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Sulfur-containing amino acids are metabolically linked by interacting pathways that impact the one-carbon metabolic cycle and generation of methyl groups, the folate cycle, and maintenance of the major cellular redox buffer; glutathione. Dysregulation of these pathways is associated with diverse pathologies, notably of the cardiovascular (CV) system, which are typically characterized by inappropriate plasma levels of sulfur-containing amino acids.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Recent Advances:<\/jats:title>\n                    <jats:p>\n                      Perhaps not surprisingly, the cellular redox state has emerged as a major regulator of many enzymatic processes within these metabolic cycles. The metabolism of cysteine can also result in the production of hydrogen sulfide (H\n                      <jats:sub>2<\/jats:sub>\n                      S), a signaling molecule whose activity is potentially linked to intracellular levels of both reactive oxygen species (ROS) and molecular oxygen.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Critical Issues:<\/jats:title>\n                    <jats:p>In most cases, the endogenous physiological sources of ROS that might mediate the interlinked metabolic pathways of sulfur-containing biomolecules remain unknown. However, the family of NADPH oxidases, and Nox4 in particular, is emerging as a likely candidate.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Future Directions:<\/jats:title>\n                    <jats:p>This review focuses on the current knowledge of key aspects of sulfur metabolism, which are regulated by redox-based chemical reactions, and the likely intracellular oxidant sources that might mediate this regulation. This knowledge will be important to guide future targeted therapeutic interventions in diverse CV disorders.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1089\/ars.2017.7224","type":"journal-article","created":{"date-parts":[[2017,6,29]],"date-time":"2017-06-29T11:01:44Z","timestamp":1498734104000},"page":"972-991","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":18,"title":["Redox-Dependent Regulation of Sulfur Metabolism in Biomolecules: Implications for Cardiovascular Health"],"prefix":"10.1177","volume":"30","author":[{"given":"Rajesh K.","family":"Mistry","sequence":"first","affiliation":[{"name":"Department of Cardiology, BHF Centre of Research Excellence, King's College London, London, United Kingdom."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alison C.","family":"Brewer","sequence":"additional","affiliation":[{"name":"Department of Cardiology, BHF Centre of Research Excellence, King's College London, London, United Kingdom."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"179","published-online":{"date-parts":[[2019,1,25]]},"reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1523\/JNEUROSCI.16-03-01066.1996"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0004032"},{"key":"e_1_3_2_4_2","first-page":"509","article-title":"Methionine adenosyltransferase, cystathionine beta-synthase and cystathionine gamma-lyase activity of rat liver subcellular particles, human blood cells and mixed white cells from rat bone marrow","volume":"48","author":"Allsop J","year":"1975","unstructured":"Allsop J, and Watts RW. 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