Role of peroxisomes in ros/rns-metabolism: Implications for human disease

Nitric Oxide and Peroxynitrite in Health and Disease

Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390 · see citing works

Crosstalk of reactive oxygen species and NF-κB signaling

Morgan, M. J., & Liu, Z.-G. (2011) · Cell Research · doi:10.1038/cr.2010.178 · Cited by 3,505 · see citing works

Reactive oxygen species, cellular redox systems, and apoptosis

Circu, M. L., & Aw, T. Y. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.022 · Cited by 3,340 · see citing works

Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production

Powers, S. K., & Jackson, M. J. (2008) · Physiological Reviews · doi:10.1152/physrev.00031.2007 · Cited by 2,459 · see citing works

Superoxide Dismutases: Role in Redox Signaling, Vascular Function, and Diseases

Fukai, T., & Ushio‐Fukai, M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3999 · Cited by 2,009 · see citing works

Extension of murine life span by overexpression of catalase targeted to mitochondria

Schriner, S. E., Linford, N. J., Martin, G. M., Treuting, P., Ogburn, C. E., Emond, M., Coskun, P. E., Ladiges, W., Wolf, N., Van Remmen, H., et al. (2005) · Science · doi:10.1126/science.1106653 · Cited by 1,724 · see citing works

Peroxisomes (microbodies and related particles).

De Duve, C., & Baudhuin, P. (1966) · Physiological Reviews · doi:10.1152/physrev.1966.46.2.323 · Cited by 1,666 · 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

Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Cycle or a Double-Edged Sword?

Malhotra, J. D., & Kaufman, R. J. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1782 · Cited by 1,555 · see citing works

The cellular production of hydrogen peroxide

Boveris, A., Oshino, N., & Chance, B. (1972) · Biochemical Journal · doi:10.1042/bj1280617 · Cited by 1,549 · see citing works

Hydrogen peroxide: a metabolic by-product or a common mediator of ageing signals?

Giorgio, M., Trinei, M., Migliaccio, E., & Pelicci, P. G. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2240 · Cited by 1,450 · see citing works

Regulation of autophagy by ROS: physiology and pathology

Scherz-Shouval, R., & Elazar, Z. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.007 · Cited by 1,263 · 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

Low antioxidant enzyme gene expression in pancreatic islets compared with various other mouse tissues

Lenzen, S., Drinkgern, J., & Tiedge, M. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(96)02051-5 · Cited by 1,167 · 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 cytoprotective role of the Keap1–Nrf2 pathway

Baird, L., & Dinkova‐Kostova, A. T. (2011) · Archives of Toxicology · doi:10.1007/s00204-011-0674-5 · Cited by 1,029 · see citing works

Investigating Mitochondrial Redox Potential with Redox-sensitive Green Fluorescent Protein Indicators

Hanson, G. T., Aggeler, R., Oglesbee, D., Cannon, M., Capaldi, R. A., Tsien, R. Y., & Remington, S. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312846200 · Cited by 988 · see citing works

Fluorescent and luminescent probes for detection of reactive oxygen and nitrogen species

Chen, X., Tian, X., Shin, I., & Yoon, J. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15037e · Cited by 980 · see citing works

The chemical biology of nitric oxide: Implications in cellular signaling

Thomas, D. D., Ridnour, L. A., Isenberg, J. S., Flores-Santana, W., Switzer, C. H., Donzelli, S., Hussain, P., Vecoli, C., Paolocci, N., Ambs, S., et al. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.020 · Cited by 975 · see citing works

Peroxisomes are signaling platforms for antiviral innate immunity

Dixit, E., Boulant, S., Zhang, Y.-J., Lee, A. S., Odendall, C., Shum, B. O. V., Hacohen, N., Chen, Z.-J. J., Whelan, S. P. J., Fransen, M., et al. (2010) · Cell · doi:10.1016/j.cell.2010.04.018 · Cited by 848 · see citing works

The role of mitochondria in reactive oxygen species metabolism and signaling

Starkov, A. A. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.015 · Cited by 846 · see citing works

Peroxisomes and oxidative stress

Schrader, M., & Fahimi, H. D. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.09.006 · Cited by 838 · see citing works

Hypolipidaemic hepatic peroxisome proliferators form a novel class of chemical carcinogens

Reddy, J. K., Azarnoff, D. L., & Hignite, C. E. (1980) · Nature · doi:10.1038/283397a0 · Cited by 835 · see citing works

COPPER-ZINC SUPEROXIDE DISMUTASE AND AMYOTROPHIC LATERAL SCLEROSIS

Valentine, J. S., Doucette, P. A., & Potter, S. Z. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161647 · Cited by 790 · see citing works

Structure and function of xanthine oxidoreductase: where are we now?

Harrison, R. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00956-5 · Cited by 787 · see citing works

Minireview: Secondary β-Cell Failure in Type 2 Diabetes—A Convergence of Glucotoxicity and Lipotoxicity

Poitout, V., & Robertson, R. P. (2002) · Endocrinology · doi:10.1210/endo.143.2.8623 · Cited by 743 · see citing works

Mitochondrial retrograde signaling

Liu, Z., & Butow, R. A. (2006) · Annual Review of Genetics · doi:10.1146/annurev.genet.40.110405.090613 · Cited by 680 · see citing works

Reactive oxygen species as universal constraints in life-history evolution

Dowling, D. K., & Simmons, L. W. (2009) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.2008.1791 · Cited by 673 · see citing works

A genetically encoded photosensitizer

Bulina, M. E., Chudakov, D. M., Britanova, O. V., Yanushevich, Y. G., Staroverov, D. B., Chepurnykh, T. V., Merzlyak, E. M., Shkrob, M., Lukyanov, S., & Lukyanov, K. A. (2005) · Nature Biotechnology · doi:10.1038/nbt1175 · Cited by 590 · see citing works

Mechanisms and Implications of Reactive Oxygen Species Generation During the Unfolded Protein Response: Roles of Endoplasmic Reticulum Oxidoreductases, Mitochondrial Electron Transport, and NADPH Oxidase

Santos, C. X. C., Tanaka, L. Y., Wosniak, J., & Laurindo, F. R. M. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2625 · Cited by 572 · see citing works

Nonequilibrium thermodynamics of thiol/disulfide redox systems: A perspective on redox systems biology

Kemp, M. L., Go, Y., & Jones, D. P. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.11.008 · Cited by 568 · see citing works

Chemistry and biochemistry of lipid peroxidation products

Guéraud, F., Atalay, M., Bresgen, N., Gašparović, A. Č., Eckl, P., Laurence Therese, H. U. C., Jouanin, I., Siems, W., & Uchida, K. (2010) · Free Radical Research · doi:10.3109/10715762.2010.498477 · Cited by 556 · see citing works

Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes

Kim, P. K., Hailey, D. W., Mullen, R. T., & Lippincott‐Schwartz, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810611105 · Cited by 533 · see citing works

Fluorescent Protein-Based Redox Probes

Meyer, A. J., & Dick, T. P. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2948 · Cited by 528 · see citing works

New insights into the role of mitochondria in aging: mitochondrial dynamics and more

Seo, A. Y., Joseph, A.-M., Dutta, D., Hwang, J. C. Y., Aris, J. P., & Leeuwenburgh, C. (2010) · Journal of Cell Science · doi:10.1242/jcs.070490 · Cited by 522 · cited 1× · see citing works

Irreversible reaction of 3-amino-1:2:4-triazole and related inhibitors with the protein of catalase

Margoliash, E., Novogrodsky, A., & Schejter, A. (1960) · Biochemical Journal · doi:10.1042/bj0740339 · Cited by 491 · see citing works

Redox Regulation in Cancer: A Double‐edged Sword with Therapeutic Potential

Acharya, A., Das, I., Chandhok, D., & Saha, T. (2009) · Oxidative Medicine and Cellular Longevity · doi:10.4161/oxim.3.1.10095 · Cited by 487 · see citing works

Cellular Metabolic Stress: Considering How Cells Respond to Nutrient Excess

Wellen, K. E., & Thompson, C. B. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.004 · Cited by 486 · see citing works

Thioredoxins and Glutaredoxins: Unifying Elements in Redox Biology

Meyer, Y., Buchanan, B. B., Vignols, F., & Reichheld, J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134201 · Cited by 482 · see citing works

Redox‐sensitive GFP in Arabidopsis thaliana is a quantitative biosensor for the redox potential of the cellular glutathione redox buffer

Meyer, A. J., Brach, T., Marty, L., Kreye, S., Rouhier, N., Jacquot, J., & Hell, R. (2007) · The Plant Journal · doi:10.1111/j.1365-313x.2007.03280.x · Cited by 467 · see citing works

Transgenic mice with increased Cu/Zn-superoxide dismutase activity: animal model of dosage effects in Down syndrome.

Epstein, C. J., Avraham, K. B., Lovett, M., Smith, S. H., Elroy‐Stein, O., Rotman, G., Bry, C., & Groner, Y. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.22.8044 · Cited by 454 · see citing works

Update on the oxidative stress theory of aging: Does oxidative stress play a role in aging or healthy aging?

Salmon, A. B., Richardson, A. G., & Pérez, V. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.015 · Cited by 444 · see citing works

Mammalian catalase: a venerable enzyme with new mysteries

Kirkman, H. N., & Gaetani, G. F. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.11.003 · Cited by 411 · see citing works

Mice Lacking Catalase Develop Normally but Show Differential Sensitivity to Oxidant Tissue Injury

Ho, Y.-S., Xiong, Y., Ma, W., Spector, A., & Ho, D. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404800200 · Cited by 403 · 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

Mitochondrial ROS Generation and Its Regulation: Mechanisms Involved in H ₂ O ₂ Signaling

Rigoulet, M., Yoboue, E. D., & Devin, A. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3363 · Cited by 394 · see citing works

PPARα: Energy Combustion, Hypolipidemia, Inflammation and Cancer

Pyper, S. R., Viswakarma, N., Yu, S., & Reddy, J. K. (2010) · Nuclear Receptor Signaling · doi:10.1621/nrs.08002 · Cited by 381 · see citing works

Cysteine-Based Redox Switches in Enzymes

Klomsiri, C., Karplus, P., & Poole, L. B. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3376 · Cited by 366 · see citing works

Axonal loss and neuroinflammation caused by peroxisome-deficient oligodendrocytes

Kassmann, C. M., Lappe-Siefke, C., Baes, M., Brügger, B., Mildner, A., Werner, H. B., Natt, O., Michaelis, T., Prinz, M., Frahm, J., et al. (2007) · Nature Genetics · doi:10.1038/ng2070 · Cited by 357 · see citing works

A possible role for plasmalogens in protecting animal cells against photosensitized killing.

Zoeller, R. A., Morand, O. H., & Raetz, C. R. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)38000-1 · Cited by 348 · see citing works

Identification of peroxisomal targeting signals located at the carboxy terminus of four peroxisomal proteins.

Gould, S. J., Keller, G. A., & Subramani, S. E. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.3.897 · Cited by 341 · see citing works

Biochemistry and genetics of inherited disorders of peroxisomal fatty acid metabolism

Veldhoven, P. P. V. (2010) · Journal of Lipid Research · doi:10.1194/jlr.r005959 · Cited by 328 · see citing works

Plasmalogens the neglected regulatory and scavenging lipid species

Wallner, S., & Schmitz, G. (2011) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2011.06.008 · Cited by 324 · see citing works

Transcription regulation of peroxisomal fatty acyl-CoA oxidase and enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase in rat liver by peroxisome proliferators.

Reddy, J. K., Goel, S. K., Nemali, M. R., Carrino, J. J., Laffler, T. G., Reddy, M. K., Sperbeck, S. J., Osumi, T., Hashimoto, T., & Lalwani, N. D. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.6.1747 · Cited by 323 · see citing works

S-Glutathionylation: From Molecular Mechanisms to Health Outcomes

Xiong, Y., Uys, J. D., Tew, K. D., & Townsend, D. M. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3540 · Cited by 314 · see citing works

There is no evidence that mitochondria are the main source of reactive oxygen species in mammalian cells

Brown, G. C., & Borutaitė, V. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.02.001 · Cited by 280 · see citing works

Peroxisomal disorders: The single peroxisomal enzyme deficiencies

Wanders, R. J. A., & Waterham, H. R. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.08.010 · Cited by 279 · see citing works

Role of Hydrogen Peroxide in NF-κB Activation: From Inducer to Modulator

Oliveira-Marques, V., Marinho, H. S., Cyrne, L., & Antunes, F. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2601 · Cited by 278 · see citing works

A mouse model for Zellweger syndrome

Baes, M., Gressens, P., Baumgart, E., Carmeliet, P., Casteels, M., Fransen, M., Evrard, P., Fahimi, D., Declercq, P. E., Collen, D., et al. (1997) · Nature Genetics · doi:10.1038/ng0997-49 · Cited by 275 · see citing works

Reactive oxygen species and peroxisomes: Struggling for balance

Bonekamp, N. A., Völkl, A., Fahimi, H. D., & Schrader, M. (2009) · BioFactors · doi:10.1002/biof.48 · Cited by 274 · see citing works

Human catalase: looking for complete identity

Goyal, M. M., & Basak, A. (2010) · Protein & Cell · doi:10.1007/s13238-010-0113-z · Cited by 273 · see citing works

Caloric restriction or catalase inactivation extends yeast chronological lifespan by inducing H 2 O 2 and superoxide dismutase activity

Mesquita, A., Weinberger, M., Silva, A., Sampaio‐Marques, B., Almeida, B., Leão, C., Costa, V., Rodrigues, F. J. S., Burhans, W. C., & Ludovico, P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004432107 · Cited by 268 · see citing works

Proteomic Analysis of Rat Liver Peroxisome

Kikuchi, M., Hatano, N., Yokota, S., Shimozawa, N., Imanaka, T., & Taniguchi, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m305623200 · Cited by 258 · see citing works

Peroxiredoxin 5: Structure, Mechanism, and Function of the Mammalian Atypical 2-Cys Peroxiredoxin

Knoops, B., Goemaere, J., der Eecken, V. V., & Declercq, J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3584 · Cited by 257 · see citing works

Discovery of the nitric oxide signaling pathway and targets for drug development

Nathan, S. B. (2009) · Frontiers in bioscience · doi:10.2741/3228 · Cited by 256 · see citing works

SnapShot: Reactive Oxygen Intermediates (ROI)

Nathan, C., & Ding, A. H. (2010) · Cell · doi:10.1016/j.cell.2010.03.008 · Cited by 240 · see citing works

Catalase enzyme mutations and their association with diseases

Góth, L., Rass, P., & Páy, A. (2004) · Molecular Diagnosis · doi:10.1007/bf03260057 · Cited by 239 · see citing works

Cellular Senescence: Molecular Mechanisms, In Vivo Significance, and Redox Considerations

Müller, M. K. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2104 · Cited by 237 · see citing works

Formation of 8-hydroxydeoxyguanosine in liver DNA of rats following long-term exposure to a peroxisome proliferator.

Kasai, H., Okada, Y., Nishimura, S., Rao, M. S. R., & Reddy, J. K. (1989) · PubMed · Cited by 230 · see citing works

Hydrogen peroxide generation in peroxisome proliferator-induced oncogenesis

Yeldandi, A. V., Rao, M. S., & Reddy, J. K. (2000) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(99)00234-1 · Cited by 225 · see citing works

Peroxisomes Are Oxidative Organelles

Antonenkov, V. D., Grunau, S., Ohlmeier, S., & Hiltunen, J. K. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2996 · Cited by 223 · see citing works

Peroxisome-generated hydrogen peroxide as important mediator of lipotoxicity in insulin-producing cells

Elsner, M., Gehrmann, W., & Lenzen, S. (2011) · Diabetes · doi:10.2337/db09-1401 · Cited by 221 · see citing works

Mammalian epoxide hydrolases in xenobiotic metabolism and signalling

Decker, M., Arand, M., & Cronin, A. (2009) · Archives of Toxicology · doi:10.1007/s00204-009-0416-0 · Cited by 216 · see citing works

Late onset neurological phenotype of the X-ALD gene inactivation in mice: a mouse model for adrenomyeloneuropathy

Pujol, A. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.5.499 · Cited by 214 · see citing works

Hydrogen Peroxide Probes Directed to Different Cellular Compartments

Malinouski, M., Zhou, Y., Belousov, V. V., Hatfield, D. L., & Gladyshev, V. N. (2011) · PLoS ONE · doi:10.1371/journal.pone.0014564 · Cited by 211 · see citing works

Mitochondrial Alterations Caused by Defective Peroxisomal Biogenesis in a Mouse Model for Zellweger Syndrome (PEX5 Knockout Mouse)

Baumgart, E., Vanhorebeek, I., Grabenbauer, M., Borgers, M., Declercq, P. E., Fahimi, H. D., & Baes, M. (2001) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)62534-5 · Cited by 210 · see citing works

The characteristics of the ‘peroxidatic’ reaction of catalase in ethanol oxidation

Oshino, N., Oshino, R., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1310555 · Cited by 201 · see citing works

Intraperoxisomal redox balance in mammalian cells: oxidative stress and interorganellar cross-talk

Ivashchenko, O., Veldhoven, P. P. V., Brees, C., Ho, Y.-S., Terlecky, S. R., & Fransen, M. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-11-0919 · Cited by 199 · see citing works

Hypermethylation of the APC (adenomatous Polyposis Coli) gene promoter region in human colorectal carcinoma

Hiltunen, M., Alhonen, L. I., Koıstınaho, J., Myöhänen, S., Pääkkönen, M. E., Marin, S., Kosma, V.-M., & Jänne, J. (1997) · International Journal of Cancer · doi:10.1002/(sici)1097-0215(19970317)70:6 · Cited by 192 · see citing works

Hereditary catalase deficiencies and increased risk of diabetes

Góth, L., & Eaton, J. W. (2000) · The Lancet · doi:10.1016/s0140-6736(00)03238-4 · Cited by 189 · see citing works

Characterization of the Oxidase Activity in Mammalian Catalase

Vetrano, A. M., Heck, D. E., Mariano, T. M., Mishin, V. M., Laskin, D. L., & Laskin, J. D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503991200 · Cited by 183 · see citing works

Pre-steady state kinetic characterization of human peroxiredoxin 5: Taking advantage of Trp84 fluorescence increase upon oxidation

Trujillo, M., Clippe, A., Manta, B., Ferrer‐Sueta, G., Smeets, A., Declercq, J., Knoops, B., & Radí, R. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.08.008 · Cited by 180 · see citing works

Peroxisome Dynamics in Cultured Mammalian Cells

Huybrechts, S. J., Veldhoven, P. P. V., Brees, C., Mannaerts, G. P., Los, G. V., & Fransen, M. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00970.x · Cited by 180 · see citing works

Gene and Protein Characterization of the Human Glutathione S-Transferase Kappa and Evidence for a Peroxisomal Localization

Morel, F., Rauch, C., Petit, E., Piton, A., Théret, N., Coles, B., & Guillouzo, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313357200 · Cited by 179 · see citing works

Peroxisome Senescence in Human Fibroblasts

Legakis, J. E., Koepke, J. I., Jedeszko, C., Barlaskar, F. M., Terlecky, L. J., Edwards, H. J., Walton, P. A., & Terlecky, S. R. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-06-0322 · Cited by 176 · see citing works

Catalase expression in delayed and premature aging mouse models☆

Brown‐Borg, H. M., & Rakoczy, S. G. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00079-6 · Cited by 174 · see citing works

Ubiquitination of Mammalian Pex5p, the Peroxisomal Import Receptor

Carvalho, A. F., Pinto, M. P., Grou, C. P. O., Alencastre, I. S., Fransen, M., Sá-Miranda, C., & Azevedo, J. E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706325200 · Cited by 174 · see citing works

Role of metabolically generated reactive oxygen species for lipotoxicity in pancreatic β ‐cells

Gehrmann, W., Elsner, M., & Lenzen, S. (2010) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01265.x · Cited by 174 · see citing works

Viral-mediated Inhibition of Antioxidant Enzymes Contributes to the Pathogenesis of Severe Respiratory Syncytial Virus Bronchiolitis

Hosakote, Y. M., Jantzi, P. D., Esham, D. L., Spratt, H. M., Kurosky, A., Casola, A., & Garofalo, R. P. (2011) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201010-1755oc · Cited by 170 · see citing works

Targeting of human catalase to peroxisomes is dependent upon a novel COOH-terminal peroxisomal targeting sequence.

Purdue, P. E., & Lazarow, P. B. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.134.4.849 · Cited by 165 · see citing works

Peroxisome Metabolism and Cellular Aging

Titorenko, V. I., & Terlecky, S. R. (2010) · Traffic · doi:10.1111/j.1600-0854.2010.01144.x · Cited by 161 · see citing works

Monitoring the in vivo redox state of plant mitochondria: Effect of respiratory inhibitors, abiotic stress and assessment of recovery from oxidative challenge

Schwarzländer, M., Fricker, M. D., & Sweetlove, L. J. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.01.020 · Cited by 161 · see citing works

Interactions of plasmalogens and their diacyl analogs with singlet oxygen in selected model systems

Broniec, A., Klosinski, R., Pawlak, A. M., Wrona, M., Thompson, D. H., & Sarna, T. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.01.002 · Cited by 159 · see citing works

Detection and manipulation of mitochondrial reactive oxygen species in mammalian cells

Forkink, M., Smeitink, J. A. M., Brock, R. E., Willems, P. H. G. M., & Koopman, W. J. H. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.01.022 · Cited by 150 · see citing works

Lack of Peroxisomal Catalase Causes a Progeric Phenotype in Caenorhabditis elegans

Petriv, O. I., & Rachubinski, R. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400207200 · Cited by 148 · see citing works

Peroxisomes as a cellular source of reactive nitrogen species signal molecules

del Río, L. A. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.10.022 · Cited by 144 · see citing works

Pxmp2 Is a Channel-Forming Protein in Mammalian Peroxisomal Membrane

Rokka, A., Antonenkov, V. D., Soininen, R., Immonen, H. L., Pirilä, P., Bergmann, U., Sormunen, R. T., Weckström, M., Benz, R., & Hiltunen, J. K. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005090 · Cited by 139 · see citing works

Hitchhiking of Cu/Zn Superoxide Dismutase to Peroxisomes – Evidence for a Natural Piggyback Import Mechanism in Mammals

Islinger, M., Li, K. W., Seitz, J., Völkl, A., & Lüers, G. H. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00966.x · Cited by 138 · see citing works

Antioxidants halt axonal degeneration in a mouse model of X‐adrenoleukodystrophy

López‐Erauskin, J., Fourcade, S., Galino, J., Ruíz, M., Schlüter, A., Naudí, A., Jové, M., Portero‐Otín, M., Pamplona, R., Ferrer, I., et al. (2011) · Annals of Neurology · doi:10.1002/ana.22363 · Cited by 135 · see citing works

Regulation of the protein disulfide proteome by mitochondria in mammalian cells

Yang, Y., Song, Y., & Loscalzo, J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702027104 · Cited by 129 · see citing works

Peroxisomal localization of inducible nitric oxide synthase in hepatocytes

Stolz, D. B., Zamora, R., Yoram Vodovotz, B., Loughran, P., Billiar, T. R., Kim, Y., Simmons, R. L., & Watkins, S. C. (2002) · Hepatology · doi:10.1053/jhep.2002.33716 · Cited by 125 · see citing works

Localization of xanthine oxidase in crystalline cores of peroxisomes. A cytochemical and biochemical study.

Angermüller, S., Bruder, G., Völkl, A., Wesch, H., & Fahimi, H. D. (1987) · PubMed · Cited by 125 · see citing works

Nuclear transport, oxidative stress, and neurodegeneration.

Patel, V. P., & Chu, C. T. (2011) · PubMed · Cited by 123 · see citing works

Nitric Oxide Uptake by Erythrocytes Is Primarily Limited by Extracellular Diffusion Not Membrane Resistance

Liu, X., Samouilov, A., Lancaster, J. R., & Zweier, J. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201939200 · Cited by 122 · see citing works

Kinetic studies on the removal of extracellular hydrogen peroxide by cultured fibroblasts.

Makino, N., Mochizuki, Y., Bannai, S., & Sugita, Y. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42214-9 · Cited by 120 · see citing works

Absence of functional peroxisomes from mouse CNS causes dysmyelination and axon degeneration

Hulshagen, L., Krysko, O., Bottelbergs, A., Huyghe, S., Klein, R., Van Veldhoven, P. P., De Deyn, P. P., D'Hooge, R., Hartmann, D., & Baes, M. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4968-07.2008 · Cited by 115 · see citing works

Characterization of Human and Murine PMP20 Peroxisomal Proteins That Exhibit Antioxidant Activity in Vitro

Yamashita, H., Avraham, S., Jiang, S., London, R., Veldhoven, P. P. V., Subramani, S. E., Rogers, R. A., & Avraham, H. K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.42.29897 · Cited by 115 · see citing works

Overexpression of catalase provides partial protection to transgenic mouse beta cells

Xu, B., Moritz, J. T., & Epstein, P. N. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00130-6 · Cited by 114 · see citing works

Restoration of Peroxisomal Catalase Import in a Model of Human Cellular Aging

Koepke, J. I., Nakrieko, K., Wood, C. S., Boucher, K. K., Terlecky, L. J., Walton, P. A., & Terlecky, S. R. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00633.x · Cited by 110 · see citing works

Structural basis for the phototoxicity of the fluorescent protein KillerRed

Carpentier, P., Violot, S., Blanchoin, L., & Bourgeois, D. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.07.041 · Cited by 110 · see citing works

A Novel Fluorescent Sensor Protein for Visualization of Redox States in the Cytoplasm and in Peroxisomes

Yano, T., Oku, M., Akeyama, N., Itoyama, A., Yurimoto, H., Kuge, S., Fujiki, Y., & Sakai, Y. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00121-10 · Cited by 110 · see citing works

Ataxia with loss of Purkinje cells in a mouse model for Refsum disease

Ferdinandusse, S., Zomer, A. W. M., Komen, J. C., Brink, C. E. V. D., Thanos, M., Hamers, F. P. T., Wanders, R. J. A., van der Saag, P. T., Poll‐The, B. T., & Brites, P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806066105 · Cited by 109 · see citing works

The peroxin Pex14p is involved in LC3-dependent degradation of mammalian peroxisomes.

Hara-Kuge, S., & Fujiki, Y. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.09.015 · Cited by 108 · see citing works

Progeric Effects of Catalase Inactivation in Human Cells

Koepke, J. I., Wood, C. S., Terlecky, L. J., Walton, P. A., & Terlecky, S. R. (2008) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2008.06.004 · Cited by 101 · see citing works

Real-time monitoring of redox changes in the mammalian endoplasmic reticulum

van Lith, M., Tiwari, S., Pediani, J. D., et al. (2011) · Journal of Cell Science · doi:10.1242/jcs.085530 · Cited by 97 · see citing works

Antiinflammatory Effects of Hydrogen Peroxide in Neutrophil Activation and Acute Lung Injury

Zmijewski, J. W., Lorne, E., Zhao, X., Tsuruta, Y., Sha, Y., Liu, G., & Abraham, E. H. (2009) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200806-851oc · Cited by 95 · see citing works

A Peroxisomal Lon Protease and Peroxisome Degradation by Autophagy Play Key Roles in Vitality of<i>Hansenula polymorpha</i>Cells

Aksam, E. B., Koek, A., Jourdan, S., Veenhuis, M., & van der Klei, I. J. (2007) · Autophagy · doi:10.4161/auto.3534 · Cited by 95 · see citing works

Organelle dynamics and dysfunction: A closer link between peroxisomes and mitochondria

Camões, F., Bonekamp, N. A., Delille, H. K., & Schrader, M. (2008) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-008-1018-3 · Cited by 91 · see citing works

Neocortical and cerebellar developmental abnormalities in conditions of selective elimination of peroxisomes from brain or from liver

Krysko, O., Hulshagen, L., Janssen, A., Schütz, G., Klein, R., De Bruycker, M., Espeel, M., Gressens, P., & Baes, M. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21097 · Cited by 90 · see citing works

Selective autophagy in the maintenance of cellular homeostasis in aging organisms

Hubbard, V. M., Valdor, R., Macián, F., & Cuervo, A. M. (2011) · Biogerontology · doi:10.1007/s10522-011-9331-x · Cited by 89 · see citing works

Multiple roles of microsomal glutathione transferase 1 in cellular protection: A mechanistic study

Johansson, K., Järvliden, J., Gogvadze, V. G., & Morgenstern, R. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.08.013 · Cited by 85 · see citing works

Selective Oxidative Stress in Cell Nuclei by Nuclear-Targeted D-Amino Acid Oxidase

Halvey, P. J., Hansen, J. M., Johnson, J. M., Go, Y., Afshin Samali, A., & Jones, D. P. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1526 · Cited by 81 · see citing works

Oligodendroglial cells in culture effectively dispose of exogenous hydrogen peroxide: comparison with cultured neurones, astroglial and microglial cells

Hirrlinger, J., Resch, A., Gutterer, J. M., & Dringen, R. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00999.x · Cited by 81 · see citing works

Catalase transgenic mice: characterization and sensitivity to oxidative stress

Chen, X., Liang, H., Remmen, H. V., Vijg, J., & Richardson, A. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.12.023 · Cited by 77 · see citing works

The Peroxisome in Oxidative Stress

Dansen, T. B., & WIRTZ, K. W. A. (2001) · IUBMB Life · doi:10.1080/152165401753311762 · Cited by 77 · see citing works

Abnormality in catalase import into peroxisomes leads to severe neurological disorder

Sheikh, F. G., Pahan, K., Khan, M., Barbosa, E., & Singh, I. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.2961 · Cited by 75 · see citing works

Impairment of peroxisomal biogenesis in human colon carcinoma

Lauer, C. (1999) · Carcinogenesis · doi:10.1093/carcin/20.6.985 · Cited by 75 · see citing works

Electron spin resonance study on the permeability of superoxide radicals in lipid bilayers and biological membranes

Mao, G. D., & Poznansky, M. J. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80675-7 · Cited by 70 · see citing works

Insights into the membrane proteome of rat liver peroxisomes: Microsomal glutathione‐S‐transferase is shared by both subcellular compartments

Islinger, M., Lüers, G. H., Zischka, H., Ueffing, M., & Völkl, A. (2005) · PROTEOMICS · doi:10.1002/pmic.200401347 · Cited by 70 · see citing works

Soluble Epoxide Hydrolase in Atherosclerosis

Wang, Y.-X. J., Ulu, A., Zhang, L.-N., & Hammock, B. D. (2010) · Current Atherosclerosis Reports · doi:10.1007/s11883-010-0108-5 · Cited by 70 · see citing works

Transformation of mammalian cells by overexpressing H2O2-generating peroxisomal fatty acyl-CoA oxidase.

Chu, S., Huang, Q. M., Alvares, K., et al. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.15.7080 · Cited by 67 · see citing works

Compartment-dependent management of H2O2 by peroxisomes

Fritz, R., Bol, J., Hebling, U., Angermüller, S., Völkl, A., Fahimi, H. D., & Mueller, S. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.01.014 · Cited by 65 · see citing works

Peroxisomes, myelination, and axonal integrity in the CNS

Baes, M., & Aubourg, P. (2009) · The Neuroscientist · doi:10.1177/1073858409336297 · Cited by 65 · see citing works

Biochemical and genetic characterization of a murine class Kappa glutathione S-transferase

Jowsey, I. R., Thomson, R. E., Orton, T. C., Elcombe, C. R., & Hayes, J. D. (2003) · Biochemical Journal · doi:10.1042/bj20030415 · Cited by 64 · see citing works

Monomeric inducible nitric oxide synthase localizes to peroxisomes in hepatocytes

Loughran, P., Stolz, D. B., Yoram Vodovotz, B., Watkins, S. C., Simmons, R. L., & Billiar, T. R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503926102 · Cited by 64 · see citing works

Renal cell carcinoma and oxidative stress: The lack of peroxisomes

Frederiks, W. M., Bosch, K. S., Hoeben, K. A., et al. (2009) · Acta Histochemica · doi:10.1016/j.acthis.2009.03.003 · Cited by 62 · see citing works

Prevention of Mammary Tumorigenesis in Acatalasemic Mice by Vitamin E Supplementation

Ishii, K., Zhen, L., Wang, D., Funamori, Y., Ogawa, K., & Taketa, K. (1996) · Japanese Journal of Cancer Research · doi:10.1111/j.1349-7006.1996.tb00277.x · Cited by 61 · see citing works

Insulinoma cells in culture show pronounced sensitivity to alloxan-induced oxidative stress

Zhang, H., �llinger, K., & Brunk, U. T. (1995) · Diabetologia · doi:10.1007/bf00401832 · Cited by 60 · see citing works

Redox-Sensitive Green Fluorescent Protein: Probes for Dynamic Intracellular Redox Responses. A Review

Cannon, M. B., & Remington, S. J. (2008) · Methods in molecular biology · doi:10.1007/978-1-59745-129-1_4 · Cited by 60 · see citing works

Immunocytochemical investigation of catalase and peroxisomal lipid β-oxidation enzymes in human hepatocellular tumors and liver cirrhosis

Litwin, J. A., Beier, K., Völkl, A., Hofmann, W. J., & Fahimi, H. D. (1999) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/s004280050432 · Cited by 57 · see citing works

Hypocatalasemic Fibroblasts Accumulate Hydrogen Peroxide and Display Age-Associated Pathologies

Wood, C. S., Koepke, J. I., Teng, H., Boucher, K. K., Katz, S., Chang, P., Terlecky, L. J., Papanayotou, I., Walton, P. A., & Terlecky, S. R. (2006) · Traffic · doi:10.1111/j.1600-0854.2005.00358.x · Cited by 55 · see citing works

Mitochondrial Targeting of a Catalase Transgene Product by Plasmid Liposomes Increases RadioresistanceIn VitroandIn Vivo

Epperly, M. W., Melendez, J. A., Zhang, X., Nie, S., Pearce, L. L., Peterson, J., Franicola, D., Dixon, T. M., Greenberger, B. A., Komanduri, P., et al. (2009) · Radiation Research · doi:10.1667/rr1424.1 · Cited by 55 · see citing works

A Role for Hydrogen Peroxide in the Pro‐apoptotic Effects of Photodynamic Therapy

Price, M., Terlecky, S. R., & Kessel, D. H. (2009) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.2009.00589.x · Cited by 55 · see citing works

Reining in H2O2 for Safe Signaling

Tolédano, M. B., Planson, A., & Delaunay, A. (2010) · Cell · doi:10.1016/j.cell.2010.02.003 · Cited by 52 · see citing works

A role for myelin-associated peroxisomes in maintaining paranodal loops and axonal integrity

Kassmann, C. M., Quintes, S., Rietdorf, J., Möbius, W., Sereda, M. W., Nientiedt, T., Saher, G., Baes, M., & Nave, K.-A. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.032 · Cited by 52 · see citing works

Expression of the Hydrogen Peroxide-Generating Enzyme Fatty Acyl CoA Oxidase Activates NF-kappa B

LI, Y., Tharappel, J. C., Cooper, S., Glenn, M., Glauert, H. P., & Spear, B. T. (2000) · DNA and Cell Biology · doi:10.1089/104454900314627 · Cited by 52 · see citing works

Sensitive and real-time determination of H2O2 release from intact peroxisomes

Mueller, S., Weber, A., Fritz, R., Mütze, S., Rost, D., Walczak, H., Völkl, A., & Stremmel, W. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3630483 · Cited by 51 · see citing works

Phytanoyl-CoA hydroxylase: recognition of 3-methyl-branched acyl-CoAs and requirement for GTP or ATP and Mg2+ in addition to its known hydroxylation cofactors

Croes, K., Foulon, V., Casteels, M., Veldhoven, P. P. V., & Mannaerts, G. P. (2000) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)32411-1 · Cited by 44 · see citing works

Photosensitized killing of cultured fibroblasts from patients with peroxisomal disorders due to pyrene fatty acid-mediated ultraviolet damage.

Höefler, G., Paschke, E., Hoefler, S., Moser, A. B., & Moser, H. W. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115509 · Cited by 43 · see citing works

A specific fluorescence probe for hydrogen peroxide detection in peroxisomes

Gehrmann, W., & Elsner, M. (2011) · Free Radical Research · doi:10.3109/10715762.2011.560148 · Cited by 37 · see citing works

Stereochemical features of the hydrolysis of 9,10-epoxystearic acid catalysed by plant and mammalian epoxide hydrolases

Summerer, S., Hanano, A., Utsumi, S., et al. (2002) · Biochemical Journal · doi:10.1042/bj20011778 · Cited by 35 · see citing works

The ascorbic acid paradox

Osiecki, M. J., Ghanavi, P., Atkinson, K., Nielsen, L. K., & Doran, M. R. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.08.052 · Cited by 31 · see citing works

Differential subcellular localization of endogenous and transfected soluble epoxide hydrolase in mammalian cells: evidence for isozyme variants

Mullen, R. T., Trelease, R. N., Duerk, H., et al. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00142-8 · Cited by 22 · see citing works

Targeted intracellular catalase delivery protects neonatal rat myocytes from hypoxia-reoxygenation and ischemia-reperfusion injury

Undyala, V. V. R., Terlecky, S. R., & Heide, R. S. V. (2010) · Cardiovascular Pathology · doi:10.1016/j.carpath.2010.06.011 · Cited by 22 · see citing works

Mitochondrial targeting of peroxiredoxin 5 is preserved from annelids to mammals but is absent in pig Sus scrofa domesticus

der Eecken, V. V., Clippe, A., Veldhoven, P. P. V., & Knoops, B. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.06.013 · Cited by 16 · see citing works

Assessment of Physiological Redox State with Novel FRET Protein Probes

Oku, M., & Sakai, Y. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4251 · Cited by 14 · see citing works

Genotypes of the glutathione S-transferase superfamily do not correlate with outcome of childhood acute lymphoblastic leukemia

Sala, A., Lanciotti, M., Valsecchi, M. G., et al. (2003) · Leukemia · doi:10.1038/sj.leu.2402888 · Cited by 13 · see citing works

Investigation of peroxisomal lipid beta-oxidation enzymes in guinea pig liver peroxisomes by immunoblotting and immunocytochemistry.

Yamamoto, H., Völkl, A., & Fahimi, H. D. (1992) · Journal of Histochemistry & Cytochemistry · doi:10.1177/40.12.1360481 · Cited by 10 · see citing works

High sensitivity to hepato-tumorigenesis in hypocatalasemic C3H/C(s)b/Gen mice exposed to low doses of 252Cf fission neutrons and 60Co gamma-rays.

Yamada, K., Ito, A., Watanabe, H., et al. (1997) · PubMed · Cited by 7 · see citing works

ROS and the DNA damage response in cancer

Srinivas, U. S., Tan, B. W. Q., Vellayappan, B. A., & Jeyasekharan, A. D. (2019) · Redox Biology · doi:10.1016/j.redox.2018.101084 · Cited by 2,144 · see citing works

Reactive Oxygen Species in Metabolic and Inflammatory Signaling

Forrester, S. J., Kikuchi, D. S., Hernandes, M. S., Xu, Q., & Griendling, K. K. (2018) · Circulation Research · doi:10.1161/circresaha.117.311401 · Cited by 2,081 · see citing works

Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease

Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130 · see citing works

ROS, Cell Senescence, and Novel Molecular Mechanisms in Aging and Age‐Related Diseases

Davalli, P., Mitic, T., Caporali, A., Lauriola, A., & D’Arca, D. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3565127 · Cited by 1,059 · see citing works

Oxidative Stress in Aging Human Skin

Rinnerthaler, M., Bischof, J., Streubel, M., Trost, A., & Richter, K. (2015) · Biomolecules · doi:10.3390/biom5020545 · Cited by 1,053 · see citing works

ROS Generation and Antioxidant Defense Systems in Normal and Malignant Cells

Snezhkina, A. V., Kudryavtseva, A. V., Kardymon, O. L., Savvateeva, M. V., Melnikova, N. V., Krasnov, G. S., & Dmitriev, A. A. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6175804 · Cited by 934 · see citing works

Functions of ROS in Macrophages and Antimicrobial Immunity

Herb, M., & Schramm, M. (2021) · Antioxidants · doi:10.3390/antiox10020313 · Cited by 633 · see citing works

ROS production in phagocytes: Why, when, and where?

Dupré-Crochet, S., Erard, M., & Nüβe, O. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.1012544 · Cited by 467 · see citing works

The Peroxisome-Mitochondria Connection: How and Why?

Fransen, M., Lismont, C., & Walton, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061126 · Cited by 351 · see citing works

Metabolic Interplay between Peroxisomes and Other Subcellular Organelles Including Mitochondria and the Endoplasmic Reticulum

Wanders, R. J. A., Waterham, H. R., & Ferdinandusse, S. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00083 · Cited by 366 · see citing works

Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact

Shai, N., Yifrach, E., van Roermund, C. W. T., Cohen, N., Bibi, C., IJlst, L., Cavellini, L., Meurisse, J., Schuster, R., Zada, L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03957-8 · Cited by 320 · see citing works

Redox interplay between mitochondria and peroxisomes

Lismont, C., Nordgren, M., Van Veldhoven, P. P., & Fransen, M. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00035 · Cited by 214 · see citing works

Peroxisomes in brain development and function

Berger, J., Dorninger, F., Forss-Petter, S., & Kunze, M. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.12.005 · Cited by 194 · see citing works

Does PGC1α/FNDC5/BDNF Elicit the Beneficial Effects of Exercise on Neurodegenerative Disorders?

Jodeiri Farshbaf, M., Ghaedi, K., Megraw, T. L., Curtiss, J., Shirani Faradonbeh, M., Vaziri, P., & Nasr-Esfahani, M. H. (2016) · NeuroMolecular Medicine · doi:10.1007/s12017-015-8370-x · Cited by 101 · see citing works

Spaceflight Activates Autophagy Programs and the Proteasome in Mouse Liver

Blaber, E., Pecaut, M., & Jonscher, K. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18102062 · Cited by 70 · see citing works

Peroxisomal ABC Transporters: An Update

Tawbeh, A., Gondcaille, C., Trompier, D., & Savary, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116093 · Cited by 68 · see citing works

Peroxisome degradation in mammals: mechanisms of action, recent advances, and perspectives

Nordgren, M., Wang, B., Apanasets, O., & Fransen, M. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00145 · Cited by 67 · see citing works

Mitochondrial dysfunction and oxidative damage cooperatively fuel axonal degeneration in X-linked adrenoleukodystrophy

Fourcade, S., López-Erauskin, J., Ruiz, M., Ferrer, I., & Pujol, A. (2014) · Biochimie · doi:10.1016/j.biochi.2013.09.012 · Cited by 55 · see citing works

Global analysis of S-nitrosylation sites in the wild type (APP) transgenic mouse brain: Clues for synaptic pathology

Zaręba-Kozioł, M., Szwajda, A., Dadlez, M., Wysłouch-Cieszyńska, A., & Lalowski, M. (2014) · Molecular &amp; Cellular Proteomics · doi:10.1074/mcp.m113.036079 · Cited by 39 · see citing works

Mitochondrial free radical theory of aging: Who moved my premise?: MFRTA: Who moved my premise?

Liu, Y., Long, J., & Liu, J. (2014) · Geriatrics &amp; Gerontology International · doi:10.1111/ggi.12296 · Cited by 27 · see citing works

When friendship turns sour: Effective communication between mitochondria and intracellular organelles in parkinson’s disease

Lin, T.-K., Lin, K.-J., Lin, K.-L., Liou, C.-W., Chen, S.-D., Chuang, Y.-C., Wang, P.-W., Chuang, J.-H., & Wang, T.-J. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.607392 · Cited by 19 · see citing works

Hansenula polymorpha : A Versatile Model Organism in Peroxisome Research

van der Klei, I. J., & Veenhuis, M. (2002) · doi:10.1002/3527602356.ch6 · Cited by 14 · see citing works

Pex24 and Pex32 tether peroxisomes to the ER for organelle biogenesis, positioning and segregationPreprint

Wu, F., de Boer, R., Krikken, A. M., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.05.977884 · Cited by 6 · see citing works

Interactions between nitric oxide, oxygen, reactive oxygen species and reactive nitrogen species

Brown, G. C., & Borutaitė, V. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340953 · Cited by 57 · see citing works

Peroxisome-Mediated Reactive Oxygen Species Signals Modulate Programmed Cell Death in Plants

Huang, L., Liu, Y., Wang, X., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231710087 · Cited by 35 · see citing works

Peroxisome biogenesis and the role of protein import

Brown, L., & Baker, A. (2003) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2003.tb00241.x · Cited by 81 · see citing works