Cell signaling mediated by nitrated cyclic guanine nucleotide
Abstract
We recently clarified the physiological formation of 8-nitroguanosine 3',5'-cyclic monophosphate (8-nitro-cGMP) and its critical roles in nitric oxide (NO) signal transductions. This discovery of 8-nitro-cGMP is the first demonstration of a nitrated cyclic nucleotide functioning as a new second messenger in mammals since the identification of cGMP more than 40 years ago. By means of chemical analyses, e.g., liquid chromatography-tandem mass spectrometry, we unequivocally identified 8-nitro-cGMP formation, which depended on NO production, in several types of cultured cells, including macrophages and glial cells. Most important, we previously showed that 8-nitro-cGMP as an electrophile reacted with particular sulfhydryls of proteins to generate a unique post-translational modification that we called protein S-guanylation. In fact, certain specific intracellular proteins, such as the redox-sensor protein Keap1, readily underwent S-guanylation induced by 8-nitro-cGMP. 8-Nitro-cGMP activated the Nrf2 signaling pathway by triggering dissociation of Keap1, via S-guanylation of its highly nucleophilic cysteine sulfhydryls. We also determined that S-guanylation of Keap1 was involved in cytoprotective actions of NO and 8-nitro-cGMP by inducing oxidative stress response genes such as heme oxygenase-1. Such unique chemical properties of 8-nitro-cGMP shed light on new areas of NO and cGMP signal transduction. Protein S-guanylation induced by 8-nitro-cGMP may thus have important implications in NO-related physiology and pathology, pharmaceutical chemistry, and development of therapeutics for many diseases.
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?
Nitration of both fatty acids and guanine nucleotides has been shown to elicit responses that are protective against inflammatory tissue injury.
“nitration of both fatty acids and guanine nucleotides has been shown to elicit responses that are protective against inflammatory tissue injury[115, 116].”
From Current perspectives and challenges in understanding the role of nitrite as an integral player in nitric oxide biology and therapy (2011) · cites this paper as [115]
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
Beckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., & Freeman, B. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1620 · Cited by 7,029 · see citing works
Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach?
Trachootham, D., Alexandre, J., & Huang, P. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2803 · Cited by 5,452 · see citing works
Localization of nitric oxide synthase indicating a neural role for nitric oxide
Bredt, D. S., Hwang, P. M., & Snyder, S. H. (1990) · Nature · doi:10.1038/347768a0 · Cited by 2,981 · see citing works
Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., & Talalay, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172398899 · Cited by 1,947 · see citing works
Nrf2–Keap1 defines a physiologically important stress response mechanism
Motohashi, H., & Yamamoto, M. (2004) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2004.09.003 · Cited by 1,725 · see citing works
Biochemistry of oxidative stress
Halliwell, B. B. (2007) · Biochemical Society Transactions · doi:10.1042/bst0351147 · Cited by 1,546 · see citing works
Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
Eiserich, J. P., Hristova, M., Cross, C. E., Jones, A. D., Freeman, B. A., Halliwell, B., & van der Vliet, A. (1998) · Nature · doi:10.1038/34923 · Cited by 1,496 · see citing works
Nitric oxide, oxidants, and protein tyrosine nitration
Radí, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307446101 · Cited by 1,456 · 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
Superoxide Anion Radical (O·̄2), Superoxide Dismutases, and Related Matters
Fridovich, I. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18515 · Cited by 1,337 · see citing works
Kobayashi, A., Kang, M.-I., Watai, Y., Tong, K. I., Shibata, T., Uchida, K., & Yamamoto, M. P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.221-229.2006 · Cited by 933 · see citing works
Itoh, K., Tong, K. I., & Yamamoto, M. P. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.02.075 · Cited by 866 · see citing works
Cyclic guanosine monophosphate as a mediator of vasodilation.
Murad, F. (1986) · Journal of Clinical Investigation · doi:10.1172/jci112536 · Cited by 799 · see citing works
Tong, K. I., Katoh, Y., Kusunoki, H., Itoh, K., Tanaka, T., & Yamamoto, M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.8.2887-2900.2006 · Cited by 759 · see citing works
Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer
Padmanabhan, B., Tong, K. I., Ohta, T., Nakamura, Y., Scharlock, M., Ohtsuji, M., Kang, M.-I., Kobayashi, A., Yokoyama, S., & Yamamoto, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.013 · Cited by 735 · see citing works
Kobayashi, M., Li, L., Iwamoto, N., Nakajima‐Takagi, Y., Kaneko, H., Nakayama, Y., Eguchi, M., Wada, Y., Kumagai, Y., & Yamamoto, M. P. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01080-08 · Cited by 641 · see citing works
Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling
Lo, S., Li, X., Henzl, M. T., Beamer, L. J., & Hannink, M. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601243 · Cited by 604 · see citing works
Estévez, A. G., Crow, J. P., Sampson, J. B., Reiter, C., Zhuang, Y., Richardson, G. J., Tarpey, M. M., Barbeito, L., & Beckman, J. S. (1999) · Science · doi:10.1126/science.286.5449.2498 · Cited by 596 · see citing works
Levonen, A., Landar, A. L., Ramachandran, A., CEASER, E. K., Dickinson, D. A., Zanoni, G., Morrow, J. D., & Darley-Usmar, V. M. (2004) · Biochemical Journal · doi:10.1042/bj20031049 · Cited by 559 · see citing works
Physiological Significance of Reactive Cysteine Residues of Keap1 in Determining Nrf2 Activity
Yamamoto, T., Suzuki, T., Kobayashi, A., Wakabayashi, J., Maher, J. M., Motohashi, H., & Yamamoto, M. P. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01704-07 · Cited by 515 · see citing works
<i>S</i> -Nitrosylation in Cardiovascular Signaling
Lima, B., Forrester, M. T., Hess, D. T., & Stamler, J. S. (2010) · Circulation Research · doi:10.1161/circresaha.109.207381 · Cited by 490 · see citing works
Tong, K. I., Padmanabhan, B., Kobayashi, A., Shang, C., Hirotsu, Y., Yokoyama, S., & Yamamoto, M. P. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00753-07 · Cited by 447 · see citing works
The Role of Keap1 in Cellular Protective Responses
Dinkova‐Kostova, A. T., Holtzclaw, W. D., & Kensler, T. W. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050217c · Cited by 378 · see citing works
How Many Transcription Factors Does It Take to Turn On the Heme Oxygenase-1 Gene?
Alam, J., & Cook, J. L. (2006) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2006-0340tr · Cited by 378 · see citing works
NO-dependent protein nitration: a cell signaling event or an oxidative inflammatory response?
Schopfer, F. J. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.10.006 · Cited by 369 · see citing works
Protein S-guanylation by the biological signal 8-nitroguanosine 3′,5′-cyclic monophosphate
Sawa, T., Zaki, M. H., Okamoto, T., Akuta, T., Tokutomi, Y., Kim‐Mitsuyama, S., Ihara, H., Kobayashi, A., Yamamoto, M. P., Fujii, S., et al. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.33 · Cited by 273 · 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
Ogura, T., Tong, K. I., Mio, K., Maruyama, Y., Kurokawa, H., Sato, C., & Yamamoto, M. P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914036107 · Cited by 232 · see citing works
Nitro-fatty Acid Reaction with Glutathione and Cysteine
Baker, L. M. S., Baker, P. R. S., Golin-Bisello, F., Schopfer, F. J., Fink, M., Woodcock, S. R., Branchaud, B. P., Radi, R., & Freeman, B. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704085200 · Cited by 200 · see citing works
Transduction of Redox Signaling by Electrophile-Protein Reactions
Rudolph, T. K., & Freeman, B. Α. (2009) · Science Signaling · doi:10.1126/scisignal.290re7 · Cited by 200 · see citing works
Doi, K., Akaike, T., Fujii, S., Tanaka, S., Ikebe, N., Beppu, T., Shibahara, S., Ogawa, M., & Maeda, H. (1999) · British Journal of Cancer · doi:10.1038/sj.bjc.6690624 · Cited by 182 · see citing works
8-Nitroguanosine formation in viral pneumonia and its implication for pathogenesis
Akaike, T., Okamoto, S., Sawa, T., Yoshitake, J., Tamura, F., Ichimori, K., Miyazaki, K., Sasamoto, K., & Maeda, H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0235623100 · Cited by 170 · see citing works
Antiapoptotic effect of haem oxygenase-1 induced by nitric oxide in experimental solid tumour
Tanaka, S., Akaike, T., Fang, J. Q., Beppu, T., Ogawa, M., Tamura, F., Miyamoto, Y., & Maeda, H. (2003) · British Journal of Cancer · doi:10.1038/sj.bjc.6600830 · Cited by 166 · see citing works
Role of nitrosative stress in the pathogenesis of diabetic vascular dysfunction
Szabo, C. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2008.00086.x · Cited by 165 · see citing works
Fujii, S., Sawa, T., Ihara, H., Tong, K. I., Ida, T., Okamoto, T., Ahmed, K. A., Ishima, Y., Motohashi, H., Yamamoto, M. P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145441 · Cited by 151 · see citing works
Covalent adduction of nucleophilic amino acids by 4-hydroxynonenal and 4-oxononenal
Doorn, J. A., & Petersen, D. R. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00178-3 · Cited by 147 · see citing works
Ohshima, H., Sawa, T., & Akaike, T. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1033 · Cited by 138 · see citing works
Oxidants, nitrosants, and the lung
van der Vliet, A., & Cross, C. E. (2000) · The American Journal of Medicine · doi:10.1016/s0002-9343(00)00479-4 · Cited by 120 · see citing works
Oh, J. Y., Giles, N. M., Landar, A. L., & Darley-Usmar, V. M. (2008) · Biochemical Journal · doi:10.1042/bj20071189 · Cited by 106 · see citing works
Prospective Type 1 and Type 2 Disulfides of Keap1 Protein
Holland, R., Hawkins, A., Eggler, A. L., Mesecar, A. D., Fabris, D., & Fishbein, J. C. (2008) · Chemical Research in Toxicology · doi:10.1021/tx800226m · Cited by 95 · see citing works
Keap1 modification and nuclear accumulation in response to S-nitrosocysteine
Buckley, B. J., Li, S., & Whorton, A. R. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.10.055 · Cited by 61 · see citing works
Nitric Oxide as an Endogenous Mutagen for Sendai Virus without Antiviral Activity
Yoshitake, J., Akaike, T., Akuta, T., Tamura, F., Ogura, T., Esumi, H., & Maeda, H. (2004) · Journal of Virology · doi:10.1128/jvi.78.16.8709-8719.2004 · Cited by 61 · see citing works
Zaki, M. H., Fujii, S., Okamoto, T., Islam, S., Khan, S., Ahmed, K. A., Sawa, T., & Akaike, T. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803363 · Cited by 55 · see citing works
Superoxide generation mediated by 8-nitroguanosine, a highly redox-active nucleic acid derivative
Sawa, T., Akaike, T., Ichimori, K., Akuta, T., Kaneko, K., Nakayama, H., Stuehr, D. J., & Maeda, H. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.10.003 · Cited by 55 · see citing works
Sawa, T., Tatemichi, M., Akaike, T., Barbin, A., & Ohshima, H. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.09.035 · Cited by 50 · see citing works
Guanine Nitration in Idiopathic Pulmonary Fibrosis and Its Implication for Carcinogenesis
Terasaki, Y., Akuta, T., Terasaki, M., Sawa, T., Mori, T., Okamoto, T., Ozaki, M., Takeya, M., & Akaike, T. (2006) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200510-1580oc · Cited by 47 · see citing works
Sawa, T., Arimoto, H., & Akaike, T. (2010) · Bioconjugate Chemistry · doi:10.1021/bc900396u · Cited by 41 · see citing works
8-Nitroguanosines as chemical probes of the protein S-guanylation
Saito, Y., Taguchi, H., Fujii, S., Sawa, T., Kida, E., Kabuto, C., Akaike, T., & Arimoto, H. (2008) · Chemical Communications · doi:10.1039/b810771h · Cited by 26 · see citing works
A New Paradigm for Antimicrobial Host Defense Mediated by a Nitrated Cyclic Nucleotide
Okamoto, T., Khan, S., Oyama, K., Fujii, S., Sawa, T., & Akaike, T. (2009) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.sr09-70 · Cited by 15 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Maia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401 · see citing works
Nitric oxide signaling: Classical, less classical, and nonclassical mechanisms
Martı́nez-Ruiz, A., Cadenas, S., & Lamas, S. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.010 · Cited by 336 · see citing works
The Chemical Biology of Naphthoquinones and Its Environmental Implications
Kumagai, Y., Shinkai, Y., Miura, T., & Cho, A. K. (2012) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134517 · Cited by 332 · see citing works
Hydrogen sulfide anion regulates redox signaling via electrophile sulfhydration
Nishida, M., Sawa, T., Kitajima, N., Ono, K., Inoue, H., Ihara, H., Motohashi, H., Yamamoto, M. P., Suematsu, M., Kurose, H., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1018 · Cited by 294 · see citing works
Turpaev, K. T. (2013) · Biochemistry (Moscow) · doi:10.1134/s0006297913020016 · Cited by 135 · see citing works
Kolbert, Z., Feigl, G., Bordé, Á., Molnár, Á., & Erdei, L. (2017) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2017.01.028 · Cited by 120 · see citing works
Protein S‐sulfhydration by hydrogen sulfide in cardiovascular system
Meng, G., Zhao, S., Xie, L., Han, Y., & Ji, Y. H. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13825 · Cited by 112 · see citing works
Redox Signaling Regulated by Cysteine Persulfide and Protein Polysulfidation
Kasamatsu, S., Nishimura, A., Morita, M., Matsunaga, T., Hamid, H. A., & Akaike, T. (2016) · Molecules · doi:10.3390/molecules21121721 · Cited by 108 · see citing works
Ferulic acid ethyl ester as a potential therapy in neurodegenerative disorders
Rukhsana Sultana, A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.015 · Cited by 94 · see citing works
Ahmed, K. A., Sawa, T., Ihara, H., Kasamatsu, S., Yoshitake, J., Rahaman, M. M., Okamoto, T., Fujii, S., & Akaike, T. (2011) · Biochemical Journal · doi:10.1042/bj20111130 · Cited by 65 · see citing works
Vitturi, D. A., & Patel, R. P. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.05.037 · Cited by 59 · see citing works
Formation, signaling functions, and metabolisms of nitrated cyclic nucleotide
Sawa, T., Ihara, H., Ida, T., Fujii, S., Nishida, M., & Akaike, T. (2013) · Nitric Oxide · doi:10.1016/j.niox.2013.04.004 · Cited by 58 · see citing works
Akhtar, M. W., Sunico, C. R., Nakamura, T., & Lipton, S. A. (2012) · International Journal of Cell Biology · doi:10.1155/2012/463756 · Cited by 52 · see citing works
Cole, C., Thomas, S. M., Filak, H. C., Henson, P. M., & Lenz, L. L. (2012) · Immunity · doi:10.1016/j.immuni.2012.03.011 · Cited by 45 · see citing works
Unoki, T., Akiyama, M., & Kumagai, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020545 · Cited by 43 · see citing works
Regulation of redox signalling by an electrophilic cyclic nucleotide
Akaike, T., Nishida, M., & Fujii, S. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs145 · Cited by 34 · see citing works
Sawa, T., Ono, K., Tsutsuki, H., Zhang, T., Ida, T., Nishida, M., & Akaike, T. (2018) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2018.01.002 · Cited by 33 · see citing works
Antioxidative and anti-inflammatory actions of reactive cysteine persulfides
Zhang, T., Tsutsuki, H., Ono, K., Akaike, T., & Sawa, T. (2020) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.20-13 · Cited by 33 · see citing works
S -Guanylation Proteomics for Redox-Based Mitochondrial Signaling
Rahaman, M. M., Sawa, T., Ahmed, K. A., Khan, S., Inoue, H., Irie, A., Fujii, S., & Akaike, T. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4606 · Cited by 29 · see citing works
Akashi, S., Ahmed, K. A., Sawa, T., Ono, K., Tsutsuki, H., Burgoyne, J. R., Ida, T., Horio, E., Prysyazhna, O. D., Oike, Y., et al. (2016) · Biochemistry · doi:10.1021/acs.biochem.5b00774 · Cited by 27 · see citing works
Cabrera, M., Mastandrea, I., Otero, G., Cerecetto, H., & González, M. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.02.041 · Cited by 24 · see citing works
Fujii, S., & Akaike, T. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5067 · Cited by 21 · see citing works
Rychter, M., Gaucher, C., Boudier, A., Leroy, P., & Lulek, J. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.07.003 · Cited by 21 · see citing works
Ihara, H., Kitamura, A., Kasamatsu, S., Ida, T., Kakihana, Y., Tsutsuki, H., Sawa, T., Watanabe, Y., & Akaike, T. (2017) · Biochemical Journal · doi:10.1042/bcj20160999 · Cited by 21 · see citing works
Salmi, M. L., Clark, G., & Roux, S. J. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00427 · Cited by 19 · see citing works
Moustafa, A., & Habara, Y. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5108 · Cited by 19 · see citing works
Tazawa, H., Kawaguchi, T., Kobayashi, T., Kuramitsu, Y., Wada, S., Satomi, Y., Nishino, H., Kobayashi, M., Kanda, Y., Osaki, M., et al. (2013) · Experimental Cell Research · doi:10.1016/j.yexcr.2013.08.006 · Cited by 18 · see citing works
Zhu, J. K., Song, S., Sun, Z., Lian, L., Shi, L., Ren, A., & Zhao, M. (2021) · Environmental Microbiology · doi:10.1111/1462-2920.15400 · Cited by 17 · see citing works
Role of NO-dependent Posttranslational Modifications in Switching Metabolic Pathways
Romero‐Puertas, M. C., & Sandalio, L. M. (2016) · Advances in botanical research · doi:10.1016/bs.abr.2015.10.005 · Cited by 15 · see citing works
Regulation of redox signaling by reactive sulfur species
Kasamatsu, S., & Ihara, H. (2021) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.20-124 · Cited by 12 · see citing works
Persulfide-Dependent Regulation of Electrophilic Redox Signaling in Neural Cells
Kasamatsu, S. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8130 · Cited by 10 · see citing works
Endo, S., Nishiyama, A., Suyama, M., Takemura, M., Soda, M., Chen, H., Tajima, K., El-Kabbani, O. A. L., Bunai, Y., Hara, A., et al. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.09.023 · Cited by 10 · see citing works
Shang, G., Akaike, T., Jiang, T., Chen, Q., Nong, Z., & Li, H. (2012) · Free Radical Research · doi:10.3109/10715762.2012.701292 · Cited by 10 · see citing works
Combating Oxidative/Nitrosative Stress with Electrophilic Counterattack Strategies
Satoh, T., Akhtar, M. W., & Lipton, S. A. (2013) · Springer eBooks · doi:10.1007/978-94-007-5787-5_10 · Cited by 8 · see citing works
Cabrera, M., de Ovalle, S., Bollati‐Fogolín, M., Nascimento, F., Corbelini, P. F., Janarelli, F., Kawano, D. F., Eifler-Lima, V. L., González, M., & Cerecetto, H. (2015) · Future Science OA · doi:10.4155/fso.15.18 · Cited by 7 · see citing works
Peroxynitrite‐Promoted Persulfide Prodrugs with Protective Potential against Paracetamol Poisoning
Xu, Y., Xu, B., Wang, J., Jin, H., Xu, S., Wang, G., & Zhen, L. (2022) · Chemistry - A European Journal · doi:10.1002/chem.202200540 · Cited by 6 · see citing works
Strategies of Pathogens to Escape from NO-Based Host Defense
Simone, G. D., di Masi, A., & Ascenzi, P. (2022) · Antioxidants · doi:10.3390/antiox11112176 · Cited by 6 · see citing works
Frontiers in nitric oxide and redox signaling
Akaike, T., van der Vliet, A., & Eaton, P. (2011) · Nitric Oxide · doi:10.1016/j.niox.2011.05.002 · Cited by 6 · see citing works
Mohammed, C. M., & Al-Habib, O. A. M. (2025) · Tissue and Cell · doi:10.1016/j.tice.2025.102761 · Cited by 5 · see citing works
Tlenek azotu i tlenek węgla - dwa ważne gazotransmitery.
Tadeusiewicz, J., & Olas, B. (2014) · Cited by 4 · see citing works
Redox Signaling and Reactive Sulfur Species to Regulate Electrophilic Stress
Kanda, H., & Kumagai, Y. (2020) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.20-00096 · Cited by 3 · see citing works
S-guanylation proteomics for redox-based mitochondrial signaling
Sawa, T., Rahaman, M. M., Ahmed, K. A., Irie, A., Fujii, S., & Akaike, T. (2012) · Nitric Oxide · doi:10.1016/j.niox.2012.04.041 · Cited by 1 · see citing works
Regulation of Redox Signaling by a Nitrated Nucleotide and Reactive Cysteine Persulfides
Sawa, T., Kumagai, Y., & Akaike, T. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804273-1.00017-x · Cited by 1 · see citing works
Antioxidant Adaptive Response of Malignant Glioma Related to Resistance to Antitumor Treatment
Sawa, T., & Akaike, T. (2012) · InTech eBooks · doi:10.5772/23429
Nishida, M., Toyama, T., Kumagai, Y., & Numaga‐Tomita, T. (2014) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.14-00209-1
Reactive sulfur species-modified protein thiols: new methods for polysulfurated protein analysis
Kasamatsu, S., Fujii, S., & Akaike, T. (2016) · Folia Pharmacologica Japonica · doi:10.1254/fpj.147.299
Overview of Gas-sensing Systems
Aono, S. (2017) · Royal Society of Chemistry eBooks · doi:10.1039/9781788012836-00001
Nitric oxide alters hyaluronan deposition by airway smooth muscle cells
Majors, A. K., Chakravarti, R., Ruple, L. M., Leahy, R., Stuehr, D. J., Lauer, M. E., ERZURUM, S. C., Janocha, A. J., & Aronica, M. A. (2018) · PLoS ONE · doi:10.1371/journal.pone.0200074
- Authors
- Akaike, T., Fujii, S., Sawa, T., & Ihara, H.
- Affiliations
- Kumamoto University (JP)
- Osaka Prefecture University (JP)
- Corresponding author
- Akaike, Takaaki
- Venue
- Nitric Oxide
- Publisher
- Elsevier BV
- Published
- 2010-11
- Volume
- 23
- Issue
- 3
- Pages
- 166-174
- ISSN
- 1089-8603 (ISSN-L)
- OpenAlex
- W1984465237
- Cited by
- 49
- References
- 49
- Citations by year
- 2025: 1 · 2022: 2 · 2021: 2 · 2020: 4 · 2018: 2 · 2017: 5 · 2016: 6 · 2015: 1 · 2014: 4 · 2013: 6 · 2012: 9
- FWCI
- 0.71
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nitric Oxide (publishedVersion)
- PubMed (publishedVersion)
- Kumamoto University Repository (Kumamoto University) (submittedVersion)
- Kumamoto University Repository System (submittedVersion)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- Ministry of Health, Labour and Welfare
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Phosphodiesterase function and regulation
- Keywords
- 8-nitro-cGMP, nitric oxide signaling, cGMP signaling, second messengers, Keap1, Nrf2 signaling, sulfhydryl modification, oxidative stress response, heme oxygenase-1, macrophages, glial cells, redox signaling
- MeSH terms
- Cyclic GMP, Humans, Nitric Oxide, Signal Transduction
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