 260 · see citing works
Formation and reactions of sulfenic acids in proteins
Allison, W. S. (1976) · Accounts of Chemical Research · doi:10.1021/ar50104a003 · Cited by 255 · see citing works
Wu, D., Ré, D. B., Nagai, M., Ischiropoulos, H., & Przedborski, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603670103 · Cited by 253 · see citing works
Superoxide dismutase: A comparison of rate constants
Forman, H. J., & Fridovich, I. (1973) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(73)90636-x · Cited by 252 · see citing works
Rab27a regulates phagosomal pH and NADPH oxidase recruitment to dendritic cell phagosomes
Jancic, C. C., Savina, A., Wasmeier, C., Tolmachova, T., Benna, J. E., Dang, P. M., Pascolo, S., Gougerot-Pocidalo, M.-A., Raposo, G., Seabra, M. C., et al. (2007) · Nature Cell Biology · doi:10.1038/ncb1552 · Cited by 250 · see citing works
NADPH Oxidase Inhibits the Pathogenesis of Systemic Lupus Erythematosus
Campbell, A. M., Kashgarian, M. J., & Shlomchik, M. J. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3004801 · Cited by 246 · see citing works
Polyphosphoinositide binding domains: Key to inositol lipid biology
Hammond, G. R. V., & Balla, T. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2015.02.013 · Cited by 245 · see citing works
Park, L., Anrather, J., Zhou, P., Frys, K., Pitstick, R., Younkin, S., Carlson, G. A., & Iadecola, C. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.5207-04.2005 · Cited by 244 · see citing works
Regulated Hydrogen Peroxide Production by Duox in Human Airway Epithelial Cells
Forteza, R., Salathe, M. A., Miot, F., Forteza, R., & Conner, G. E. (2005) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2004-0302oc · Cited by 240 · see citing works
Kinetics and Mechanism of the Reaction of Cysteine and Hydrogen Peroxide in Aqueous Solution
Luo, D., Smith, S. W., & Anderson, B. D. (2004) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.20253 · Cited by 228 · see citing works
Neurotoxic Activation of Microglia Is Promoted by a Nox1-Dependent NADPH Oxidase
Chéret, C., Gervais, A., Lelli, A., Colin, C., Amar, L., Ravassard, P., Mallet, J., Cumano, A., Krause, K.-H., & Mallat, M. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.3568-08.2008 · Cited by 225 · see citing works
Hara‐Chikuma, M., Satooka, H., Watanabe, S., Honda, T., Miyachi, Y., Watanabe, T., & Verkman, A. S. (2015) · Nature Communications · doi:10.1038/ncomms8454 · Cited by 219 · see citing works
Nitric oxide signaling: no longer simply on or off
Cary, S. P., Winger, J. A., Derbyshire, E. R., & Marletta, M. A. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.02.003 · Cited by 219 · see citing works
Stöcker, S., Laer, K. V., Mijušković, A., & Dick, T. P. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7162 · Cited by 219 · see citing works
Superoxide and iron: Partners in crime
Liochev, S. I., & Fridovich, I. (1999) · International Union of Biochemistry and Molecular Biology: Life · doi:10.1080/152165499307161 · Cited by 219 · see citing works
Verkman, A. S. (2011) · Journal of Cell Science · doi:10.1242/jcs.079467 · Cited by 216 · see citing works
Miller, F. J., Filali, M. S., Huss, G. J., Stanić, B., Chamseddine, A., Barna, T. J., & Lamb, F. S. (2007) · Circulation Research · doi:10.1161/circresaha.107.151076 · Cited by 214 · see citing works
Finegold, A. A., Shatwell, K. P., Segal, A. W., Klausner, R. D., & Dancis, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31021 · Cited by 213 · see citing works
Volonté, D., Zhang, K., Lisanti, M. P., & Galbiati, F. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-11-0529 · Cited by 210 · see citing works
Piccoli, C., Ria, R., Scrima, R., Cela, O., D'Aprile, A., Boffoli, D., Falzetti, F., Tabilio, A., & Capitanio, N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500047200 · Cited by 209 · see citing works
Cheng, G., & Lambeth, J. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m305968200 · Cited by 209 · see citing works
Signaling Components of Redox Active Endosomes: The Redoxosomes
Oakley, F. D., Abbott, D., Li, Q., & Engelhardt, J. F. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2363 · Cited by 209 · see citing works
Clathrin and Membrane Microdomains Cooperatively Regulate RbohD Dynamics and Activity in Arabidopsis
Hao, H., Fan, L., Chen, T., Li, R., Li, X., He, Q., Botella, M. A., & Lin, J. (2014) · The Plant Cell · doi:10.1105/tpc.113.122358 · Cited by 205 · see citing works
Zhang, W., Wang, T., Qin, L., Gao, H., Wilson, B. C., Ali, S. F., Zhang, W., Hong, J., & Liu, B. (2004) · The FASEB Journal · doi:10.1096/fj.03-0983fje · Cited by 204 · see citing works
Synaptic localization of a functional NADPH oxidase in the mouse hippocampus
Tejada-Simon, M. V., Serrano, F., Villasana, L., Kanterewicz, B. I., Wu, G., Quinn, M. T., & Klann, E. (2005) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2005.01.007 · Cited by 203 · see citing works
Radical induction theory of ulcerative colitis.
Pravda, J. (2005) · World Journal of Gastroenterology · doi:10.3748/wjg.v11.i16.2371 · Cited by 202 · see citing works
Lipid Raft Clustering and Redox Signaling Platform Formation in Coronary Arterial Endothelial Cells
Zhang, A. Y., Yi, F., Zhang, G., Gulbins, E., & Li, P. (2005) · Hypertension · doi:10.1161/01.hyp.0000196727.53300.62 · Cited by 202 · see citing works
Geiszt, M., Lekstrom, K. J., Brenner, S., Hewitt, S. M., Dana, R., Malech, H. L., & Leto, T. L. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.1.299 · Cited by 201 · see citing works
Hematologically important mutations: X-linked chronic granulomatous disease (third update)
Roos, D., Kuhns, D. B., Maddalena, A., Roesler, J., López, J. Á., Ariga, T., Avčin, T., de Boer, M., Bustamante, J. C., Condino‐Neto, A., et al. (2010) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2010.07.012 · Cited by 200 · see citing works
Phenotype analysis of aquaporin-8 null mice
Yang, B., Song, Y., Zhao, D., & Verkman, A. S. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00564.2004 · Cited by 200 · see citing works
Kim, Y. S., Choi, D. H., Block, M. L., Lorenzl, S., Yang, L., Kim, Y., Sugama, S., Cho, B. P., Hwang, O., Browne, S. E., et al. (2006) · The FASEB Journal · doi:10.1096/fj.06-5865com · Cited by 199 · see citing works
Deficiency of Reduced Nicotinamide-Adenine Dinucleotide Oxidase in Chronic Granulomatous Disease
Baehner, R. L., & Karnovsky, M. L. (1968) · Science · doi:10.1126/science.162.3859.1277 · Cited by 199 · see citing works
The physiological role of reversible methionine oxidation
Drazic, A., & Winter, J. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.01.001 · Cited by 198 · cited 1× · see citing works
“methionine, the second sulfur-containing amino acid, might provide an analogous redox-dependent system [48].”
BackgroundBiological Production, Detection, and Fate of Hydrogen Peroxide
Winterbourn, C. C. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7425 · Cited by 197 · see citing works
Intracellular generation of superoxide by the phagocyte NADPH oxidase: How, where, and what for?
Bylund, J., Brown, K. L., Movitz, C., Dahlgren, C., & Karlsson, A. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.016 · Cited by 196 · see citing works
Coant, N., Mkaddem, S. B., Pédruzzi, E., Guichard, C., Tréton, X., Ducroc, R. A., Freund, J., Cazals-Hatem, D. L., Bouhnik, Y., Woerther, P., et al. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01194-09 · Cited by 191 · see citing works
Chemokine-dependent T cell migration requires aquaporin-3–mediated hydrogen peroxide uptake
Hara‐Chikuma, M., Chikuma, S., Sugiyama, Y., Kabashima, K., Verkman, A. S., Inoue, S., & Miyachi, Y. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20112398 · Cited by 188 · see citing works
Hoffmann, M. H., & Griffiths, H. R. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.03.016 · Cited by 187 · see citing works
Aquaporin-11: a channel protein lacking apparent transport function expressed in brain.
Gorelick, D. A., Prætorius, J., Tsunenari, T., Nielsen, S. M., & Agre, P. C. (2006) · BMC Biochemistry · doi:10.1186/1471-2091-7-14 · Cited by 186 · see citing works
Nox NADPH Oxidases and the Endoplasmic Reticulum
Laurindo, F. R. M., Araujo, T. L. S., & Abrahão, T. B. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5605 · Cited by 185 · see citing works
Badaut, J., Hirt, L., Granziera, C., Bogousslavsky, J., Magistretti, P. J., & Regli, L. (2001) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200105000-00001 · Cited by 181 · see citing works
NADPH Oxidase 1-Mediated Oxidative Stress Leads to Dopamine Neuron Death in Parkinson's Disease
Choi, D.-H., Cristóvão, A. C., Guhathakurta, S., Lee, J., JOH, T. H., Beal, M. F., & Kim, Y.-S. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3960 · Cited by 180 · see citing works
Concepts of oxidative stress and antioxidant defense in Crohn’s disease
Alzoghaibi, M. A. (2013) · World Journal of Gastroenterology · doi:10.3748/wjg.v19.i39.6540 · Cited by 179 · see citing works
Mechanisms and Function of DUOX in Epithelia of the Lung
Fischer, H. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2558 · Cited by 178 · see citing works
Yeh, D. C., Duncan, J. A., Yamashita, S., & Michel, T. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.46.33148 · Cited by 178 · see citing works
The phagocyte NADPH oxidase depends on cholesterol‐enriched membrane microdomains for assembly
Vilhardt, F., & van Deurs, B. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600066 · Cited by 171 · see citing works
Schlegel, A., Volonté, D., Engelman, J. A., Galbiati, F., Mehta, P., Zhang, X.-L., Scherer, P. E., & Lisanti, M. P. (1998) · Cellular Signalling · doi:10.1016/s0898-6568(98)00007-2 · Cited by 169 · see citing works
Espey, M. G., Thomas, D. D., Miranda, K. M., & Wink, D. A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.152157599 · Cited by 169 · see citing works
Sessa, W. C., Barber, C. M., & Lynch, K. R. (1993) · Circulation Research · doi:10.1161/01.res.72.4.921 · Cited by 166 · see citing works
Dugan, L. L., Ali, S. S., Shekhtman, G., Roberts, A. J., Lucero, J., Quick, K. L., & Behrens, M. M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005518 · Cited by 165 · see citing works
Cristóvão, A. C., Choi, D.-H., Baltazar, G., Beal, M. F., & Kim, Y.-S. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2459 · Cited by 165 · see citing works
Case, A. J. (2017) · Antioxidants · doi:10.3390/antiox6040082 · Cited by 165 · see citing works
Genetic disorders coupled to ROS deficiency
O’Neill, S., Brault, J., Stasia, M.-J., & Knaus, U. G. (2015) · Redox Biology · doi:10.1016/j.redox.2015.07.009 · Cited by 164 · see citing works
Water Channel Protein AQP3 Is Present in Epithelia Exposed to the Environment of Possible Water Loss
Matsuzaki, T., Suzuki, T., Koyama, H., Tanaka, S., & Takata, K. (1999) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215549904701007 · Cited by 164 · see citing works
Roos, D., Kuhns, D. B., Maddalena, A., Bustamante, J. C., Kannengiesser, C., de Boer, M., van Leeuwen, K., Köker, M. Y., Wolach, B., Roesler, J., et al. (2010) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2010.01.009 · Cited by 163 · see citing works
Constitutive NADPH-Dependent Electron Transferase Activity of the Nox4 Dehydrogenase Domain
Nisimoto, Y., Jackson, H. M., Ogawa, H., Kawahara, T., & Lambeth, J. D. (2010) · Biochemistry · doi:10.1021/bi9022285 · Cited by 161 · see citing works
Oshikawa, J., Urao, N., Kim, H. W., Kaplan, N., Razvi, M., McKinney, R. D., Poole, L. B., Fukai, T., & Ushio‐Fukai, M. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010189 · Cited by 160 · see citing works
DeYulia, G. J., Cárcamo, J. M., Bórquez-Ojeda, O., Shelton, C. C., & Golde, D. W. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501154102 · Cited by 159 · see citing works
Kishida, K. T., Hoeffer, C. A., Hu, D., Pao, M., Holland, S. M., & Klann, E. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00269-06 · Cited by 159 · see citing works
Nitric oxide synthase uncoupling: A therapeutic target in cardiovascular diseases
Roe, N. D., & Ren, J. T. (2012) · Vascular Pharmacology · doi:10.1016/j.vph.2012.02.004 · Cited by 157 · see citing works
Schäppi, M. G., Jaquet, V., Belli, D. C., & Krause, K. (2008) · Seminars in Immunopathology · doi:10.1007/s00281-008-0119-2 · Cited by 156 · see citing works
Brown, J. R., Goldblatt, D., Buddle, J. C., Morton, L., & Thrasher, A. J. (2003) · Journal of Leukocyte Biology · doi:10.1189/jlb.1202599 · Cited by 156 · see citing works
Redox Regulation in the Extracellular Environment
Ottaviano, F. G., Handy, D. E., & Loscalzo, J. (2007) · Circulation Journal · doi:10.1253/circj.72.1 · Cited by 155 · see citing works
Membrane Lipid Organization Is Critical for Human Neutrophil Polarization
Pierini, L. M., Eddy, R. J., Fuortes, M., Seveau, S. M., Casulo, C., & Maxfield, F. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212386200 · Cited by 152 · see citing works
Yamamoto, N., Yoneda, K., Asai, K., Sobue, K., Tada, T., Fujita, Y., Katsuya, H., Fujita, M., Aihara, N., Mase, M., et al. (2001) · Molecular Brain Research · doi:10.1016/s0169-328x(01)00064-x · Cited by 152 · see citing works
Nox5 and the Regulation of Cellular Function
Fulton, D. J. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2587 · Cited by 151 · see citing works
Aquaporin-9 facilitates membrane transport of hydrogen peroxide in mammalian cells
Watanabe, S., Moniaga, C. S., Nielsen, S., & Hara‐Chikuma, M. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.01.153 · Cited by 147 · see citing works
Brinckmann, R., Schnurr, K., Heydeck, D., Rosenbach, T., Kolde, G., & Kühn, H. (1998) · Blood · doi:10.1182/blood.v91.1.64 · Cited by 146 · see citing works
Aquaporins in the Colon as a New Therapeutic Target in Diarrhea and Constipation
Ikarashi, N., Kon, R., & Sugiyama, K. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17071172 · Cited by 146 · see citing works
Redox modifier genes in amyotrophic lateral sclerosis in mice
Marden, J. J., Harraz, M. M., Williams, A. J., Nelson, K., Luo, M., Paulson, H., & Engelhardt, J. F. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31265 · Cited by 145 · see citing works
Phagosomal proteolysis in dendritic cells is modulated by NADPH oxidase in a pH‐independent manner
Rybicka, J. M., Balce, D. R., Chaudhuri, S., Allan, E. R. O., & Yates, R. M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.440 · Cited by 141 · see citing works
Relationships between EGFR Signaling–competent and Endocytosis-competent Membrane Microdomains
Puri, C., Tosoni, D., Comai, R., Rabellino, A., Segat, D., Caneva, F., Luzzi, P., Fiore, P. P. D., & Tacchetti, C. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-07-0596 · Cited by 141 · see citing works
Current Concepts of Hyperinflammation in Chronic Granulomatous Disease
Rieber, N. P., Hector, A., Kuijpers, T. W., Roos, D., & Hartl, D. (2011) · Clinical and Developmental Immunology · doi:10.1155/2012/252460 · Cited by 140 · see citing works
Quantitative biology of hydrogen peroxide signaling
Antunes, F., & de Brito, P. M. (2017) · Redox Biology · doi:10.1016/j.redox.2017.04.039 · Cited by 140 · see citing works
Goyette, P., Labbé, C., Trinh, T. T., Xavier, R. J., & Rioux, J. D. (2007) · Annals of Medicine · doi:10.1080/07853890701197615 · Cited by 139 · see citing works
Lipid Rafts and Caveolae and Their Role in Compartmentation of Redox Signaling
Patel, H. H., & Insel, P. A. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2365 · Cited by 139 · see citing works
Kotsias, F., Hoffmann, E., Amigorena, S., & Savina, A. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4557 · Cited by 139 · see citing works
Calcium signal transduction from caveolae
Isshiki, M., & Anderson, R. G. W. (1999) · Cell Calcium · doi:10.1054/ceca.1999.0073 · Cited by 136 · see citing works
Oxidative gating of water channels (aquaporins) in corn roots
Ye, Q., & Steudle, E. (2005) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2005.01423.x · Cited by 136 · see citing works
NADPH oxidase is required for NMDA receptor‐dependent activation of ERK in hippocampal area CA1
Kishida, K. T., Pao, M., Holland, S. M., & Klann, E. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03189.x · Cited by 135 · see citing works
Reactive Oxygen Species Deficiency Induces Autoimmunity with Type 1 Interferon Signature
Kelkka, T., Kienhöfer, D., Hoffmann, M. H., Linja, M., Wing, K., Sareila, O., Hultqvist, M. H., Laajala, E., Chen, Z. J., Vasconcelos, J. H. L., et al. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5828 · Cited by 135 · see citing works
Felley‐Bosco, E., Bender, F. C., Courjault, F., Bron, C., & Quest, A. F. G. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250406797 · Cited by 134 · see citing works
Barrett, D. M., Black, S. M., Todor, H., Schmidt‐Ullrich, R., Dawson, K. S., & Mikkelsen, R. B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411523200 · Cited by 133 · see citing works
Platelet-derived Growth Factor Receptor-mediated Signal Transduction from Endosomes
Wang, Y., Pennock, S., Chen, X., Kazlauskas, A., & Wang, Z. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311494200 · Cited by 132 · see citing works
Lipid Raft Redox Signaling: Molecular Mechanisms in Health and Disease
Jin, S., Zhou, F., Katirai, F., & Li, P. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3619 · Cited by 129 · see citing works
Neutrophil leukocyte motility requires directed water influx
Loitto, V. M., Forslund, T., Sundqvist, T., Magnusson, K., & Gustafsson, M. (2002) · Journal of Leukocyte Biology · doi:10.1189/jlb.71.2.212 · Cited by 126 · see citing works
Flagged first, then by citations
3 of the 319 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Reactive oxygen species (ROS) as pleiotropic physiological signalling agents
Sies, H., & Jones, D. P. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0230-3 · Cited by 5,335 · see citing works
Defining roles of specific reactive oxygen species (ROS) in cell biology and physiology
Sies, H., Belousov, V. V., Chandel, N. S., Davies, M. J., Jones, D. P., Mann, G. E., Murphy, M. P., Yamamoto, M., & Winterbourn, C. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00456-z · Cited by 1,735 · see citing works
Wang, P., Liu, W., Han, C., Wang, S., Bai, M., & Song, C. (2023) · Journal of Integrative Plant Biology · doi:10.1111/jipb.13601 · Cited by 571 · see citing works
Fundamentals of redox regulation in biology
Sies, H., Mailloux, R. J., & Jakob, U. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00730-2 · Cited by 546 · see citing works
Interrelation between ROS and Ca2+ in aging and age-related diseases
Madreiter‐Sokolowski, C. T., Thomas, C., & Ristow, M. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101678 · Cited by 365 · see citing works
Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342 · see citing works
Superoxide Radicals in the Execution of Cell Death
Fujii, J., Homma, T., & Osaki, T. (2022) · Antioxidants · doi:10.3390/antiox11030501 · Cited by 321 · see citing works
Reactive oxygen species: a volatile driver of field cancerization and metastasis
Liao, Z., Chua, D., & Tan, N. S. (2019) · Molecular Cancer · doi:10.1186/s12943-019-0961-y · Cited by 284 · see citing works
On the Origin and Fate of Reactive Oxygen Species in Plant Cell Compartments
Janků, M., Luhová, L., & Petřivalský, M. (2019) · Antioxidants · doi:10.3390/antiox8040105 · Cited by 251 · see citing works
Yang, J., Griffin, A. S., Qiang, Z., & Ren, J. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01243-0 · Cited by 211 · see citing works
Redox-Mediated Mechanism of Chemoresistance in Cancer Cells
Kim, E.-K., Jang, M., Song, M.-J., Kim, D., Kim, Y., & Jang, H. H. (2019) · Antioxidants · doi:10.3390/antiox8100471 · Cited by 140 · see citing works
Eastman, C. L., D’Ambrosio, R., & Ganesh, T. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.107907 · Cited by 137 · see citing works
Human aquaporin-11 guarantees efficient transport of H2O2 across the endoplasmic reticulum membrane
Bestetti, S., Galli, M., Sorrentino, I., Pinton, P., Rimessi, A., Sitia, R., & Medraño-Fernández, I. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101326 · Cited by 120 · see citing works
Characterization of aquaporin-driven hydrogen peroxide transport
Wang, H., Schoebel, S., Schmitz, F., Dong, H., & Hedfalk, K. (2020) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2019.183065 · Cited by 107 · see citing works
Oxidative Stress as a Common Key Event in Developmental Neurotoxicity
Nishimura, Y., Kanda, Y., Sone, H., & Aoyama, H. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6685204 · Cited by 89 · see citing works
Monitoring the Redox Status in Multiple Sclerosis
Tanaka, M., & Vécsei, L. (2020) · Biomedicines · doi:10.3390/biomedicines8100406 · Cited by 88 · see citing works
Nordzieke, D. E., Fernandes, T. R., Ghalid, M. E., Turrà, D., & Pietro, A. D. (2019) · New Phytologist · doi:10.1111/nph.16085 · Cited by 73 · see citing works
Self-citationReactive oxygen species-upregulating nanomedicines towards enhanced cancer therapy
Ding, Y., Pan, Q., Gao, W., Pu, Y., Luo, K., & He, B. (2022) · Biomaterials Science · doi:10.1039/d2bm01833k · Cited by 71 · see citing works
Hatami, M., & Ghorbanpour, M. (2024) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2024.108847 · Cited by 68 · see citing works
Henríquez‐Olguín, C., Meneses‐Valdés, R., & Jensen, T. E. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101473 · Cited by 65 · see citing works
Menegazzi, M., Masiello, P., & Novelli, M. (2020) · Antioxidants · doi:10.3390/antiox10010018 · Cited by 64 · see citing works
Yaghobi, M., & Heidari, P. (2023) · Genes · doi:10.3390/genes14010202 · Cited by 61 · see citing works
Novelli, M., Masiello, P., Beffy, P., & Menegazzi, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218108 · Cited by 62 · see citing works
Pathways for Sensing and Responding to Hydrogen Peroxide at the Endoplasmic Reticulum
Roscoe, J. M., & Sevier, C. S. (2020) · Cells · doi:10.3390/cells9102314 · Cited by 55 · see citing works
Voronina, M. V., Frolova, A. S., Kolesova, E. P., Kuldyushev, N. A., Parodi, A., & Zamyatnin, A. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25074087 · Cited by 57 · see citing works
Dental resin monomers induce early and potent oxidative damage on human odontoblast-like cells
Baldión, P. A., Velandia-Romero, M. L., & Castellanos, J. E. (2020) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2020.109336 · Cited by 39 · see citing works
Transfer of H2O2 from Mitochondria to the endoplasmic reticulum via Aquaporin-11
Sorrentino, I., Galli, M., Medraño-Fernández, I., & Sitia, R. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102410 · Cited by 38 · see citing works
Bruder-Nascimento, T. B., Callera, G. E., Montezano, A. C. I., de Chantemèle, E. J. B., Tostes, R. C., & Touyz, R. M. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.01.043 · Cited by 37 · see citing works
Lipid metabolism transcriptomics of murine microglia in Alzheimer’s disease and neuroinflammation
Shippy, D. C., & Ulland, T. K. (2023) · Scientific Reports · doi:10.1038/s41598-023-41897-6 · Cited by 35 · see citing works
Dynamics of intracellular and intercellular redox communication
Sies, H. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.11.002 · Cited by 33 · see citing works
How the Disruption of Mitochondrial Redox Signalling Contributes to Ageing
Castejón‐Vega, B., Cordero, M. D., & Sanz, A. (2023) · Antioxidants · doi:10.3390/antiox12040831 · Cited by 30 · see citing works
Turovsky, E. A., Varlamova, E. G., & Plotnikov, E. Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168805 · Cited by 30 · see citing works
Kubicová, L., Hadaček, F., Bachmann, G., Weckwerth, W., & Chobot, V. (2019) · Antioxidants · doi:10.3390/antiox8100476 · Cited by 29 · see citing works
Diabetes Mellitus and Periodontitis Share Intracellular Disorders as the Main Meeting Point
Portes, J., Bullón, B., Quiles, J. L., Battino, M. A., & Bullón, P. (2021) · Cells · doi:10.3390/cells10092411 · Cited by 29 · see citing works
Pulmonary hypertension and oxidative stress: Where is the link?
Rawat, M., Lakshminrusimha, S., & Vento, M. (2022) · Seminars in Fetal and Neonatal Medicine · doi:10.1016/j.siny.2022.101347 · Cited by 29 · see citing works
Aquaporins – Expression, purification and characterization
Bill, R. M., & Hedfalk, K. (2021) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2021.183650 · Cited by 27 · see citing works
Reactive Oxygen Species (ROS) and ROS Scavengers in Plant Abiotic Stress Response
Singh, A., & Satheeshkumar, P. K. (2024) · Springer eBooks · doi:10.1007/978-981-97-1883-2_3 · Cited by 25 · see citing works
Therapeutic role of flavonoids in lung inflammatory disorders
Beigh, S., Rehman, M. U., Khan, A., Patil, B. R., Makeen, H. A., Rasool, S., Rashid, S., Arafah, A. M., & Kamal, M. A. (2022) · Phytomedicine Plus · doi:10.1016/j.phyplu.2022.100221 · Cited by 24 · see citing works
Turovsky, E. A., Varlamova, E. G., Gudkov, S. V., & Plotnikov, E. Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413216 · Cited by 22 · see citing works
Novel and Converging Ways of NOX2 and SOD3 in Trafficking and Redox Signaling in Macrophages
Petersen, S. V., Poulsen, N. B., Matthiesen, C. L., & Vilhardt, F. (2021) · Antioxidants · doi:10.3390/antiox10020172 · Cited by 21 · see citing works
Ding, M., Zhu, Y. S., Xu, X., He, H., Jiang, T., Mo, X., Wang, Z., Yu, W., & Ou, H. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c07874 · Cited by 20 · see citing works
Gwak, H., Hong, S., Lee, S. H., Kim, I. W., Kim, Y., Kim, H., Pahk, K. J., & Kim, S. Y. (2025) · Aging Cell · doi:10.1111/acel.14486 · Cited by 14 · see citing works
Li, Q., Zhong, J., Luo, H., Urbonaviciute, V., Xu, Z., He, C., & Holmdahl, R. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04501-0 · Cited by 13 · see citing works
Thermoprotection by a cell membrane–localized metacaspase in a green alga
Zou, Y., Sabljić, I., Horbach, N., Dauphinee, A. N., Åsman, A. K. M., Sancho-Temiño, L., Minina, E. A., Drąg, M., Stael, S., Poręba, M., et al. (2023) · The Plant Cell · doi:10.1093/plcell/koad289 · Cited by 13 · see citing works
Siebieszuk, A., Sejbuk, M., & Witkowska, A. M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242216169 · Cited by 12 · see citing works
Expression of CD70 Modulates Nitric Oxide and Redox Status in Endothelial Cells
Pandey, A. K., Waldeck‐Weiermair, M., Wells, Q. S., Xiao, W., Yadav, S., Eroğlu, E., Michel, T. M., & Loscalzo, J. (2022) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.122.317866 · Cited by 12 · see citing works
Aquaporins Display a Diversity in their Substrates
Sachdeva, R., Priyadarshini, P., & Gupta, S. (2022) · The Journal of Membrane Biology · doi:10.1007/s00232-022-00257-7 · Cited by 12 · see citing works
Kano, R., Shirakawa, H., Poole, D. C., Hoshino, D., & Kano, Y. (2025) · Redox Biochemistry and Chemistry · doi:10.1016/j.rbc.2025.100056 · Cited by 10 · see citing works
Gut microbes involvement in gastrointestinal cancers through redox regulation
Yangyanqiu, W., Chu, J., Yuqing, Y., Zhanbo, Q., & Han, S. (2023) · Gut Pathogens · doi:10.1186/s13099-023-00562-z · Cited by 9 · see citing works
Bianchini, B. H. S., Martelossi-Cebinelli, G., Carneiro, J. A., Rasquel-Oliveira, F. S., Casagrande, R., & Verri, W. A., Jr. (2025) · Future Pharmacology · doi:10.3390/futurepharmacol5040060 · Cited by 10 · see citing works
Lolicato, F., Steringer, J. P., Saleppico, R., Beyer, D., Fernandez-Sobaberas, J., Unger, S., Klein, S., Riegerová, P., Wegehingel, S., Müller, H.-M., et al. (2024) · eLife · doi:10.7554/elife.88579 · Cited by 9 · see citing works
Natural Compounds as a Strategy to Optimize “ In Vitro ” Expansion of Stem Cells
Maraldi, T., Prata, C., Marrazzo, P., Hrelia, S., & Angeloni, C. (2019) · Rejuvenation Research · doi:10.1089/rej.2019.2187 · Cited by 10 · see citing works
Potential of Metabolomics in Plant Abiotic Stress Management
Singh, N. K., Mansoori, A., Dey, D., Kumar, R., & Kumar, A. (2021) · Springer eBooks · doi:10.1007/978-981-16-2956-3_7 · Cited by 9 · see citing works
Roles of microglial membranes in Alzheimer's disease
Shin, J., & Lee, J. C. (2020) · Current topics in membranes · doi:10.1016/bs.ctm.2020.08.007 · Cited by 7 · see citing works
Trans-Ancestry Mutation Landscape of Hepatoblastoma Genomes in Children
Liu, J., Gao, C., Wang, L., Jian, X., Ma, M., Li, T., Hao, X., Zhang, Q., Chen, Y., Zhao, J., et al. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.669560 · Cited by 7 · see citing works
Reciprocal Regulation of Shh Trafficking and H2O2 Levels via a Noncanonical BOC-Rac1 Pathway
Thauvin, M., Amblard, I., Rampon, C., Mourton, A., Quéguiner, I., Li, C., Gautier, A., Joliot, A., Volovitch, M., & Vriz, S. (2022) · Antioxidants · doi:10.3390/antiox11040718 · Cited by 7 · see citing works
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Seitz, R., Müller, M. A., & Gülow, K. (2026) · Antioxidants · doi:10.3390/antiox15030280 · Cited by 6 · see citing works
Oprea, S., Panţu, C., Costea, D., Dumitru, A. V., Tătaru, C.-I., Dobrin, N., Rădoi, M. P., Munteanu, O., & Breazu, A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms27010069 · Cited by 5 · see citing works
High-resolution structure of a fish aquaporin reveals a novel extracellular fold
Zeng, J., Schmitz, F., Isaksson, S., Glas, J., Arbab, O., Andersson, M., Sundell, K. S., Eriksson, L. A., Swaminathan, K., Törnroth‐Horsefield, S., et al. (2022) · Life Science Alliance · doi:10.26508/lsa.202201491 · Cited by 5 · see citing works
Zhang, M., Tran, N. T., Zhang, Y., Yang, Q., Tang, Y., Zhang, Y., & Li, S. (2023) · Aquaculture · doi:10.1016/j.aquaculture.2023.739760 · Cited by 5 · see citing works
Interception Proximity Labeling for Interrogating Cell Efflux Microenvironment
Wang, G., Li, Q., Guo, Y., Chen, L., Yao, Y., Zhong, Y., Sun, J., Yan, X., Wang, H., Wang, X., et al. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c03879 · Cited by 5 · see citing works
Song, Y., Zhang, Q., Li, Y., Lin, J., & Lin, J. (2023) · Advanced Materials Technologies · doi:10.1002/admt.202301147 · Cited by 4 · see citing works
Exquisite sensitivity of Polycystin-1 to H2O2 concentration in the endoplasmic reticulum
Speranza, E. A., Sorrentino, I., Boletta, A., & Sitia, R. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103486 · Cited by 4 · see citing works
Antioxidant Defense Strategies Against Diaporthe eres Infection in Hongyang Kiwifruit
Ling, L.-Z., Yang, T., Long, X., Pan, S., & Zhang, S. (2025) · Biology · doi:10.3390/biology14091169 · Cited by 3 · see citing works
Saadaoui, M., Morlevat, T., Loison, O., Blavignac, C., Faize, M., Rifai, L. A., Nouri, C., Dich, J., Magliaraschi, N., Philippe, G., et al. (2025) · Physiological and Molecular Plant Pathology · doi:10.1016/j.pmpp.2025.102995 · Cited by 3 · see citing works
Physiological roles of reactive oxygen species in sleep homeostasis
Tian, Y., Liu, X., & Liu, D. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.10.273 · Cited by 3 · see citing works
A Biophysical Approach to SARS-CoV-2 Pathogenicity
Messori, C. (2021) · OALib · doi:10.4236/oalib.1108183 · Cited by 3 · see citing works
An artificial nucleoside that simultaneously detects and combats drug resistance to doxorubicin
Choi, J., & Berdis, A. J. (2019) · European Journal Of Haematology · doi:10.1111/ejh.13347 · Cited by 3 · see citing works
Non-coding RNAs and Aquaporin 4: Their Role in the Pathogenesis of Neurological Disorders
Yaghoobi, Z., Nazeri, S. S. S. B., Asadi, A., Derafsh, E., Taheri, A. T., Tamtaji, Z., Dadgostar, E., Rahmati‐Dehkordi, F., Aschner, M., Mirzaei, H., et al. (2023) · Neurochemical Research · doi:10.1007/s11064-023-04067-8 · Cited by 3 · see citing works
The Gordian knot of the immune-redox systems’ interactions in psychosis
Karanikas, E. (2023) · International Clinical Psychopharmacology · doi:10.1097/yic.0000000000000481 · Cited by 3 · see citing works
Aquaporins: Gatekeepers in the borders of oxidative stress and redox signaling
Medraño-Fernández, I., & Sitia, R. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-818606-0.00011-0 · Cited by 3 · see citing works
Redox signals and oxidative stress in the control of mitochondrial protein import
Hasberg, L., Lauterbach, V. K., Ochsenreiter, T., & Riemer, J. (2026) · Protein Science · doi:10.1002/pro.70665 · Cited by 2 · see citing works
Targeting the Metabolism in Cancer Cells for Cancer Therapy
Mohan, M., Rafi, S. T. M., Muthusami, S., Ramalingam, S., Sambandam, Y., Selvendiran, K., Ramachandran, I., & Kumaran, R. (2022) · Handbook of Oxidative Stress in Cancer: Therapeutic Aspects · doi:10.1007/978-981-16-1247-3_216-1 · Cited by 2 · see citing works
Stimulus-Responsive Delivery Systems for Gene Therapy Products
Sakhno, N. G., & Gunar, O. V. (2025) · Applied Biochemistry and Microbiology · doi:10.1134/s0003683825700334 · Cited by 1 · see citing works
Making sense of subcellular H2O2 in mammals
Waldeck‐Weiermair, M., Covington, T. A., Pandey, A. K., & Michel, T. M. (2026) · Redox Biochemistry and Chemistry · doi:10.1016/j.rbc.2026.100080 · Cited by 1 · see citing works
Molecular Insights and Conventional Breeding Approaches to Enhance Drought Resilience in Sorghum
Demissie, H. S. (2026) · Advances in Agriculture · doi:10.1155/aia/4262743 · Cited by 1 · see citing works
Effects of usEPs on Plasma Membranes—Pores, Channels, and Repair
Beebe, S. J. (2021) · Series in bioengineering · doi:10.1007/978-981-10-5113-5_2 · Cited by 1 · see citing works
Targeting the Metabolism in Cancer Cells for Cancer Therapy
Mohan, M., Rafi, S. T. M., Muthusami, S., Ramalingam, S., Sambandam, Y., Selvendiran, K., Ramachandran, I., & Kumaran, R. (2022) · Handbook of Oxidative Stress in Cancer: Therapeutic Aspects · doi:10.1007/978-981-16-5422-0_216 · Cited by 1 · see citing works
Lolicato, F., Steringer, J., Saleppico, R., Beyer, D., Fernandez-Sobaberas, J., Unger, S., Klein, S., Riegerová, P., Wegehingel, S., Müller, H., et al. (2023) · doi:10.7554/elife.88579.2 · Cited by 1 · see citing works
p22phox y NADPH oxidasas en la hematopoyesis in vivo
Bermejo, R. (2020) · doi:10.14201/gredos.144241
Lolicato, F., Steringer, J., Saleppico, R., Beyer, D., Fernandez-Sobaberas, J., Unger, S., Klein, S., Riegerová, P., Wegehingel, S., Müller, H., et al. (2023) · doi:10.1101/2023.04.12.536539
Wu, Y.-H., Lai, K.-H., Chen, C.-C., Lai, T.-M., & Huang, P.-W. D. (2023) · Cureus · doi:10.7759/cureus.43606
Lolicato, F., Steringer, J. P., Saleppico, R., Beyer, D., Fernandez-Sobaberas, J., Unger, S., Klein, S., Riegerová, P., Wegehingel, S., Müller, H.-M., et al. (2024) · eLife · doi:10.7554/elife.88579.3
Xie, M., Niu, X., Sun, F., & Shi, L. (2026) · Journal of Alzheimer s Disease · doi:10.1177/13872877261443968
Investigating the toxicity of lemongrass oil in a Drosophila melanogaster model
Fathima, N., Kumar, J. R., Ramkrishna, M. K., & Prasad, N. (2025) · International Journal of Health & Allied Sciences · doi:10.4103/ijhas.ijhas_50_25
Mansuri, S., Mahalingam, P., Sarkar, P., Rawat, G., Katsuda, Y., & Kanvah, S. (2026) · The Analyst · doi:10.1039/d6an00871b
Camara, L. R. P., & Vilas‐Boas, E. A. (2026) · Frontiers in Network Physiology · doi:10.3389/fnetp.2026.1864821
Wang, T., & Xiao, Q. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1936991
- Authors
- Nordzieke, D. E., & Medraño-Fernandez, I.
- Affiliations
- University of Göttingen (DE)
- Protein Transport and Secretion Unit, Division of Genetics and Cell Biology, Istituto di Ricovero e Cura a Carattere Scientifico (IRCCS) Ospedale San Raffaele, Università Vita-Salute San Raffaele, 20132 Milan, Italy
- Corresponding author
- Nordzieke, Daniela E.
- Venue
- Antioxidants
- Publisher
- MDPI AG
- Published
- 2018-11-20
- Volume
- 7
- Issue
- 11
- Pages
- 168
- ISSN
- 2076-3921 (ISSN-L)
- PMC
- PMC6262572
- OpenAlex
- W2901436247
- Cited by
- 90
- References
- 319
- Citations by year
- 2026: 9 · 2025: 9 · 2024: 8 · 2023: 17 · 2022: 14 · 2021: 11 · 2020: 10 · 2019: 12
- FWCI
- 0.81
- Type
- journal article
- Language
- en
- Open access
- gold
- dx.doi.org
- Licence
- Locations
- Antioxidants (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- GoeScholar The Publication Server of the Georg-August-Universität Göttingen (Georg-August-Universität Göttingen) (submittedVersion, cc-by)
- Funders
- Deutsche Forschungsgemeinschaft (NO 1230/2-1)
- Associazione Italiana per la Ricerca sul Cancro (IG 2016-18824)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- plasma membrane, redox signaling, reactive oxygen species, NADPH oxidase, lipid rafts, caveolae, oxidative stress, inflammatory bowel disease, neurodegenerative diseases, signal transduction
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