Nitrite Reductase Activity and Inhibition of H2S Biogenesis by Human Cystathionine ß-Synthase

The L-Arginine-Nitric Oxide Pathway

Epstein, F. H., Moncada, S., & Higgs, A. (1993) · New England Journal of Medicine · doi:10.1056/nejm199312303292706 · Cited by 6,678 · see citing works

The nitrate-nitrite-nitric oxide pathway in physiology and therapeutics

Lundberg, J. O., Weitzberg, E., & Gladwin, M. T. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2466 · Cited by 2,739 · cited 1× · see citing works

H ₂ S as a Physiologic Vasorelaxant: Hypertension in Mice with Deletion of Cystathionine γ-Lyase

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

Hydrogen sulphide and its therapeutic potential

Szabó, C. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2425 · Cited by 2,039 · 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

Nitric oxide : biology and pathobiology

Ignarro, L. J. (2000) · Cited by 1,300 · see citing works

3-Mercaptopyruvate Sulfurtransferase Produces Hydrogen Sulfide and Bound Sulfane Sulfur in the Brain

Shibuya, N., Tanaka, M., Yoshida, M., Ogasawara, Y., Togawa, T., Ishii, K., & Kimura, H. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2253 · Cited by 920 · see citing works

Enzyme-independent formation of nitric oxide in biological tissues

Zweier, J. L., Wang, P., Samouilov, A., & Kuppusamy, P. (1995) · Nature Medicine · doi:10.1038/nm0895-804 · Cited by 788 · 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

Characterization of the enzymic capacity for cysteine desulphhydration in liver and kidney of the rat

Stipanuk, M. H., & Beck, P. W. (1982) · Biochemical Journal · doi:10.1042/bj2060267 · Cited by 710 · see citing works

Stomach NO synthesis

Benjamin, N., O'Driscoll, F., Dougall, H., Duncan, C., Smith, L., Golden, M., & McKenzie, H. (1994) · Nature · doi:10.1038/368502a0 · Cited by 665 · see citing works

Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values

Furne, J. K., Saeed, A., & Levitt, M. D. (2008) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.90566.2008 · Cited by 628 · see citing works

Relative Contributions of Cystathionine β-Synthase and γ-Cystathionase to H2S Biogenesis via Alternative Trans-sulfuration Reactions

Singh, S., Padovani, D., Leslie, R. A., Chiku, T., & Banerjee, R. V. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.010868 · Cited by 615 · see citing works

Deoxymyoglobin Is a Nitrite Reductase That Generates Nitric Oxide and Regulates Mitochondrial Respiration

Shiva, S., Huang, Z., Grubina, R., Sun, J., Ringwood, L. A., MacArthur, P. H., Xu, X., Murphy, E., Darley-Usmar, V. M., & Gladwin, M. T. (2007) · Circulation Research · doi:10.1161/01.res.0000260171.52224.6b · Cited by 599 · see citing works

The Quantitatively Important Relationship between Homocysteine Metabolism and Glutathione Synthesis by the Transsulfuration Pathway and Its Regulation by Redox Changes

Mosharov, E. V., Cranford, M. R., & Banerjee, R. V. (2000) · Biochemistry · doi:10.1021/bi001088w · Cited by 526 · 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

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

H2S Biogenesis by Human Cystathionine γ-Lyase Leads to the Novel Sulfur Metabolites Lanthionine and Homolanthionine and Is Responsive to the Grade of Hyperhomocysteinemia

Chiku, T., Padovani, D., Zhu, W., Singh, S., Vitvitsky, V., & Banerjee, R. V. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808026200 · Cited by 454 · see citing works

Chemical Characterization of the Smallest <i>S</i> -Nitrosothiol, HSNO; Cellular Cross-talk of H ₂ S and <i>S</i> -Nitrosothiols

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

Production of the Neuromodulator H2S by Cystathionine β-Synthase via the Condensation of Cysteine and Homocysteine

Chen, X., Jhee, K.-H., & Kruger, W. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400481200 · Cited by 330 · see citing works

Hydrogen Sulfide: From Brain to Gut

Kimura, H. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2919 · Cited by 315 · see citing works

Structure of human cystathionine β‐synthase: a unique pyridoxal 5′‐phosphate‐dependent heme protein

Meier, M., Janošík, M., Kéry, V., Kraus, J., & Burkhard, P. (2001) · EMBO Journal · doi:10.1093/emboj/20.15.3910 · Cited by 301 · see citing works

The functional nitrite reductase activity of the heme-globins

Gladwin, M. T., & Kim-Shapiro, D. B. (2008) · Blood · doi:10.1182/blood-2008-01-115261 · Cited by 293 · see citing works

Cooperativity in the dissociation of nitric oxide from hemoglobin.

Moore, E. G., & Gibson, Q. H. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33557-3 · Cited by 292 · see citing works

Human neuroglobin functions as a redox-regulated nitrite reductase

Tiso, M., Tejero, J., Basu, S., Azarov, I., Wang, X., Simplaceanu, V., Frizzell, S., Jayaraman, T., Geary, L., Shapiro, C., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.159541 · Cited by 287 · see citing works

The Quantitative Significance of the Transsulfuration Enzymes for H 2 S Production in Murine Tissues

Kabil, Ö., Vitvitsky, V., Xie, P., & Banerjee, R. V. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3781 · Cited by 275 · see citing works

Murine cystathionine γ-lyase: complete cDNA and genomic sequences, promoter activity, tissue distribution and developmental expression

Ishii, I., Akahoshi, N., Yu, X., Kobayashi, Y., Namekata, K., Komaki, G., & Kimura, H. (2004) · Biochemical Journal · doi:10.1042/bj20040243 · Cited by 274 · see citing works

Interactions of Multiple Gas-Transducing Systems: Hallmarks and Uncertainties of CO, NO, and H 2 S Gas Biology

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

Structure and Kinetic Analysis of H2S Production by Human Mercaptopyruvate Sulfurtransferase

Yadav, P. K., Yamada, K., Chiku, T., Koutmos, M., & Banerjee, R. V. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.466177 · Cited by 245 · see citing works

A Functional Transsulfuration Pathway in the Brain Links to Glutathione Homeostasis

Vitvitsky, V., THOMAS, M. P., Ghorpade, A., Gendelman, H. E., & Banerjee, R. V. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602799200 · Cited by 242 · see citing works

Evidence for Heme-mediated Redox Regulation of Human Cystathionine β-Synthase Activity

Taoka, S., Ohja, S., Shan, X., Kruger, W. D., & Banerjee, R. V. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.39.25179 · Cited by 239 · see citing works

Cystathionine β-Synthase: Structure, Function, Regulation, and Location of Homocystinuria-causing Mutations

Miles, E. W., & Kraus, J. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400005200 · Cited by 236 · 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

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

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

PLP-dependent H2S biogenesis

Singh, S., & Banerjee, R. V. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.02.004 · Cited by 188 · see citing works

Transsulfuration depends on heme in addition to pyridoxal 5'-phosphate. Cystathionine beta-synthase is a heme protein.

Kéry, V., Bukovská, G., & Kraus, J. P. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47244-4 · Cited by 179 · see citing works

Reactions of ferrous neuroglobin and cytoglobin with nitrite under anaerobic conditions

Petersen, M. G., Dewilde, S., & Fago, A. (2008) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2008.05.008 · Cited by 144 · see citing works

Characterization of the Mechanism and Magnitude of Cytoglobin-mediated Nitrite Reduction and Nitric Oxide Generation under Anaerobic Conditions

Li, H., Hemann, C., Abdelghany, T. M., El-Mahdy, M. A., & Zweier, J. L. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.342378 · Cited by 132 · see citing works

Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme.

Taoka, S., Lepore, B. W., Kabil, O., Ojha, S., Ringe, D., & Banerjee, R. (2002) · Biochemistry · doi:10.1021/bi026052d · Cited by 129 · see citing works

Reaction mechanism and regulation of cystathionine β-synthase

Banerjee, R. V., Evande, R., Kabil, Ö., Ojha, S., & Taoka, S. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/s1570-9639(03)00044-x · Cited by 125 · see citing works

Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine β-synthase

Koutmos, M., Kabil, Ö., Smith, J. L., & Banerjee, R. V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011448107 · Cited by 114 · see citing works

Characterization of the Heme and Pyridoxal Phosphate Cofactors of Human Cystathionine β-Synthase Reveals Nonequivalent Active Sites

Taoka, S., West, M., & Banerjee, R. V. (1999) · Biochemistry · doi:10.1021/bi9826052 · Cited by 106 · see citing works

Plant and Cyanobacterial Hemoglobins Reduce Nitrite to Nitric Oxide under Anoxic Conditions

Sturms, R., DiSpirito, A. A., & Hargrove, M. S. (2011) · Biochemistry · doi:10.1021/bi2004312 · Cited by 105 · see citing works

Properties of an unusual heme cofactor in PLP-dependent cystathionine β-synthase

Singh, S., Madzelan, P., & Banerjee, R. V. (2007) · Natural Product Reports · doi:10.1039/b604182p · Cited by 70 · see citing works

Active Cystathionine β-Synthase Can Be Expressed in Heme-free Systems in the Presence of Metal-substituted Porphyrins or a Chemical Chaperone

Majtán, T., Singh, L. R., Wang, L., Kruger, W. D., & Kraus, J. P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805928200 · Cited by 63 · see citing works

Modulation of the heme electronic structure and cystathionine β-synthase activity by second coordination sphere ligands: The role of heme ligand switching in redox regulation

Singh, S., Madzelan, P., Stasser, J. P., Weeks, C. L., Becker, D., Spiro, T. G., Penner‐Hahn, J. E., & Banerjee, R. V. (2009) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2009.01.009 · Cited by 58 · see citing works

Reversible Heme-Dependent Regulation of Human Cystathionine β-Synthase by a Flavoprotein Oxidoreductase

Kabil, Ö., Weeks, C. L., Carballal, S., Gherasim, C., Álvarez, B., Spiro, T. G., & Banerjee, R. V. (2011) · Biochemistry · doi:10.1021/bi201270q · Cited by 55 · see citing works

Nitric oxide

Benarroch, E. E. (2011) · Neurology · doi:10.1212/wnl.0b013e318233b3e4 · Cited by 54 · see citing works

Nitrite Reductase Activity of Hemoglobin S (Sickle) Provides Insight into Contributions of Heme Redox Potential Versus Ligand Affinity

Grubina, R., Basu, S., Tiso, M., Kim‐Shapiro, D. B., & Gladwin, M. T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705222200 · Cited by 49 · see citing works

Two novel mutations of theFMO3 gene in a proband with trimethylaminuria

Akerman, B. R., Forrest, S. M., Chow, L., Youil, R., Knight, M. A., & Treacy, E. P. (1999) · Human Mutation · doi:10.1002/(sici)1098-1004(1999)13:5 · Cited by 45 · see citing works

Integrating nitric oxide, nitrite and hydrogen sulfide signaling in the physiological adaptations to hypoxia: A comparative approach

Fago, A., Jensen, F. B., Tota, B., Feelisch, M., Olson, K. R., Helbo, S., Lefevre, S., Mancardi, D., Palumbo, A., Sandvik, G. K., et al. (2012) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2012.01.011 · Cited by 42 · see citing works

Effects of Heme Ligand Mutations Including a Pathogenic Variant, H65R, on the Properties of Human Cystathionine β-Synthase

Ojha, S., Wu, J., LoBrutto, R., & Banerjee, R. V. (2002) · Biochemistry · doi:10.1021/bi011827o · Cited by 38 · see citing works

Kinetics of Reversible Reductive Carbonylation of Heme in Human Cystathionine β-Synthase

Carballal, S., Cuevasanta, E., Marmisolle, I., Kabil, Ö., Gherasim, C., Ballou, D. P., Banerjee, R. V., & Álvarez, B. (2013) · Biochemistry · doi:10.1021/bi4004556 · Cited by 31 · see citing works

Mercuric chloride-induced spin or ligation state changes in ferric or ferrous human cystathionine β-synthase inhibit enzyme activity

Taoka, S., Green, E. L., Loehr, T. M., & Banerjee, R. V. (2001) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(01)00336-1 · Cited by 30 · see citing works

Structure of human R-state aquomethemoglobin at 2.0 Å resolution

Yi, J., Thomas, L. M., & Richter-Addo, G. B. (2011) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309111012528 · Cited by 29 · see citing works

Characterization of Erythrocytic Uptake and Release and Disposition Pathways of Nitrite, Nitrate, Methemoglobin, and Iron-Nitrosyl Hemoglobin in the Human Circulation

Hon, Y. Y., Sun, H., Dejam, A., & Gladwin, M. T. (2010) · Drug Metabolism and Disposition · doi:10.1124/dmd.110.034355 · Cited by 27 · see citing works

Correction to Kinetics of Reversible Reductive Carbonylation of Heme in Human Cystathionine β-Synthase

Carballal, S., Cuevasanta, E., Marmisolle, I., Kabil, Ö., Gherasim, C., Ballou, D. P., Banerjee, R. V., & Álvarez, B. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b01326 · Cited by 26 · see citing works

Characterization of the Heme and Pyridoxal Phosphate Cofactors of Human Cystathionine β-Synthase Reveals Nonequivalent Active Sites

Taoka, S., West, M., & Banerjee, R. V. (1999) · Biochemistry · doi:10.1021/bi995077i · Cited by 23 · see citing works

Impeded Electron Transfer From a Pathogenic FMN Domain Mutant of Methionine Synthase Reductase and Its Responsiveness to Flavin Supplementation

Gherasim, C., Zaman, U., Raza, A. S., & Banerjee, R. V. (2008) · Biochemistry · doi:10.1021/bi8008328 · Cited by 14 · see citing works

Quantitative Systems Pharmacology Model of NO Metabolome and Methemoglobin Following Long‐Term Infusion of Sodium Nitrite in Humans

Vega‐Villa, K. R., Pluta, R. M., Lonser, R. R., & Woo, S. (2013) · CPT Pharmacometrics & Systems Pharmacology · doi:10.1038/psp.2013.35 · Cited by 7 · see citing works

Correction for Koutmos et al., Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine β-synthase

(2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102185108 · Cited by 1 · see citing works

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

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

Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation

Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works

Cystathionine-β-synthase: Molecular Regulation and Pharmacological Inhibition

Zuhra, K., Augsburger, F., Majtán, T., & Szabó, C. (2020) · Biomolecules · doi:10.3390/biom10050697 · Cited by 244 · 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

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

S-Glutathionylation Enhances Human Cystathionine β-Synthase Activity Under Oxidative Stress Conditions

Niu, W., Yadav, P. K., Adamec, J., & Banerjee, R. V. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5891 · Cited by 114 · see citing works

Sulfide Homeostasis and Nitroxyl Intersect via Formation of Reactive Sulfur Species in Staphylococcus aureus

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

Inorganic sulfur–nitrogen compounds: from gunpowder chemistry to the forefront of biological signaling

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

Catalytic promiscuity and heme-dependent redox regulation of H2S synthesis

Banerjee, R. V. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.02.021 · Cited by 67 · see citing works

NO• Binds Human Cystathionine β-Synthase Quickly and Tightly

Vicente, J. B., Colaço, H. G., Mendes, M. I. S., Sarti, P., Leandro, P., & Giuffrè, A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.507533 · Cited by 66 · see citing works

Pharmacology and therapeutic role of inorganic nitrite and nitrate in vasodilatation

Bailey, J., Feelisch, M., Horowitz, J. D., Frenneaux, M. P., & Madhani, M. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.06.009 · Cited by 60 · see citing works

Bioenergetic relevance of hydrogen sulfide and the interplay between gasotransmitters at human cystathionine β-synthase

Vicente, J. B., Malagrinò, F., Arese, M., Forte, E., Sarti, P., & Giuffrè, A. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.03.030 · Cited by 51 · see citing works

Allosteric control of human cystathionine β-synthase activity by a redox active disulfide bond

Niu, W., Wang, J., Qian, J., Wang, M., Wu, P., Chen, F., & Yan, S. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000103 · Cited by 49 · see citing works

S-Adenosyl-l-methionine Modulates CO and NO• Binding to the Human H2S-generating Enzyme Cystathionine β-Synthase

Vicente, J. B., Colaço, H. G., Sarti, P., Leandro, P., & Giuffrè, A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.681221 · Cited by 45 · see citing works

A Metabolic Paradigm for Hydrogen Sulfide Signaling via Electron Transport Chain Plasticity

Hanna, D. A., Kumar, R., & Banerjee, R. V. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0067 · Cited by 44 · see citing works

Melatonin, Its Metabolites and Their Interference with Reactive Nitrogen Compounds

Hardeland, R. (2021) · Molecules · doi:10.3390/molecules26134105 · Cited by 45 · see citing works

The impact of human and mouse differences in NOS2 gene expression on the brain’s redox and immune environment

Hoos, M. D., Vitek, M. P., Ridnour, L. A., Wilson, J. G., Jansen, M., Everhart, A. L., Wink, D. A., & Colton, C. A. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-50 · Cited by 35 · see citing works

Hydrogen Sulfide Oxidation: Adaptive Changes in Mitochondria of SW480 Colorectal Cancer Cells upon Exposure to Hypoxia

Malagrinò, F., Zuhra, K., Mascolo, L., Mastronicola, D., Vicente, J. B., Forte, E., & Giuffrè, A. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8102936 · Cited by 36 · see citing works

Endogenous Hemoprotein-Dependent Signaling Pathways of Nitric Oxide and Nitrite

Dent, M. R., DeMartino, A. W., Tejero, J., & Gladwin, M. T. (2021) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.1c01048 · Cited by 35 · see citing works

The multifaceted roles of sulfane sulfur species in cancer-associated processes

Zuhra, K., Tomé, C. S., Forte, E., Vicente, J. B., & Giuffrè, A. (2020) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148338 · Cited by 32 · see citing works

The human B12 trafficking protein CblC processes nitrocobalamin

Mascarenhas, R., Li, Z., Gherasim, C., Ruetz, M., & Banerjee, R. V. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014094 · Cited by 28 · see citing works

Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine β-Synthase

Carballal, S., Cuevasanta, E., Yadav, P. K., Gherasim, C., Ballou, D. P., Alvarez, B., & Banerjee, R. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.718734 · Cited by 24 · see citing works

Homocysteine, Infections, Polyamines, Oxidative Metabolism, and the Pathogenesis of Dementia and Atherosclerosis

McCully, K. S. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160549 · Cited by 22 · see citing works

A Clinically Relevant Variant of the Human Hydrogen Sulfide‐Synthesizing Enzyme Cystathionine β‐Synthase: Increased CO Reactivity as a Novel Molecular Mechanism of Pathogenicity?

Vicente, J. B., Colaço, H. G., Malagrinò, F., Santo, P. E., Gutierres, A., Bandeiras, T. M., Leandro, P., Brito, J. A., & Giuffrè, A. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/8940321 · Cited by 17 · 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

Hyperhomocysteinemia, Suppressed Immunity, and Altered Oxidative Metabolism Caused by Pathogenic Microbes in Atherosclerosis and Dementia

McCully, K. S. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00324 · Cited by 15 · see citing works

Nitric oxide dioxygenation (NOD) reactions of Co III -peroxo and Ni III -peroxo complexes: NOD versus NO activation

Yenuganti, M., Das, S. K., kulbir, K., Ghosh, S., Bhardwaj, P., Pawar, S. S., Sahoo, S. C., & Kumar, P. (2020) · Inorganic Chemistry Frontiers · doi:10.1039/d0qi01023e · Cited by 14 · see citing works

Nitric oxide monooxygenation (NOM) reaction of cobalt-nitrosyl {Co(NO)} 8 to Co II -nitrito {Co II (NO 2 − )}: base induced hydrogen gas (H 2 ) evolution

Das, S. K., kulbir, K., Ghosh, S., Sahoo, S. C., & Kumar, P. (2020) · Chemical Science · doi:10.1039/d0sc01572e · Cited by 14 · see citing works

Selective monitoring and treatment of neuroblastoma cells with hydrogen sulfide activatable phototheranostic agent

Dirak, M., Kepil, D., Almammadov, T., Elmazoğlu, Z., Cetin, S., Ozogul, N., Gunbas, G. E., & Kölemen, S. (2022) · Dyes and Pigments · doi:10.1016/j.dyepig.2022.111011 · Cited by 14 · see citing works

Overview of cysteine metabolism

Carballal, S., & Banerjee, R. V. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90219-9.00016-9 · Cited by 12 · see citing works

Disease-causing cystathionine β-synthase linker mutations impair allosteric regulation

Roman, J. V., Mascarenhas, R., Ceric, K., Ballou, D. P., & Banerjee, R. V. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105449 · Cited by 11 · see citing works

Mechanistic insights into nitric oxide oxygenation (NOO) reactions of {CrNO} 5 and {CoNO} 8

S, A. K. C., Das, S. K., kulbir, K., Bhardwaj, P., Sk, M. P., & Kumar, P. (2023) · Dalton Transactions · doi:10.1039/d3dt03177b · Cited by 6 · see citing works

Understanding the role of R266K mutation in cystathionine β-synthase (CBS) enzyme: an in silico study

Bhatt, A., & Ali, M. E. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2021.1975564 · Cited by 6 · see citing works

Heme-Thiolate Perturbation in Cystathionine β-Synthase by Mercury Compounds

Benchoam, D., Cuevasanta, E., Plana, L. J., Capece, L., Banerjee, R. V., & Álvarez, B. (2021) · ACS Omega · doi:10.1021/acsomega.0c05475 · Cited by 5 · see citing works

H2S‐induced gastric fundus smooth muscle tension potentiation is mediated by the phosphoinositide 3‐kinase/Akt/endothelial nitric oxide synthase pathway

Meng, X., Huang, X., Lu, H., Zhang, C., Kim, Y., Chen, J., & Xu, W. (2017) · Experimental Physiology · doi:10.1113/ep086288 · Cited by 4 · see citing works

Hydrogen sulfide in the brain as a silent neuroprotector in Alzheimer’s disease

Layal, H., Rajbongshi, J., Kumar, R., Pandey, S., Mishra, R., & Yadav, P. K. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.08.057 · Cited by 3 · see citing works

Structure and function of persulfide dioxygenase from Pseudomonas aeruginosa: Implications on H2S homeostasis and interplay with nitric oxide

Giordano, F., Troilo, F., Nastasi, M. R., Caruso, L., Mellini, M., Travaglini‐Allocatelli, C., Giardina, G., Vicente, J. B., Rampioni, G., Matteo, A. D., et al. (2025) · iScience · doi:10.1016/j.isci.2025.114586 · Cited by 1 · see citing works

Comparative Transcriptomics Reveals Metabolic Adaptations of Priestia megaterium BZ-95 to Different Nitrogen Sources

Jiang, H. C., Jin, Z. Y., Zhao, Y., & Ji, X. S. (2026) · Microorganisms · doi:10.3390/microorganisms14020397 · Cited by 1 · see citing works

Exploring the carbonic anhydrase-mimetic [(PMDTA) 2 ZnII2(OH − ) 2 ] 2+ for nitric oxide monooxygenation

Das, S. K., & Kumar, P. (2024) · Dalton Transactions · doi:10.1039/d4dt00407h · Cited by 1 · see citing works

Conclusion: Results support the physiological role of NO in CBS regulation. Significance: CBS may integrate the cross-talk among NO, CO, and H2S, major modulators in human (patho)physiology.

Mendes, M. I. S., Sarti, P., Leandro, P., & Giuffrè, A. (2014)

Gaseous inhibition of the transsulfuration pathway by cystathionine β-synthase

McFarlane, N. R., Gui, J., Oláh, J., & Harvey, J. N. (2024) · Physical Chemistry Chemical Physics · doi:10.1039/d4cp01321b

Human mitochondrial persulfide dioxygenase is potently and reversibly inhibited by nitric oxide

Giordano, F., Silva, D. H. P., Forte, E., Giuffrè, A., & Vicente, J. B. (2026) · Biochimie · doi:10.1016/j.biochi.2026.01.001

Nitrite Reductase Activity and Inhibition of H2S Biogenesis by Human Cystathionine

Gherasim, C., Yadav, P. K., Kabil, Ö., Niu, W.-N., & Banerjee, R. (2013)

Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine β-Synthase

Carballal, S., Cuevasanta, E., Yadav, P. K., Gherasim, C., Ballou, D. P., Alvarez, B., & Banerjee, R. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.718734 · Cited by 24 · see citing works

Conclusion: Results support the physiological role of NO in CBS regulation. Significance: CBS may integrate the cross-talk among NO, CO, and H2S, major modulators in human (patho)physiology.

Mendes, M. I. S., Sarti, P., Leandro, P., & Giuffrè, A. (2014)

NO• Binds Human Cystathionine β-Synthase Quickly and Tightly

Vicente, J. B., Colaço, H. G., Mendes, M. I. S., Sarti, P., Leandro, P., & Giuffrè, A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.507533 · Cited by 66 · see citing works

Crosstalk between gasotransmitters at the H2S-synthesizing human cystathionine β-synthase: heme-based regulation by CO and NO

Vicente, J. B., Colaço, H. G., Malagrinò, F., Santo, P. E., Gutierres, A., Bandeiras, T. M., Sarti, P., Leandro, P., Brito, J. A., & Giuffrè, A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.04.523 · Cited by 2 · see citing works