The DOI matches its Crossref record; 159 of the 166 references it cites were found in a registry or an index.
The chemical biology of nitric oxide: Implications in cellular signaling
Open accessAbstract
Nitric oxide (NO) has earned the reputation of being a signaling mediator with many diverse and often opposing biological activities. The diversity in response to this simple diatomic molecule comes from the enormous variety of chemical reactions and biological properties associated with it. In the past few years, the importance of steady-state NO concentrations has emerged as a key determinant of its biological function. Precise cellular responses are differentially regulated by specific NO concentration. We propose five basic distinct concentration levels of NO activity: cGMP-mediated processes ([NO]<1-30 nM), Akt phosphorylation ([NO] = 30-100 nM), stabilization of HIF-1alpha ([NO] = 100-300 nM), phosphorylation of p53 ([NO]>400 nM), and nitrosative stress (1 microM). In general, lower NO concentrations promote cell survival and proliferation, whereas higher levels favor cell cycle arrest, apoptosis, and senescence. Free radical interactions will also influence NO signaling. One of the consequences of reactive oxygen species generation is to reduce NO concentrations. This antagonizes the signaling of nitric oxide and in some cases results in converting a cell-cycle arrest profile to a cell survival profile. The resulting reactive nitrogen species that are generated from these reactions can also have biological effects and increase oxidative and nitrosative stress responses. A number of factors determine the formation of NO and its concentration, such as diffusion, consumption, and substrate availability, which are referred to as kinetic determinants for molecular target interactions. These are the chemical and biochemical parameters that shape cellular responses to NO. Herein we discuss signal transduction and the chemical biology of NO in terms of the direct and indirect reactions.
Overview
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
Verification
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?
In the citing paper
“It is worth indicating that despite being long considered toxic species, most of these molecules have been shown to exert important signaling functions”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [937]
In the citing paper
“However, redox active molecules also serve as signaling agents for control of a variety of physiological functions as well as coordination of inflammatory and tissue restoration mechanisms [2].”
From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [2]
In the citing paper
“However, in cytokine stimulated breast cancer cells, downstream NO-mediated signaling pathways correlated with an ~300 nM NO flux, in comparison to ~1-10 μM in activated murine macrophages [2].”
From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [2]
In the citing paper
“These include NO autoxidation, protonation of nitrite, reaction of NO with O2− and metal mediated processes (Figure 3), all of which play critical roles in different compartments in cells and tissue [2].”
From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [2]
In the citing paper
“S-Nitrosothiols can participate in a variety of reactions, both enzymatic and non-enzymatic [2].”
From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [2]
In the citing paper
“The KNO for nonheme iron systems is typically lower (~106) suggesting that a higher NO flux, in the 300 nM range, is required to significantly bind NO [2].”
From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [2]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178
Nitric oxide: physiology, pathophysiology, and pharmacology.
Moncada, S., Palmer, R. M., & Higgs, E. A. (1991) · Pharmacological Reviews · doi:10.1016/s0031-6997(25)06663-3 · Cited by 15,525
Coussens, L. M., & Werb, Z. (2002) · Nature · doi:10.1038/nature01322 · Cited by 15,111
How Matrix Metalloproteinases Regulate Cell Behavior
Sternlicht, M. D., & Werb, Z. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.463 · Cited by 3,959
Free radicals in biology and medicine
Halliwell, B. B., & Gutteridge, J. M. C. (1985) · Journal of Free Radicals in Biology & Medicine · doi:10.1016/0748-5514(85)90140-0 · Cited by 2,938
Nitric oxide synthases in mammals
Knowles, R. G., & Moncada, S. (1994) · Biochemical Journal · doi:10.1042/bj2980249 · Cited by 2,752
Regulation of endothelium-derived nitric oxide production by the protein kinase Akt
Fulton, D. J., Gratton, J., McCabe, T. J. D., Fontana, J. T., Fujio, Y., Walsh, K. X., Franke, T. F., Papapetropoulos, A., & Sessa, W. C. (1999) · Nature · doi:10.1038/21218 · Cited by 2,616
Peroxynitrite oxidation of sulfhydryls.
Radí, R., Beckman, J. S., Bush, K., & Freeman, B. Α. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64313-7 · Cited by 2,492
Endothelium‐derived relaxing and contracting factors
Furchgott, R. F., & Vanhoutte, P. M. (1989) · The FASEB Journal · doi:10.1096/fasebj.3.9.2545495 · Cited by 2,007
Stuehr, D. J., & Nathan, C. F. (1989) · The Journal of Experimental Medicine · doi:10.1084/jem.169.5.1543 · Cited by 1,744
Research works printed but not linked: 2
- Wink, 1998, Chemical biology of nitric oxide: insights into regulatory, cytotoxic, and cytoprotective mechanisms of nitric oxide, Free Radic. Biol. Med., 25, 434, 10.1016/S0891-5849(98)00092-6 · DOI · Paper page
- Lymar, 1995, Rapid reaction between peroxynitrite ion and carbon dioxide: implications for biological activity, J. Am. Chem. Soc., 290, 52
Cited by
Sorted by citations
Items 501–600 of 977
Cho, S., Koman, V. B., Gong, X., Moon, S. J., Gordiichuk, P. I., & Strano, M. S. (2021) · ACS Nano · doi:10.1021/acsnano.1c04958 · Cited by 14
Huang, Z., Zhang, Y., Zheng, X., Liu, Z., Yao, D., Zhao, Y., Chen, X., & Aweya, J. J. (2021) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2021.104293 · Cited by 14
Kang, Y., Liu, Z., Li, W., Li, X., Zhang, X., Xu, Z., Gao, Y., & Qi, Y. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1004520 · Cited by 14
Alsharabasy, A. M., Aljaabary, A., Bohara, R. A., Farràs, P., Glynn, S. A., & Pandit, A. S. (2023) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.3c00115 · Cited by 14
Shuttle between arginine and lysine: influence on cancer immunonutrition
Sindhu, R., Supreeth, M., Prasad, S. K., & Thanmaya, M. (2023) · Amino Acids · doi:10.1007/s00726-023-03327-9 · Cited by 14
Nitric Oxide: Regulation and Function in Neutrophil Immune Responses
Kumar, S., & Dikshit, M. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0220 · Cited by 17
Zinellu, A., Tommasi, S., Carru, C., Sotgia, S., & Mangoni, A. A. (2024) · Translational Psychiatry · doi:10.1038/s41398-024-03157-7 · Cited by 15
Engineering Gas‐Releasing Nanomaterials for Efficient Wound Healing
Duan, Y., Li, L., Hu, J., Zheng, B., & He, K. (2024) · ChemBioChem · doi:10.1002/cbic.202400790 · Cited by 15
Shariatpanahi, M., Khodagholi, F., Ashabi, G., Khasraghi, A. A., Azimi, L., Abdollahi, M. R., Ghahremani, M. H., Ostad, S. N., Noorbakhsh, F., & Sharifzadeh, M. S. (2015) · Europe PMC (PubMed Central) · Cited by 14
Tacrine-Natural-Product Hybrids for Alzheimer’s Disease Therapy
Oset‐Gasque, M. J., & Marco, J. L. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867325666180403151725 · Cited by 14
Elhessy, H. M., Eltahry, H., Erfan, O. S., Mahdi, M. R., Hazem, N. M., & El-Shahat, M. A. (2020) · Acta Histochemica · doi:10.1016/j.acthis.2020.151633 · Cited by 14
Bioactivity of Inhaled Methane and Interactions With Other Biological Gases
Juhász, L., Tallósy, S. P., Nászai, A., Varga, G., Érces, D., & Boros, M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.824749 · Cited by 14
Tohamy, H. G., El-Neweshy, M. S., Soliman, M. M., Sayed, S. M. H., Shukry, M., Ghamry, H. I., & Abd-Ellatieff, H. A. (2022) · PLoS ONE · doi:10.1371/journal.pone.0265261 · Cited by 14
Yoshida, K., Yoshioka, M., Okamura, H., Moriyama, S., Kawazoe, K., Grenier, D., & Hinode, D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0112689 · Cited by 14
Enhancing Vascular Relaxing Effects of Nitric Oxide-Donor Ruthenium Complexes
Paulo, M., Banin, T. M., de Andrade, F. A., & Bendhack, L. M. (2014) · Future Medicinal Chemistry · doi:10.4155/fmc.14.26 · Cited by 15
Clinical, Research and Treatment Approaches to Affective Disorders
Juruena, M. F. (2012) · InTech eBooks · doi:10.5772/1482 · Cited by 14
The renaissance of nitric oxide: from improvement of stability to enhancement of endocytosis
Jia, F., Deng, Y., & Ji, J. (2018) · Materials Chemistry Frontiers · doi:10.1039/c8qm00013a · Cited by 14
Proof of concept for an optogalvanic gas sensor for NO based on Rydberg excitations
Schmidt, J., Fiedler, M., Albrecht, R., Djekic, D., Schalberger, P., Baur, H., Löw, R., Fruehauf, N., Pfau, T., Anders, J., et al. (2018) · Applied Physics Letters · doi:10.1063/1.5024321 · Cited by 16
Preserving vessel function during ischemic disease: new possibilities of inorganic nitrite therapy
Kevil, C. G., & Patel, R. P. (2008) · Expert Review of Cardiovascular Therapy · doi:10.1586/14779072.6.9.1175 · Cited by 14
Fluoridation--the Israel experience.
Kelman, A. M. (1996) · PubMed · Cited by 14
Kim, H., & Lee, D. G. (2021) · Biochemical Journal · doi:10.1042/bcj20200925 · Cited by 13
Hümmer, J., Kraus, S., Brändle, K., & Lee‐Thedieck, C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.610369 · Cited by 12
Srinontong, P., Wandee, J., & Aengwanich, W. (2023) · British Poultry Science · doi:10.1080/00071668.2023.2184247 · Cited by 13
In Situ Photo-crosslinkable Hyaluronic Acid/Gelatin Hydrogel for Local Nitric Oxide Delivery
Catori, D. M., da Silva, L. C. E., de Oliveira, M. F., Nguyen, G. H., Moses, J. C., Brisbois, E. J., Handa, H., & de Oliveira, M. G. (2023) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.3c10030 · Cited by 13
Labra‐Vázquez, P., Mudrak, V., Tassé, M., Mallet‐Ladeira, S., Sournia‐Saquet, A., Malval, J., Lacroix, P. G., & Malfant, I. (2023) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.3c03355 · Cited by 13
nNOS deficiency-induced cell proliferation depletes the neurogenic reserve
Keilhoff, G. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.10.026 · Cited by 13
Retinoblastoma protein prevents enteric nervous system defects and intestinal pseudo-obstruction
Fu, M., Landreville, S., Agapova, O. A., Wiley, L. A., Shoykhet, M., Harbour, J. W., & Heuckeroth, R. O. (2013) · Journal of Clinical Investigation · doi:10.1172/jci67653 · Cited by 13
Drerup, C., Ermert, J., & Coenen, H. H. (2016) · Molecules · doi:10.3390/molecules21091160 · Cited by 13
Bystander effects of nitric oxide in anti-tumor photodynamic therapy
Bazak, J., Fahey, J. M., Wawak, K., Korytowski, W., & Girotti, A. W. (2017) · Cancer Cell & Microenvironment · doi:10.14800/ccm.1511 · Cited by 12
Stupina, T. S., Балакина, А. А., Kondrat’eva, T., Козуб, Г. И., Санина, Н. А., & Терентьев, А. А. (2018) · Scientia Pharmaceutica · doi:10.3390/scipharm86040046 · Cited by 13
Song, Q., Li, L., Xiong, K., Tian, W., Lu, J., Wang, J., Huang, N., Tu, Q., & Yang, Z. (2019) · Biomaterials Science · doi:10.1039/c9bm00017h · Cited by 13
Girotti, A. W., & Korytowski, W. (2020) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-020-00909-2 · Cited by 14
Targeting the phosphoinositide-3-kinase/protein kinase B pathway in airway innate immunity
Gopallawa, I., & Lee, R. J. (2020) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v11.i2.30 · Cited by 14
Lu, K., Wang, Y., Zhang, H., Tian, C., Wang, W., Yang, T., Qi, B., & Wu, S. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00399 · Cited by 13
Fu, J., Zou, Y. S., Huang, Z., Chang, Y. Z., Zhou, Q., Zhang, H., Lai, Y., Peng, S., & Zhang, Y. (2015) · RSC Advances · doi:10.1039/c5ra00270b · Cited by 13
Abbasi, K., Shalileh, K., Anvari, M. S., Rabbani, S., Mahdanian, A., Ahmadi, S. H., Moshtaghi, N., Movahedi, N., & Karimi, A. (2011) · Cardiology · doi:10.1159/000324316 · Cited by 13
Romanowicz, G. E., He, W., Nielsen, M., & Frost, M. C. (2013) · Redox Biology · doi:10.1016/j.redox.2013.06.002 · Cited by 13
Nurieva, E. V., Трофимова, Т. П., Alexeev, A., Proshin, A. N., Chesnakova, E. A., Grishin, Y. K., Lyssenko, K. A., Филимонова, М. В., Бачурин, С. О., & Zefirova, O. N. (2018) · Mendeleev Communications · doi:10.1016/j.mencom.2018.07.016 · Cited by 13
Activation of endophytic bacteria useful for plants by atmospheric plasma treatment
Ji, S. H., Yoo, S., Choi, E. H., Oh, J., & Kim, S. B. (2020) · Journal of Physics D Applied Physics · doi:10.1088/1361-6463/aba92e · Cited by 13
LeBaron, T. W., Kura, B., Kaločayová, B., Tribulová, N., & Slezák, J. (2020) · Vide Leaf, Hyderabad eBooks · doi:10.37247/pamb.1.2020.22 · Cited by 13
Vitto, H. D., Mendonça, B. D. S., Elseth, K. M., Vesper, B. J., Portari, E. A., Gallo, C. V. D. M., Paradise, W. A., Rumjanek, F. D., & Radosevich, J. A. (2012) · Tumor Biology · doi:10.1007/s13277-012-0555-4 · Cited by 13
Nitric Oxide Prevents Glioblastoma Stem Cells’ Expansion and Induces Temozolomide Sensitization
Salvatori, L., Malatesta, S., Illi, B., Somma, M. P., Fionda, C., Stabile, H., Fontanella, R. A., & Gaetano, C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411286 · Cited by 12
Guo, F., Yang, X., Hu, C., Li, W., & Han, W. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115935 · Cited by 12
Function and regulation of nitric oxide signaling in Drosophila
Jeong, S. (2023) · Molecules and Cells · doi:10.1016/j.mocell.2023.12.004 · Cited by 12
Alemu, B. K., Tommasi, S., Hulin, J.-A., Meyers, J., & Mangoni, A. A. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118013 · Cited by 12
Inhibitory Effect of FMRFamide on NO Production During Immune Defense in Sepiella japonica
Zheng, L., Cao, H., Qiu, J., & Chi, C. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.825634 · Cited by 12
Bayat, R., Bekmezci, M., Akın, M., Işık, İ., & Şen, F. (2023) · ACS Applied Bio Materials · doi:10.1021/acsabm.3c00573 · Cited by 12
Nitric Oxide and the Cardiovascular System
Bohlen, H. G. (2015) · Comprehensive physiology · doi:10.1002/j.2040-4603.2015.tb00628.x · Cited by 12
Fluorescent indication that nitric oxide formation in NTS neurons is modulated by glutamate and GABA
Pajolla, G. P., Accorsi‐Mendonça, D., Rodrigues, G. J., Bendhack, L. M., Machado, B. H., & Lunardi, C. N. (2009) · Nitric Oxide · doi:10.1016/j.niox.2009.01.001 · Cited by 12
Ames, P. R. J., Ortiz-Cadenas, A., Torre, I. G.-D. L., Nava, A., Oregon-Miranda, A., Batuca, J. R., Kojima, K., Lopez, L. R., & Matsuura, E. (2010) · The British Journal of Diabetes · doi:10.1177/1474651410388057 · Cited by 12
Pernomian, L., do Prado, A. F., Silva, B. R., Azevedo, A., Pinheiro, L. C., Tanus-Santos, J. E., & Bendhack, L. M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00226 · Cited by 12
Zhao, C. Y., Greenstein, J. L., & Winslow, R. L. (2017) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2017.01.013 · Cited by 12
Hansen, M. B., Rasmussen, L. S., Garred, P., Pilely, K., Wahl, A. M., Perner, A., Madsen, M. B., Hedegaard, E. R., Simonsen, U., & Hyldegaard, O. (2017) · Shock · doi:10.1097/shk.0000000000000975 · Cited by 12
Li, H., Wang, K., Wan, Q., & Chen, Y. (2018) · Steroids · doi:10.1016/j.steroids.2018.11.018 · Cited by 12
He, W., Kwesiga, M. P., Gebreyesus, E. A., & Liu, S. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.82556 · Cited by 13
PTEN S-nitrosylation by NOS1 inhibits autophagy in NPC cells
Zhu, L., Zhang, C., & Liu, Q. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1542-0 · Cited by 12
Chou, W. K., Vaikunthan, M., Schröder, H. V., Link, A. J., Kim, H., & Brynildsen, M. P. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.01001 · Cited by 11
Nitric oxide in human gingival crevicular fluid after orthodontic force application
Ford, H., Suri, S., Nilforoushan, D., Manolson, M. F., & Gong, S. (2014) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2014.07.015 · Cited by 12
Electrochemical Biosensors for Real-Time Monitoring of Reactive Oxygen and Nitrogen Species
Liu, X., Dumitrescu, E., & Andreescu, S. (2015) · ACS symposium series · doi:10.1021/bk-2015-1200.ch013 · Cited by 12
Changes of Nitric Oxide Content in the Rat Hippocampus, Heart and Liver in Acute Phase of Ischemia
Андрианов, В. В., Георгиевна, П. С., Гульусовна, Я. Г., Denisov, A. A., Iyudin, V. S., Bogodvid, T. K., Dosina, M. O., KULCHITSKY, V. A., & Латыпович, Г. Х. (2016) · Applied Magnetic Resonance · doi:10.1007/s00723-016-0815-3 · Cited by 12
Regulating cell stress responses by nitric oxide to enhance calcium overload-mediated tumor therapy
Zhou, X., Gao, C., Liu, C., Zhang, R., Hu, Z., Ali, U., Zhang, L., Chen, X., Lü, L., Lü, L., et al. (2025) · Biomaterials · doi:10.1016/j.biomaterials.2025.123676 · Cited by 11
Nanoporous Ce-Based Metal–Organic Framework Nanoparticles for NO Sensing
Wang, J., Yin, Y., Rao, Q., Li, G., Sun, W., Hu, F., & Li, C. M. (2022) · ACS Applied Nano Materials · doi:10.1021/acsanm.1c04147 · Cited by 11
Linares, S. N., Beltrame, T., Galdino, G. A. M., Frade, M. C. M., Milan‐Mattos, J. C., Góis, M. D. O., Borghi‐Silva, A., de Biase, P. F., Manchado-Gobatto, F. D. B., Bagnato, V. S., et al. (2022) · Photonics · doi:10.3390/photonics9070481 · Cited by 14
Farahani, A., Farahani, A., Kashfi, K., & Ghasemi, A. (2025) · Medical Gas Research · doi:10.4103/mgr.medgasres-d-24-00100 · Cited by 13
Rosier, B. T., Hajishengallis, G., Wink, D. A., & Mira, Á. (2025) · Periodontology 2000 · doi:10.1111/prd.70006 · Cited by 12
Self-citationMolecular Mechanisms of Phosphodiesterase-5 Inhibitors on Neuronal Apoptosis
Duarte-Silva, E. P., & Peixoto, C. A. (2018) · DNA and Cell Biology · doi:10.1089/dna.2018.4410 · Cited by 11
An Electron‐Rich Calix[4]arene‐Based Receptor with Unprecedented Binding Affinity for Nitric Oxide
Wang, D., Ivanova, L. V., Ivanov, M. V., Mirzaei, S., Timerghazin, Q. K., Reid, S. A., & Rathore, R. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201804245 · Cited by 11
Moscoso, M. G., González‐García, Y., Martínez-Villegas, N. V., Cadenas‐Pliego, G., & Juárez‐Maldonado, A. (2021) · Theoretical and Experimental Plant Physiology · doi:10.1007/s40626-021-00205-1 · Cited by 11
Embelin and levodopa combination therapy for improved Parkinson’s disease treatment
Ramachandra, V. H., Sivanesan, S., Koppal, A., Anandakumar, S., Howell, M. D., Sukumar, E., & Vijayaraghavan, R. (2022) · Translational Neuroscience · doi:10.1515/tnsci-2022-0224 · Cited by 12
Long-Term Adaptation of Lung Tumor Cell Lines with Increasing Concentrations of Nitric Oxide Donor
Radosevich, J. A., Elseth, K. M., Vesper, B. J., Tarján, G., & Haines, G. K. (2009) · The Open Lung Cancer Journal · doi:10.2174/1876819900902010035 · Cited by 11
Wang, Z., Zhang, Y., Liu, Q., Sun, L., Lv, M., Yu, P., & Chen, X. (2018) · Xenobiotica · doi:10.1080/00498254.2018.1427905 · Cited by 11
The reactive species interactome
Cortese-Krott, M. M., Santolini, J., Wootton, S. A., Jackson, A. A., & Feelisch, M. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-818606-0.00004-3 · Cited by 11
Mahmoud, A. R., Kamel, E. O., Ahmed, M. A., Ahmed, E. A., & Abd‐Elhamid, T. H. (2019) · Cells Tissues Organs · doi:10.1159/000507048 · Cited by 11
Guo, X., Yu, H. V., Shen, W., Cai, R., Li, Y., Li, G., Zhao, W., & Wang, S. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105355 · Cited by 11
Detection of Cu(ii) and NO by ‘on–off’ aggregation in poly(aryl ether) dendron derivatives
Agarwal, C., & Prasad, E. (2012) · New Journal of Chemistry · doi:10.1039/c2nj40272f · Cited by 11
Bennacef-Heffar, N., & Laraba‐Djebari, F. (2017) · Acta Tropica · doi:10.1016/j.actatropica.2017.04.012 · Cited by 11
Li, J., Duan, M., Yao, X., Tian, D., & Tang, J. (2019) · Fitoterapia · doi:10.1016/j.fitote.2019.104410 · Cited by 11
Gautam, K., Negi, S., & Saini, V. (2021) · Free Radical Research · doi:10.1080/10715762.2021.1892091 · Cited by 11
Reactivity and Structure of Complexes of Small Molecules: Nitric Oxide
Harland, J. B., Manickas, E. C., Hunt, A. P., & Lehnert, N. (2021) · Elsevier eBooks · doi:10.1016/b978-0-08-102688-5.00111-2 · Cited by 11
Nitrite-Dependent Nitric Oxide Production Pathway: Diversity of NO Production Systems
Yamasaki, H., Watanabe, N. S., Fukuto, J., & Cohen, M. F. (2014) · Oxidative Stress in Applied Basic Research and Clinical Practice · doi:10.1007/978-1-4939-0679-6_3 · Cited by 10
Shang, Z., Shu, L., Liu, J., Meng, Q., Wang, Y., Sun, J., Zhang, R., & Zhang, Z. (2022) · Analytical Methods · doi:10.1039/d2ay01629j · Cited by 10
Switzer, C. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16302 · Cited by 10
Self-citationSheth, C. M., Enerson, B. E., Peters, D., Lawton, M. P., & Weaver, J. L. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr082 · Cited by 10
Role of Intracystic Cytokines and Nitric Oxide in Ovarian Neoplasms
Martins-Filho, A., Jammal, M. P., Micheli, D. C., Tavares‐Murta, B. M., Etchebehere, R. M., Murta, E. F. C., & Nomelini, R. S. (2017) · Scandinavian Journal of Immunology · doi:10.1111/sji.12617 · Cited by 10
Choromańska, B., Myśliwiec, P., Kozłowski, T., Łuba, M., Wojskowicz, P., Dadan, J., Myśliwiec, H., Choromańska, K., Makarewicz, K., Zalewska, A., et al. (2021) · Journal of Inflammation Research · doi:10.2147/jir.s337910 · Cited by 10
Uncovering Nitrosyl Reactivity at N‐Heterocyclic Carbene Center
Park, J., Kim, J., Jeong, G. Y., Kim, Y., & Lee, E. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202314978 · Cited by 10
da Costa, P. E., Batista, W. L., Curcio, M. F., de Moraes, M. S., Borges, R. E., do Nascimento, P. A., Travassos, L. R., & Monteiro, H. P. (2011) · Redox Report · doi:10.1179/174329211x12968219310792 · Cited by 10
Structural basis for incision at deaminated adenines in DNA and RNA by endonuclease V
Dalhus, B., Alseth, I., & Bjørås, M. (2015) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2015.03.005 · Cited by 11
de Oliveira, M. G., Doro, F. G., Tfouni, E., & Krieger, M. H. (2017) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.12755 · Cited by 10
Ramos, L. C. B., Rodrigues, F. P., Biazzotto, J. C., Machado, S. D. P., Slep, L. D., Hamblin, M. R., & da Silva, R. S. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1589-x · Cited by 10
Dutta, A., Islam, A. S. M., Maiti, D., Sasmal, M., Pradhan, C., & Ali, M. (2019) · Organic & Biomolecular Chemistry · doi:10.1039/c9ob00177h · Cited by 10
A divergent mode of activation of a nitrosyl iron complex with unusual antiangiogenic activity
Carvalho, E. M., Ridnour, L. A., Júnior, F. S. G., Cabral, P. H. B., do Nascimento, N. R. F., Wink, D. A., Franco, D. W., de Medeiros, M. J. C., Pontes, D. D. L., Longhinotti, E., et al. (2020) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2020.111133 · Cited by 10
Self-citationPillars and Gaps of S-Nitrosylation-Dependent Epigenetic Regulation in Physiology and Cancer
Salvatori, L., Spallotta, F., Gaetano, C., & Illi, B. (2021) · Life · doi:10.3390/life11121424 · Cited by 10
Hu, J., Whittaker, M. R., Duong, H. T. T., Li, Y., Boyer, C. A., & Davis, T. P. (2014) · Angewandte Chemie · doi:10.1002/ange.201403147 · Cited by 11
Dual Role of Nitric Oxide in Cancer Biology
Pervin, S., Singh, R., Sen, S., & Chaudhuri, G. (2010) · Springer eBooks · doi:10.1007/978-1-4419-1432-3_3 · Cited by 10
Intermediate Tyrosyl Radical and Amyloid Structure in Peroxide-Activated Cytoglobin
Ferreira, J. C., Marcondes, M. F., Icimoto, M. Y., Cardoso, T. H. S., Tofanello, A., Pessoto, F. S., Miranda, É. G. A., Prieto, T., Nascimento, O. R., Oliveira, V., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0136554 · Cited by 10
Ishemia-Reperfusion enhances GAPDH nitration in aging skeletal muscle
Bailey, C. E., Hammers, D. W., DeFord, J. H., Dimayuga, V. L., Amaning, J. K., Farrar, R. P., & Papaconstantinou, J. (2011) · Aging · doi:10.18632/aging.100394 · Cited by 10
NO • and Pancreatic Cancer: A Complex Interaction with Therapeutic Potential
Wang, J., & Hussain, S. P. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6809 · Cited by 10
How does the total charge and isomerism influence the Ru–NO ammine complexes?
Orenha, R. P., Tfouni, E., & Galembeck, S. E. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c8cp00865e · Cited by 10
Shimizu, T., Matsumoto, A., & Noda, M. (2019) · Infection and Immunity · doi:10.1128/iai.00334-19 · Cited by 9
Metadata
- Authors
- 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., Colton, C. A., Harris, C. C., Roberts, D. D., & Wink, D. A.
- Affiliations
- University of Illinois Chicago (US)
- National Institutes of Health (US)
- Johns Hopkins University (US)
- Duke University (US)
- Corresponding author
- Wink, David A.
- ORCID
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2008-07
- Volume
- 45
- Issue
- 1
- Pages
- 18-31
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC2572721
- OpenAlex
- W1980458823
- Cited by
- 975
- References
- 166
- Citations by year
- 2026: 33 · 2025: 44 · 2024: 37 · 2023: 54 · 2022: 57 · 2021: 73 · 2020: 58 · 2019: 55 · 2018: 54 · 2017: 45 · 2016: 53 · 2015: 63 · 2014: 67 · 2013: 50 · 2012: 69
- FWCI
- 5.87
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (K22CA113315, Z01BC010033)
- Topics
- Health Sciences › Medicine › Physiology (medical) › 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 › Biochemistry › Hemoglobin structure and function
- Keywords
- nitric oxide, signal transduction, NO concentration, cGMP signaling, Akt phosphorylation, HIF-1α stabilization, p53 phosphorylation, nitrosative stress, reactive oxygen species, reactive nitrogen species, oxidative stress, cell cycle arrest, apoptosis, senescence
- MeSH terms
- Animals, Diffusion, Humans, Kinetics, 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
