Nitric Oxide Regulates Mitochondrial Fatty Acid Metabolism Through Reversible Protein S -Nitrosylation
Open accessAbstract
S -nitrosylation increases the catalytic efficiency of an enzyme critical to fatty acid β-oxidation.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
NO from NOS-2 inhibits mitochondria.
“potentially mediated by the well-known inhibition of mitochondria by NO from NOS-2 (BalPrice et al., 2002) (Kelly and O'Neill, 2015) (Doulias et al., 2013).”
From TET2 Regulates the Neuroinflammatory Response in Microglia (2019) · cites this paper as Doulias et al., 2013
The Discussion (page unavailable) reports that eNOS-derived nitric oxide activates a mitochondrial fatty-acid oxidation enzyme; it does not address whether NO from NOS-2 inhibits mitochondria. Searches for NOS-2, inducible nitric oxide synthase, and mitochondrial respiration inhibition found no passage making that claim. (LLM, conf=0.72)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
A SIMPLE METHOD FOR THE ISOLATION AND PURIFICATION OF TOTAL LIPIDES FROM ANIMAL TISSUES
Folch, J., Lees, M., & Stanley, G. H. S. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64849-5 · Cited by 65,189 · 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
Human Fatty Liver Disease: Old Questions and New Insights
Cohen, J. C., Horton, J. D., & Hobbs, H. H. (2011) · Science · doi:10.1126/science.1204265 · Cited by 2,089 · see citing works
Protein S-nitrosylation: a physiological signal for neuronal nitric oxide
Jaffrey, S. R., Erdjument‐Bromage, H., Ferris, C. D., Tempst, P., & Snyder, S. H. (2001) · Nature Cell Biology · doi:10.1038/35055104 · Cited by 1,402 · see citing works
Stamler (2001) · doi:10.1016/s0092-8674(01)00495-0 · Cited by 1,261 · see citing works
Calorie restriction promotes mitochondrial biogenesis by inducing the expression of eNOS
Nisoli, E., Tonello, C., Cardile, A., Cozzi, V., Bracale, R., Tedesco, L., Falcone, S., Valerio, A., Cantoni, O., Clementi, E., et al. (2005) · Science · doi:10.1126/science.1117728 · Cited by 1,107 · see citing works
S-Nitrosylation of Drp1 Mediates β-Amyloid-Related Mitochondrial Fission and Neuronal Injury
Cho, D.-H., Nakamura, T., Fang, J., Cieplak, P., Godzik, A., Gu, Z., & Lipton, S. A. (2009) · Science · doi:10.1126/science.1171091 · Cited by 1,092 · see citing works
S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
Hara, M. R., Agrawal, N., Kim, S. F., Cascio, M. B., Fujimuro, M., Ozeki, Y., Takahashi, M., Cheah, J. H., Tankou, S. K., Hester, L. D., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1268 · Cited by 1,071 · see citing works
Brown, G. C., & Cooper, C. E. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01290-3 · Cited by 1,055 · see citing works
S -Nitrosylation of Parkin Regulates Ubiquitination and Compromises Parkin's Protective Function
Chung, K. K. K., Thomas, B., Li, X., Pletniková, O., Troncoso, J. C., Marsh, L., Dawson, V. L., & Dawson, T. M. (2004) · Science · doi:10.1126/science.1093891 · Cited by 765 · see citing works
Suhre, K., & Sanejouand, Y. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh368 · Cited by 689 · see citing works
Regulated Protein Denitrosylation by Cytosolic and Mitochondrial Thioredoxins
Benhar, M., Forrester, M. T., Hess, D. T., & Stamler, J. S. (2008) · Science · doi:10.1126/science.1158265 · Cited by 548 · see citing works
Nitric Oxide Regulates Exocytosis by S-Nitrosylation of N-ethylmaleimide-Sensitive Factor
Matsushita, K., Morrell, C. N., Cambien, B., Yang, S.-X., Yamakuchi, M., Bao, C., Hara, M. R., Quick, R. A., Cao, W., O'Rourke, B. P., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00803-1 · Cited by 446 · see citing works
GAPDH mediates nitrosylation of nuclear proteins
Kornberg, M. D., Sen, N., Hara, M. R., Juluri, K. R., Nguyen, J. V., Snowman, A. M., Law, L., Hester, L. D., & Snyder, S. H. (2010) · Nature Cell Biology · doi:10.1038/ncb2114 · Cited by 394 · see citing works
Kobzik, L., Stringer, B., Balligand, J., Reid, M. B., & Stamler, J. S. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.1824 · Cited by 376 · see citing works
S-Nitrosylation of mitochondrial caspases
Mannick, J. B., Schonhoff, C. M., Papeta, N., Ghafourifar, P., Szibor, M., Fang, K., & Gaston, B. M. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200104008 · Cited by 363 · see citing works
Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine
Mitchell, D. A., & Marletta, M. A. (2005) · Nature Chemical Biology · doi:10.1038/nchembio720 · Cited by 292 · see citing works
Doulias, P., Greene, J. L., Greco, T. M., Τενοπούλου, Μ., Seeholzer, S. H., Dunbrack, R. L., & Ischiropoulos, H. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008036107 · Cited by 254 · see citing works
Self-citationIzai, K., Uchida, Y., Orii, T., Yamamoto, S., & Hashimoto, T. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48390-1 · Cited by 245 · see citing works
Endogenous S -nitrosothiols protect against myocardial injury
Lima, B., Lam, G. K. W., Xie, L., Diesen, D. L., Villamizar, N. R., Nienaber, J. J., Messina, E., Bowles, D. E., Kontos, C. D., Hare, J. M., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901043106 · Cited by 223 · see citing works
Prime, T. A., Blaikie, F. H., Evans, C., Nadtochiy, S. M., James, A. M., Dahm, C. C., Vitturi, D. A., Patel, R. P., Hiley, C. R., Abakumova, I., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903250106 · Cited by 222 · see citing works
An acyl-coenzyme a dehydrogenase assay utilizing the ferricenium ion
Lehman, T. C., Hale, D. E., Bhala, A., & Thorpe, C. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90080-s · Cited by 214 · see citing works
Polynitrosylated proteins: characterization, bioactivity, and functional consequences.
Simon, D. I., Mullins, M. E., Jia, L., Gaston, B. M., Singel, D. J., & Stamler, J. S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.10.4736 · Cited by 190 · see citing works
Strauss, A. W., Powell, C. K., Hale, D. E., Anderson, M. M., Ahuja, A., Brackett, J. C., & Sims, H. F. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.23.10496 · Cited by 169 · see citing works
Aoyama, T., Souri, M., Ushikubo, S., Kamijo, T., Yamaguchi, S., Kelley, R. I., Rhead, W. J., Uetake, K., Tanaka, K., & Hashimoto, T. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117947 · Cited by 164 · see citing works
Diabetic eNOS knockout mice develop distinct macro- and microvascular complications
Mohan, S., Reddick, R. L., Musi, N., Horn, D. A., Yan, B., Prihoda, T. J., Natarajan, M., & Abboud‐Werner, S. L. (2008) · Laboratory Investigation · doi:10.1038/labinvest.2008.23 · Cited by 127 · see citing works
The Application and Usefulness of the Ratio kcat/KM
Koshland, D. E. (2002) · Bioorganic Chemistry · doi:10.1006/bioo.2002.1246 · Cited by 107 · see citing works
Keene, S. D., Greco, T. M., Parastatidis, I., Lee, S. H., Hughes, E. G., Balice‐Gordon, R. J., Speicher, D. W., & Ischiropoulos, H. (2009) · PROTEOMICS · doi:10.1002/pmic.200800385 · Cited by 73 · see citing works
Self-citationMeasurement of S -Nitrosylation Occupancy in the Myocardium With Cysteine-Reactive Tandem Mass Tags
Kohr, M. J., Aponte, A. M., Sun, J., Guček, M., Steenbergen, C., & Murphy, E. (2012) · Circulation Research · doi:10.1161/circresaha.112.271320 · Cited by 70 · see citing works
Lymphocyte Development Requires S-nitrosoglutathione Reductase
Yang, Z., Wang, Z., Doulias, P., Wei, W., Ischiropoulos, H., Locksley, R. M., & Liu, L. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000080 · Cited by 61 · see citing works
Self-citationImpairment of endothelial nitric oxide synthase causes abnormal fat and glycogen deposition in liver
Schild, L., Dombrowski, F., Lendeckel, U., Schulz, C., Gardemann, A., & Keilhoff, G. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2007.12.007 · Cited by 49 · see citing works
de Oliveira, C. P. M. S., de Lima, V. M. R., Simplicio, F. I., Soriano, F. G., de Mello, E. S., de Souza, H. P., Alves, V. A. F., Laurindo, F. R. M., Carrilho, F. J., & de Oliveira, M. G. (2008) · Journal of the American College of Nutrition · doi:10.1080/07315724.2008.10719703 · Cited by 38 · see citing works
Identification of the Catalytic Base in Long Chain Acyl-CoA Dehydrogenase
Djordjević, S., Yu, D. L., Paschke, R., Frerman, F. E., Strauss, A. W., & Kim, J. J. (1994) · Biochemistry · doi:10.1021/bi00180a021 · Cited by 38 · see citing works
Evaluation of Liver Fatty Acid Oxidation in the Leptin-Deficient Obese Mouse
Brix, A. E., Elgavish, A., Nagy, T. R., Gower, B. A., Rhead, W. J., & Wood, P. A. (2002) · Molecular Genetics and Metabolism · doi:10.1006/mgme.2002.3298 · Cited by 37 · see citing works
Dysregulation of very long chain acyl-CoA dehydrogenase coupled with lipid peroxidation
Kabuyama, Y., Suzuki, T., Nakazawa, N., Yamaki, J., Homma, Y., & Homma, Y. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00231.2009 · Cited by 28 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- [18]Koshland DE The application and usefulness of the ratio k(cat)/K(M). Bioorg. Chem 2002 30 211 213 12406705
Cited by
Sorted by citations
Metabolic reprogramming in macrophages and dendritic cells in innate immunity
Kelly, B., & O'Neill, L. A. (2015) · Cell Research · doi:10.1038/cr.2015.68 · Cited by 1,876 · see citing works
The emerging role of Nrf2 in mitochondrial function
Dinkova-Kostova, A. T., & Abramov, A. Y. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.04.036 · Cited by 983 · see citing works
The Biochemistry and Physiology of Mitochondrial Fatty Acid β-Oxidation and Its Genetic Disorders
Houten, S. M., Violante, S. N., Ventura, F. V., & Wanders, R. J. A. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105045 · Cited by 938 · see citing works
Nitric oxide synthase in innate and adaptive immunity: an update
Bogdan, C. (2015) · Trends in Immunology · doi:10.1016/j.it.2015.01.003 · Cited by 862 · see citing works
Role of liver sinusoidal endothelial cells in non-alcoholic fatty liver disease
Hammoutene, A., & Rautou, P.-E. (2019) · Journal of Hepatology · doi:10.1016/j.jhep.2019.02.012 · Cited by 364 · see citing works
Functions and dysfunctions of nitric oxide in brain
Picón-Pagès, P., Garcia-Buendia, J., & Muñoz, F. J. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.11.007 · Cited by 357 · see citing works
Redox regulation of mitochondrial function with emphasis on cysteine oxidation reactions
Mailloux, R. J., Jin, X., & Willmore, W. G. (2013) · Redox Biology · doi:10.1016/j.redox.2013.12.011 · Cited by 312 · see citing works
Nitric oxide in liver diseases
Iwakiri, Y., & Kim, M. Y. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.05.001 · Cited by 302 · see citing works
An overview of mechanisms of redox signaling
Forman, H. J., Ursini, F., & Maiorino, M. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.01.018 · Cited by 306 · see citing works
Regulation of obesity and insulin resistance by nitric oxide
Sansbury, B. E., & Hill, B. G. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.05.016 · Cited by 274 · see citing works
“in NOS3-KO mice [344].”
Regulation of protein function and signaling by reversible cysteine S-nitrosylation
Gould, N., Doulias, P.-T., Tenopoulou, M., Raju, K., & Ischiropoulos, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.460261 · Cited by 274 · see citing works
Self-citationSite-Specific Nitrosoproteomic Identification of EndogenouslyS-Nitrosylated Proteins in Arabidopsis
Hu, J., Huang, X., Chen, L., Sun, X., Lu, C., Zhang, L., Wang, Y., & Zuo, J. (2015) · PLANT PHYSIOLOGY · doi:10.1104/pp.15.00026 · Cited by 252 · see citing works
Chemical methods for mapping cysteine oxidation
Alcock, L. J., Perkins, M. V., & Chalker, J. M. (2017) · Chemical Society Reviews · doi:10.1039/c7cs00607a · Cited by 249 · see citing works
Nitric Oxide in Macrophage Immunometabolism: Hiding in Plain Sight
Palmieri, E. M., McGinity, C., Wink, D. A., & McVicar, D. W. (2020) · Metabolites · doi:10.3390/metabo10110429 · Cited by 237 · see citing works
“Others have referred to evidence that many metabolic enzymes could be s-nitrosated by NO [143] and assumed that cysteine nitrosation could affect the activity of these enzymes in immune cells as well [144].”
BackgroundSite-specific mapping and quantification of protein S-sulphenylation in cells
Yang, J. H., Gupta, V., Carroll, K. S., & Liebler, D. C. (2014) · Nature Communications · doi:10.1038/ncomms5776 · Cited by 232 · see citing works
Levonen, A., Hill, B. G., Kansanen, E., Zhang, J., & Darley-Usmar, V. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.025 · Cited by 232 · see citing works
Mitochondrial Redox Signaling and Oxidative Stress in Kidney Diseases
Aranda‐Rivera, A. K., Cruz‐Gregorio, A., Aparicio‐Trejo, O. E., & Pedraza‐Chaverrí, J. (2021) · Biomolecules · doi:10.3390/biom11081144 · Cited by 229 · see citing works
iNOS as a metabolic enzyme under stress conditions
Anavi, S., & Tirosh, O. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.10.411 · Cited by 226 · see citing works
Molecular Mechanisms of Nitric Oxide in Cancer Progression, Signal Transduction, and Metabolism
Somasundaram, V., Basudhar, D., Bharadwaj, G., No, J. H., Ridnour, L. A., Cheng, R. Y. S., Fujita, M., Thomas, D. D., Anderson, S. K., McVicar, D. W., et al. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7527 · Cited by 215 · 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
S-Nitrosylation: An Emerging Paradigm of Redox Signaling
Fernando, V., Zheng, X., Walia, Y., Sharma, V., Letson, J., & Furuta, S. (2019) · Antioxidants · doi:10.3390/antiox8090404 · Cited by 211 · see citing works
Metabolic reprogramming by the S-nitroso-CoA reductase system protects against kidney injury
Zhou, H., Zhang, R., Anand, P., Stomberski, C. T., Qian, Z., Hausladen, A., Wang, L., Rhee, E. P., Parikh, S. M., Karumanchi, S. A., et al. (2018) · Nature · doi:10.1038/s41586-018-0749-z · Cited by 211 · see citing works
The Expanding Landscape of the Thiol Redox Proteome
Yang, J. H., Carroll, K. S., & Liebler, D. C. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o115.056051 · Cited by 205 · see citing works
Peroxisomal metabolism and oxidative stress
Nordgren, M., & Fransen, M. (2013) · Biochimie · doi:10.1016/j.biochi.2013.07.026 · Cited by 201 · see citing works
Emerging Regulatory Paradigms in Glutathione Metabolism
Liu, Y., Hyde, A. S., Simpson, M. A., & Barycki, J. J. (2014) · Advances in cancer research · doi:10.1016/b978-0-12-420117-0.00002-5 · Cited by 186 · see citing works
Protein S -Nitrosylation as a Therapeutic Target for Neurodegenerative Diseases
Nakamura, T., & Lipton, S. A. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.10.002 · Cited by 160 · see citing works
Arginine and the metabolic regulation of nitric oxide synthesis in cancer
Keshet, R., & Erez, A. (2018) · Disease Models & Mechanisms · doi:10.1242/dmm.033332 · Cited by 159 · see citing works
Mitochondrial fatty acid synthesis, fatty acids and mitochondrial physiology
Kastaniotis, A. J., Autio, K. J., Kerätär, J. M., Monteuuis, G., Mäkelä, A. M., Nair, R., Pietikäinen, L. P., Shvetsova, A., Chen, Z., & Hiltunen, J. K. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.08.011 · Cited by 158 · see citing works
Post-translational modifications in mitochondria: protein signaling in the powerhouse
Stram, A. R., & Payne, R. M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2280-4 · Cited by 149 · see citing works
Puyaubert, J., Fares, A., Rézé, N., Peltier, J., & Baudouin, E. (2013) · Plant Science · doi:10.1016/j.plantsci.2013.10.014 · Cited by 147 · see citing works
Zhang, H., Gong, W., Wu, S., & Perrett, S. (2022) · Cells · doi:10.3390/cells11050829 · Cited by 139 · see citing works
Nitric Oxide: The Forgotten Child of Tumor Metabolism
Rizi, B. S., Achreja, A., & Nagrath, D. (2017) · Trends in cancer · doi:10.1016/j.trecan.2017.07.005 · Cited by 137 · see citing works
Qu, Z., Meng, F., Bomgarden, R. D., Viner, R., Li, J., Rogers, J. C., Cheng, J. J., Greenlief, C. M., Cui, J., Lubahn, D. B., et al. (2014) · Journal of Proteome Research · doi:10.1021/pr401179v · Cited by 133 · see citing works
Eckert, A., Nisbet, R. M., Grimm, A., & Götz, J. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.08.013 · Cited by 127 · see citing works
Gould, N. S., Evans, P., Martínez-Acedo, P., Marino, S. M., Gladyshev, V. N., Carroll, K. S., & Ischiropoulos, H. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.06.010 · Cited by 128 · see citing works
Self-citationRegulation of brain glutamate metabolism by nitric oxide and S-nitrosylation
Raju, K., Doulias, P., Evans, P., Krizman, E. N., Jackson, J. G., Horyn, O., Daikhin, Y., Nissim, I. B., Yudkoff, M., Nissim, I., et al. (2015) · Science Signaling · doi:10.1126/scisignal.aaa4312 · Cited by 124 · see citing works
Self-citationMailloux, R. J. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101472 · Cited by 115 · see citing works
Biochemistry of proinflammatory macrophage activation
Nonnenmacher, Y., & Hiller, K. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2784-1 · Cited by 110 · see citing works
TET2 Regulates the Neuroinflammatory Response in Microglia
Carrillo-Jimenez, A., Deniz, Ö., Niklison-Chirou, M. V., Ruiz, R., Bezerra-Salomão, K., Stratoulias, V., Amouroux, R., Yip, P. K., Vilalta, A., Cheray, M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.09.013 · Cited by 104 · see citing works
Immunometabolism of Phagocytes During Mycobacterium tuberculosis Infection
Kumar, R., Singh, P., Kolloli, A., Shi, L., Bushkin, Y., Tyagi, S., & Subbian, S. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00105 · Cited by 99 · see citing works
Morris, G., Berk, M., Klein, H. C., Walder, K. R., Gałecki, P., & Maes, M. H. J. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9975-2 · Cited by 99 · see citing works
Wickramasinghe, N. M., Sachs, D. M., Shewale, B., Gonzalez, D. M., Dhanan-Krishnan, P., Torre, D., LaMarca, E. A., Raimo, S., Dariolli, R., Serasinghe, M. N., et al. (2022) · Cell stem cell · doi:10.1016/j.stem.2022.02.011 · Cited by 97 · see citing works
Self-citationSalimian Rizi, B., Caneba, C., Nowicka, A., Nabiyar, A. W., Liu, X., Chen, K., Klopp, A., & Nagrath, D. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-1337 · Cited by 98 · see citing works
Léveillard, T., Philp, N. J., & Sennlaub, F. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030762 · Cited by 100 · see citing works
S -nitrosation of proteins relevant to Alzheimer’s disease during early stages of neurodegeneration
Seneviratne, U. I., Nott, A., Bhat, V. B., Ravindra, K. C., Wishnok, J. S., Tsai, L., & Tannenbaum, S. R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1521318113 · Cited by 97 · see citing works
Jadiya, P., Garbincius, J. F., & Elrod, J. W. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01224-4 · Cited by 94 · see citing works
Identification of S-nitroso-CoA reductases that regulate protein S-nitrosylation
Anand, P., Hausladen, A., Wang, Y., Zhang, G., Stomberski, C. T., Brunengraber, H., Hess, D. T., & Stamler, J. S. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417816112 · Cited by 93 · see citing works
Longen, S., Richter, F. M., Köhler, Y., Wittig, I., Beck, K., & Pfeilschifter, J. M. (2016) · Scientific Reports · doi:10.1038/srep29808 · Cited by 93 · see citing works
Nitric Oxide and Mitochondrial Function in Neurological Diseases
Ghasemi, M., Mayasi, Y. M., Hannoun, A., Eslami, S. M., & Carandang, R. A. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.02.017 · Cited by 93 · see citing works
Noncanonical transnitrosylation network contributes to synapse loss in Alzheimer’s disease
Nakamura, T., Oh, C.-K., Liao, L., Zhang, X., Lopez, K. M., Gibbs, D., Deal, A. K., Scott, H. R., Spencer, B. J., Masliah, E., et al. (2020) · Science · doi:10.1126/science.aaw0843 · Cited by 88 · see citing works
Aravamudan, B., Thompson, M. A., Pabelick, C. M., & Prakash, Y. S. (2013) · Expert Review of Respiratory Medicine · doi:10.1586/17476348.2013.834252 · Cited by 88 · see citing works
Jin, Z., Kho, J., Dawson, B., Jiang, M., Chen, Y., Ali, S., Burrage, L. C., Grover, M., Palmer, D. J., Turner, D. L., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci138935 · Cited by 83 · see citing works
Endothelial dysfunction in neuroprogressive disorders—causes and suggested treatments
Morris, G., Puri, B. K., OLIVE, L. S., Carvalho, A. F., Berk, M., Walder, K. R., Gustad, L. T., & Maes, M. H. J. (2020) · BMC Medicine · doi:10.1186/s12916-020-01749-w · Cited by 83 · see citing works
Signaling by S-nitrosylation in the heart
Murphy, E., Kohr, M., Menazza, S., Nguyen, T., Evangelista, A., Sun, J., & Steenbergen, C. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.01.003 · Cited by 82 · see citing works
Arginine metabolism in myeloid cells in health and disease
Karadima, E., Chavakis, T., & Alexaki, V. I. (2025) · Seminars in Immunopathology · doi:10.1007/s00281-025-01038-9 · Cited by 83 · see citing works
Redox Signaling from and to Peroxisomes: Progress, Challenges, and Prospects
Fransen, M., & Lismont, C. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7515 · Cited by 80 · see citing works
Induction, Propagation, and Activity of Host Nitric Oxide: Lessons from Leishmania Infection
Olekhnovitch, R., & Bousso, P. (2015) · Trends in Parasitology · doi:10.1016/j.pt.2015.08.001 · Cited by 78 · see citing works
Morris, G., Puri, B. K., Walder, K. R., Berk, M., Stubbs, B., Maes, M. H. J., & Carvalho, A. F. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1028-6 · Cited by 78 · see citing works
Qian, Q., Zhang, Z., Orwig, A., Chen, S., Ding, W., Xu, Y., Kunz, R. C., Lind, N. R. L., Stamler, J. S., & Yang, L. (2017) · Diabetes · doi:10.2337/db17-0223 · Cited by 76 · see citing works
Nrf2 as a regulator of energy metabolism and mitochondrial function
Luchkova, A. Y., Mata, A., & Cadenas, S. (2024) · FEBS Letters · doi:10.1002/1873-3468.14993 · Cited by 80 · see citing works
Metabolic reprogramming & inflammation: Fuelling the host response to pathogens
Gleeson, L. E., & Sheedy, F. J. (2016) · Seminars in Immunology · doi:10.1016/j.smim.2016.10.007 · Cited by 74 · see citing works
Havalová, H., Ondrovičová, G., Keresztesová, B., Bauer, J., Pevala, V., Kutějová, E., & Kunová, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158077 · Cited by 74 · see citing works
Nitrosothiol formation and S-nitrosation signaling through nitric oxide synthases
Wynia‐Smith, S. L., & Smith, B. C. (2016) · Nitric Oxide · doi:10.1016/j.niox.2016.10.001 · Cited by 73 · see citing works
Farahani, A., Farahani, A., Kashfi, K., & Ghasemi, A. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107781 · Cited by 76 · see citing works
Margaritelis, N. V., Cobley, J. N., Paschalis, V., Veskoukis, A. S., Theodorou, A. A., Kyparos, A., & Nikolaidis, M. G. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.12.011 · Cited by 71 · see citing works
Nrf2 Activation in Chronic Kidney Disease: Promises and Pitfalls
Aranda‐Rivera, A. K., Cruz‐Gregorio, A., Pedraza‐Chaverrí, J., & Scholze, A. (2022) · Antioxidants · doi:10.3390/antiox11061112 · Cited by 70 · see citing works
Nitric oxide regulation of cellular metabolism: Adaptive tuning of cellular energy
Pappas, G., Wilkinson, M. L., & Gow, A. J. (2022) · Nitric Oxide · doi:10.1016/j.niox.2022.11.006 · Cited by 71 · see citing works
Dysregulated cellular metabolism in atherosclerosis: mediators and therapeutic opportunities
Stroope, C., Nettersheim, F. S., Coon, B. G., Finney, A. C., Schwartz, M. A., Ley, K. F., Rom, O., & Yurdagul, A. (2024) · Nature Metabolism · doi:10.1038/s42255-024-01015-w · Cited by 72 · see citing works
Chemical-proteomic strategies to investigate cysteine posttranslational modifications
Couvertier, S. M., Zhou, Y., & Weerapana, E. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.09.024 · Cited by 68 · see citing works
H2O2 release from the very long chain acyl-CoA dehydrogenase
Kakimoto, P. A., Tamaki, F. K., Cardoso, A. R., Marana, S. R., & Kowaltowski, A. J. (2015) · Redox Biology · doi:10.1016/j.redox.2015.02.003 · Cited by 67 · see citing works
Duan, J., Gaffrey, M. J., & Qian, W. (2017) · Molecular BioSystems · doi:10.1039/c6mb00861e · Cited by 67 · see citing works
Myalgic encephalomyelitis or chronic fatigue syndrome: how could the illness develop?
Morris, G., Maes, M. H. J., Berk, M., & Puri, B. K. (2019) · Metabolic Brain Disease · doi:10.1007/s11011-019-0388-6 · Cited by 66 · see citing works
The Relationship between Metabolism and the Autophagy Machinery during the Innate Immune Response
Martinez, J., Verbist, K., Wang, R., & Green, D. R. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.05.012 · Cited by 67 · see citing works
Lu, C., Kavalier, A. R., Lukyanov, E., & Gross, S. S. (2013) · Methods · doi:10.1016/j.ymeth.2013.05.020 · Cited by 67 · see citing works
Nakamura, T., & Lipton, S. A. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7916 · Cited by 65 · see citing works
Tonazzi, A., Giangregorio, N., Console, L., Palmieri, F., & Indiveri, C. (2021) · Biomolecules · doi:10.3390/biom11040521 · Cited by 64 · see citing works
Mitochondrial proteome research: the road ahead
Baker, Z. N., Forny, P., & Pagliarini, D. (2023) · Nature reviews. Molecular cell biology · doi:10.1038/s41580-023-00650-7 · Cited by 50 · see citing works
Mass spectrometry in studies of protein thiol chemistry and signaling: Opportunities and caveats
Devarie‐Baez, N. O., Reisz, J. A., & Furdui, C. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.09.016 · Cited by 64 · see citing works
Escudero, S., Zaganjor, E., Lee, S., Mill, C. P., Morgan, A. M., Crawford, E. B., Chen, J., Wales, T. E., Mourtada, R., Luccarelli, J., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.02.005 · Cited by 64 · see citing works
Lu, D., Yang, Z., Xia, Q., Gao, S., Sun, S., Luo, X., Li, Z., Zhang, X., & Li, X. (2020) · Cell Biology International · doi:10.1002/cbin.11443 · Cited by 64 · see citing works
Endothelial nitric oxide synthase-derived nitric oxide in the regulation of metabolism
Τενοπούλου, Μ., & Doulias, P. (2020) · F1000Research · doi:10.12688/f1000research.19998.1 · Cited by 63 · see citing works
Self-citationThe role of S-nitrosylation of PFKM in regulation of glycolysis in ovarian cancer cells
Gao, W., Huang, M., Chen, X., Chen, J., Zou, Z., Li, L., Ji, K., Nie, Z., Yang, B., Wei, Z., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03681-0 · Cited by 62 · see citing works
Figueiredo-Freitas, C., Dulce, R. A., Foster, M. W., Liang, J., Yamashita, A., Lima‐Rosa, F. L., Thompson, J. W., Moseley, M. A., Hare, J. M., Nogueira, L., et al. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6275 · Cited by 63 · see citing works
Nitric oxide and tumor metabolic reprogramming
Lopez-Sanchez, L. M., Aranda, E., & Rodríguez‐Ariza, A. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.113769 · Cited by 61 · see citing works
‘SNO’-Storms Compromise Protein Activity and Mitochondrial Metabolism in Neurodegenerative Disorders
Nakamura, T., & Lipton, S. A. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.10.004 · Cited by 60 · see citing works
Protein Microarray Characterization of the S-Nitrosoproteome
Lee, Y.-I., Giovinazzo, D., Kang, H. C., Lee, Y., Jeong, J. S., Doulias, P., Xie, Z., Hu, J., Ghasemi, M., Ischiropoulos, H., et al. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.032235 · Cited by 59 · see citing works
Self-citationDifferential alkylation-based redox proteomics – Lessons learnt
Wojdyła, K., & Rogowska-Wrzesińska, A. (2015) · Redox Biology · doi:10.1016/j.redox.2015.08.005 · Cited by 59 · see citing works
Ptc7p Dephosphorylates Select Mitochondrial Proteins to Enhance Metabolic Function
Guo, X. Q., Niemi, N. M., Hutchins, P. D., Condon, S. G. F., Jochem, A., Ulbrich, A., Higbee, A. J., Russell, J. D., Senes, A., Coon, J. J., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2016.12.049 · Cited by 59 · see citing works
Similarities in the Metabolic Reprogramming of Immune System and Endothelium
Tang, C.-Y., & Mauro, C. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00837 · Cited by 60 · see citing works
Rhee, S. G., & Kil, I. S. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.011 · Cited by 57 · see citing works
Mitochondria in metabolic disease: Getting clues from proteomic studies
Peinado, J. R., Díaz‐Ruiz, A., Frühbeck, G., & Malagón, M. M. (2013) · PROTEOMICS · doi:10.1002/pmic.201300376 · Cited by 57 · see citing works
Phenolics and anthocyanins in berries of European cranberry and their antimicrobial activity
Česonienė, L., Jasutienė, I., & Šarkinas, A. (2024) · PubMed · doi:10.5281/zenodo.11174808 · Cited by 56 · see citing works
Kramer, P. A., Duan, J., Qian, W.-J., & Marcinek, D. J. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00347 · Cited by 54 · see citing works
Richardson, R. B., & Mailloux, R. J. (2023) · Antioxidants · doi:10.3390/antiox12030674 · Cited by 55 · see citing works
Certo, M., Elkafrawy, H., Pucino, V., Cucchi, D., Cheung, K. C.-P., & Mauro, C. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15002 · Cited by 52 · see citing works
The Physiological and Pathological Role of Acyl-CoA Oxidation
Szrok-Jurga, S., Czumaj, A., Turyn, J., Hebanowska, A., Świerczyński, J., Śledziński, T., & Stelmańska, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914857 · Cited by 52 · see citing works
Harnessing Redox Cross-Reactivity To Profile Distinct Cysteine Modifications
Majmudar, J. D., Konopko, A. M., Labby, K. J., Tom, C. T. M. B., Crellin, J. E., Prakash, A., & Martin, B. R. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.5b06806 · Cited by 51 · see citing works
Heterogeneity of glycolysis in cancers and therapeutic opportunities
Warmoes, M. O., & Locasale, J. W. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.07.019 · Cited by 50 · see citing works
Diers, A. R., Keszler, Á., & Hogg, N. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.07.026 · Cited by 50 · see citing works
Evaluation of the Molecular Mechanisms of Sepsis Using Proteomics
He, M., Chen, S., & Ding, R. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.733537 · Cited by 49 · see citing works
- Authors
- Doulias, P.-T., Tenopoulou, M., Greene, J. L., Raju, K., & Ischiropoulos, H.
- Affiliations
- Children's Hospital of Philadelphia (US)
- Children’s Hospital of Philadelphia Research Institute and Departments of Pediatrics and Pharmacology, Raymond and Ruth Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104, USA.
- Corresponding author
- Raju, Karthik
- Ischiropoulos, Harry
- Venue
- Science Signaling
- Published
- 2013-01
- Volume
- 6
- Issue
- 256
- Pages
- rs1-rs1
- ISSN
- 1937-9145 (ISSN-L)
- 1945-0877
- PMC
- PMC4010156
- OpenAlex
- W2160610690
- Cited by
- 250
- References
- 35
- Citations by year
- 2026: 6 · 2025: 18 · 2024: 17 · 2023: 16 · 2022: 15 · 2021: 21 · 2020: 23 · 2019: 16 · 2018: 17 · 2017: 16 · 2016: 20 · 2015: 24 · 2014: 20 · 2013: 20
- FWCI
- 12.55
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science Signaling (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (AG 13966, R01AG013966, T32AG000255)
- National Heart, Lung, and Blood Institute (R01HL054926, HL054926)
- National Institute of Environmental Health Sciences (ES013508, P30ES013508)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- nitric oxide, S-nitrosylation, S-nitrosocysteine, post-translational modification, mitochondrial fatty acid metabolism, fatty acid beta-oxidation, VLCAD, endothelial nitric oxide synthase, mitochondrial bioenergetics, glycolysis, gluconeogenesis, TCA cycle, oxidative phosphorylation
- MeSH terms
- Analysis of Variance, Animals, Cysteine, Energy Metabolism, Fatty Acids, Liver, Mitochondria, Nitric Oxide, Oxidation-Reduction, Protein Processing, Post-Translational, Mass Spectrometry, Signal Transduction, Mutagenesis, Site-Directed, DNA Primers, S-Nitrosothiols, Proteomics, Acyl-CoA Dehydrogenase, Long-Chain, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review