{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T02:31:57Z","timestamp":1791945117485,"version":"4.3.4"},"reference-count":32,"publisher":"Springer Science and Business Media LLC","issue":"4","license":[{"start":{"date-parts":[[2014,3,23]],"date-time":"2014-03-23T00:00:00Z","timestamp":1395532800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J Thromb Thrombolysis"],"published-print":{"date-parts":[[2014,11]]},"DOI":"10.1007\/s11239-014-1063-8","type":"journal-article","created":{"date-parts":[[2014,3,22]],"date-time":"2014-03-22T07:15:09Z","timestamp":1395472509000},"page":"540-545","source":"Crossref","is-referenced-by-count":18,"title":["Impact of homocysteine-thiolactone on plasma fibrin networks"],"prefix":"10.1007","volume":"38","author":[{"given":"Valeria","family":"Genoud","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana Mar\u00eda","family":"Lauricella","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luc\u00eda C.","family":"Kordich","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Irene","family":"Quintana","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2014,3,23]]},"reference":[{"key":"1063_CR1","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1055\/s-2007-994932","volume":"25","author":"SC Guba","year":"1999","unstructured":"Guba SC, Fonseca V, Fink LM (1999) Hyperhomocysteinemia and thrombosis. Semin Thromb Hemost 25:291\u2013309","journal-title":"Semin Thromb Hemost"},{"key":"1063_CR2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1182\/blood.V90.1.1","volume":"90","author":"A D'Angelo","year":"1997","unstructured":"D\u00b4Angelo A, Selhub J (1997) Homocysteine and thrombotic disease. Blood 90:1\u201311","journal-title":"Blood"},{"key":"1063_CR3","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1055\/s-2000-8472","volume":"26","author":"C Guldener Van","year":"2000","unstructured":"Van Guldener C, Stehouwer CD (2000) Hyperhomocysteinemia, vascular pathology, and endothelial dysfunction. Semin Thromb Hemost 26:281\u2013289","journal-title":"Semin Thromb Hemost"},{"key":"1063_CR4","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1007\/s00726-006-0432-9","volume":"32","author":"J Per\u0142a-Kaj\u00e1n","year":"2007","unstructured":"Per\u0142a-Kaj\u00e1n J, Twardowski T, Jakubowski H (2007) Mechanisms of homocysteine toxicity in humans. Amino Acids 32:561\u2013572","journal-title":"Amino Acids"},{"key":"1063_CR5","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1515\/CCLM.2007.038","volume":"45","author":"MM Casta\u00f1on","year":"2007","unstructured":"Casta\u00f1on MM, Lauricella AM, Kordich L, Quintana I (2007) Plasma homocysteine cutoff values for venous thrombosis. Clin Chem Lab Med 45:232\u2013236","journal-title":"Clin Chem Lab Med"},{"key":"1063_CR6","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1373\/clinchem.2003.021634","volume":"50","author":"H Refsum","year":"2004","unstructured":"Refsum H, Smith AD, Ueland PM, Nexo E, Clarke R, McPartlin J, Johnston C, Engbaek F, Schneede J, McPartlin C, Scott JM (2004) Facts and recommendations about total homocysteine determinations: an expert opinion. Clin Chem 50:3\u201332","journal-title":"Clin Chem"},{"key":"1063_CR7","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/0014-5793(93)81283-6","volume":"317","author":"H Jakubowski","year":"1993","unstructured":"Jakubowski H, Goldman E (1993) Synthesis of homocysteine thiolactone by methionyl-tRNA synthetase in cultured mammalian cells. FEBS Lett 317:237\u2013240","journal-title":"FEBS Lett"},{"key":"1063_CR8","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1055\/s-2000-8467","volume":"26","author":"HJ Blom","year":"2000","unstructured":"Blom HJ (2000) Consequences of homocysteine export and oxidation in the vascular system. Semin Thromb Hemost 26:227\u2013232","journal-title":"Semin Thromb Hemost"},{"key":"1063_CR9","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"},{"issue":"11","key":"1063_CR10","doi-asserted-by":"crossref","first-page":"1883","DOI":"10.1089\/ars.2007.1809","volume":"9","author":"AV Glushchenko","year":"2007","unstructured":"Glushchenko AV, Jacobsen DW (2007) Molecular targeting of proteins by L-homocysteine: mechanistic implications for vascular disease. Antioxid Redox Signal 9(11):1883\u20131898","journal-title":"Antioxid Redox Signal"},{"key":"1063_CR11","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":"1063_CR12","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1016\/j.cccn.2005.07.007","volume":"364","author":"X Yang","year":"2006","unstructured":"Yang X, Gao Y, Zhou J, Zhen Y, Yang Y, Wang J, Song L, Liu Y, Xu H, Chen Z, Hui R (2006) Plasma homocysteine thiolactone adducts associated with risk of coronary heart disease. Clin Chim Acta 364:230\u2013234","journal-title":"Clin Chim Acta"},{"issue":"suppl 1","key":"1063_CR13","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1111\/j.1538-7836.2007.02504.x","volume":"5","author":"JW Weisel","year":"2007","unstructured":"Weisel JW (2007) Structure of fibrin: impact on clot stability. J Thromb Haemost 5(suppl 1):116\u2013124","journal-title":"J Thromb Haemost"},{"key":"1063_CR14","doi-asserted-by":"crossref","first-page":"206","DOI":"10.2174\/187152508784871981","volume":"6","author":"M Hoffman","year":"2008","unstructured":"Hoffman M (2008) Alterations of fibrinogen structure in human disease. Cardiovasc Hematol Agents Med Chem 6:206\u2013211","journal-title":"Cardiovasc Hematol Agents Med Chem"},{"key":"1063_CR15","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1046\/j.1538-7836.2003.00053.x","volume":"1","author":"DL Sauls","year":"2003","unstructured":"Sauls DL, Wolberg AS, Hoffman M (2003) Elevated plasma homocysteine leads to alterations in fibrin clot structure and stability: implications for the mechanism of thrombosis in hyperhomocysteinemia. J Thromb Haemost 1:300\u2013306","journal-title":"J Thromb Haemost"},{"key":"1063_CR16","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/S0049-3848(02)00191-3","volume":"107","author":"AM Lauricella","year":"2002","unstructured":"Lauricella AM, Quintana IL, Kordich LC (2002) Effects of homocysteine thiol group on fibrin networks: another possible mechanism of harm. Thromb Res 107:75\u201379","journal-title":"Thromb Res"},{"key":"1063_CR17","doi-asserted-by":"crossref","first-page":"379","DOI":"10.3233\/BIR-2009-0459","volume":"46","author":"AM Rojas","year":"2009","unstructured":"Rojas AM, Kordich L, Lauricella AM (2009) Homocysteine modifies fibrin clot deformability: another possible explanation of harm. Biorheology 46:379\u2013387","journal-title":"Biorheology"},{"key":"1063_CR18","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.thromres.2009.08.013","volume":"127","author":"IL Quintana","year":"2009","unstructured":"Quintana IL, Oberholzer MV, Kordich L, Lauricella AM (2009) Impaired fibrin gel permeability by high homocysteine levels. Thromb Res 127:35\u201338","journal-title":"Thromb Res"},{"key":"1063_CR19","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1097\/01.mbc.0000220238.99843.45","volume":"17","author":"AM Lauricella","year":"2006","unstructured":"Lauricella AM, Quintana I, Casta\u00f1on M, Sassetti B, Kordich L (2006) Influence of homocysteine on fibrin network lysis. Blood Coagul Fibrinolysis 17:181\u2013186","journal-title":"Blood Coagul Fibrinolysis"},{"key":"1063_CR20","doi-asserted-by":"crossref","first-page":"186","DOI":"10.4149\/gpb_2010_02_186","volume":"29","author":"B Olas","year":"2010","unstructured":"Olas B, Kolodziejczyk J, Malinowska J (2010) May modifications of human plasma proteins stimulated by homocysteine and its thiolactone induce changes of hemostatic function of plasma in vitro? Gen Physiol Biophys 29:186\u2013193","journal-title":"Gen Physiol Biophys"},{"key":"1063_CR21","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.thromres.2010.11.027","volume":"127","author":"J Malinowska","year":"2011","unstructured":"Malinowska J, Nowak P, Olas B (2011) Comparison of the effect of homocysteine in the reduced form, its thiolactone and protein homocysteinylation on hemostatic properties of plasma. Thromb Res 127:214\u2013219","journal-title":"Thromb Res"},{"key":"1063_CR22","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1055\/s-2007-994933","volume":"25","author":"MW Mosesson","year":"1999","unstructured":"Mosesson MW (1999) Dysfibrinogenemia and thrombosis. Semin Thromb Hemost 25:311\u2013319","journal-title":"Semin Thromb Hemost"},{"key":"1063_CR23","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1097\/00001721-200209000-00008","volume":"13","author":"AS Wolberg","year":"2002","unstructured":"Wolberg AS, Gabriel DA, Hoffman M (2002) Analyzing fibrin clot structure using a microplate reader. Blood Coagul Fibrinolysis 13:533\u2013539","journal-title":"Blood Coagul Fibrinolysis"},{"key":"1063_CR24","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1097\/00001721-200112000-00003","volume":"12","author":"DA Meh","year":"2001","unstructured":"Meh DA, Mosesson MW, DiOrio JP, Siebenlist KR, Hernandez I, Amrani DL, Stojanovich L (2001) Disintegration and reorganization of fibrin networks during tissue-type plasminogen activator-induced clot lysis. Blood Coagul Fibrinolysis 12:627\u2013637","journal-title":"Blood Coagul Fibrinolysis"},{"key":"1063_CR25","doi-asserted-by":"crossref","first-page":"1354","DOI":"10.1161\/01.ATV.20.5.1354","volume":"20","author":"JP Collet","year":"2000","unstructured":"Collet JP, Park D, Lesty C, Soria J, Soria C, Montalescot G, Weisel JW (2000) Influence of fibrin network conformation and fibrin fiber diameter on fibrinolysis speed: dynamic and structural approaches by confocal microscopy. Arterioscler Thromb Vasc Biol 20:1354\u20131361","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"1063_CR26","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1055\/s-0038-1648820","volume":"72","author":"JH Wu","year":"1994","unstructured":"Wu JH, Siddiqui K, Diamond SL (1994) Transport phenomena and clot dissolving therapy: an experimental investigation of diffusion-controlled and permeation-enhanced fibrinolysis. Thromb Haemost 72:105\u2013112","journal-title":"Thromb Haemost"},{"key":"1063_CR27","doi-asserted-by":"crossref","first-page":"21331","DOI":"10.1074\/jbc.M212734200","volume":"278","author":"JP Collet","year":"2003","unstructured":"Collet JP, Lesty C, Montalescot G, Weisel JW (2003) Dynamic changes of fibrin architecture during fibrin formation and intrinsic fibrinolysis of fibrin-rich clots. J Biol Chem 278:21331\u201321335","journal-title":"J Biol Chem"},{"key":"1063_CR28","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1097\/00001721-199509000-00011","volume":"6","author":"ME Carr","year":"1995","unstructured":"Carr ME, Alving BM (1995) Effect of fibrin structure on plasmin-mediated dissolution of plasma clots. Blood Coagul Fibrinolysis 6:567\u2013573","journal-title":"Blood Coagul Fibrinolysis"},{"key":"1063_CR29","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1055\/s-0037-1613567","volume":"89","author":"K Kolev","year":"2003","unstructured":"Kolev K, Machovich R (2003) Molecular and cellular modulation of fibrinolysis. Thromb Haemost 89:610\u2013621","journal-title":"Thromb Haemost"},{"key":"1063_CR30","doi-asserted-by":"crossref","first-page":"2480","DOI":"10.1021\/bi052076j","volume":"45","author":"DL Sauls","year":"2006","unstructured":"Sauls DL, Lockhart E, Warren ME, Lenkowski A, Wilhelm SE, Hoffman M (2006) Modification of fibrinogen by homocysteine thiolactone increases resistance to fibrinolysis: a potential mechanism of the thrombotic tendency in hyperhomocysteinemia. Biochemistry 45:2480\u20132487","journal-title":"Biochemistry"},{"key":"1063_CR31","doi-asserted-by":"crossref","first-page":"1397","DOI":"10.1161\/01.ATV.0000219688.43572.75","volume":"26","author":"A Undas","year":"2006","unstructured":"Undas A, Brozek J, Jankowski M, Siudak Z, Szczeklik A, Jakubowski H (2006) Plasma homocysteine affects fibrin clot permeability and resistance to lysis in human subjects. Arterioscler Thromb Vasc Biol 26:1397\u20131404","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"1063_CR32","author":"AP Cellai","year":"2013","unstructured":"Cellai AP, Lami D, Antonucci E, Liotta AA, Rogolino A, Fedi S, Fiorillo C, Becatti M, Cenci C, Marcucci R, Abbate R, Prisco D (2013) Hyperhomocysteinemia in patients with pulmonary embolism is associated with impaired plasma fibrinolytic capacity. J Thromb Thrombolysis. doi: 10.1007\/s11239-013-0981-1","journal-title":"J Thromb Thrombolysis"}],"container-title":["Journal of Thrombosis and Thrombolysis"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11239-014-1063-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s11239-014-1063-8\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11239-014-1063-8","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,8,16]],"date-time":"2020-08-16T17:42:33Z","timestamp":1597599753000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s11239-014-1063-8"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,3,23]]},"references-count":32,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2014,11]]}},"alternative-id":["1063"],"URL":"https:\/\/doi.org\/10.1007\/s11239-014-1063-8","relation":{},"ISSN":["0929-5305","1573-742X"],"issn-type":[{"value":"0929-5305","type":"print"},{"value":"1573-742X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,3,23]]}}}