Nitrosopersulfide (SSNO−) accounts for sustained NO bioactivity of S-nitrosothiols following reaction with sulfide
Open accessAbstract
Sulfide salts are known to promote the release of nitric oxide (NO) from S-nitrosothiols and potentiate their vasorelaxant activity, but much of the cross-talk between hydrogen sulfide and NO is believed to occur via functional interactions of cell regulatory elements such as phosphodiesterases. Using RFL-6 cells as an NO reporter system we sought to investigate whether sulfide can also modulate nitrosothiol-mediated soluble guanylyl cyclase (sGC) activation following direct chemical interaction. We find a U-shaped dose response relationship where low sulfide concentrations attenuate sGC stimulation by S-nitrosopenicillamine (SNAP) and cyclic GMP levels are restored at equimolar ratios. Similar results are observed when intracellular sulfide levels are raised by pre-incubation with the sulfide donor, GYY4137. The outcome of direct sulfide/nitrosothiol interactions also critically depends on molar reactant ratios and is accompanied by oxygen consumption. With sulfide in excess, a 'yellow compound' accumulates that is indistinguishable from the product of solid-phase transnitrosation of either hydrosulfide or hydrodisulfide and assigned to be nitrosopersulfide (perthionitrite, SSNO(-); λ max 412 nm in aqueous buffers, pH 7.4; 448 nm in DMF). Time-resolved chemiluminescence and UV-visible spectroscopy analyses suggest that its generation is preceded by formation of the short-lived NO-donor, thionitrite (SNO(-)). In contrast to the latter, SSNO(-) is rather stable at physiological pH and generates both NO and polysulfides on decomposition, resulting in sustained potentiation of SNAP-induced sGC stimulation. Thus, sulfide reacts with nitrosothiols to form multiple bioactive products; SSNO(-) rather than SNO(-) may account for some of the longer-lived effects of nitrosothiols and contribute to sulfide and NO signaling.
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SSNO- is potentially a better signaling molecule than HSNO.
“The resulting nitroso compound, nitrosopersulfide (perthionitrite; SSNO -) appears, from our recent work [19] and that of Seel et al. [58,59], to be considerably more stable than HSNO -even in the presence of high concentrations of thiols -and, therefore, a potentially better signaling molecule.”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [19]
SSNO- is considerably more stable than HSNO even in the presence of high concentrations of thiols.
“The resulting nitroso compound, nitrosopersulfide (perthionitrite; SSNO -) appears, from our recent work [19] and that of Seel et al. [58,59], to be considerably more stable than HSNO -even in the presence of high concentrations of thiols -and, therefore, a potentially better signaling molecule.”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [19]
SSNO- was able to release NO and induce sGC-dependent cGMP production in cells.
“Indeed, we found that SSNO -was able to release NO and induce sGC-dependent cGMP production in cells [19], but its detection in cells/tissues necessitates development of specific and sufficiently sensitive analytical methods, a task that has not yet been accomplished.”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [19]
The NO-containing yellow compound formed from nitrite and S8 is assigned to be nitrosopersulfide, SSNO-.
“Based on Seel's earlier findings [58,68,69] we assign this product to be nitrosopersulfide, SSNO - [19].”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [19]
Taken together, nitrite reacts with S8 and, seemingly less efficiently, with polysulfides in non-aqueous polar solvents to form products including SSNO-.
“Taken together, nitrite reacts with S8 and, seemingly less efficiently, with polysulfides in non-aqueous polar solvents leading to the formation of similar products as observed previously in the reaction of NO with sulfide [69], and nitrosothiols with thiols [70], and with sulfide [19,71] including SSNO -.”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [19]
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 [19]
SSNO- has pharmacological activity leading to sGC activation with concomitant cGMP formation in cells.
“Evidence of pharmacological activity of SSNO -leading to sGC activation with concomitant cGMP formation in cells was presented by us recently [19].”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [19]
Contrary to nitrosothiols, SSNO- like polysulfides is unstable under strong acidic conditions, leading to rapid decomposition and excision of S8.
“Contrary to nitrosothiols, SSNO -like polysulfides is unstable under strong acidic conditions, leading to rapid decomposition and excision of S8 [19].”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [19]
SSNO- is a colored species containing a sulfane sulfur and a nitrosonium (NO+) moiety attached to opposite ends of a sulfur atom.
“SSNO -is a colored species containing a sulfane sulfur and a nitrosonium (NO + ) moiety attached to opposite ends of a sulfur atom.”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [19]
SSNO- formally belongs to the group of polysulfides (Sx2-).
“It formally belongs to the group of polysulfides (Sx 2-);”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [19]
Contrary to polysulfides and other nitrosothiols, SSNO- is stable in the presence of millimolar concentrations of reduced thiols, including cysteine and glutathione (even DTT).
“however, contrary to polysulfides and other nitrosothiols, it is stable in the presence of millimolar concentrations of reduced thiols, including cysteine and glutathione (even dithiotheritol, DTT) [19].”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [19]
If sulfide is in excess over nitrosothiols (found in tissues typically at nM concentrations), SSNO- is likely to accumulate and may more easily transport and release NO than GSNO or S-nitrosoalbumin.
“If sulfide is in excess over the nitrosothiol (which are found in tissues typically at nM concentrations), SSNO -is likely to accumulate and may more easily transport and release NO than GSNO or S-nitrosoalbumin [19].”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [19]
SSNO- should be sufficiently stable in the reducing environment of the cell; at the same time, it is a better NO releaser than the parent nitrosothiol.
“SSNO -should be sufficiently stable in the reducing environment of the cell; at the same time, it is a better NO releaser than the parent nitrosothiol [19].”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [19]
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Cites
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
Physiological Implications of Hydrogen Sulfide: A Whiff Exploration That Blossomed
Wang, R. (2012) · Physiological Reviews · doi:10.1152/physrev.00017.2011 · Cited by 1,939 · see citing works
Two's company, three's a crowd: can H 2 S be the third endogenous gaseous transmitter?
Wang, R. T. (2002) · The FASEB Journal · doi:10.1096/fj.02-0211hyp · Cited by 1,808 · 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
H 2 S: A Universal Defense Against Antibiotics in Bacteria
Shatalin, K. Y., Shatalina, E., Mironov, A. S., & Nudler, E. (2011) · Science · doi:10.1126/science.1209855 · Cited by 769 · 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
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
Coletta, C., Papapetropoulos, A., Erdelyi, K., Olah, G., Módis, K., Panopoulos, P., Asimakopoulou, A., Gerö, D., Sharina, I., Martin, E., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1202916109 · Cited by 677 · see citing works
The chemistry of the hydrogen sulfide and iron sulfide systems in natural waters
MORSE, J., MILLERO, F., CORNWELL, J., & RICKARD, D. (1987) · Earth-Science Reviews · doi:10.1016/0012-8252(87)90046-8 · Cited by 660 · see citing works
The Chemistry of S-Nitrosothiols
Williams, D. L. H. (1999) · Accounts of Chemical Research · doi:10.1021/ar9800439 · Cited by 499 · 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
Polysulfides Link H 2 S to Protein Thiol Oxidation
Greiner, R., Pálinkás, Z., Bäsell, K., Becher, D., Antelmann, H., Nagy, P., & Dick, T. P. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5041 · Cited by 471 · see citing works
The novel proangiogenic effect of hydrogen sulfide is dependent on Akt phosphorylation
CAI, W., WANG, M., MOORE, P., JIN, H., YAO, T., & Zhu, Y. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.05.026 · Cited by 421 · see citing works
Fukuto, J. M., Carrington, S. J., Tantillo, D. J., Harrison, J. G., Ignarro, L. J., Freeman, B. A., Chen, A., & Wink, D. A. (2012) · Chemical Research in Toxicology · doi:10.1021/tx2005234 · Cited by 389 · 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
Ali, M. Y., Ping, C. Y., Mok, Y.-Y. P., Ling, L. H., Whiteman, M., Bhatia, M., & Moore, P. K. (2006) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706906 · Cited by 349 · see citing works
Production and Physiological Effects of Hydrogen Sulfide
Kimura, H. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5309 · Cited by 347 · see citing works
Polysulfides are possible H 2 S‐derived signaling molecules in rat brain
Kimura, Y., Mikami, Y., Oosumi, K., Tsugane, M., Oka, J., & Kimura, H. (2013) · The FASEB Journal · doi:10.1096/fj.12-226415 · Cited by 342 · see citing works
Hydrogen Sulfide Is an Endogenous Inhibitor of Phosphodiesterase Activity
Bucci, M., Papapetropoulos, A., Vellecco, V., Zhou, Z., Pyriochou, A., Roussos, C., Roviezzo, F., Brancaleone, V., & Cirino, G. (2010) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.209783 · Cited by 337 · see citing works
Filipovic, M. R., Miljkovic, J. L., Nauser, T., Royzen, M., Klos, K., Shubina, T., Koppenol, W. H., Lippard, S. J., & Ivanović-Burmazović, I. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3009693 · Cited by 336 · 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
Chemical aspects of hydrogen sulfide measurements in physiological samples
Nagy, P., Pálinkás, Z., Nagy, A., Budai, B., Tóth, I., & Vasas, A. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.05.037 · Cited by 285 · see citing works
Kajimura, M., Fukuda, R., Bateman, R. M., Yamamoto, T., & Suematsu, M. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2657 · Cited by 265 · see citing works
Honda, A., Adams, S., Sawyer, C. L., Lev‐Ram, V., Tsien, R. Y., & Dostmann, W. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051631298 · Cited by 265 · see citing works
The chemical biology of S-nitrosothiols
Broniowska, K. A., & Hogg, N. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4590 · Cited by 259 · see citing works
Nitrosation Reactions and the Chemistry of Nitric Oxide
(2004) · Elsevier eBooks · doi:10.1016/b978-0-444-51721-0.x5000-2 · Cited by 229 · see citing works
Hydrogen sulphide and angiogenesis: mechanisms and applications
Szabó, C., & Papapetropoulos, A. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2010.01191.x · Cited by 217 · see citing works
Chemical nature of nitric oxide storage forms in rat vascular tissue
Rodriguez, J., Maloney, R. E., Rassaf, T., Bryan, N. S., & Feelisch, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0234600100 · Cited by 210 · see citing works
A Practical Look at the Chemistry and Biology of Hydrogen Sulfide
Olson, K. R. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4401 · Cited by 206 · 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
Levitt, M. D., Abdel-Rehim, M. S., & Furne, J. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3525 · Cited by 177 · 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
Metal ion catalysis in nitrosothiol (RSNO) decomposition
McAninly, J., Williams, D. L. H., Askew, S. C., Butler, A. R., & Russell, C. (1993) · Journal of the Chemical Society, Chemical Communications · doi:10.1039/c39930001758 · Cited by 150 · cited 1× · see citing works
“Transition metals in aqueous buffers can trigger nitrosothiol decomposition [35]; in our hands, SNAP alone produced a very small NO signal when experiments were carried out in the presence of the metal chelator DTPA (100 mM; Fig.”
cGMP-Dependent Protein Kinase Contributes to Hydrogen Sulfide-Stimulated Vasorelaxation
Bucci, M., Papapetropoulos, A., Vellecco, V., Zhou, Z., Altaany, Z., Giannogonas, P., Cantalupo, A., Dhayade, S., Karalis, K. P., Wang, R., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0053319 · Cited by 140 · see citing works
Hydrogen sulfide and oxygen sensing in the cardiovascular system
Olson, K. R., & Whitfield, N. L. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2921 · Cited by 136 · 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
Alexey Kamyshny, Gun, J., Rizkov, D., Voitsekovski, T., & Lev, O. E. (2007) · Environmental Science & Technology · doi:10.1021/es062637+ · Cited by 130 · see citing works
Signaling pathways for the vascular effects of hydrogen sulfide
Wang, R. (2011) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0b013e3283430651 · Cited by 129 · see citing works
Bioassay Discrimination between Nitric Oxide (NO·) and Nitroxyl (NO−) Using L-Cysteine
Pino, R. Z., & Feelisch, M. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1668 · Cited by 121 · 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
A simple and sensitive bioassay method for detection of EDRF with RFL-6 rat lung fibroblasts
Ishii, K., Sheng, H., Warner, T. D., Förstermann, U., & Murad, F. (1991) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1991.261.2.h598 · Cited by 93 · 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
Yong, Q.-C., Cheong, J. L., Hua, F., Deng, L.-W., Khoo, Y. M., Lee, H.-S., Perry, A., Wood, M., Whiteman, M., & Bian, J.-S. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3572 · Cited by 85 · see citing works
Two's Company: Composition, Structure and Performance of Entrepreneurial Pairs
Coad, A., & Timmermans, B. (2012) · European Management Review · doi:10.1111/emre.12030 · Cited by 79 · see citing works
Molecular mechanisms of nitrovasodilator bioactivation
Noack, E., & Feelisch, M. (1991) · Steinkopff eBooks · doi:10.1007/978-3-642-72461-9_5 · Cited by 78 · see citing works
Structure and stability of SiH+4
Gordon, M. S. (1978) · Chemical Physics Letters · doi:10.1016/0009-2614(78)85008-8 · Cited by 71 · 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
Heme-assisted S-Nitrosation Desensitizes Ferric Soluble Guanylate Cyclase to Nitric Oxide
Fernhoff, N. B., Derbyshire, E. R., Underbakke, E. S., & Marletta, M. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.393892 · Cited by 67 · 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
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
Kinetics of the reaction of nitric oxide with sulfite and bisulfite ions in aqueous solution
Littlejohn, D., Hu, K., & Chang, S. G. (1986) · Inorganic Chemistry · doi:10.1021/ic00238a007 · Cited by 43 · see citing works
UV-, VIS- and IR-light-induced isomerization of HSNO in a low-temperature matrix
Müller, R. P., Nonella, M., Russegger, P., & Huber, J. R. (1984) · Chemical Physics · doi:10.1016/0301-0104(84)85116-2 · Cited by 40 · see citing works
Riego, J. A., Broniowska, K. A., Kettenhofen, N. J., & Hogg, N. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.04.027 · Cited by 37 · 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
Seel, F., & Wagner, M. (1985) · Zeitschrift für Naturforschung B · doi:10.1515/znb-1985-0612 · Cited by 29 · see citing works
Zur Kenntnis der schwefligen Säure. III Das Sulfinimid und seine Isomeren
Goehring, M., & Messner, J. (1952) · Zeitschrift für anorganische und allgemeine Chemie · doi:10.1002/zaac.19522680107 · Cited by 28 · see citing works
Novel Method for Measuring S-Nitrosothiols Using Hydrogen Sulfide
Teng, X., Isbell, T. S., Crawford, J. H., Bosworth, C. A., Giles, G. I., Koenitzer, J. R., Lancaster, J. R., Doeller, J. E., Kraus, D. W., & Patel, R. P. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)01209-3 · Cited by 28 · see citing works
Embracing sulfide and CO to understand nitric oxide biology
Feelisch, M., & Olson, K. R. (2013) · Nitric Oxide · doi:10.1016/j.niox.2013.06.004 · Cited by 20 · 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
Yoon, P. J., Parajuli, S. P., Zuo, D. C., Shahi, P. K., Oh, H. J., Shin, H. R., Lee, M., Yeum, C. H., Choi, S., & Jun, J. Y. (2011) · Chonnam Medical Journal · doi:10.4068/cmj.2011.47.2.72 · Cited by 16 · see citing works
Kraft, P., Haynes‐Johnson, D., Bhattacharjee, S., Lundeen, S. G., & Qiu, Y. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.04.006 · Cited by 9 · see citing works
ChemInform Abstract: Reaction of Sulfides with Nitrogen Monoxide in Aqueous Solution
SEEL, F., & WAGNER, M. (1988) · ChemInform · doi:10.1002/chin.198824008 · Cited by 9 · see citing works
Flagged first, then by citations
2 of the 64 references couldn’t be matched to a known paper.
Cited by
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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 1,041 · 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
Dóka, É., Pader, I., Bíró, A., Johansson, K., Cheng, Q., Ballagó, K., Prigge, J. R., Pastor‐Flores, D., Dick, T. P., Schmidt, E. E., et al. (2016) · Science Advances · doi:10.1126/sciadv.1500968 · Cited by 330 · 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
Heme Oxygenases in Cardiovascular Health and Disease
Ayer, A., Zarjou, A., Agarwal, A., & Stocker, R. (2016) · Physiological Reviews · doi:10.1152/physrev.00003.2016 · Cited by 243 · 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
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
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 180 · 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 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
Hydrogen 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
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
Trionnaire, S. L., Perry, A., Szczęsny, B., Szabó, C., Winyard, P. G., Whatmore, J. L., Wood, M. E., & Whiteman, M. (2014) · MedChemComm · doi:10.1039/c3md00323j · Cited by 128 · see citing works
Muñoz-Vargas, M. Á., González‐Gordo, S., Cañas, A., López-Jaramillo, J., Palma, J. M., & Corpas, F. J. (2018) · Nitric Oxide · doi:10.1016/j.niox.2018.10.002 · Cited by 118 · 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
Self-citationThe 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
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
Bianco, C. L., Chavez, T. A., Alfaro, V. S., Saund, S. S., Nguyen, Q. N. N., Tantillo, D. J., Ichimura, A. S., Toscano, J. P., & Fukuto, J. M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.09.020 · Cited by 109 · 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
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
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
The Triple Crown: NO, CO, and H2S in cancer cell biology
Oza, P. P., & Kashfi, K. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108502 · Cited by 78 · 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
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
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
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
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
The mechanism of action and role of hydrogen sulfide in the control of vascular tone
Dongó, E., Beliczai-Marosi, G., Dybvig, A., & Kiss, L. (2017) · Nitric Oxide · doi:10.1016/j.niox.2017.10.010 · Cited by 66 · 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
The Intersection of NO and H2S: Persulfides Generate NO from Nitrite through Polysulfide Formation
Bailey, T. S., Henthorn, H. A., & Pluth, M. D. (2016) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.6b01660 · Cited by 62 · see citing works
Kharbech, O., Massoud, M. B., Sakouhi, L., Djebali, W., Mur, L. A. J., & Chaoui, A. (2020) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2020.06.002 · Cited by 60 · see citing works
The dichotomous role of H2S in cancer cell biology? Déjà vu all over again
Kashfi, K. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.01.042 · Cited by 59 · see citing works
Rational Design of a Dual‐Reactivity‐Based Fluorescent Probe for Visualizing Intracellular HSNO
Chen, W., Matsunaga, T., Neill, D. L., Yang, C., Akaike, T., & Xian, M. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201908950 · Cited by 57 · see citing works
Signaling Paradigms of H2S-Induced Vasodilation: A Comprehensive Review
Munteanu, C., Popescu, C., Vlădulescu-Trandafir, A.-I., & Onose, G. (2024) · Antioxidants · doi:10.3390/antiox13101158 · Cited by 55 · see citing works
Tomášová, L., Pavlovičová, M., Máleková, Ľ., Mišák, A., Kristek, F., Grman, M., Čačányiová, S., Tomasek, M., Tomaskova, Z. S., Perry, A., et al. (2014) · Nitric Oxide · doi:10.1016/j.niox.2014.12.012 · Cited by 52 · see citing works
Protein Persulfidation: Recent Progress and Future Directions
Luo, S., Kong, C., Ye, D., Liu, X., Wang, Y., Meng, G., Han, Y., Xie, L., & Ji, Y. H. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0064 · Cited by 49 · see citing works
Are Reactive Sulfur Species the New Reactive Oxygen Species?
Olson, K. R. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8132 · Cited by 49 · see citing works
Gasotransmitters in pregnancy: from conception to uterine involution†
Guerra, D. D., & Hurt, K. J. (2019) · Biology of Reproduction · doi:10.1093/biolre/ioz038 · Cited by 44 · see citing works
On the possible biological relevance of HSNO isomers: a computational investigation
Ivanova, L. V., Anton, B. J., & Timerghazin, Q. K. (2014) · Physical Chemistry Chemical Physics · doi:10.1039/c4cp00469h · Cited by 43 · see citing works
H2S Regulation of Nitric Oxide Metabolism
Kolluru, G. K., Yuan, S. S., Shen, X., & Kevil, C. G. (2015) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2014.11.040 · Cited by 43 · see citing works
Gao, Y. H., Toubaei, A., Kong, X., & Wu, G. (2015) · Chemistry - A European Journal · doi:10.1002/chem.201503353 · Cited by 42 · see citing works
Reactivity of a Nickel Sulfide with Carbon Monoxide and Nitric Oxide
Hartmann, N. J., Wu, G. X., & Hayton, T. W. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b08084 · Cited by 41 · see citing works
Wedmann, R., Ivanović‐Burmazović, I., & Filipović, M. R. (2017) · Interface Focus · doi:10.1098/rsfs.2016.0139 · Cited by 40 · see citing works
Nitrosopersulfide (SSNO − ) targets the Keap-1/Nrf2 redox system
Cortese-Krott, M. M., Pullmann, D., & Feelisch, M. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.09.022 · Cited by 39 · see citing works
Marcolongo, J. P., Morzan, U. N., Zeida, A., Scherlis, D. A., & Olabe, J. A. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c6cp06314d · Cited by 36 · see citing works
NO-ferroheme is a signaling entity in the vasculature
Kleschyov, A. L., Zhuge, Z., Schiffer, T. A., Guimarães, D. D., Zhang, G., Montenegro, M. F., Tesse, A., Weitzberg, E., Carlström, M., & Lundberg, J. O. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01411-5 · Cited by 36 · see citing works
Investigations on the role of hemoglobin in sulfide metabolism by intact human red blood cells
Bianco, C. L., Savitsky, A., Feelisch, M., & Cortese-Krott, M. M. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.01.045 · Cited by 35 · see citing works
Hartle, M. D., Meininger, D. J., Zakharov, L. N., Tonzetich, Z. J., & Pluth, M. D. (2015) · Dalton Transactions · doi:10.1039/c5dt03355a · Cited by 34 · see citing works
Mišák, A., Grman, M., Bačová, Z., Režuchová, I., Hudecová, S., Ondriašová, E., Križanová, O., Brezová, V., Chovanec, M., & Ondriaš, K. (2017) · Nitric Oxide · doi:10.1016/j.niox.2017.09.006 · Cited by 35 · see citing works
Photochemistry of nitric oxide and S-nitrosothiols in human skin
Pelegrino, M. T., Paganotti, A., Seabra, A. B., & Weller, R. (2020) · Histochemistry and Cell Biology · doi:10.1007/s00418-020-01858-w · Cited by 34 · see citing works
Sun, H., Wu, Z., Nie, X.-W., Wang, X., & Bian, J. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.651884 · Cited by 34 · see citing works
Role of nitroxyl (HNO) in cardiovascular system: From biochemistry to pharmacology
Sun, H., Wu, Z., Cao, L., Zhu, M., Nie, X.-W., Huang, D., Sun, M., & Bian, J. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104961 · Cited by 32 · see citing works
Disulfide reductase systems in liver
Miller, C. G., & Schmidt, E. E. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14498 · Cited by 30 · see citing works
The Role of Hydrogen Sulphide in Blood Pressure Regulation
Čačányiová, S., Berenyiová, A., & Kristek, F. (2016) · Physiological Research · doi:10.33549/physiolres.933438 · Cited by 31 · see citing works
Physiological roles of hydrogen sulfide and polysulfides
Kimura, H. (2016) · Folia Pharmacologica Japonica · doi:10.1254/fpj.147.23 · Cited by 29 · see citing works
Kobayashi, J., Ohtake, K., Murata, I., & Sonoda, K. (2022) · Nitric Oxide · doi:10.1016/j.niox.2022.09.004 · Cited by 28 · see citing works
Andrés, C. M. C., Lobo, F., de la Lastra, J. M. P., Munguira, E. B., Andrés, C., & Lebeña, E. P. (2025) · Current Issues in Molecular Biology · doi:10.3390/cimb47090765 · Cited by 25 · see citing works
Single-Component Photo-Responsive Template for the Controlled Release of NO and H 2 S 2
Roy, B., Shieh, M., Xu, S. J., Ni, X., & Xian, M. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c09914 · Cited by 25 · see citing works
Gasotransmitters and Stomatal Closure: Is There Redundancy, Concerted Action, or Both?
Scuffi, D., Lamattina, L., & García‐Mata, C. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.00277 · Cited by 24 · see citing works
Fukudome, M., Shimada, H., Uchi, N., Osuki, K.-I., Ishizaki, H., Murakami, E., Kawaguchi, M., & Uchiumi, T. (2020) · Antioxidants · doi:10.3390/antiox9020145 · Cited by 23 · see citing works
Bogdándi, V., Ditrói, T., Bátai, I. Z., Sándor, Z., Minnion, M., Vasas, A., Galambos, K., Buglyó, P., Pintér, E., Feelisch, M., et al. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8049 · Cited by 23 · see citing works
Fida, T. T., Voordouw, J. K., Ataeian, M., Kleiner, M., Okpala, G. N., Mand, J., & Voordouw, G. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00981 · Cited by 22 · see citing works
Reactions between nitrosopersulfide and heme proteins
Bolden, C. A., King, S. B., & Kim‐Shapiro, D. B. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.09.005 · Cited by 21 · see citing works
Drobna, M., MISAK, A., Holland, T., Kristek, F., Grman, M., TOMASOVA, L., Berenyiová, A., Čačányiová, S., & Ondriaš, K. (2015) · Physiological Research · doi:10.33549/physiolres.932772 · Cited by 21 · see citing works
On the Relationship between Lean Practices and Environmental Performance
Dieste, M., & Panizzolo, R. (2018) · IOP Conference Series Earth and Environmental Science · doi:10.1088/1755-1315/151/1/012034 · Cited by 21 · see citing works
Cortese-Krott, M. M. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8171 · Cited by 20 · see citing works
Pelegrino, M. T., Weller, R., Paganotti, A., & Seabra, A. B. (2019) · Nitric Oxide · doi:10.1016/j.niox.2019.11.003 · Cited by 19 · see citing works
The Roles of NO and H2S in Sperm Biology: Recent Advances and New Perspectives
Kadlec, M., Ros‐Santaella, J. L., & Pintus, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062174 · Cited by 18 · see citing works
Hydropersulfides (RSSH) and Nitric Oxide (NO) Signaling: Possible Effects on S-Nitrosothiols (RS-NO)
Fukuto, J. M., Pérez‐Ternero, C., Zarenkiewicz, J., Lin, J., Hobbs, A. J., & Toscano, J. P. (2022) · Antioxidants · doi:10.3390/antiox11010169 · Cited by 17 · see citing works
Heine, C. L., Schmidt, R., Geckl, K., Schrammel, A., Gesslbauer, B., Schmidt, K., Mayer, B., & Gorren, A. C. F. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.660316 · Cited by 17 · see citing works
Thionitrous Acid/Thionitrite and Perthionitrite Intermediates in the “Crosstalk” of NO and H 2 S
Marcolongo, J. P., Zeida, A., Slep, L. D., & Olabe, J. A. (2017) · Advances in inorganic chemistry · doi:10.1016/bs.adioch.2017.02.002 · Cited by 17 · see citing works
Specific Reactions of RSNO, HSNO, and HNO and Their Applications in the Design of Fluorescent Probes
Wang, Y., Xu, S. J., & Xian, M. (2020) · Chemistry - A European Journal · doi:10.1002/chem.202001885 · Cited by 17 · see citing works
Tsikas, D., & Böhmer, A. (2017) · Nitric Oxide · doi:10.1016/j.niox.2017.02.001 · Cited by 17 · see citing works
Grman, M., Nasim, M. J., Leontiev, R., Mišák, A., Jakusova, V., Ondriaš, K., & Jacob, C. (2017) · Antioxidants · doi:10.3390/antiox6010014 · Cited by 16 · see citing works
Kumar, M. R., & Farmer, P. J. (2019) · Molecules · doi:10.3390/molecules24173090 · Cited by 16 · see citing works
Hossain, M. K., Basak, A., & Majumdar, A. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c01529 · Cited by 15 · see citing works
Kolliyedath, G., Sahana, T., Johnson, S. M., & Kundu, S. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202313187 · Cited by 15 · see citing works
Cooperative Interactions Between NO and H 2 S: Chemistry, Biology, Physiology, Pathophysiology
Kevil, C. G., Cortese-Krott, M. M., Nagy, P., Papapetropoulos, A., Feelisch, M., & Szabó, C. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804273-1.00005-3 · Cited by 15 · see citing works
Fernandes, D., Nunes, J., Tomé, C. S., Zuhra, K., Costa, J. M. F., Antunes, A. M. M., Giuffrè, A., & Vicente, J. B. (2021) · Antioxidants · doi:10.3390/antiox10091391 · Cited by 15 · see citing works
Davis, A. G., & Pluth, M. D. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202413092 · Cited by 14 · see citing works
Hassan, A., Maulood, I. M., & Salihi, A. B. (2021) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2021.9646 · Cited by 14 · see citing works
Electrophilic sulfhydration of 8-nitro-cGMP involves sulfane sulfur
Terzić, V., Padovani, D., Balland, V., Artaud, I., & Galardon, E. (2014) · Organic & Biomolecular Chemistry · doi:10.1039/c4ob00868e · Cited by 14 · see citing works
Atta, S., Mandal, A., & Majumdar, A. (2024) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.4c02527 · Cited by 13 · see citing works
Rational Design of a Dual‐Reactivity‐Based Fluorescent Probe for Visualizing Intracellular HSNO
Chen, W. Q., Matsunaga, T., Neill, D. L., Yang, C., Akaike, T., & Xian, M. (2019) · Angewandte Chemie · doi:10.1002/ange.201908950 · Cited by 13 · see citing works
Nitric Oxide and Hydrogen Sulfide: A Nice Pair in the Respiratory System
Fuschillo, S., Palomba, L., Capparelli, R., Motta, A., & Maniscalco, M. (2020) · Current Medicinal Chemistry · doi:10.2174/0929867327666200310120550 · Cited by 12 · see citing works
- Authors
- Cortese-Krott, M. M., Fernandez, B. O., Santos, J. L. T., Mergia, E., Grman, M., Nagy, P., Kelm, M., Butler, A., & Feelisch, M.
- Affiliations
- Heinrich Heine University Düsseldorf (DE)
- Southampton General Hospital (GB)
- Ruhr University Bochum (DE)
- Slovak Academy of Sciences (SK)
- National Institute of Oncology (HU)
- University of St Andrews (GB)
- Corresponding author
- Feelisch, Martin
- ORCID
- Venue
- Redox Biology
- Publisher
- Elsevier BV
- Published
- 2014
- Volume
- 2
- Pages
- 234-244
- ISSN
- 2213-2317 (ISSN-L)
- PMC
- PMC3909780
- OpenAlex
- W2037151440
- Cited by
- 153
- References
- 64
- Citations by year
- 2026: 6 · 2025: 11 · 2024: 6 · 2023: 7 · 2022: 7 · 2021: 5 · 2020: 17 · 2019: 11 · 2018: 12 · 2017: 22 · 2016: 20 · 2015: 14 · 2014: 14
- FWCI
- 10.37
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Redox Biology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- ePrints Soton (University of Southampton) (acceptedVersion)
- University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- St Andrews Research Repository (St Andrews Research Repository) (submittedVersion, cc-by)
- Funders
- European Network on Gasotransmitters
- FP7 Marie Curie International Reintegration program (PIRG08-GA-2010-277006, to PN)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- S-nitrosothiols, sulfide, nitric oxide, hydrogen sulfide signaling, transnitrosation, thionitrites, GYY4137, cyclic GMP, polysulfides, oxygen consumption
- MeSH terms
- Soluble Guanylyl Cyclase, Animals, Cell Line, Cyclic GMP, Guanylate Cyclase, Morpholines, Nitric Oxide, Nitroso Compounds, Organothiophosphorus Compounds, Oxygen Consumption, Sulfides, Receptors, Cytoplasmic and Nuclear, Nitric Oxide Donors, S-Nitrosothiols, Rats
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