Chemical Characterization of the Smallest S -Nitrosothiol, HSNO; Cellular Cross-talk of H 2 S and S -Nitrosothiols
Open accessAbstract
Dihydrogen sulfide recently emerged as a biological signaling molecule with important physiological roles and significant pharmacological potential. Chemically plausible explanations for its mechanisms of action have remained elusive, however. Here, we report that H(2)S reacts with S-nitrosothiols to form thionitrous acid (HSNO), the smallest S-nitrosothiol. These results demonstrate that, at the cellular level, HSNO can be metabolized to afford NO(+), NO, and NO(-) species, all of which have distinct physiological consequences of their own. We further show that HSNO can freely diffuse through membranes, facilitating transnitrosation of proteins such as hemoglobin. The data presented in this study explain some of the physiological effects ascribed to H(2)S, but, more broadly, introduce a new signaling molecule, HSNO, and suggest that it may play a key role in cellular redox regulation.
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?
S-nitrosothiols rapidly react with sulfide in vitro, leading to formation of S/N-hybrid species including thionitrite and nitrosopersulfide.
“the latter have been shown to rapidly react with sulfide in vitro, leading to formation of S/N-hybrid species including thionitrite (SNO -) and nitrosopersulfide (SSNO -).”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [18]
Further products of the reaction might be nitroxyl and nitrous oxide (N2O).
“As expected, by considering the chemistry of the reaction (Fig. 2), further products of this reaction might be nitroxyl as proposed previously [16,18,30], and nitrous oxide (N2O).”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [18]
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
Density-functional thermochemistry. III. The role of exact exchange
Becke, A. D. (1993) · The Journal of Chemical Physics · doi:10.1063/1.464913 · Cited by 103,767 · see citing works
Lee, C., Yang, W., & Parr, R. G. (1988) · Physical Review B · doi:10.1103/physrevb.37.785 · Cited by 100,874 · see citing works
Dunning, T. H. (1989) · The Journal of Chemical Physics · doi:10.1063/1.456153 · Cited by 31,693 · see citing works
Vosko, S. H., Wilk, L., & Nusair, M. (1980) · Canadian Journal of Physics · doi:10.1139/p80-159 · Cited by 20,807 · see citing works
Electron affinities of the first-row atoms revisited. Systematic basis sets and wave functions
Kendall, R. A., Dunning, T. H., & Harrison, R. J. (1992) · The Journal of Chemical Physics · doi:10.1063/1.462569 · Cited by 15,736 · see citing works
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
Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
Palmer, R. M. J., Ferrige, A. G., & Moncada, S. (1987) · Nature · doi:10.1038/327524a0 · Cited by 10,704 · see citing works
Woon, D. E., & Dunning, T. H. (1993) · The Journal of Chemical Physics · doi:10.1063/1.464303 · Cited by 9,612 · see citing works
Biochemistry of nitric oxide and its redox-activated forms
Stamler, J. S., Singel, D. J., & Loscalzo, J. (1992) · Science · doi:10.1126/science.1281928 · Cited by 2,744 · see citing works
Yang, G., Wu, L., Jiang, B., Yang, W., Qi, J., Cao, K., Meng, Q., Mustafa, A. K., Mu, W., Zhang, S., et al. (2008) · Science · doi:10.1126/science.1162667 · Cited by 2,310 · see citing works
S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
Jia, L., Bonaventura, C., Bonaventura, J., & Stamler, J. S. (1996) · Nature · doi:10.1038/380221a0 · Cited by 1,586 · see citing works
Hydrogen Sulfide and Cell Signaling
Li, L., Rose, P. E., & Moore, P. K. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010510-100505 · Cited by 1,289 · see citing works
Protein S-nitrosylation in health and disease: a current perspective
Foster, M. W., Hess, D. T., & Stamler, J. S. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.06.007 · Cited by 752 · see citing works
Methods in Nitric Oxide Research
Young, J. (1997) · Physiological Measurement · doi:10.1088/0967-3334/18/1/008 · Cited by 750 · see citing works
Redox Biochemistry of Hydrogen Sulfide
Kabil, Ö., & Banerjee, R. V. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.128363 · Cited by 745 · see citing works
Hydrogen Sulfide Mediates Cardioprotection Through Nrf2 Signaling
Calvert, J. W., Jha, S. K., Gundewar, S., Elrod, J. W., Ramachandran, A., Pattillo, C. B., Kevil, C. G., & Lefer, D. J. (2009) · Circulation Research · doi:10.1161/circresaha.109.199919 · Cited by 722 · see citing works
Hydrogen Sulfide as Endothelium-Derived Hyperpolarizing Factor Sulfhydrates Potassium Channels
Mustafa, A. K., Sikka, G., Gazi, S. K., Steppan, J., Jung, S. M., Bhunia, A. K., Barodka, V. M., Gazi, F. K., Barrow, R. K., Wang, R., et al. (2011) · Circulation Research · doi:10.1161/circresaha.111.240242 · Cited by 619 · see citing works
Arnelle, D. R., & Stamler, J. S. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1231 · Cited by 604 · see citing works
Mechanism of Nitric Oxide Release from S-Nitrosothiols
Singh, R. J., Hogg, N., Joseph, J., & Kalyanaraman, B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.31.18596 · Cited by 600 · see citing works
Regulated Protein Denitrosylation by Cytosolic and Mitochondrial Thioredoxins
Benhar, M., Forrester, M. T., Hess, D. T., & Stamler, J. S. (2008) · Science · doi:10.1126/science.1158265 · Cited by 548 · see citing works
Mechanistic aspects of the reactions of nitric oxide with transition-metal complexes
Ford, P. C., & Lorkovic, I. M. (2002) · Chemical Reviews · doi:10.1021/cr0000271 · Cited by 525 · see citing works
H2S-induced vasorelaxation and underlying cellular and molecular mechanisms
Zhao, W., & Wang, R. T. (2002) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00013.2002 · Cited by 505 · see citing works
Chemistry of Nitric Oxide Relevant to Biology
McCleverty, J. A. (2004) · Chemical Reviews · doi:10.1021/cr020623q · Cited by 504 · see citing works
Hydrogen sulfide as a gasotransmitter
Gadalla, M. M., & Snyder, S. H. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06580.x · Cited by 499 · see citing works
<i>S</i> -Nitrosylation in Cardiovascular Signaling
Lima, B., Forrester, M. T., Hess, D. T., & Stamler, J. S. (2010) · Circulation Research · doi:10.1161/circresaha.109.207381 · Cited by 490 · see citing works
Singel, D. J., & Stamler, J. S. (2005) · Annual Review of Physiology · doi:10.1146/annurev.physiol.67.060603.090918 · Cited by 481 · see citing works
Making and working with hydrogen sulfide
Hughes, M., Centelles, M. N., & Moore, K. P. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.09.018 · Cited by 454 · see citing works
The Biochemistry and Physiology of S-Nitrosothiols
Hogg, N. (2002) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.42.092501.104328 · Cited by 412 · see citing works
Regulation by S-Nitrosylation of Protein Post-translational Modification
Hess, D. T., & Stamler, J. S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.285742 · Cited by 385 · see citing works
Whiteman, M., Li, L., Kostetski, I., Chu, S. H., Siau, J. L., Bhatia, M., & Moore, P. K. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.02.154 · Cited by 377 · see citing works
Cysteine regulation of protein function – as exemplified by NMDA-receptor modulation
Lipton, S. A., Choi, Y.-B., Takahashi, H., Zhang, D., Li, W., Godzik, A., & Bankston, L. A. (2002) · Trends in Neurosciences · doi:10.1016/s0166-2236(02)02245-2 · Cited by 375 · see citing works
The basic chemistry of nitrogen monoxide and peroxynitrite
Koppenol, W. H. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00093-8 · Cited by 338 · see citing works
The chemistry of the <i>S</i> -nitrosoglutathione/glutathione system
Singh, S. P., Wishnok, J. S., Keshive, M., Deen, W. M., & Tannenbaum, S. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14428 · Cited by 336 · see citing works
Li, L., Hsu, A., & Moore, P. K. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.05.005 · Cited by 331 · see citing works
Measurement of plasma hydrogen sulfide in vivo and in vitro
Shen, X., Pattillo, C. B., Pardue, S., Bir, S. C., Wang, R., & Kevil, C. G. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.01.025 · Cited by 325 · see citing works
Direct Detection of Nitroxyl in Aqueous Solution Using a Tripodal Copper(II) BODIPY Complex
Rosenthal, J., & Lippard, S. J. (2010) · Journal of the American Chemical Society · doi:10.1021/ja909148v · Cited by 267 · see citing works
Nitric Oxide in Cell Survival: A Janus Molecule
Calabrese, V., Cornelius, C., Rizzarelli, E., Owen, J. B., Dinkova‐Kostova, A. T., & Butterfield, D. A. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2721 · Cited by 195 · see citing works
High Turnover Rates for Hydrogen Sulfide Allow for Rapid Regulation of Its Tissue Concentrations
Vitvitsky, V., Kabil, Ö., & Banerjee, R. V. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4310 · Cited by 191 · see citing works
Polynitrosylated proteins: characterization, bioactivity, and functional consequences.
Simon, D. I., Mullins, M. E., Jia, L., Gaston, B. M., Singel, D. J., & Stamler, J. S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.10.4736 · Cited by 190 · see citing works
Planchet, É. (2006) · Journal of Experimental Botany · doi:10.1093/jxb/erl070 · Cited by 189 · see citing works
Decomposition ofS-Nitrosoglutathione in the Presence of Copper Ions and Glutathione
Gorren, A. C. F., Schrammel, A., Schmidt, K., & Mayer, B. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0247 · Cited by 181 · see citing works
The mechanism of transmembrane S -nitrosothiol transport
Zhang, Y., & Hogg, N. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401167101 · Cited by 172 · see citing works
Keszler, Á., Zhang, Y., & Hogg, N. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.10.026 · Cited by 157 · see citing works
Meyer, D. J., Kramer, H., Özer, N., Coles, B., & KETTERER, B. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00429-3 · Cited by 156 · see citing works
Nitric oxide activates Nrf2 through S-nitrosylation of Keap1 in PC12 cells
Um, H.-C., Jang, J.-H., Kim, D.-H., Lee, C., & Surh, Y.-J. (2011) · Nitric Oxide · doi:10.1016/j.niox.2011.06.001 · Cited by 153 · see citing works
S−N Dissociation Energies of S-Nitrosothiols: On the Origins of Nitrosothiol Decomposition Rates
Bartberger, M. D., Mannion, J. D., Powell, S. C., Stamler, J. S., Houk, K. N., & Toone, E. J. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0109390 · Cited by 137 · see citing works
Hydrogen sulfide interacts with nitric oxide in the heart: possible involvement of nitroxyl
Yong, Q. C., Hu, L.-F., Wang, S., Huang, D., & Bian, J. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq248 · Cited by 133 · see citing works
NITROXYL (HNO): Chemistry, Biochemistry, and Pharmacology
Fukuto, J. M., Switzer, C., Miranda, K. M., & Wink, D. A. (2005) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.45.120403.095959 · Cited by 130 · see citing works
Kawano, T., Zoga, V., Kimura, M., Liang, M.-Y., Wu, H.-E., Gemes, G., McCallum, J. B., Kwok, W., Hogan, Q. H., & Sarantopoulos, C. D. (2009) · Molecular Pain · doi:10.1186/1744-8069-5-12 · Cited by 123 · see citing works
Bazylinski, D. A., & Hollocher, T. C. (1985) · Journal of the American Chemical Society · doi:10.1021/ja00312a031 · Cited by 118 · see citing works
Wang, X., Kettenhofen, N. J., Shiva, S., Hogg, N., & Gladwin, M. T. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.12.032 · Cited by 111 · see citing works
Filipović, M. R., Miljković, J. L., Allgäuer, A., Chaurio, R. A., Shubina, T. E., i, M. H., & Ivanović‐Burmazović, I. (2011) · Biochemical Journal · doi:10.1042/bj20111389 · Cited by 109 · see citing works
Mechanism of Aerobic Decomposition of Angeli's Salt (Sodium Trioxodinitrate) at Physiological pH
Miranda, K. M., Dutton, A. S., Ridnour, L. A., Foreman, C. A., Ford, E., Paolocci, N., Katori, T., Tocchetti, C. G., Mancardi, D., Thomas, D. D., et al. (2004) · Journal of the American Chemical Society · doi:10.1021/ja045480z · Cited by 107 · see citing works
Catalysis of Electron Transfer by Selenocysteine
Nauser, T., Dockheer, S. M., Kissner, R., & Koppenol, W. H. (2006) · Biochemistry · doi:10.1021/bi0602260 · Cited by 105 · see citing works
Nakamura, T., & Lipton, S. A. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3570 · Cited by 104 · see citing works
Generation, Translocation, and Action of Nitric Oxide in Living Systems
Tennyson, A. G., & Lippard, S. J. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.09.009 · Cited by 104 · see citing works
The Specificity of Nitroxyl Chemistry Is Unique Among Nitrogen Oxides in Biological Systems
Flores‐Santana, W., Salmon, D. J., Donzelli, S., Switzer, C., Basudhar, D., Ridnour, L. A., Cheng, R. Y. S., Glynn, S. A., Paolocci, N., Fukuto, J. M., et al. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3841 · Cited by 99 · 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
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
Fukuto, J. M., & Carrington, S. J. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3855 · Cited by 86 · see citing works
Microwave spectrum, structure, and dipole moment of cis-thionylimide
Kirchhoff, W. H. (1969) · Journal of the American Chemical Society · doi:10.1021/ja01038a006 · Cited by 76 · see citing works
Kinetics of reduction of tyrosine phenoxyl radicals by glutathione
Folkes, L. K., Trujillo, M., Bartesaghi, S., Radí, R., & Wardman, P. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.12.006 · Cited by 74 · 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
Stamler, J. S., & Hess, D. T. (2010) · Nature Cell Biology · doi:10.1038/ncb1110-1024 · Cited by 70 · see citing works
Structure and stability of HSNO, the simplest S-nitrosothiol
Timerghazin, Q. K., Peslherbe, G. H., & English, A. M. (2008) · Physical Chemistry Chemical Physics · doi:10.1039/b715025c · Cited by 68 · see citing works
Pulsradiolyse des Schwefelwasserstoffs in wäßriger Lösung
Karmann, W., Meißner, G., & Henglein, A. (1967) · Zeitschrift für Naturforschung B · doi:10.1515/znb-1967-0311 · Cited by 62 · see citing works
PNP-Perthionitrit und PNP-Monothionitrit / PNP-Perthionitrite and PNP-M onothionitrite
Seel, F., Kuhn, R., Simon, G., & Wagner, M. (1985) · Zeitschrift für Naturforschung B · doi:10.1515/znb-1985-1203 · Cited by 59 · see citing works
SNO-ing at the Nociceptive Synapse?
Tegeder, I., Scheving, R., Wittig, I., & Geißlinger, G. (2011) · Pharmacological Reviews · doi:10.1124/pr.110.004200 · Cited by 57 · see citing works
Nonella, M., Huber, J. R., & Ha, T. K. (1987) · The Journal of Physical Chemistry · doi:10.1021/j100304a014 · Cited by 55 · see citing works
Nitrosation, thiols, and hemoglobin: energetics and kinetics
Koppenol, W. H. (2012) · Inorganic Chemistry · doi:10.1021/ic202561f · Cited by 54 · see citing works
Reactivity of sulfur nucleophiles towards S-nitrosothiols
Munro, A. P., & Williams, D. L. H. (2000) · Journal of the Chemical Society Perkin Transactions 2 · doi:10.1039/b004415f · Cited by 53 · see citing works
Sonnenschein, K., de GROOT, H., & Kirsch, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405987200 · Cited by 47 · see citing works
Nitric oxide synthase inhibition abrogates hydrogen sulfide-induced cardioprotection in mice
Sojitra, B., Bulani, Y., Putcha, U. K., Kanwal, A., Gupta, P., Kuncha, M., & Banerjee, S. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-011-1044-6 · Cited by 46 · see citing works
Quiroga, S. L., Almaraz, A. E., Amorebieta, V. T., Perissinotti, L. L., & Olabe, J. A. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201002322 · Cited by 43 · see citing works
Broniowska, K. A., Zhang, Y., & Hogg, N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603248200 · Cited by 37 · see citing works
The transfusion problem: role of aberrant S‐nitrosylation
Reynolds, J. D. H., Hess, D. T., & Stamler, J. S. (2011) · Transfusion · doi:10.1111/j.1537-2995.2011.03097.x · Cited by 37 · see citing works
On the multireference character of S-nitrosothiols: A theoretical study of HSNO
Timerghazin, Q. K., English, A. M., & Peslherbe, G. H. (2008) · Chemical Physics Letters · doi:10.1016/j.cplett.2008.01.062 · Cited by 35 · see citing works
Über die Umsetzung von Sulfiden mit Stickstoffmonoxid in Wäßrigen Lösungen
SEEL, F., & Wagner, M. (1988) · Zeitschrift für anorganische und allgemeine Chemie · doi:10.1002/zaac.19885580118 · Cited by 30 · see citing works
15N NMR and electronic properties of S-nitrosothiols
Wang, K., Hou, Y., Zhang, W., Ksebati, M. B., Xian, M., Cheng, J., & Wang, P. G. (1999) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(99)00499-0 · Cited by 26 · see citing works
The hypothesis of the main role of H2S in coupled sulphide-nitroso signalling pathway
Bertova, A., Čačányiová, S., Kristek, F., Križanová, O., Ondriaš, K., & Tomaskova, Z. S. (2010) · General Physiology and Biophysics · doi:10.4149/gpb_2010_04_402 · Cited by 24 · see citing works
In vitro formation of S‐nitrosohemoglobin in red cells by inducible nitric oxide synthase
Mamone, G., Sannolo, N., Malorni, A., & Ferranti, P. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01527-6 · Cited by 23 · see citing works
S-nitroso-albumin carries a thiol-labile pool of nitric oxide, which causes venodilation in the rat
Orie, N. N., Vallance, P. J., Jones, D. P., & Moore, K. P. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01014.2004 · Cited by 21 · see citing works
Generation and Detection of S-Nitrosothiols
Lindermayr, C., Sell, S., & Durner, J. (2008) · Methods in molecular biology · doi:10.1007/978-1-59745-129-1_15 · Cited by 19 · see citing works
Electronic structures and electronic spectra of the linkage isomers NSO− and SNO−
Chivers, T., da Silva, A. B. F., Treu, O., & Trsic, M. (1987) · Journal of Molecular Structure · doi:10.1016/0022-2860(87)87066-7 · Cited by 10 · see citing works
Flagged first, then by citations
Research works printed but not linked: 7
- Timerghazin Q. K.; English A. M.; Peslherbe G. H. Chem. Phys. Lett. 2008, 454, 24– 29.
- a Nonella M.; Huber J. R.; Ha T.-K. J. Phys. Chem. 1987, 91, 5203– 5209. b Structural isomer of HSNO is known as thionylimide (HNSO). Kirchhoff W. H. J. Am. Chem. Soc. 1969, 91, 20437– 20442.
- Karmann W.; Meissner G.; Henglein A. Z. Naturforsch., B 1967, 22, 273– 282.
- a Becke A. D. In The Challenge of d- and f-electrons: Theory and Computation; Salahub D. R., Zerner M. C., Eds.; American Chemical Society: Washington, DC, 1989; Chapter 12, p 165. b Vosko S. H.; Wilk L.; Nusair M. Can. J. Phys. 1980, 58, 1200. c Lee C.; Yang W.; Parr R. G. Phys. Rev. B 1988, 37, 785. 9944570 d Becke A. D. J. Chem. Phys. 1993, 98, 5648. e Kendall R. A.; Dunning T. H. Jr.; Harrison R. J. J. Chem. Phys. 1992, 96, 6796– 6806. f Woon D. E.; Dunning T. H. Jr. J. Chem. Phys. 1993, 98, 1358– 13571. g Dunning T. H. Jr. J. Chem. Phys. 1989, 90, 1007– 1023.
- a Mills G.; Schmidt K. H.; Matheson M. S.; Meisel D. J. Phys. Chem. 1987, 91, 1590– 96. b Chivers T.; Da Silva A. B. F.; Treu O. Jr.; Trsic M. J. Mol. Struct. 1987, 162, 351– 357.
- Seel F.; Wagner M. Z. Anorg. Allg. Chem. 1988, 558, 189– 192.
- Munro A. P.; Williams L. H. J. Chem. Soc., Perkin Trans. 2 2000, 1794– 1797.
Cited by
Sorted by citations
Chemical Biology of H 2 S Signaling through Persulfidation
Filipović, M. R., Živanović, J., Álvarez, B., & Banerjee, R. V. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00205 · Cited by 1,039 · see citing works
Nitric oxide synthase in innate and adaptive immunity: an update
Bogdan, C. (2015) · Trends in Immunology · doi:10.1016/j.it.2015.01.003 · Cited by 862 · see citing works
Hydrogen sulfide chemical biology: pathophysiological roles and detection
Kolluru, G. K., Shen, X., Bir, S. C., & Kevil, C. G. (2013) · Nitric Oxide · doi:10.1016/j.niox.2013.07.002 · Cited by 480 · see citing works
Enzymology of H 2 S Biogenesis, Decay and Signaling
Kabil, Ö., & Banerjee, R. V. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5339 · Cited by 474 · see citing works
Regulators of the transsulfuration pathway
Sbodio, J. I., Snyder, S. H., & Paul, B. D. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14446 · Cited by 379 · see citing works
Decreased Endogenous Production of Hydrogen Sulfide Accelerates Atherosclerosis
Mani, S., Li, H., Untereiner, A., Wu, L., Yang, G., Austin, R. C., Dickhout, J. G., Lhoták, Š., Meng, Q. H., & Wang, R. (2013) · Circulation · doi:10.1161/circulationaha.113.002208 · Cited by 377 · see citing works
Eberhardt, M. J., Dux, M., Namer, B., Miljković, J. L., Cordasic, N., Will, C., Kichko, T. I., de la Roche, J., Fischer, M. J. M., Suárez, S., et al. (2014) · Nature Communications · doi:10.1038/ncomms5381 · Cited by 379 · 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
Broniowska, K. A., Diers, A. R., & Hogg, N. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.02.004 · Cited by 357 · 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
Aroca, Á., Benito, J. M., Gotor, C., & Romero, L. C. (2017) · Journal of Experimental Botany · doi:10.1093/jxb/erx294 · Cited by 320 · see citing works
The physiological role of hydrogen sulfide and beyond
Kimura, H. (2014) · Nitric Oxide · doi:10.1016/j.niox.2014.01.002 · Cited by 295 · see citing works
Stomberski, C. T., Hess, D. T., & Stamler, J. S. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7403 · Cited by 292 · 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
Detection of Protein S‐Sulfhydration by a Tag‐Switch Technique
Zhang, D., Mačinković, I., Devarie‐Baez, N. O., Pan, J. H., Park, C., Carroll, K. S., Filipović, M. R., & Xian, M. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201305876 · Cited by 289 · see citing works
Physiological role of hydrogen sulfide and polysulfide in the central nervous system
Kimura, H. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.09.003 · Cited by 285 · see citing works
Hydrogen sulfide signaling in mitochondria and disease
Murphy, B., Bhattacharya, R., & Mukherjee, P. (2019) · The FASEB Journal · doi:10.1096/fj.201901304r · Cited by 279 · 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
A timeline of hydrogen sulfide (H2S) research: From environmental toxin to biological mediator
Szabó, C. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.09.010 · Cited by 271 · see citing works
H2S and its role in redox signaling
Kabil, O., Motl, N., & Banerjee, R. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.01.002 · Cited by 240 · see citing works
Wrobel, A. T., Johnstone, T. C., Liang, A. D., Lippard, S. J., & Rivera‐Fuentes, P. (2014) · Journal of the American Chemical Society · doi:10.1021/ja500315x · Cited by 211 · see citing works
Hydrogen sulfide and nitric oxide interactions in inflammation
Faro, M. L. L., Fox, B., Whatmore, J. L., Winyard, P. G., & Whiteman, M. (2014) · Nitric Oxide · doi:10.1016/j.niox.2014.05.014 · Cited by 210 · see citing works
Hydrogen sulfide, a signaling molecule in plant stress responses
Zhang, J., Zhou, M., Zhou, H., Zhao, D., Gotor, C., Romero, L. C., Shen, J., Ge, Z., Zhang, Z., Shen, W., et al. (2020) · Journal of Integrative Plant Biology · doi:10.1111/jipb.13022 · Cited by 208 · see citing works
Persulfidation (S-sulfhydration) and H2S
Filipović, M. R. (2015) · Handbook of experimental pharmacology · doi:10.1007/978-3-319-18144-8_2 · Cited by 210 · 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
Hydrogen sulfide (H2S) signaling in plant development and stress responses
Liu, H., Wang, J., Liu, J., Liu, T., & Xue, S. (2021) · aBIOTECH · doi:10.1007/s42994-021-00035-4 · Cited by 192 · see citing works
Natural Products Containing a Nitrogen–Sulfur Bond
Petkowski, J. J., Bains, W., & Seager, S. (2018) · Journal of Natural Products · doi:10.1021/acs.jnatprod.7b00921 · Cited by 180 · see citing works
Bailey, T. S., & Pluth, M. D. (2013) · Journal of the American Chemical Society · doi:10.1021/ja408909h · Cited by 178 · 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
A tale of two gases: NO and H2S, foes or friends for life?
Kolluru, G. K., Shen, X., & Kevil, C. G. (2013) · Redox Biology · doi:10.1016/j.redox.2013.05.001 · Cited by 168 · see citing works
Reactive sulfur species (RSS): persulfides, polysulfides, potential, and problems
Lau, N., & Pluth, M. D. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.08.012 · Cited by 168 · see citing works
H2S biosynthesis and catabolism: new insights from molecular studies
Rose, P. E., Moore, P. K., & Zhu, Y. Z. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2406-8 · Cited by 165 · 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
Signaling by hydrogen sulfide and cyanide through post-translational modification
Gotor, C., García, I., Aroca, Á., Laureano‐Marín, A. M., Arenas-Alfonseca, L., Jurado-Flores, A., Moreno, I., & Romero, L. C. (2019) · Journal of Experimental Botany · doi:10.1093/jxb/erz225 · Cited by 165 · see citing works
The role of H2S bioavailability in endothelial dysfunction
Wang, R., Szabó, C., Ichinose, F., Ahmed, A., Whiteman, M., & Papapetropoulos, A. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.05.007 · Cited by 159 · see citing works
Functional and Molecular Insights of Hydrogen Sulfide Signaling and Protein Sulfhydration
Sen, N. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.12.015 · Cited by 151 · see citing works
Signaling and stress: The redox landscape in NOS2 biology
Thomas, D. D., Heinecke, J. L., Ridnour, L. A., Cheng, R. Y., Kesarwala, A. H., Switzer, C. H., McVicar, D. W., Roberts, D. D., Glynn, S., Fukuto, J. M., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.002 · Cited by 150 · see citing works
Hydrogen Sulfide and Polysulfides as Biological Mediators
Kimura, H. (2014) · Molecules · doi:10.3390/molecules191016146 · Cited by 150 · 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
Generation of HNO and HSNO from Nitrite by Heme‐Iron‐Catalyzed Metabolism with H<sub>2</sub>S
Miljkovic, J. L., Kenkel, I., Ivanović‐Burmazović, I., & Filipovic, M. R. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201305669 · Cited by 148 · see citing works
Self-citationHydrogen sulfide in pharmacology and medicine – An update
Bełtowski, J. (2015) · Pharmacological Reports · doi:10.1016/j.pharep.2015.01.005 · Cited by 148 · 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
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
Hydrogen sulfide and polysulfides as signaling molecules
Kimura, H. (2015) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.91.131 · Cited by 141 · see citing works
Hydrogen sulfide and nitric oxide interactions in inflammation
Whiteman, M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.021 · Cited by 141 · 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
Mechanistic Chemical Perspective of Hydrogen Sulfide Signaling
Nagy, P. (2015) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2014.11.036 · Cited by 132 · see citing works
Miyamoto, R., Koike, S., Takano, Y., Shibuya, N., Kimura, Y., Hanaoka, K., Urano, Y., Ogasawara, Y., & Kimura, H. (2017) · Scientific Reports · doi:10.1038/srep45995 · Cited by 131 · see citing works
Sulfur as a Signaling Nutrient Through Hydrogen Sulfide
Kabil, Ö., Vitvitsky, V., & Banerjee, R. V. (2014) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071813-105654 · Cited by 127 · see citing works
Filipović, M. R., Eberhardt, M. J., Prokopović, V. Z., Mijušković, A., Oreščanin-Dušić, Z., Reeh, P. W., & Ivanović‐Burmazović, I. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm3012036 · Cited by 125 · see citing works
Regulation of vascular tone homeostasis by NO and H2S: Implications in hypertension
Gheibi, S., Jeddi, S., Kashfi, K., & Ghasemi, A. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.01.017 · Cited by 120 · 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
A New Hope for a Devastating Disease: Hydrogen Sulfide in Parkinson’s Disease
Cao, X., Cao, L., Ding, L., & Bian, J.-S. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0617-0 · Cited by 112 · see citing works
The Reactive Sulfur Species Concept: 15 Years On
Giles, G. I., Nasim, M. J., Ali, W., & Jacob, C. (2017) · Antioxidants · doi:10.3390/antiox6020038 · Cited by 113 · see citing works
The CsoR ‐like sulfurtransferase repressor ( CstR ) is a persulfide sensor in S taphylococcus aureus
Luebke, J. L., Shen, J., Bruce, K. E., Kehl‐Fie, T. E., Peng, H., Skaar, E. P., & Giedroc, D. P. (2014) · Molecular Microbiology · doi:10.1111/mmi.12835 · Cited by 112 · see citing works
Working with “H2S”: Facts and apparent artifacts
Wedmann, R., Bertlein, S., Mačinković, I., Boeltz, S., Miljković, J. L., Munoz, L. E., i, M. H., & Filipović, M. R. (2014) · Nitric Oxide · doi:10.1016/j.niox.2014.06.003 · Cited by 110 · see citing works
Hydrogen sulfide signaling in plant adaptations to adverse conditions: molecular mechanisms
Aroca, Á., Zhang, J., Xie, Y., Romero, L. C., & Gotor, C. (2021) · Journal of Experimental Botany · doi:10.1093/jxb/erab239 · 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
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
Fluorescence chemosensors for hydrogen sulfide detection in biological systems
Guo, Z. H., Chen, G., Zeng, G., Li, Z., Chen, A., Wang, J., & Jiang, L. (2014) · The Analyst · doi:10.1039/c4an01909a · Cited by 102 · see citing works
An Update on Hydrogen Sulfide and Nitric Oxide Interactions in the Cardiovascular System
Wu, D., Hu, Q., & Zhu, D. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/4579140 · Cited by 100 · see citing works
Physiological Roles of Hydrogen Sulfide and Polysulfides
Kimura, H. (2015) · Handbook of experimental pharmacology · doi:10.1007/978-3-319-18144-8_3 · Cited by 99 · see citing works
Signalling by hydrogen sulfide and polysulfides via protein S‐sulfuration
Kimura, H. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14579 · 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
Suárez, S., Neuman, N. I., Muñoz, M., Álvarez, L., Bikiel, D. E., Brondino, C. D., Ivanović‐Burmazović, I., Miljković, J. L., Filipović, M. R., Marti, M. A., et al. (2015) · Journal of the American Chemical Society · doi:10.1021/ja512343w · Cited by 96 · 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
Signaling by hydrogen sulfide (H2S) and polysulfides (H2Sn) in the central nervous system
Kimura, H. (2019) · Neurochemistry International · doi:10.1016/j.neuint.2019.01.027 · Cited by 91 · see citing works
Biological signaling by small inorganic molecules
Basudhar, D., Ridnour, L. A., Cheng, R. Y. S., Kesarwala, A. H., Heinecke, J. L., & Wink, D. A. (2015) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2015.06.001 · Cited by 92 · see citing works
Saying NO to H2S: A Story of HNO, HSNO, and SSNO–
Ivanović‐Burmazović, I., & Filipović, M. R. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b02592 · Cited by 87 · 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
Kawagoe, R., Takashima, I., Uchinomiya, S., & Ojida, A. (2016) · Chemical Science · doi:10.1039/c6sc03856e · Cited by 85 · see citing works
Plasma Free H 2 S Levels are Elevated in Patients With Cardiovascular Disease
Peter, E. A., Shen, X., Shah, S. H., Pardue, S., Glawe, J. D., Zhang, W., Reddy, P. C., Akkuş, N. İ., Varma, J., & Kevil, C. G. (2013) · Journal of the American Heart Association · doi:10.1161/jaha.113.000387 · Cited by 84 · see citing works
Time-Resolved Electrochemical Quantification of Azanone (HNO) at Low Nanomolar Level
Suárez, S., Bikiel, D. E., Wetzler, D. E., Marti, M. A., & Doctorovich, F. A. (2013) · Analytical Chemistry · doi:10.1021/ac402134b · Cited by 82 · see citing works
Wedmann, R., Zahl, A., Shubina, T. E., Dürr, M., Heinemann, F. W., Bugenhagen, B., Burger, P., Ivanović‐Burmazović, I., & Filipović, M. R. (2015) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.5b00831 · Cited by 82 · see citing works
Estrogen Receptors and Estrogen-Induced Uterine Vasodilation in Pregnancy
Bai, J., Qi, Q.-R., Li, Y., Day, R., Makhoul, J., Magness, R. R., & Chen, D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124349 · Cited by 82 · see citing works
Synthesis, Metabolism, and Signaling Mechanisms of Hydrogen Sulfide: An Overview
Bełtowski, J. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9528-8_1 · Cited by 81 · 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
Modes of Physiologic H 2 S Signaling in the Brain and Peripheral Tissues
Paul, B. D., & Snyder, S. H. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5917 · Cited by 76 · see citing works
Metal-Based Optical Probes for Live Cell Imaging of Nitroxyl (HNO)
Rivera‐Fuentes, P., & Lippard, S. J. (2015) · Accounts of Chemical Research · doi:10.1021/acs.accounts.5b00388 · Cited by 75 · see citing works
Peng, H., Shen, J., Edmonds, K. A., Luebke, J. L., Hickey, A. K., Palmer, L. D., Chang, F. J., Bruce, K. E., Kehl‐Fie, T. E., Skaar, E. P., et al. (2017) · mSphere · doi:10.1128/msphere.00082-17 · Cited by 75 · see citing works
Working with nitric oxide and hydrogen sulfide in biological systems
Yuan, S. S., Patel, R. P., & Kevil, C. G. (2014) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00327.2014 · Cited by 74 · see citing works
The Role of Protein Persulfidation in Brain Aging and Neurodegeneration
Petrovic, D., Kouroussis, E., Vignane, T., & Filipović, M. R. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.674135 · Cited by 74 · see citing works
Emerging Roles of Carbonyl Sulfide in Chemical Biology: Sulfide Transporter or Gasotransmitter?
Steiger, A. K., Zhao, Y., & Pluth, M. D. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7119 · Cited by 74 · see citing works
Signaling by sulfur-containing molecules. Quantitative aspects
Koppenol, W. H., & Bounds, P. L. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.09.012 · Cited by 73 · 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
Nava, M., Martin‐Drumel, M., Lopez, C. A., Crabtree, K. N., Womack, C. C., Nguyễn, T. L., Thorwirth, S., Cummins, C. C., Stanton, J. F., & McCarthy, M. C. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b05886 · Cited by 70 · see citing works
O→S Relay Deprotection: A General Approach to Controllable Donors of Reactive Sulfur Species
Kang, J., Xu, S. J., Radford, M. N., Zhang, W., Kelly, S. S., Day, J. J., & Xian, M. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201802845 · Cited by 70 · see citing works
Advances in spectroscopy and dynamics of small and medium sized molecules and clusters
Hochlaf, M. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp01980g · Cited by 68 · see citing works
A switchable NO-releasing nanomedicine for enhanced cancer therapy and inhibition of metastasis
Xu, Y., Ren, H., Liu, J., Wang, Y., Meng, Z., He, Z., Miao, W., Chen, G., & Li, X. (2019) · Nanoscale · doi:10.1039/c9nr00732f · Cited by 69 · see citing works
Szijártó, I. A., Markó, L., Filipović, M. R., Miljković, J. L., Tabeling, C., Tsvetkov, D., Wang, N., Rabelo, L. A., Witzenrath, M., Diedrich, A., et al. (2018) · Hypertension · doi:10.1161/hypertensionaha.117.10562 · Cited by 69 · see citing works
Reactions of HNO with Metal Porphyrins: Underscoring the Biological Relevance of HNO
Doctorovich, F. A., Bikiel, D. E., Pellegrino, J., Suárez, S., & Marti, M. A. (2014) · Accounts of Chemical Research · doi:10.1021/ar500153c · Cited by 67 · see citing works
H2S-Donating Doxorubicins May Overcome Cardiotoxicity and Multidrug Resistance
Chegaev, K. Y., Rolando, B., Cortese, D., Gazzano, E., Buondonno, I., Lazzarato, L., Fanelli, M., Hattinger, C. M., Serra, M., Riganti, C., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00184 · Cited by 67 · see citing works
Tian, X., Li, Z., Lau, C., & Lu, J. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b03712 · Cited by 67 · see citing works
H2S-Mediated Protein S-Sulfhydration: A Prediction for Its Formation and Regulation
Ju, Y., Fu, M., Stokes, E., Wu, L., & Yang, G. (2017) · Molecules · doi:10.3390/molecules22081334 · Cited by 67 · see citing works
The reaction products of sulfide and S-nitrosoglutathione are potent vasorelaxants
Berenyiová, A., Grman, M., Mijušković, A., Staško, A., Mišák, A., Nagy, P., Ondriašová, E., Čačányiová, S., Brezová, V., Feelisch, M., et al. (2014) · Nitric Oxide · doi:10.1016/j.niox.2014.12.008 · Cited by 66 · see citing works
Mass spectrometry in studies of protein thiol chemistry and signaling: Opportunities and caveats
Devarie‐Baez, N. O., Reisz, J. A., & Furdui, C. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.09.016 · Cited by 64 · see citing works
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
NO/H2S “Crosstalk” Reactions. The Role of Thionitrites (SNO–) and Perthionitrites (SSNO–)
Marcolongo, J. P., Venâncio, M. F., Rocha, W. R., Doctorovich, F. A., & Olabe, J. A. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b01978 · Cited by 63 · see citing works
Regulation of carbohydrate metabolism by nitric oxide and hydrogen sulfide: Implications in diabetes
Gheibi, S., Samsonov, A. P., Gheibi, S., Vazquez, A. B., & Kashfi, K. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.113819 · Cited by 63 · see citing works
- Authors
- Filipovic, M. R., Miljkovic, J. L., Nauser, T., Royzen, M., Klos, K., Shubina, T., Koppenol, W. H., Lippard, S. J., & Ivanović-Burmazović, I.
- Affiliations
- Department of Chemistry and Pharmacy, University of Erlangen-Nürnberg, 91058 Erlangen, Germany
- ETH Zurich (CH)
- Massachusetts Institute of Technology (US)
- Friedrich-Alexander-Universität Erlangen-Nürnberg (DE)
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2012-07-17
- Volume
- 134
- Issue
- 29
- Pages
- 12016-12027
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- PMC
- PMC3408084
- OpenAlex
- W2409299056
- Cited by
- 336
- References
- 84
- Citations by year
- 2026: 8 · 2025: 14 · 2024: 9 · 2023: 14 · 2022: 16 · 2021: 20 · 2020: 29 · 2019: 27 · 2018: 23 · 2017: 39 · 2016: 33 · 2015: 37 · 2014: 37 · 2013: 27 · 2012: 2
- FWCI
- 14.11
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of the American Chemical Society (publishedVersion, other-oa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DSpace@MIT (Massachusetts Institute of Technology) (submittedVersion, cc-by-nc)
- Funders
- National Science Foundation
- Eidgenössische Technische Hochschule Zürich
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- S-nitrosothiols, hydrogen sulfide signaling, transnitrosation, hemoglobin, nitric oxide, redox regulation, signal transduction, membrane diffusion
- MeSH terms
- Diffusion, Erythrocytes, Hemoglobins, Humans, Hydrogen Sulfide, Nitric Oxide, Nitrosation, S-Nitrosothiols, S-Nitrosoglutathione, Human Umbilical Vein Endothelial Cells
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
