{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,11]],"date-time":"2026-06-11T21:05:05Z","timestamp":1781211905613,"version":"3.54.1"},"reference-count":31,"publisher":"Springer Science and Business Media LLC","issue":"1-2","license":[{"start":{"date-parts":[[2017,11,29]],"date-time":"2017-11-29T00:00:00Z","timestamp":1511913600000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/501100004564","name":"Ministarstvo Prosvete, Nauke i Tehnolo\u0161kog Razvoja","doi-asserted-by":"publisher","award":["175043"],"award-info":[{"award-number":["175043"]}],"id":[{"id":"10.13039\/501100004564","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004564","name":"Ministarstvo Prosvete, Nauke i Tehnolo\u0161kog Razvoja","doi-asserted-by":"publisher","award":["173040"],"award-info":[{"award-number":["173040"]}],"id":[{"id":"10.13039\/501100004564","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Cell Biochem"],"published-print":{"date-parts":[[2018,7]]},"DOI":"10.1007\/s11010-017-3238-z","type":"journal-article","created":{"date-parts":[[2017,11,29]],"date-time":"2017-11-29T08:35:54Z","timestamp":1511944554000},"page":"143-148","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Effects of homocysteine and its related compounds on oxygen consumption of the rat heart tissue homogenate: the role of different gasotransmitters"],"prefix":"10.1007","volume":"444","author":[{"given":"Jovana Jakovljevi\u0107","family":"Uzelac","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marina","family":"Stani\u0107","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Danijela","family":"Krsti\u0107","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mirjana","family":"\u010colovi\u0107","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dragan","family":"Djuri\u0107","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2017,11,29]]},"reference":[{"key":"3238_CR1","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1583\/08-2385.1","volume":"15","author":"HM Heneghan","year":"2008","unstructured":"Heneghan HM, Sultan S (2008) Homocysteine, the cholesterol of the 21st century. Impact of hyperhomocysteinemia on patency and amputation-free survival after intervention for critical limb ischemia. J Endovasc Ther 15:399\u2013407","journal-title":"J Endovasc Ther"},{"key":"3238_CR2","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1358\/dot.2003.39.3.799452","volume":"39","author":"ED Kaplan","year":"2003","unstructured":"Kaplan ED (2003) Association between homocyst(e)ine levels and risk of vascular events. Drugs Today 39:175\u2013192","journal-title":"Drugs Today"},{"key":"3238_CR3","doi-asserted-by":"crossref","first-page":"2015","DOI":"10.1001\/jama.288.16.2015","volume":"288","author":"Homocysteine Studies C","year":"2002","unstructured":"Homocysteine Studies C (2002) Homocysteine and risk of ischemic heart disease and stroke: a meta-analysis. JAMA 288:2015\u20132022","journal-title":"JAMA"},{"key":"3238_CR4","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.biopha.2003.11.005","volume":"58","author":"DM Townsend","year":"2004","unstructured":"Townsend DM, Tew KD, Tapiero H (2004) Sulfur containing amino acids and human disease. Biomed Pharmacother 58:47\u201355","journal-title":"Biomed Pharmacother"},{"key":"3238_CR5","doi-asserted-by":"crossref","first-page":"1935","DOI":"10.1016\/S0021-9258(19)67504-6","volume":"272","author":"H Jakubowski","year":"1997","unstructured":"Jakubowski H (1997) Metabolism of homocysteine thiolactone in human cell cultures. Possible mechanism for pathological consequences of elevated homocysteine levels. J Biol Chem 272:1935\u20131942","journal-title":"J Biol Chem"},{"key":"3238_CR6","doi-asserted-by":"crossref","first-page":"4071","DOI":"10.1096\/fj.08-112086","volume":"22","author":"H Jakubowski","year":"2008","unstructured":"Jakubowski H, Boers GH, Strauss KA (2008) Mutations in cystathionine beta-synthase or methylenetetrahydrofolate reductase gene increase N-homocysteinylated protein levels in humans. FASEB J 22:4071\u20134076","journal-title":"FASEB J"},{"key":"3238_CR7","doi-asserted-by":"crossref","first-page":"2277","DOI":"10.1096\/fasebj.13.15.2277","volume":"13","author":"H Jakubowski","year":"1999","unstructured":"Jakubowski H (1999) Protein homocysteinylation: possible mechanism underlying pathological consequences of elevated homocysteine levels. FASEB J 13:2277\u20132283","journal-title":"FASEB J"},{"key":"3238_CR8","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1007\/s11010-009-0040-6","volume":"327","author":"A Rasic-Markovic","year":"2009","unstructured":"Rasic-Markovic A, Stanojlovic O, Hrncic D, Krstic D, Colovic M, Susic V et al (2009) The activity of erythrocyte and brain Na+\/K+ and Mg2+-ATPases in rats subjected to acute homocysteine and homocysteine thiolactone administration. Mol Cell Biochem 327:39\u201345","journal-title":"Mol Cell Biochem"},{"key":"3238_CR9","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1172\/JCI108520","volume":"58","author":"LA Harker","year":"1976","unstructured":"Harker LA, Ross R, Slichter SJ, Scott CR (1976) Homocystine-induced arteriosclerosis. The role of endothelial cell injury and platelet response in its genesis. J Clin Investig 58:731\u2013741","journal-title":"J Clin Investig"},{"key":"3238_CR10","doi-asserted-by":"crossref","first-page":"1340","DOI":"10.1016\/S0022-3565(24)36716-3","volume":"281","author":"M Flesch","year":"1997","unstructured":"Flesch M, Kilter H, Cremers B, Lenz O, Sudkamp M, Kuhn-Regnier F et al (1997) Acute effects of nitric oxide and cyclic GMP on human myocardial contractility. J Pharmacol Exp Ther 281:1340\u20131349","journal-title":"J Pharmacol Exp Ther"},{"key":"3238_CR11","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1023\/A:1011453809750","volume":"6","author":"WJ Paulus","year":"2001","unstructured":"Paulus WJ (2001) The role of nitric oxide in the failing heart. Heart Fail Rev 6:105\u2013118","journal-title":"Heart Fail Rev"},{"key":"3238_CR12","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1038\/sj.bjp.0706906","volume":"149","author":"MY Ali","year":"2006","unstructured":"Ali MY, Ping CY, Mok YY, Ling L, Whiteman M, Bhatia M et al (2006) Regulation of vascular nitric oxide in vitro and in vivo; a new role for endogenous hydrogen sulphide? Br J Pharmacol 149:625\u2013634","journal-title":"Br J Pharmacol"},{"key":"3238_CR13","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1080\/10715760701263265","volume":"41","author":"H Laggner","year":"2007","unstructured":"Laggner H, Muellner MK, Schreier S, Sturm B, Hermann M, Exner M et al (2007) Hydrogen sulphide: a novel physiological inhibitor of LDL atherogenic modification by HOCl. Free Radic Res 41:741\u2013747","journal-title":"Free Radic Res"},{"key":"3238_CR14","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1111\/j.1471-4159.2004.02617.x","volume":"90","author":"M Whiteman","year":"2004","unstructured":"Whiteman M, Armstrong JS, Chu SH, Jia-Ling S, Wong BS, Cheung NS et al (2004) The novel neuromodulator hydrogen sulfide: an endogenous peroxynitrite \u2018scavenger\u2019? J Neurochem 90:765\u2013768","journal-title":"J Neurochem"},{"key":"3238_CR15","doi-asserted-by":"crossref","first-page":"794","DOI":"10.1016\/j.bbrc.2004.11.110","volume":"326","author":"M Whiteman","year":"2005","unstructured":"Whiteman M, Cheung NS, Zhu YZ, Chu SH, Siau JL, Wong BS et al (2005) Hydrogen sulphide: a novel inhibitor of hypochlorous acid-mediated oxidative damage in the brain? Biochem Biophys Res Commun 326:794\u2013798","journal-title":"Biochem Biophys Res Commun"},{"key":"3238_CR16","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/j.bbrc.2006.02.154","volume":"343","author":"M Whiteman","year":"2006","unstructured":"Whiteman M, Li L, Kostetski I, Chu SH, Siau JL, Bhatia M et al (2006) Evidence for the formation of a novel nitrosothiol from the gaseous mediators nitric oxide and hydrogen sulphide. Biochem Biophys Res Commun 343:303\u2013310","journal-title":"Biochem Biophys Res Commun"},{"key":"3238_CR17","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1097\/CRD.0b013e31819d813a","volume":"17","author":"SJ Peterson","year":"2009","unstructured":"Peterson SJ, Frishman WH, Abraham NG (2009) Targeting heme oxygenase: therapeutic implications for diseases of the cardiovascular system. Cardiol Rev 17:99\u2013111","journal-title":"Cardiol Rev"},{"key":"3238_CR18","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1007\/s00134-008-1010-2","volume":"34","author":"M Bauer","year":"2008","unstructured":"Bauer M, Huse K, Settmacher U, Claus RA (2008) The heme oxygenase-carbon monoxide system: regulation and role in stress response and organ failure. Intensive Care Med 34:640\u2013648","journal-title":"Intensive Care Med"},{"key":"3238_CR19","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1016\/j.mito.2011.05.006","volume":"11","author":"A Pecinov\u00e1","year":"2011","unstructured":"Pecinov\u00e1 A, Drahota Z, N\u016fskov\u00e1 H, Pecina P, Hou\u0161t\u011bk J (2011) Evaluation of basic mitochondrial functions using rat tissue homogenates. Mitochondrion 11:722\u2013728","journal-title":"Mitochondrion"},{"key":"3238_CR20","doi-asserted-by":"crossref","first-page":"30808","DOI":"10.1074\/jbc.273.46.30808","volume":"273","author":"RC Austin","year":"1998","unstructured":"Austin RC, Sood SK, Dorward AM, Singh G, Shaughnessy SG, Pamidi S, Outinen PA, Weitz JI (1998) Homocysteine-dependent alterations in mitochondrial gene expression, function and structure. J Biol Chem. 273:30808\u201330817","journal-title":"J Biol Chem"},{"key":"3238_CR21","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1155\/2013\/318471","volume":"2013","author":"V Zivkovic","year":"2013","unstructured":"Zivkovic V, Jakovljevic V, Pechanova O, Srejovic I, Joksimovic J, Selakovic D et al (2013) Effects of dl-homocysteine thiolactone on cardiac contractility, coronary flow, and oxidative stress markers in the isolated rat heart: the role of different gasotransmitters. Biomed Res Int. 2013:318\u2013471","journal-title":"Biomed Res Int"},{"key":"3238_CR22","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1016\/j.resmic.2013.03.002","volume":"164","author":"M Stanic","year":"2013","unstructured":"Stanic M, Zakrzewska J, Hadzibrahimovic M, Zizic M, Markovic Z, Vucinic Z et al (2013) Oxygen regulation of alternative respiration in fungus Phycomyces blakesleeanus: connection with phosphate metabolism. Res Microbiol 164:770\u2013778","journal-title":"Res Microbiol"},{"key":"3238_CR23","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0021-9258(19)52451-6","volume":"193","author":"OH Lowry","year":"1951","unstructured":"Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193:265\u2013275","journal-title":"J Biol Chem"},{"issue":"Suppl 9","key":"3238_CR24","first-page":"155","volume":"59","author":"H Jakubowski","year":"2008","unstructured":"Jakubowski H (2008) The pathophysiological hypothesis of homocysteine thiolactone-mediated vascular disease. J Physiol Pharmacol 59(Suppl 9):155\u2013167","journal-title":"J Physiol Pharmacol"},{"key":"3238_CR25","doi-asserted-by":"crossref","first-page":"1704","DOI":"10.1515\/CCLM.2007.338","volume":"45","author":"H Jakubowski","year":"2007","unstructured":"Jakubowski H (2007) The molecular basis of homocysteine thiolactone-mediated vascular disease. Clin Chem Lab Med 45:1704\u20131716","journal-title":"Clin Chem Lab Med"},{"key":"3238_CR26","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1046\/j.1432-1327.1999.00249.x","volume":"261","author":"S Dopner","year":"1999","unstructured":"Dopner S, Hildebrandt P, Rosell FI, Mauk AG, von Walter M, Buse G et al (1999) The structural and functional role of lysine residues in the binding domain of cytochrome c in the electron transfer to cytochrome c oxidase. Eur J Biochem 261:379\u2013391","journal-title":"Eur J Biochem"},{"key":"3238_CR27","doi-asserted-by":"crossref","first-page":"6225","DOI":"10.1021\/bi602463m","volume":"46","author":"J Perla-Kajan","year":"2007","unstructured":"Perla-Kajan J, Marczak L, Kajan L, Skowronek P, Twardowski T, Jakubowski H (2007) Modification by homocysteine thiolactone affects redox status of cytochrome C. Biochemistry 46:6225\u20136231","journal-title":"Biochemistry"},{"issue":"1\u20132","key":"3238_CR28","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1007\/s11010-012-1398-4","volume":"370","author":"V Zivkovic","year":"2012","unstructured":"Zivkovic V, Jakovljevic V, Djordjevic D, Vuletic M, Barudzic N, Djuric D (2012) The effects of homocysteine-related compounds on cardiac contractility, coronary flow, and oxidative stress markers in isolated rat heart. Mol Cell Biochem 370(1\u20132):59\u201367","journal-title":"Mol Cell Biochem"},{"key":"3238_CR29","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/BJ20081386","volume":"417","author":"MP Murphy","year":"2009","unstructured":"Murphy MP (2009) How mitochondria produce reactive oxygen species. Biochem J 417:1\u201313","journal-title":"Biochem J"},{"key":"3238_CR30","doi-asserted-by":"crossref","first-page":"1182","DOI":"10.1161\/01.ATV.20.5.1182","volume":"20","author":"DW Jacobsen","year":"2000","unstructured":"Jacobsen DW (2000) Hyperhomocysteinemia and oxidative stress: time for a reality check? Arterioscler Thromb Vasc Biol 20:1182\u20131184","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"3238_CR31","doi-asserted-by":"crossref","first-page":"1906","DOI":"10.1074\/jbc.M107256200","volume":"277","author":"CC Winterbourn","year":"2002","unstructured":"Winterbourn CC, Peskin AV, Parsons-Mair HN (2002) Thiol oxidase activity of copper, zinc superoxide dismutase. J Biol Chem 277:1906\u20131911","journal-title":"J Biol Chem"}],"container-title":["Molecular and Cellular Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s11010-017-3238-z\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11010-017-3238-z.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11010-017-3238-z.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,6,27]],"date-time":"2025-06-27T19:40:27Z","timestamp":1751053227000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s11010-017-3238-z"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,11,29]]},"references-count":31,"journal-issue":{"issue":"1-2","published-print":{"date-parts":[[2018,7]]}},"alternative-id":["3238"],"URL":"https:\/\/doi.org\/10.1007\/s11010-017-3238-z","relation":{},"ISSN":["0300-8177","1573-4919"],"issn-type":[{"value":"0300-8177","type":"print"},{"value":"1573-4919","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,11,29]]}}}