Small molecule signaling agents: the integrated chemistry and biochemistry of nitrogen oxides, oxides of carbon, dioxygen, hydrogen sulfide, and their derived species
Open accessAbstract
Several small molecule species formally known primarily as toxic gases have, over the past 20 years, been shown to be endogenously generated signaling molecules. The biological signaling associated with the small molecules NO, CO, H₂S (and the nonendogenously generated O₂), and their derived species have become a topic of extreme interest. It has become increasingly clear that these small molecule signaling agents form an integrated signaling web that affects/regulates numerous physiological processes. The chemical interactions between these species and each other or biological targets is an important factor in their roles as signaling agents. Thus, a fundamental understanding of the chemistry of these molecules is essential to understanding their biological/physiological utility. This review focuses on this chemistry and attempts to establish the chemical basis for their signaling functions.
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?
Nitrite is swallowed and can undergo downstream reactions, including formation of NO and NO-donating species following protonation to HNO2 and secondary nitrosating and nitrating species in the low pH of the stomach, or further reduction by enteric bacterial nitrite reductases.
“Nitrite is then swallowed where it can undergo a diversity of downstream reactions, including formation of NO and NO-donating species following a) protonation to HNO2 and an array of secondary nitrosating and nitrating species in reactions facilitated by the low pH of the stomach[80,83,89–91], or b) further reduction by enteric bacterial nitrite reductases (NiRs)[74].”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [91]
H2S is a biologically important thiol that shares significant overlapping signaling activity with NO, reacts with NO-derived reactive species and has been implicated in modulating the pathogenesis of several inflammatory bowel diseases.
“H2S is a biologically important thiol that shares significant overlapping signaling activity with NO, reacts with NO-derived reactive species and has been implicated in modulating the pathogenesis of several inflammatory bowel diseases[91,343,344].”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [91]
H2S directly interfaces with nitrogen oxide reduction and the generation of intestinal NO by serving as an electron donor during nitrite reduction to NO by nitrite reductase, or by reacting with the nitrogen oxide S-nitrosothiol.
“H2S directly interfaces with nitrogen oxide reduction and the generation of intestinal NO by serving as an electron donor during nitrite reduction to NO by nitrite reductase, or by reacting with the nitrogen oxide S-nitrosothiol[91,102,346].”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [91]
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
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 · see citing works
Free Radicals in Biology and Medicine
Halliwell, B., & Gutteridge, J. M. C. (2015) · doi:10.1093/acprof:oso/9780198717478.001.0001 · Cited by 8,990 · see citing works
Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly
Beckman, J. S., & Koppenol, W. H. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.271.5.c1424 · Cited by 5,513 · see citing works
Rate Constants for Reactions of Inorganic Radicals in Aqueous Solution
Neta, P., Huie, R. E., & Ross, A. B. (1988) · Journal of Physical and Chemical Reference Data · doi:10.1063/1.555808 · Cited by 3,651 · see citing works
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455 · see citing works
Dioxygen Activation at Mononuclear Nonheme Iron Active Sites: Enzymes, Models, and Intermediates
Costas, M., Mehn, M. P., Jensen, M. P., & QUE, L. J. (2004) · Chemical Reviews · doi:10.1021/cr020628n · Cited by 2,475 · 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
The reaction of NO with superoxide
Huie, R. E., & Padmaja, S. (1993) · Free Radical Research Communications · doi:10.3109/10715769309145868 · Cited by 2,121 · see citing works
Hydrocarbon Bond Dissociation Energies
McMillen, D. F., & Golden, D. M. (1982) · Annual Review of Physical Chemistry · doi:10.1146/annurev.pc.33.100182.002425 · Cited by 2,009 · see citing works
Jones, M., Ibels, L. S., Schenkel, B., & Zagari, M. J. (2004) · Kidney International · doi:10.1111/j.1523-1755.2004.00450.x · Cited by 1,812 · see citing works
Nitrite reduction to nitric oxide by deoxyhemoglobin vasodilates the human circulation
Cosby, K., Partovi, K. S., Crawford, J. H., Patel, R. P., Reiter, C. D., Martyr, S., Yang, B. K., Waclawiw, M. A., Zalos, G., Xu, X., et al. (2003) · Nature Medicine · doi:10.1038/nm954 · Cited by 1,807 · see citing works
Principles of structure, bonding, and reactivity for metal nitrosyl complexes
Enemark, J. H., & Feltham, R. D. (1974) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(00)80259-3 · Cited by 1,656 · see citing works
Standard Electrode Potentials and Temperature Coefficients in Water at 298.15 K
Bratsch, S. G. (1989) · Journal of Physical and Chemical Reference Data · doi:10.1063/1.555839 · Cited by 1,589 · see citing works
The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide
Pryor, W. A., & Squadrito, G. L. (1995) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1995.268.5.l699 · Cited by 1,511 · see citing works
Protein Radicals in Enzyme Catalysis
Stubbe, J., & van der Donk, W. A. (1998) · Chemical Reviews · doi:10.1021/cr9400875 · Cited by 1,378 · see citing works
Reactivity of Dioxygen−Copper Systems
Lewis, E. A., & Tolman, W. B. (2004) · Chemical Reviews · doi:10.1021/cr020633r · Cited by 1,296 · see citing works
Singlet oxygen: there is indeed something new under the sun
Ogilby, P. R. (2010) · Chemical Society Reviews · doi:10.1039/b926014p · Cited by 1,270 · see citing works
H 2 S Signals Through Protein S-Sulfhydration
Mustafa, A. K., Gadalla, M. M., Sen, N., Kim, S., Mu, W., Gazi, S. K., Barrow, R. K., Yang, G., Wang, R., & Snyder, S. H. (2009) · Science Signaling · doi:10.1126/scisignal.2000464 · Cited by 1,235 · see citing works
Robertson, C. A., Evans, D. H., & Abrahamse, H. (2009) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2009.04.001 · Cited by 1,201 · see citing works
Hydrogen Peroxide: A Signaling Messenger
Stone, J. R., & Yang, S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.243 · Cited by 1,175 · see citing works
Guanylate cyclase and the ⋅NO/cGMP signaling pathway
Denninger, J. W., & Marletta, M. A. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00024-9 · Cited by 1,040 · 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
Regulation of Oxygen Homeostasis by Hypoxia-Inducible Factor 1
Semenza, G. L. (2009) · Physiology · doi:10.1152/physiol.00045.2008 · Cited by 926 · see citing works
Hydroxylation of HIF-1: Oxygen Sensing at the Molecular Level
Semenza, G. L. (2004) · Physiology · doi:10.1152/physiol.00001.2004 · Cited by 901 · see citing works
H 2 S Induces a Suspended Animation-Like State in Mice
Blackstone, E., Morrison, M., & Roth, M. B. (2005) · Science · doi:10.1126/science.1108581 · Cited by 802 · see citing works
Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
Winterbourn, C. C., & Metodiewa, D. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00051-9 · Cited by 799 · see citing works
Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
Hirsilä, M., Koivunen, P., Günzler, V., Kivirikko, K. I., & Myllyharju, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304982200 · Cited by 794 · see citing works
Chemical biology of peroxynitrite: Kinetics, diffusion, and radicals
Ferrer-Sueta, G., & Radi, R. (2009) · ACS Chemical Biology · doi:10.1021/cb800279q · Cited by 776 · see citing works
Transition metals as catalysts of “autoxidation” reactions
Miller, D. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90148-c · Cited by 739 · see citing works
Singlet oxygen in plants: production, detoxification and signaling
Triantaphylidès, C., & Havaux, M. (2009) · Trends in Plant Science · doi:10.1016/j.tplants.2009.01.008 · Cited by 715 · see citing works
Thermochemistry and kinetics of sulfur-containing molecules and radicals
Benson, S. W. (1978) · Chemical Reviews · doi:10.1021/cr60311a003 · Cited by 706 · see citing works
Redistribution of Intracellular Oxygen in Hypoxia by Nitric Oxide: Effect on HIF1α
Hagen, T., Taylor, C. T., Lam, F., & Moncada, S. (2003) · Science · doi:10.1126/science.1088805 · Cited by 704 · see citing works
Iron-sulfur proteins: ancient structures, still full of surprises
Beinert, H. (2000) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750050002 · Cited by 667 · see citing works
Reduction Potentials Involving Inorganic Free Radicals in Aqueous Solution
Stanbury, D. M. (1989) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60194-4 · Cited by 656 · see citing works
The emerging biology of the nitrite anion
Gladwin, M. T., Schechter, A. N., Kim-Shapiro, D. B., Patel, R. P., Hogg, N., Shiva, S., Cannon, R. O., Kelm, M., Wink, D. A., Espey, M. G., et al. (2005) · Nature Chemical Biology · doi:10.1038/nchembio1105-308 · Cited by 609 · see citing works
The novel neuromodulator hydrogen sulfide: an endogenous peroxynitrite ‘scavenger’?
Whiteman, M., Armstrong, J. S., Chu, S. H., Siau, J. L., Wong, B., Cheung, N. S., Halliwell, B. B., & Moore, P. K. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02617.x · Cited by 604 · see citing works
Liu, X., Miller, M. J. S., Joshi, M. S., Thomas, D. D., & Lancaster, J. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2175 · Cited by 602 · see citing works
Kinetics of oxidation of aqueous sulfide by oxygen
Chen, K. Y., & Morris, J. C. (1972) · Environmental Science & Technology · doi:10.1021/es60065a008 · Cited by 594 · see citing works
Biological inorganic chemistry: structure and reactivity
(2007) · Choice Reviews Online · doi:10.5860/choice.44-6242 · Cited by 575 · see citing works
Nitrogen dioxide and carbonate radical anion: two emerging radicals in biology
Augusto, O., Bonini, M. G., Amanso, A. M., Linares, E., Santos, C. C. X., & De Menezes, S. L. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00786-4 · Cited by 555 · see citing works
Forman, H., Fukuto, J., & Torres, M. (2004) · American Journal of Physiology - Cell Physiology · doi:10.1152/ajpcell.00516.2003 · Cited by 538 · see citing works
(1995) · Springer eBooks · doi:10.1007/978-94-007-0874-7 · Cited by 514 · see citing works
Nitric oxide and iron proteins
Cooper, C. E. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00021-3 · Cited by 510 · see citing works
Mustafa, A. K., Gadalla, M. M., & Snyder, S. H. (2009) · Science Signaling · doi:10.1126/scisignal.268re2 · Cited by 497 · see citing works
Free radical biology and medicine: it's a gas, man!
Pryor, W. A., Houk, K. N., Foote, C. S., Fukuto, J. M., Ignarro, L. J., Squadrito, G. L., & Davies, K. J. A. (2006) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00614.2005 · Cited by 465 · see citing works
Nucleophilic reactivity constants toward methyl iodide and trans-dichlorodi(pyridine)platinum(II)
Pearson, R. G., Sobel, H. R., & Songstad, J. (1968) · Journal of the American Chemical Society · doi:10.1021/ja01004a021 · Cited by 455 · see citing works
Shafirovich, V., & Lymar, S. V. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.112202099 · Cited by 440 · see citing works
Regulation of HIF-1α Stability through S-Nitrosylation
Li, F., Sonveaux, P., Rabbani, Z. N., Liu, S., Yan, B., Huang, Q., Vujašković, Ž., Dewhirst, M. W., & Li, C. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.024 · Cited by 439 · see citing works
Autoxidation kinetics of aqueous nitric oxide
Ford, P. C., Wink, D. A., & Stanbury, D. M. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81748-o · Cited by 419 · see citing works
Nitric Oxide Impairs Normoxic Degradation of HIF-1α by Inhibition of Prolyl Hydroxylases
Metzen, E., Zhou, J., Jelkmann, W., Fandrey, J., & Brüne, B. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-12-0791 · Cited by 414 · see citing works
Reduction of nitrite to nitric oxide catalyzed by xanthine oxidoreductase
Godber, B. L. J., Doel, J. J., Sapkota, G. P., Blake, D. R., Stevens, C. R., Eisenthal, R., & Harrison, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7757 · Cited by 411 · see citing works
The reduction potential of nitric oxide (NO) and its importance to NO biochemistry
Bartberger, M. D., Liu, W., Ford, E., Miranda, K. M., Switzer, C., Fukuto, J. M., Farmer, P. J., Wink, D. A., & Houk, K. N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162095599 · Cited by 384 · see citing works
On the Mechanism of Inactivation of Xanthine Oxidase by Cyanide
Massey, V., & Edmondson, D. E. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62575-x · Cited by 368 · see citing works
Wong, P. S.-Y., Hyun, J., Fukuto, J. M., Shirota, F. N., DeMaster, E. G., Shoeman, D. W., & Nagasawa, H. T. (1998) · Biochemistry · doi:10.1021/bi973153g · Cited by 363 · see citing works
Traylor, T. G., & Sharma, V. S. (1992) · Biochemistry · doi:10.1021/bi00126a001 · Cited by 354 · see citing works
Trafficking in persulfides: delivering sulfur in biosynthetic pathways
Mueller, E. G. (2006) · Nature Chemical Biology · doi:10.1038/nchembio779 · Cited by 351 · see citing works
Prütz, W. A., Mönig, H., Butler, J., & Land, E. J. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90780-5 · Cited by 338 · see citing works
The Reaction of Nitric Oxide with Organic Peroxyl Radicals
Padmaja, S., & Huie, R. E. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.2079 · Cited by 323 · see citing works
Sulfenic Acid Formation in Human Serum Albumin by Hydrogen Peroxide and Peroxynitrite
Carballal, S., Radí, R., KIRK, M. C., Barnes, S., Freeman, B. Α., & Álvarez, B. (2003) · Biochemistry · doi:10.1021/bi027434m · Cited by 313 · see citing works
Lahiri, S., Roy, A., Baby, S. M., Hoshi, T., Semenza, G. L., & Prabhakar, N. R. (2006) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2005.07.001 · Cited by 312 · see citing works
Nature of O2 and CO binding to metalloporphyrins and heme proteins.
Collman, J. P., Brauman, J. I., Halbert, T. R., & Suslick, K. S. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.10.3333 · Cited by 310 · see citing works
Reversible conversion of nitroxyl anion to nitric oxide by superoxide dismutase.
Murphy, M. E., & Sies, H. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10860 · Cited by 303 · see citing works
Pryor, W. A., Church, D. F., Govindan, C. K., & Crank, G. (1982) · The Journal of Organic Chemistry · doi:10.1021/jo00340a038 · Cited by 293 · see citing works
Spectroscopic studies and bonding model for nitric oxide complexes of iron porphyrins
Wayland, B. B., & Olson, L. W. (1974) · Journal of the American Chemical Society · doi:10.1021/ja00826a013 · Cited by 293 · see citing works
Thomas, D. D., Espey, M. G., Ridnour, L. A., Hofseth, L. J., Mancardi, D., Harris, C. C., & Wink, D. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400453101 · Cited by 289 · see citing works
Inhibition of Hypoxia-inducible Factor 1 Activation by Carbon Monoxide and Nitric Oxide
Huang, E. L., Willmore, W. G., Gu, J., Goldberg, M. A., & Bunn, H. F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.9038 · Cited by 287 · see citing works
The Molecular Mechanism of Autoxidation for Myoglobin and Hemoglobin: A Venerable Puzzle
Shikama, K. (1998) · Chemical Reviews · doi:10.1021/cr970042e · Cited by 279 · see citing works
Molecular Mechanisms of Hydrogen Sulfide Toxicity
Truong, D. H., Eghbal, M. A., Hindmarsh, W., Roth, S. H., & O’Brien, P. J. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600959607 · Cited by 264 · see citing works
Rubbo, H., Parthasarathy, S., Barnes, S., KIRK, M. C., Kalyanaraman, B., & Freeman, B. Α. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.9935 · Cited by 263 · see citing works
Paolocci, N., Jackson, M. I., Lopez, B., Miranda, K. M., Tocchetti, C. G., Wink, D. A., Hobbs, A. J., & Fukuto, J. M. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2006.11.002 · Cited by 243 · see citing works
Carbon monoxide-dependent energy metabolism in anaerobic bacteria and archaea
Oelgeschläger, E., & Rother, M. (2008) · Archives of Microbiology · doi:10.1007/s00203-008-0382-6 · Cited by 236 · see citing works
Ford, E., Hughes, M., & Wardman, P. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00850-x · Cited by 229 · see citing works
Chin, B. Y., Jiang, G., Wegiel, B., Wang, H. J., MacDonald, T. Y., Zhang, X., Gallo, D. J., Cszimadia, E., Bach, F. H., Lee, P. J., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609611104 · Cited by 228 · see citing works
The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal
Forman, H. J., Fukuto, J. M., Miller, T., Zhang, H., Rinna, A., & Levy, S. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.06.011 · Cited by 226 · see citing works
Influence of globin structures on the state of the heme. IV. Ferrous low spin derivatives
Perutz, M. F., Kilmartin, J. V., Nagai, K., Szabó, A., & Simon, S. R. (1976) · Biochemistry · doi:10.1021/bi00647a022 · Cited by 226 · see citing works
Banerjee, R. V., & Zou, C.-G. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.08.037 · Cited by 226 · see citing works
Nitric Oxide, Cytochrome C Oxidase, and the Cellular Response to Hypoxia
Taylor, C. T., & Moncada, S. (2010) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.108.181628 · Cited by 220 · see citing works
Nitric oxide signaling: no longer simply on or off
Cary, S. P., Winger, J. A., Derbyshire, E. R., & Marletta, M. A. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.02.003 · Cited by 219 · see citing works
(1995) · Springer eBooks · doi:10.1007/978-1-4613-9783-0 · Cited by 217 · see citing works
Nitrite reductase activity of cytochrome c
Basu, S., Azarova, N. A., Font, M. D., King, S. B., Hogg, N., Gladwin, M. T., Shiva, S., & Kim-Shapiro, D. B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806934200 · Cited by 214 · see citing works
Goodrich, L. E., Paulat, F., Praneeth, V. K. K., & Lehnert, N. (2010) · Inorganic Chemistry · doi:10.1021/ic902304a · Cited by 204 · see citing works
Biological Chemistry of Carbon Monoxide
Piantadosi, C. A. (2002) · Antioxidants and Redox Signaling · doi:10.1089/152308602753666316 · Cited by 201 · see citing works
The reaction of H2S with oxidized thiols: generation of persulfides and implications to H2S biology
Francoleon, N. E., Carrington, S. J., & Fukuto, J. M. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.09.015 · Cited by 199 · see citing works
Self-citationNature of the bound oxygen in a series of cobalt dioxygen adducts
Tovrog, B. S., Kitko, D. J., & Drago, R. S. (1976) · Journal of the American Chemical Society · doi:10.1021/ja00433a016 · Cited by 198 · see citing works
Characterization of NO binding to human cystathionine β-synthase:
Taoka, S., & Banerjee, R. V. (2001) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(01)00335-x · Cited by 196 · see citing works
Gladwin, M. T., Grubina, R., & Doyle, M. P. (2009) · Accounts of Chemical Research · doi:10.1021/ar800089j · Cited by 194 · see citing works
Oxidation and Nitrosation of Thiols at Low Micromolar Exposure to Nitric Oxide
Jourd’heuil, D., Jourd’heuil, F. L., & Feelisch, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300203200 · Cited by 194 · see citing works
An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems
Stone, J. R. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.12.029 · Cited by 192 · see citing works
Kinetics of oxygenation of reduced sulfur species in aqueous solution
O’Brien, D. J., & Birkner, F. B. (1977) · Environmental Science & Technology · doi:10.1021/es60135a009 · Cited by 191 · see citing works
Bonini, M. G., & Augusto, O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008456200 · Cited by 191 · see citing works
Wood, J. L. (1987) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(87)43009-7 · Cited by 177 · see citing works
Sexton, D. J., Muruganandam, A., McKenney, D. J., & Mutus, B. (1994) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1994.tb05065.x · Cited by 174 · see citing works
Kim‐Shapiro, D. B., Gladwin, M. T., Patel, R. P., & Hogg, N. (2004) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2004.10.034 · Cited by 172 · see citing works
HIF hydroxylation and cellular oxygen sensing
Metzen, E., & Ratcliffe, P. J. (2004) · Biological Chemistry · doi:10.1515/bc.2004.016 · Cited by 171 · see citing works
Nitric oxide complexes of metalloporphyrins: an overview of some mechanistic studies
Hoshino, M., Laverman, L. E., & Ford, P. C. (1999) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(98)00228-8 · Cited by 168 · see citing works
Oxyradical reactions: from bond‐dissociation energies to reduction potentials
Koppenol, W. H. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80239-f · Cited by 167 · see citing works
On the acidity and reactivity of HNO in aqueous solution and biological systems
Bartberger, M. D., Fukuto, J. M., & Houk, K. N. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041481598 · Cited by 167 · see citing works
Kinetics and mechanism of oxidation of hydrogen sulfide by hydrogen peroxide in acidic solution
Hoffmann, M. R. (1977) · Environmental Science & Technology · doi:10.1021/es60124a004 · Cited by 160 · see citing works
Berchner‐Pfannschmidt, U., Yamac, H., Trinidad, B., & Fandrey, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607065200 · Cited by 157 · see citing works
Yasinska, I. M., & Sumbayev, V. V. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00807-x · Cited by 156 · see citing works
Nitric oxide rapidly scavenges tyrosine and tryptophan radicals
Eiserich, J. P., Butler, J., van der Vliet, A., Cross, C. E., & Halliwell, B. B. (1995) · Biochemical Journal · doi:10.1042/bj3100745 · Cited by 151 · see citing works
An overview of the biological significance of endogenous gases: new roles for old molecules
Li, L., & Moore, P. K. (2007) · Biochemical Society Transactions · doi:10.1042/bst0351138 · Cited by 151 · see citing works
DeMaster, E. G., Quast, B. J., Redfern, B., & Nagasawa, H. T. (1995) · Biochemistry · doi:10.1021/bi00036a023 · Cited by 147 · see citing works
The Resolution of Active and Inactive Xanthine Oxidase by Affinity Chromatography
Edmondson, D. E., Massey, V., Palmer, G., Beacham, L. M., & Elion, G. B. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45598-1 · Cited by 142 · see citing works
Wayland, B. B., Minkiewicz, J. V., & Abd-Elmageed, M. E. (1974) · Journal of the American Chemical Society · doi:10.1021/ja00816a022 · Cited by 142 · see citing works
Inhibition of cellular respiration by endogenously produced carbon monoxide
D’Amico, G., Lam, F., Hagen, T., & Moncada, S. (2006) · Journal of Cell Science · doi:10.1242/jcs.02914 · Cited by 132 · see citing works
Acidity of the Carbonate Radical
Czapski, G., Lymar, S. V., & Schwarz, H. A. (1999) · The Journal of Physical Chemistry A · doi:10.1021/jp984769y · Cited by 131 · see citing works
Nitric oxide and superoxide: Interference with hypoxic signaling
Brüne, B., & ZHOU, J. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.03.005 · Cited by 126 · see citing works
Siddiq, A., Aminova, L. R., & Ratan, R. R. (2007) · Neurochemical Research · doi:10.1007/s11064-006-9268-7 · Cited by 121 · see citing works
Kortemme, T., Darby, N. J., & Creighton, T. E. (1996) · Biochemistry · doi:10.1021/bi9617724 · Cited by 120 · see citing works
Nitric oxide regulation of mitochondrial oxygen consumption I: cellular physiology
Giulivi, C., Kato, K., & Cooper, C. E. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00307.2006 · Cited by 119 · see citing works
Structure of proline 3‐hydroxylase
Clifton, I. J., Hsueh, L., Baldwin, J. E., Harlos, K., & Schofield, C. J. (2001) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02617.x · Cited by 113 · see citing works
Crystal structures of the nitrite and nitric oxide complexes of horse heart myoglobin
Copeland, D. M., Soares, A. S., West, A. H., & Richter-Addo, G. B. (2006) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2006.04.011 · Cited by 113 · see citing works
Budde, M. W., & Roth, M. B. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-03-0199 · Cited by 112 · see citing works
Efficient Trapping of HNO by Deoxymyoglobin
Sulc, F., Immoos, C. E., Pervitsky, D., & Farmer, P. J. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0376184 · Cited by 110 · see citing works
HIF‐1α protein as a target for S‐nitrosation
Sumbayev, V. V., Budde, A., Zhou, J., & Brüne, B. (2003) · FEBS Letters · doi:10.1016/s0014-5793(02)03887-5 · Cited by 108 · see citing works
Taoka, S., West, M., & Banerjee, R. V. (1999) · Biochemistry · doi:10.1021/bi9826052 · Cited by 106 · see citing works
Madej, E., Folkes, L. K., Wardman, P., Czapski, G., & Goldstein, S. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.02.015 · Cited by 105 · see citing works
Mechanisms of Peroxynitrite-Mediated Nitration of Tyrosine
Günaydin, H., & Houk, K. N. (2009) · Chemical Research in Toxicology · doi:10.1021/tx800463y · Cited by 105 · see citing works
Nervous control of circulation – The role of gasotransmitters, NO, CO, and H2S
Olson, K. R., & Donald, J. A. (2009) · Acta Histochemica · doi:10.1016/j.acthis.2008.11.004 · Cited by 105 · see citing works
Hoffmann, M. R., & Lim, B. C. (1979) · Environmental Science & Technology · doi:10.1021/es60159a014 · Cited by 104 · see citing works
Hay, D. L. (2009) · Science Signaling · doi:10.1126/scisignal.262tr1 · Cited by 101 · see citing works
Fukuto, J. M., & Ignarro, L. J. (1997) · Accounts of Chemical Research · doi:10.1021/ar960010y · Cited by 101 · see citing works
The Effects of Nitroxyl (HNO) on Soluble Guanylate Cyclase Activity
Miller, T. W., Cherney, M. M., Lee, A. J., Francoleon, N. E., Farmer, P. J., King, S. B., Hobbs, A. J., Miranda, K. M., Burstyn, J. N., & Fukuto, J. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014282 · Cited by 99 · see citing works
Yi, J., Heinecke, J. L., Tan, H., Ford, P. C., & Richter-Addo, G. B. (2009) · Journal of the American Chemical Society · doi:10.1021/ja904726q · Cited by 96 · see citing works
Ligand discrimination in soluble guanylate cyclase and the H-NOX family of heme sensor proteins
Boon, E. M., & Marletta, M. A. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2005.08.015 · Cited by 96 · see citing works
Evidence for an Active Site Persulfide Residue in Rabbit Liver Aldehyde Oxidase
Branzoli, U., & Massey, V. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42426-5 · Cited by 94 · see citing works
Koppenol, W. H., & Kissner, R. (1998) · Chemical Research in Toxicology · doi:10.1021/tx970200x · Cited by 93 · see citing works
Das, T. N., Huie, R. E., Neta, P., & Padmaja, S. (1999) · The Journal of Physical Chemistry A · doi:10.1021/jp9907544 · Cited by 92 · see citing works
Interaction of Cu,Zn Superoxide Dismutase with Hydrogen Sulfide
Searcy, D. G., Whitehead, J., & Maroney, M. J. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1228 · Cited by 91 · see citing works
Ondriaš, K., Staško, A., Čačányiová, S., Sulová, Z., Križanová, O., Kristek, F., Máleková, Ľ., Knezl, V., & Breier, A. (2008) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-008-0519-0 · Cited by 90 · see citing works
Miranda, K. M., Nagasawa, H. T., & Toscano, J. P. (2005) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026054679290 · Cited by 90 · see citing works
S-Nitrosothiols and role of metal ions in decomposition to nitric oxide
Williams, D. L. H. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)68032-x · Cited by 88 · see citing works
Interaction of Proteins with Sulfide
Cavallini, D., Federici, G., & Barboni, E. (1970) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1970.tb00275.x · Cited by 86 · see citing works
de Beus, M. D., Chung, J. F., & Colón, W. (2004) · Protein Science · doi:10.1110/ps.03576904 · Cited by 86 · see citing works
General bonding model for linear and bent transition metal-nitrosyl complexes
Mingos, D. M. P. (1973) · Inorganic Chemistry · doi:10.1021/ic50123a052 · Cited by 81 · see citing works
[5] Perthiols as antioxidants: Radical-scavenging andprooxidative mechanisms
Everett, S. A., & Wardman, P. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)51110-5 · Cited by 80 · see citing works
A Novel Enhancing Mechanism for Hydrogen Sulfide-producing Activity of Cystathionine β-Synthase
Eto, K., & Kimura, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205835200 · Cited by 80 · see citing works
Liu, X., Pan, L., Yang, Z. R., Gong, Q., Rose, P. E., & Zhu, Y. Z. (2010) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.33.1550 · Cited by 78 · see citing works
Carbon monoxide-driven reduction of ferric heme and heme proteins.
Bickar, D., Bonaventura, C., & Bonaventura, J. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90579-x · Cited by 73 · see citing works
Catalytic autoxidation of hydrogen sulfide in wastewater
Κοτρωνάρου, Α., & Hoffmann, M. R. (1991) · Environmental Science & Technology · doi:10.1021/es00018a021 · Cited by 70 · see citing works
Linkage Isomerism in Nitrite Reduction by Cytochrome cd1 Nitrite Reductase
Silaghi-Dumitrescu, R. L. (2004) · Inorganic Chemistry · doi:10.1021/ic035403p · Cited by 70 · see citing works
Thermal and photochemical reactions of sulfhydryl radicals. Implications for colloid photocorrosion
Mills, G., Schmidt, K. H., Matheson, M. S., & Meisel, D. (1987) · The Journal of Physical Chemistry · doi:10.1021/j100290a060 · Cited by 70 · see citing works
Reactive oxygen species attenuate nitric-oxide-mediated hypoxia-inducible factor-1α stabilization
Köhl, R., Zhou, J., & Brüne, B. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.12.012 · Cited by 69 · see citing works
Kim, E., Feng, J., Bramlett, M. R., & Lindahl, P. A. (2004) · Biochemistry · doi:10.1021/bi036062u · Cited by 69 · see citing works
Grahame, D. A., & DeMoll, E. (1995) · Biochemistry · doi:10.1021/bi00014a015 · Cited by 69 · see citing works
A Microscopic Study of the Deoxyhemoglobin-Catalyzed Generation of Nitric Oxide from Nitrite Anion
Perissinotti, L. L., Marti, M. A., Doctorovich, F. A., Luque, F. J., & Estrin, D. A. (2008) · Biochemistry · doi:10.1021/bi801104c · Cited by 67 · see citing works
Thermochemical Properties of Peroxides and Peroxyl Radicals
Jönsson, M. (1996) · The Journal of Physical Chemistry · doi:10.1021/jp9601126 · Cited by 66 · see citing works
Reaction of Cystine with Sodium Sulfide in Sodium Hydroxide Solution
Rao, G., & Gorin, G. (1959) · The Journal of Organic Chemistry · doi:10.1021/jo01088a005 · Cited by 66 · see citing works
Wink, D. A., Wink, C. B., Nims, R. W., & Ford, P. C. (1994) · Environmental Health Perspectives · doi:10.1289/ehp.94102s311 · Cited by 63 · see citing works
Yukl, E. T., de Vries, S., & Moënne‐Loccoz, P. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9026924 · Cited by 63 · see citing works
Sandy, J. D., Davies, R. C., & Neuberger, A. (1975) · Biochemical Journal · doi:10.1042/bj1500245 · Cited by 59 · see citing works
Heme-based sensors: theoretical modeling of heme-ligand–protein interactions
Spiro, T. G., & Jarzęcki, A. A. (2001) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(01)00271-x · Cited by 58 · see citing works
Thermodynamics of reactions involving nitrogen-oxygen compounds
Koppenol, W. H. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)68005-7 · Cited by 57 · see citing works
Quantification of intermediates formed during the reduction of nitrite by deoxyhemoglobin
Salgado, M. T., Nagababu, E., & Rifkind, J. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808647200 · Cited by 56 · see citing works
Direct measurement of the binding energy of the NO dimer
Wade, E. A., Cline, J. I., Lorenz, K. T., Hayden, C. C., & Chandler, D. W. (2002) · The Journal of Chemical Physics · doi:10.1063/1.1459702 · Cited by 55 · see citing works
Kinetic feasibility of nitroxyl reduction by physiological reductants and biological implications
Jackson, M. I., Han, T. H., Serbulea, L., Dutton, A. S., Ford, E., Miranda, K. M., Houk, K. N., Wink, D. A., & Fukuto, J. M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.06.034 · Cited by 54 · see citing works
Zhao, Y., Bartberger, M. D., Goto, K., Shimada, K., Kawashima, T., & Houk, K. N. (2005) · Journal of the American Chemical Society · doi:10.1021/ja042247s · Cited by 54 · see citing works
Valentine, W. N., Toohey, J. I., Paglia, D. E., Nakatani, M., & Brockway, R. A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.5.1394 · Cited by 49 · see citing works
From O2 to H2S: A landscape view of gas biology.
Kashiba, M., Kajimura, M., Goda, N., & Suematsu, M. (2002) · The Keio Journal of Medicine · doi:10.2302/kjm.51.1 · Cited by 46 · see citing works
The origin of the long N-N bond in N2O2: an ab initio valence bond study
Harcourt, R. D. (1990) · Journal of Molecular Structure THEOCHEM · doi:10.1016/0166-1280(90)85140-i · Cited by 45 · see citing works
The heats of formation of HNO and of DNO
Dixon, R. N. (1996) · The Journal of Chemical Physics · doi:10.1063/1.471714 · Cited by 42 · see citing works
Günaydin, H., & Houk, K. N. (2008) · Journal of the American Chemical Society · doi:10.1021/ja711365e · Cited by 42 · see citing works
Photochemistry of the S-Nitroso Derivatives of Hexane-l-thiol and Hexane-l,6-dithiol
Barrett, J., FITZGIBBONS, L. J., Glauser, J., Still, R. H., & Young, P. N. W. (1966) · Nature · doi:10.1038/211848a0 · Cited by 33 · see citing works
Theoretical Investigation of Nitration and Nitrosation of Dimethylamine by N2O4
Lv, C. L., Liu, Y. D., & Zhong, R. (2008) · The Journal of Physical Chemistry A · doi:10.1021/jp8029924 · Cited by 28 · see citing works
Bonaventura, C., Godette, G., Tesh, S., Holm, D. E., Bonaventura, J., Crumbliss, A. L., Pearce, L. L., & Peterson, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.9.5499 · Cited by 28 · see citing works
Mechanisms of hypoxic signal transduction regulated by reactive nitrogen species
Sumbayev, V. V., & Yasinska, I. M. (2007) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.2007.01919.x · Cited by 26 · see citing works
Cravatt, B. F., & Kodadek, T. J. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.12.011 · Cited by 25 · see citing works
Activation of porcine heart mitochondrial malate dehydrogenase by zero valence sulfur and rhodanese
Finazzi‐Agrò, A., Mavelli, I., CANNELLA, C., & Federici, G. (1976) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(76)91181-5 · Cited by 23 · see citing works
Electrochemical studies of S-nitrosothiols
Hou, Y., Wang, J., Arias, F., Echegoyen, L. A., & Wang, P. G. (1998) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(98)00563-0 · Cited by 23 · see citing works
Interactive Endogenous Small Molecule (Gaseous) Signaling: Implications for Teratogenesis
Fukuto, J. M., & Collins, M. (2007) · Current Pharmaceutical Design · doi:10.2174/138161207782110525 · Cited by 22 · see citing works
Louit, G., Hanédanian, M., Taran, F., Coffigny, H., Renault, J., & Pin, S. (2008) · The Analyst · doi:10.1039/b813871k · Cited by 22 · see citing works
Catalytic autoxidation of chemical contaminants by hybrid complexes of cobalt(II) phthalocyanine
Hong, A. P., Boyce, S. D., & Hoffmann, M. R. (1989) · Environmental Science & Technology · doi:10.1021/es00063a004 · Cited by 19 · see citing works
Mechanism of reaction of nitrogen dioxide with alkenes in solution
Chatterjee, J., COOMBES, R. G., Barnes, J. R., & Fildes, M. J. (1995) · Journal of the Chemical Society Perkin Transactions 2 · doi:10.1039/p29950001031 · Cited by 18 · see citing works
Sumbayev, V. V., & Yasinska, I. M. (2006) · Free Radical Research · doi:10.1080/10715760600649648 · Cited by 17 · see citing works
Spin trapping of nitrogen dioxide and of radicals generated from nitrous acid
Astolfi, P., Greci, L., & Panagiotaki, M. (2005) · Free Radical Research · doi:10.1080/10715760500045582 · Cited by 17 · see citing works
The reactions of nitrogen dioxide with dienes
Claridge, R. P., Deeming, A. J., Paul, N., Tocher, D. A., & Ridd, J. H. (1998) · Journal of the Chemical Society Perkin Transactions 1 · doi:10.1039/a806451b · Cited by 15 · see citing works
Gullotti, M., Santagostini, L., Monzani, E., & Casella, L. (2007) · Inorganic Chemistry · doi:10.1021/ic700852c · Cited by 11 · see citing works
Comments on the cis, trans, and cyclic dimers of nitric oxide
Ritchie, J. P. (1983) · The Journal of Physical Chemistry · doi:10.1021/j100237a006 · Cited by 10 · see citing works
Jursic, B. S. (1999) · Journal of Molecular Structure THEOCHEM · doi:10.1016/s0166-1280(99)00047-0 · Cited by 8 · see citing works
Flagged first, then by citations
Research works printed but not linked: 5
- [10]Sawyer DT Oxygen Chemistry 1991 Oxford University Press New York
- [33]Que L, Jr. Bertini I Gray HB Stiefel EI Valentine JS Dioxyen Activating Enzymes Biological Inorganic Chemistry, Structure and Reactivity 2007 388 413 University Science Books Sausalito, CA. Chapter XI.5
- [99]Richter-Addo GB Legzdins P Metal Nitrosyls 1992 Oxford University Press New York
- [112]Pearson RG Sobel H Songstad J Nucleophilic reactivity constants toward methyl iodide and trans-[Pt(py)2Cl2]. J. Am. Chem. Soc 1968 90 319 326
- [132]March J In Advanced Organic Chemistry 1992 351 352 Wiley New York 4th ed.
Cited by
Sorted by citations
13 reasons why the brain is susceptible to oxidative stress
Cobley, J. N., Fiorello, M. L., & Bailey, D. M. (2018) · Redox Biology · doi:10.1016/j.redox.2018.01.008 · Cited by 1,215 · see citing works
Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling
Ida, T., Sawa, T., Ihara, H., Tsuchiya, Y., Watanabe, Y., Kumagai, Y., Suematsu, M., Motohashi, H., Fujii, S., Matsunaga, T., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321232111 · Cited by 934 · see citing works
Surface Structure-Dependent Molecular Oxygen Activation of BiOCl Single-Crystalline Nanosheets
Zhao, K., Zhang, L., Wang, J., Li, Q., He, W., & Yin, J. J. (2013) · Journal of the American Chemical Society · doi:10.1021/ja4092903 · Cited by 655 · see citing works
Physiological roles of hydrogen sulfide in mammalian cells, tissues, and organs
Cirino, G., Szabó, C., & Papapetropoulos, A. (2022) · Physiological Reviews · doi:10.1152/physrev.00028.2021 · Cited by 568 · see citing works
Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics
Akaike, T., Ida, T., Wei, F., Nishida, M., Kumagai, Y., Alam, M. M., Ihara, H., Sawa, T., Matsunaga, T., Kasamatsu, S., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01311-y · Cited by 546 · see citing works
Fluorescent small organic probes for biosensing
Tian, X., Murfin, L. C., Wu, L., Lewis, S. E., & James, T. D. (2021) · Chemical Science · doi:10.1039/d0sc06928k · Cited by 528 · see citing works
Ono, K., Akaike, T., Sawa, T., Kumagai, Y., Wink, D. A., Tantillo, D. J., Hobbs, A. J., Nagy, P., Xian, M., Lin, J., et al. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.09.007 · Cited by 422 · see citing works
Cortese-Krott, M. M., Koning, A. M., Kuhnle, G., Nagy, P., Bianco, C. L., Pasch, A., Wink, D. A., Fukuto, J. M., Jackson, A. A., van Goor, H., et al. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7083 · Cited by 363 · see citing works
Hydrogen sulfide (H 2 S) releasing agents: chemistry and biological applications
Zhao, Y., Biggs, T. D., & Xian, M. (2014) · Chemical Communications · doi:10.1039/c4cc00968a · Cited by 356 · see citing works
Chemical foundations of hydrogen sulfide biology
Li, Q., & Lancaster, J. R. (2013) · Nitric Oxide · doi:10.1016/j.niox.2013.07.001 · Cited by 334 · see citing works
S -Sulfhydration: A Cysteine Posttranslational Modification in Plant Systems
Aroca, Á., Serna, A., Gotor, C., & Romero, L. C. (2015) · PLANT PHYSIOLOGY · doi:10.1104/pp.15.00009 · Cited by 326 · see citing works
Chen, W., Pacheco, A., Takano, Y., Day, J. J., Hanaoka, K., & Xian, M. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201604892 · Cited by 294 · see citing works
Shandilya, S., Kumar, S., Jha, N. K., Kesari, K. K., & Ruokolainen, J. (2021) · Journal of Advanced Research · doi:10.1016/j.jare.2021.09.005 · Cited by 300 · see citing works
Cortese-Krott, M. M., Kuhnle, G., Dyson, A., Fernandez, B. O., Grman, M., DuMond, J. F., Barrow, M. P., McLeod, G. S., Nakagawa, H., Ondriaš, K., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1509277112 · Cited by 289 · see citing works
Biological nitric oxide signalling: chemistry and terminology
Heinrich, T. A., da Silva, R. S., Miranda, K. M., Switzer, C., Wink, D. A., & Fukuto, J. M. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12217 · Cited by 287 · see citing works
Antioxidants from Plants Protect against Skin Photoaging
Petruk, G., Del Giudice, R., Rigano, M. M., & Monti, D. M. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1454936 · Cited by 283 · see citing works
Lehnert, N., Kim, E., Dong, H. T., Harland, J. B., Hunt, A. P., Manickas, E. C., Oakley, K. M., Pham, J., Reed, G. C., & Alfaro, V. S. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00253 · Cited by 277 · see citing works
pH-Controlled Hydrogen Sulfide Release for Myocardial Ischemia-Reperfusion Injury
Kang, J., Li, Z., Organ, C. L., Park, C., Yang, C., Pacheco, A., Wang, D., Lefer, D. J., & Xian, M. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b01373 · Cited by 274 · see citing works
Peng, B., Chen, W., Liu, C., Rosser, E. W., Pacheco, A., Zhao, Y., Aguilar, H. C., & Xian, M. (2013) · Chemistry - A European Journal · doi:10.1002/chem.201303757 · Cited by 258 · see citing works
Nitric oxide and hydrogen sulfide in plants: which comes first?
Corpas, F. J., González‐Gordo, S., Cañas, A., & Palma, J. M. (2019) · Journal of Experimental Botany · doi:10.1093/jxb/erz031 · Cited by 253 · see citing works
Novel lead structures and activation mechanisms for CO ‐releasing molecules ( CORMs )
Schatzschneider, U. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12688 · Cited by 251 · see citing works
Biological signaling by carbon monoxide and carbon monoxide-releasing molecules
Motterlini, R., & Foresti, R. (2017) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00360.2016 · Cited by 247 · see citing works
Liu, C., Chen, W., Shi, W. S., Peng, B., Zhao, Y., Ma, H., & Xian, M. (2014) · Journal of the American Chemical Society · doi:10.1021/ja502968x · Cited by 236 · see citing works
A Luminescent and Biocompatible PhotoCORM
Pierri, A. E., Pallaoro, A., Wu, G. X., & Ford, P. C. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3084434 · Cited by 214 · see citing works
Biological chemistry of hydrogen sulfide and persulfides
Cuevasanta, E., Möller, M. N., & Álvarez, B. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.09.018 · Cited by 202 · see citing works
Shimizu, T., Huang, D., Fang, Y., Stráňava, M., Bartošová, M., Fojtíková, V., & Martínková, M. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00018 · Cited by 196 · see citing works
Enhanced activation of molecular oxygen and degradation of tetracycline over Cu-S4 atomic clusters
Li, H., Sun, S., Ji, H., Liu, W., & Shen, Z. (2020) · Applied Catalysis B: Environmental · doi:10.1016/j.apcatb.2020.118966 · Cited by 188 · see citing works
Koch, C. D., Gladwin, M. T., Freeman, B. A., Lundberg, J. O., Weitzberg, E., & Morris, A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.12.015 · Cited by 186 · see citing works
Self-citationThe interplay between autophagy and ROS in tumorigenesis
Kongara, S., & Karantza, V. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00171 · Cited by 182 · see citing works
Hydrogen sulfide, an enhancer of vascular nitric oxide signaling: mechanisms and implications
Szabó, C. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00282.2016 · Cited by 179 · see citing works
Antioxidant and Cell‐Signaling Functions of Hydrogen Sulfide in the Central Nervous System
Shefa, U., Kim, M., Jeong, N. Y., & Jung, J. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1873962 · Cited by 176 · see citing works
Zhao, Y., Bhushan, S., Yang, C., Otsuka, H., Stein, J. D., Pacheco, A., Peng, B., Devarie‐Baez, N. O., Aguilar, H. C., Lefer, D. J., et al. (2013) · ACS Chemical Biology · doi:10.1021/cb400090d · Cited by 170 · see citing works
Chemiluminescent probes for imaging H 2 S in living animals
Cao, J., Lopez, R., Thacker, J. M., Moon, J. Y., Jiang, C., Morris, S. N. S., Bauer, J. H., Tao, P., Mason, R. P., & Lippert, A. R. (2015) · Chemical Science · doi:10.1039/c4sc03516j · Cited by 168 · see citing works
Hydrogen Sulfide Biochemistry and Interplay with Other Gaseous Mediators in Mammalian Physiology
Giuffrè, A., & Vicente, J. B. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/6290931 · Cited by 166 · see citing works
Nitrite and nitrate chemical biology and signalling
DeMartino, A. W., Kim‐Shapiro, D. B., Patel, R. P., & Gladwin, M. T. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14484 · Cited by 156 · see citing works
Cortese-Krott, M. M., Fernandez, B. O., Santos, J. L. T., Mergia, E., Grman, M., Nagy, P., Kelm, M., Butler, A., & Feelisch, M. (2014) · Redox Biology · doi:10.1016/j.redox.2013.12.031 · Cited by 153 · see citing works
Interaction of Hydrogen Sulfide with Nitric Oxide in the Cardiovascular System
Nagpure, B. V., & Bian, J. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/6904327 · Cited by 145 · see citing works
Hydrogen Sulfide as an Oxygen Sensor
Olson, K. R. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2014.5930 · Cited by 144 · see citing works
Hydrogen Sulfide: From a Toxic Molecule to a Key Molecule of Cell Life
Aroca, Á., Gotor, C., Bassham, D. C., & Romero, L. C. (2020) · Antioxidants · doi:10.3390/antiox9070621 · Cited by 144 · see citing works
Jurcău, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111847 · Cited by 150 · see citing works
Light-Induced Hydrogen Sulfide Release from “Caged” gem-Dithiols
Devarie‐Baez, N. O., Bagdon, P. E., Peng, B., Zhao, Y., Park, C., & Xian, M. (2013) · Organic Letters · doi:10.1021/ol401118k · Cited by 141 · see citing works
Nitric Oxide Releasing Materials Triggered by Near-Infrared Excitation Through Tissue Filters
Burks, P. T., Garcia, J. V., Gonzalezirias, R., Tillman, J. T., Niu, M., Mikhailovsky, A. A., Zhang, J., Zhang, F., & Ford, P. C. (2013) · Journal of the American Chemical Society · doi:10.1021/ja408516w · Cited by 138 · see citing works
H2S and polysulfide metabolism: Conventional and unconventional pathways
Olson, K. R. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.12.010 · Cited by 134 · see citing works
Nitric oxide and hydrogen sulfide crosstalk during heavy metal stress in plants
Shivaraj, S. M., Vats, S., Bhat, J. A., Dhakte, P., Goyal, V., Khatri, P., Kumawat, S., Singh, A. K., Prasad, M., Sonah, H., et al. (2019) · Physiologia Plantarum · doi:10.1111/ppl.13028 · Cited by 129 · see citing works
PhotoCORMs: CO release moves into the visible
Wright, M. A., & Wright, J. A. (2016) · Dalton Transactions · doi:10.1039/c5dt04849d · Cited by 129 · see citing works
Kinetic Insights into Hydrogen Sulfide Delivery from Caged-Carbonyl Sulfide Isomeric Donor Platforms
Zhao, Y., Henthorn, H. A., & Pluth, M. D. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b09527 · Cited by 123 · see citing works
Fukuto, J. M., Cisneros, C. J., & Kinkade, R. L. (2012) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2012.08.027 · Cited by 118 · see citing works
Yamasaki, H., & Cohen, M. F. (2016) · Nitric Oxide · doi:10.1016/j.niox.2016.04.002 · Cited by 115 · see citing works
Carbon disulfide. Just toxic or also bioregulatory and/or therapeutic?
DeMartino, A. W., Zigler, D. F., Fukuto, J. M., & Ford, P. C. (2016) · Chemical Society Reviews · doi:10.1039/c6cs00585c · Cited by 115 · see citing works
On the chemical biology of the nitrite/sulfide interaction
Cortese-Krott, M. M., Fernandez, B. O., Kelm, M., Butler, A. R., & Feelisch, M. (2015) · Nitric Oxide · doi:10.1016/j.niox.2014.12.009 · Cited by 115 · see citing works
CO-releasing Metal Carbonyl Compounds as Antimicrobial Agents in the Post-antibiotic Era
Wareham, L. K., Poole, R. K., & Tinajero‐Trejo, M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.642926 · Cited by 114 · see citing works
Miller, T. W., Kaur, S., Ivins-O'Keefe, K., & Roberts, D. D. (2013) · Matrix Biology · doi:10.1016/j.matbio.2013.02.009 · Cited by 109 · see citing works
Zhu, T., Ren, N., Liu, X., Dong, Y., Wang, R., Gao, J., Sun, J., Zhu, Y., Wang, L., Fan, C., et al. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202015650 · Cited by 106 · see citing works
Millikin, R. J., Bianco, C. L., White, C. J., Saund, S. S., Henriquez, S., Alfaro, V. S., Akaike, T., Kumagai, Y., Soeda, S., Toscano, J. P., et al. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.05.013 · Cited by 106 · see citing works
Hydrogen Sulfide and Persulfides Oxidation by Biologically Relevant Oxidizing Species
Benchoam, D., Cuevasanta, E., Möller, M. N., & Álvarez, B. (2019) · Antioxidants · doi:10.3390/antiox8020048 · Cited by 105 · see citing works
Potential biological chemistry of hydrogen sulfide (H2S) with the nitrogen oxides
Bruce King, S. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.11.005 · Cited by 103 · see citing works
Han, Q., Mou, Z., Wang, H., Tang, X., Dong, Z., Wang, L., Dong, X. Z., & Liu, W. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b01391 · Cited by 102 · see citing works
Fluorescent Organic Small Molecule Probes for Bioimaging and Detection Applications
Yang, Y., Gao, F., Wang, Y., Li, H., Zhang, J., Sun, Z., & Jiang, Y. (2022) · Molecules · doi:10.3390/molecules27238421 · Cited by 102 · see citing works
Hydrogen sulfide, nitric oxide, and neurodegenerative disorders
Panthi, S., Manandhar, S., & Gautam, K. (2018) · Translational Neurodegeneration · doi:10.1186/s40035-018-0108-x · Cited by 100 · see citing works
Nitric oxide and hydrogen sulfide: the gasotransmitter paradigm of the vascular system
Cirino, G., Vellecco, V., & Bucci, M. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13815 · Cited by 98 · see citing works
The solution chemistry of nitric oxide and other reactive nitrogen species
Ford, P. C., & Miranda, K. M. (2020) · Nitric Oxide · doi:10.1016/j.niox.2020.07.004 · Cited by 100 · see citing works
Activatable Probes for Ratiometric Imaging of Endogenous Biomarkers In Vivo
Fu, Q., Yang, X. P., Wang, M., Zhu, K., Wang, Y., & Song, J. (2024) · ACS Nano · doi:10.1021/acsnano.3c10659 · Cited by 97 · see citing works
Molecular oxygen activation: Innovative techniques for environmental remediation.
Zhou, L., Liu, Y., Shi, H., Qing, Y., Chen, C., Shen, L.-G., Zhou, M.-Z., Li, B.-S., & Lin, H. (2023) · Water Research · doi:10.1016/j.watres.2023.121075 · Cited by 90 · see citing works
Exercise redox biochemistry: Conceptual, methodological and technical recommendations
Cobley, J. N., Close, G. L., Bailey, D. M., & Davison, G. W. (2017) · Redox Biology · doi:10.1016/j.redox.2017.03.022 · Cited by 96 · see citing works
Marhenke, J., Trevino, K. M., & Works, C. (2015) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2015.02.017 · Cited by 95 · see citing works
Investigating the Role and Scope of Catalysts in Inverse Vulcanization
Dodd, L. J., Omar, Ö. H., Wu, X., & Hasell, T. (2021) · ACS Catalysis · doi:10.1021/acscatal.0c05010 · Cited by 94 · 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
Zhao, Y., Cerda, M. M., & Pluth, M. D. (2018) · Chemical Science · doi:10.1039/c8sc05200j · Cited by 93 · see citing works
S-sulfhydration as a cellular redox regulation
Iciek, M., Kowalczyk‐Pachel, D., Bilska‐Wilkosz, A., Kwiecień, I., Górny, M., & Włodek, L. B. (2015) · Bioscience Reports · doi:10.1042/bsr20150147 · Cited by 92 · see citing works
Design, Synthesis, and Cardioprotective Effects of N -Mercapto-Based Hydrogen Sulfide Donors
Zhao, Y., Yang, C., Organ, C. L., Li, Z., Bhushan, S., Otsuka, H., Pacheco, A., Kang, J., Aguilar, H. C., Lefer, D. J., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01033 · Cited by 91 · see citing works
Liu, H., & Xue, S. (2021) · Plant Communications · doi:10.1016/j.xplc.2021.100179 · Cited by 91 · see citing works
9-Fluorenylmethyl (Fm) Disulfides: Biomimetic Precursors for Persulfides
Park, C., Johnson, B. A., Duan, J., Park, J.-J., Day, J. J., Gang, D. R., Qian, W., & Xian, M. (2016) · Organic Letters · doi:10.1021/acs.orglett.5b03557 · Cited by 89 · see citing works
Fang, Y., Chen, W., Shi, W. S., Li, H., Xian, M., & Ma, H. (2017) · Chemical Communications · doi:10.1039/c7cc04093h · Cited by 88 · see citing works
Regulation of mitochondrial function and energetics by reactive nitrogen oxides
Larsen, F. J., Schiffer, T. A., Weitzberg, E., & Lundberg, J. O. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.08.580 · Cited by 87 · see citing works
Detection of Nitric Oxide and Nitroxyl with Benzoresorufin-Based Fluorescent Sensors
Apfel, U., Buccella, D., Wilson, J. J., & Lippard, S. J. (2013) · Inorganic Chemistry · doi:10.1021/ic302793w · Cited by 87 · see citing works
Pelegrino, M. T., Lima, B. D. A., Nascimento, M. H. M., Lombello, C. B., Brocchi, M., & Seabra, A. B. (2018) · Polymers · doi:10.3390/polym10040452 · Cited by 86 · see citing works
Mechanisms underlying blood pressure reduction by dietary inorganic nitrate
Carlström, M., Lundberg, J. O., & Weitzberg, E. (2018) · Acta Physiologica · doi:10.1111/apha.13080 · Cited by 86 · see citing works
Recent advances in the chemical biology of nitroxyl (HNO) detection and generation
Miao, Z., & King, S. B. (2016) · Nitric Oxide · doi:10.1016/j.niox.2016.04.006 · Cited by 85 · see citing works
Umezawa, K., Kamiya, M., & Urano, Y. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201804309 · Cited by 83 · see citing works
Gasotransmitter Heterocellular Signaling
Kolluru, G. K., Shen, X., Yuan, S. S., & Kevil, C. G. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6909 · Cited by 83 · see citing works
Carbon Monoxide as a Potential Therapeutic Agent: A Molecular Analysis of Its Safety Profiles
Bansal, S., Liu, D., Mao, Q., Bauer, N., & Wang, B. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00823 · Cited by 81 · see citing works
The chemical biology of hydropersulfides (RSSH): Chemical stability, reactivity and redox roles
Saund, S. S., Alfaro, V. S., Henriquez, S., Nguyen, Q. N. N., Bianco, C. L., Soeda, S., Millikin, R. J., White, C. J., Le, H. H., Ono, K., et al. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.10.016 · Cited by 80 · see citing works
H2S Donors and Their Use in Medicinal Chemistry
Magli, E., Perissutti, E., Santagada, V., Caliendo, G., Corvino, A., Esposito, G., Esposito, G., Fiorino, F., Migliaccio, M., Scognamiglio, A., et al. (2021) · Biomolecules · doi:10.3390/biom11121899 · Cited by 78 · see citing works
Contribution of NRF2 to sulfur metabolism and mitochondrial activity
Alam, M. M., Kishino, A., Sung, E., Sekine, H., Abe, T., Murakami, S., Akaike, T., & Motohashi, H. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102624 · Cited by 72 · see citing works
Cortese-Krott, M. M., Butler, A. R., Woollins, J. D., & Feelisch, M. (2016) · Dalton Transactions · doi:10.1039/c5dt05034k · Cited by 70 · see citing works
Light triggered uncaging of hydrogen sulfide (H 2 S) with real-time monitoring
Venkatesh, Y., Das, J., Chaudhuri, A., Karmakar, A., Maiti, T. K., & Singh, N. D. P. (2018) · Chemical Communications · doi:10.1039/c8cc01172a · Cited by 69 · see citing works
Visible Light-Activated PhotoCORMs
Kottelat, E., & Zobi, F. (2017) · Inorganics · doi:10.3390/inorganics5020024 · Cited by 68 · see citing works
Interactions of reactive sulfur species with metalloproteins
Domán, A., Dóka, É., Garai, D., Bogdándi, V., Balla, G., Balla, J., & Nagy, P. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102617 · Cited by 67 · see citing works
Huang, M., & Li, J. (2019) · Acta Physiologica · doi:10.1111/apha.13351 · Cited by 67 · see citing works
Ex Tenebris Lux: Illuminating Reactive Oxygen and Nitrogen Species with Small Molecule Probes
Cabello, M. C., Chen, G., Melville, M. J., Osman, R., Kumar, G., Domaille, D. W., & Lippert, A. R. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00892 · Cited by 67 · see citing works
Myoglobin functions in the heart
Hendgen-Cotta, U. B., Kelm, M., & Rassaf, T. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.05.005 · Cited by 67 · see citing works
Synthesis and evaluation of phosphorodithioate-based hydrogen sulfide donors
Park, C., Zhao, Y., Zhu, Z., Pacheco, A., Peng, B., Devarie‐Baez, N. O., Bagdon, P. E., Zhang, H., & Xian, M. (2013) · Molecular BioSystems · doi:10.1039/c3mb70145j · Cited by 65 · see citing works
Enzymatic Regulation and Biological Functions of Reactive Cysteine Persulfides and Polysulfides
Sawa, T., Motohashi, H., Ihara, H., & Akaike, T. (2020) · Biomolecules · doi:10.3390/biom10091245 · Cited by 65 · see citing works
Paul, S., & Roychoudhury, A. (2019) · Physiologia Plantarum · doi:10.1111/ppl.13021 · Cited by 64 · see citing works
Mao, Q., Kawaguchi, A. T., Mizobata, S., Motterlini, R., Foresti, R., & Kitagishi, H. (2021) · Communications Biology · doi:10.1038/s42003-021-01880-1 · Cited by 64 · see citing works
Laureano‐Marín, A. M., Moreno, I., Romero, L. C., & Gotor, C. (2016) · PLANT PHYSIOLOGY · doi:10.1104/pp.16.00110 · Cited by 64 · see citing works
Wareham, L. K., Southam, H. M., & Poole, R. K. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170311 · Cited by 65 · see citing works
Nitric Oxide and Hydrogen Sulfide Regulation of Ischemic Vascular Growth and Remodeling
Rajendran, S., Shen, X., Glawe, J. D., Kolluru, G. K., & Kevil, C. G. (2019) · Comprehensive physiology · doi:10.1002/cphy.c180026 · Cited by 68 · see citing works
Objective Pain Assessment: a Key for the Management of Chronic Pain
Xu, X., & Huang, Y. (2020) · F1000Research · doi:10.12688/f1000research.20441.1 · Cited by 63 · see citing works
Zhao, Q., Yin, C., Kang, J., Wen, Y., & Huo, F. (2018) · Dyes and Pigments · doi:10.1016/j.dyepig.2018.06.029 · Cited by 62 · see citing works
- Authors
- Fukuto, J. M., Carrington, S. J., Tantillo, D. J., Harrison, J. G., Ignarro, L. J., Freeman, B. A., Chen, A., & Wink, D. A.
- Affiliations
- Sonoma State University (US)
- University of California, Davis (US)
- University of California, Los Angeles (US)
- Department of Pharmacology and Chemical Biology, University of Pittsburgh, E13s40 Thomas E. Starzl Biomedical Science Tower, Lothrop Street, Pittsburgh, Pennsylvania 15261, United States
- National Institutes of Health (US)
- Corresponding author
- Fukuto, Jon M.
- Venue
- Chemical Research in Toxicology
- Publisher
- American Chemical Society (ACS)
- Published
- 2012-02-09
- Volume
- 25
- Issue
- 4
- Pages
- 769-793
- ISSN
- 0893-228X (ISSN-L)
- 1520-5010
- PMC
- PMC4061765
- OpenAlex
- W2040148126
- Cited by
- 389
- References
- 180
- Citations by year
- 2026: 11 · 2025: 25 · 2024: 21 · 2023: 17 · 2022: 26 · 2021: 36 · 2020: 33 · 2019: 39 · 2018: 38 · 2017: 35 · 2016: 35 · 2015: 22 · 2014: 21 · 2013: 23 · 2012: 7
- FWCI
- 2.55
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Chemical Research in Toxicology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL064937, R37HL058115, R01HL058115)
- 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 › Biochemistry › Sulfur Compounds in Biology
- Keywords
- small molecule signaling, nitrogen oxides, nitric oxide, carbon monoxide, hydrogen sulfide, molecular oxygen, reactive oxygen species, gasotransmitters, endogenous signaling molecules, gas-gas interactions
- MeSH terms
- Carbon Monoxide, Hydrogen Sulfide, Myoglobin, Nitrogen Oxides, Oxygen, Signal Transduction, Reactive Oxygen Species, Reactive Nitrogen Species, Hypoxia-Inducible Factor 1, alpha Subunit
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
