{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T03:50:55Z","timestamp":1777521055685,"version":"3.51.4"},"reference-count":38,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2017,10,26]],"date-time":"2017-10-26T00:00:00Z","timestamp":1508976000000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/501100005363","name":"Universidad de Buenos Aires","doi-asserted-by":"publisher","award":["UBACYT 20020130100741BA"],"award-info":[{"award-number":["UBACYT 20020130100741BA"]}],"id":[{"id":"10.13039\/501100005363","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005363","name":"Universidad de Buenos Aires","doi-asserted-by":"publisher","award":["UBACYT 20020130100212"],"award-info":[{"award-number":["UBACYT 20020130100212"]}],"id":[{"id":"10.13039\/501100005363","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002923","name":"Consejo Nacional de Investigaciones Cient\u00edficas y T\u00e9cnicas","doi-asserted-by":"publisher","award":["PIP 11220110100653"],"award-info":[{"award-number":["PIP 11220110100653"]}],"id":[{"id":"10.13039\/501100002923","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["J Thromb Thrombolysis"],"published-print":{"date-parts":[[2018,1]]},"DOI":"10.1007\/s11239-017-1574-1","type":"journal-article","created":{"date-parts":[[2017,10,26]],"date-time":"2017-10-26T12:21:48Z","timestamp":1509020508000},"page":"66-76","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Structural changes of fibrinogen molecule mediated by the N-homocysteinylation reaction"],"prefix":"10.1007","volume":"45","author":[{"given":"Valeria","family":"Genoud","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paula G.","family":"Quintana","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Silvana","family":"Gionco","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alicia","family":"Baldessari","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Irene","family":"Quintana","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2017,10,26]]},"reference":[{"key":"1574_CR1","doi-asserted-by":"crossref","first-page":"1646","DOI":"10.1111\/j.1538-7836.2005.01364.x","volume":"3","author":"SR Lentz","year":"2005","unstructured":"Lentz SR (2005) Mechanisms of homocysteine-induced atherothrombosis. J Thromb Haemost 3:1646\u20131654","journal-title":"J Thromb Haemost"},{"key":"1574_CR2","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.1007\/s00726-015-1956-7","volume":"47","author":"D Gurda","year":"2015","unstructured":"Gurda D, Handschuh L, Kotkowiak W, Jakubowski H (2015) Homocysteine thiolactone and N-homocysteinylated protein induce pro-atherogenic changes in gene expression in human vascular endothelial cells. Amino Acids 47:1319\u20131339","journal-title":"Amino Acids"},{"key":"1574_CR3","doi-asserted-by":"crossref","first-page":"2239","DOI":"10.1016\/j.bbagen.2015.08.013","volume":"1850","author":"GS Sharma","year":"2015","unstructured":"Sharma GS, Kumar T, Dar TA, Singh LR (2015) Protein N-homocysteinylation: from cellular toxicity to neurodegeneration. Biochim Biophys Acta 1850:2239\u20132245","journal-title":"Biochim Biophys Acta"},{"key":"1574_CR4","doi-asserted-by":"crossref","first-page":"1582","DOI":"10.1016\/S0021-9258(17)35979-3","volume":"261","author":"JD Finkelstein","year":"1986","unstructured":"Finkelstein JD, Martin JJ (1986) Methionine metabolism in mammals. Adaptation to methionine excess. J Biol Chem 261:1582\u20131587","journal-title":"J Biol Chem"},{"key":"1574_CR5","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1002\/wrna.122","volume":"3","author":"H Jakubowski","year":"2012","unstructured":"Jakubowski H (2012) Quality control in tRNA charging. Wiley Interdiscip Rev RNA 3:295\u2013310","journal-title":"Wiley Interdiscip Rev RNA"},{"key":"1574_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":"1574_CR7","doi-asserted-by":"crossref","first-page":"331","DOI":"10.7326\/0003-4819-131-5-199909070-00003","volume":"131","author":"J Selhub","year":"1999","unstructured":"Selhub J (1999) Serum total homocysteine concentrations in the third national health and nutrition examination survey (1991\u20131994): population reference ranges AND contribution of vitamin status to high serum concentrations. Ann Intern Med 131:331\u2013339","journal-title":"Ann Intern Med"},{"key":"1574_CR8","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":"1574_CR9","doi-asserted-by":"crossref","first-page":"1764","DOI":"10.1093\/clinchem\/39.9.1764","volume":"39","author":"PM Ueland","year":"1993","unstructured":"Ueland PM, Refsum H, Stabler SP, Malinow MR, Andersson A, Allen RH (1993) Total homocysteine in plasma or serum: methods and clinical applications. Clin Chem 39:1764\u20131779","journal-title":"Clin Chem"},{"key":"1574_CR10","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":"1574_CR11","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":"1574_CR12","doi-asserted-by":"crossref","first-page":"20313","DOI":"10.1074\/jbc.272.33.20313","volume":"272","author":"BS Berlett","year":"1997","unstructured":"Berlett BS, Stadtman ER (1997) Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 272:20313\u201320316","journal-title":"J Biol Chem"},{"key":"1574_CR13","doi-asserted-by":"crossref","first-page":"4003","DOI":"10.1073\/pnas.0307446101","volume":"101","author":"R Radi","year":"2004","unstructured":"Radi R (2004) Nitric oxide, oxidants, and protein tyrosine nitration. Proc Natl Acad Sci USA 101:4003\u20134008","journal-title":"Proc Natl Acad Sci USA"},{"key":"1574_CR14","first-page":"19","volume":"124","author":"H Vlassara","year":"1994","unstructured":"Vlassara H (1994) Recent progress on the biologic and clinical significance of advanced glycosylation end products. J Lab Clin Med 124:19\u201330","journal-title":"J Lab Clin Med"},{"key":"1574_CR15","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1007\/s10930-013-9540-z","volume":"33","author":"V Genoud","year":"2014","unstructured":"Genoud V, Casta\u00f1on M, Lauricella AM, Quintana I (2014) Characterization of N-homocysteinylated albumin adducts. Protein J 33:85\u201391","journal-title":"Protein J"},{"key":"1574_CR16","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.ab.2008.05.049","volume":"380","author":"H Jakubowski","year":"2008","unstructured":"Jakubowski H (2008) New method for the determination of protein N-linked homocysteine. Anal Biochem 380:257\u2013261","journal-title":"Anal Biochem"},{"key":"1574_CR17","doi-asserted-by":"crossref","first-page":"30425","DOI":"10.1074\/jbc.C200267200","volume":"277","author":"H Jakubowski","year":"2002","unstructured":"Jakubowski H (2002) Homocysteine is a protein amino acid in humans: implications for homocysteine-linked disease. J Biol Chem 277:30425\u201330428","journal-title":"J Biol Chem"},{"key":"1574_CR18","first-page":"16365","volume":"136","author":"J Brosnan","year":"2006","unstructured":"Brosnan J, Brosnan M (2006) Pathophysiological consequences of homocysteine excess, 5th amino acid assessment workshop. J Nutr 136:16365\u201316405","journal-title":"J Nutr"},{"key":"1574_CR19","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"},{"key":"1574_CR20","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":"1574_CR21","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1007\/s00726-013-1617-7","volume":"46","author":"M Sikora","year":"2014","unstructured":"Sikora M, Marczak L, Kubalska J, Graban A, Jakubowski H (2014) Identification of N-homocysteinylation sites in plasma proteins. Amino Acids 46:235\u2013244","journal-title":"Amino Acids"},{"key":"1574_CR22","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":"1574_CR23","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/0003-9861(59)90090-6","volume":"82","author":"GL Ellman","year":"1959","unstructured":"Ellman GL (1959) Tissue sulfhydryl groups. Arch Biochem Biophys 82:70\u201377","journal-title":"Arch Biochem Biophys"},{"key":"1574_CR24","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","volume":"227","author":"UK Laemmli","year":"1970","unstructured":"Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680\u2013685","journal-title":"Nature"},{"key":"1574_CR25","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/0005-2795(72)90262-0","volume":"257","author":"J Mcdonagh","year":"1972","unstructured":"Mcdonagh J, Messel H, Mcdonagh RP, Murano G, Blomback AB (1972) Molecular weight analysis of fibrinogen and fibrin chains by an improved sodium dodecyl sulfate gel electrophoresis method. Biochim Biophys Acta 257:135\u2013142","journal-title":"Biochim Biophys Acta"},{"key":"1574_CR26","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0049-3848(96)00111-9","volume":"83","author":"B Blomb\u00e4ck","year":"1996","unstructured":"Blomb\u00e4ck B (1996) Fibrinogen and fibrin\u2014proteins with complex roles in hemostasis and thrombosis. Thromb Res 83:1\u201375","journal-title":"Thromb Res"},{"key":"1574_CR27","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1016\/0021-9673(91)80095-X","volume":"559","author":"M Zhu","year":"1991","unstructured":"Zhu M, Rodriguez R, Wehr T (1991) Optimizing separation parameters in capillary isoelectric focusing. J Chromatogr A 559:479\u2013488","journal-title":"J Chromatogr A"},{"key":"1574_CR28","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1055\/s-0038-1646157","volume":"70","author":"AH Henschen","year":"1993","unstructured":"Henschen AH (1993) Human fibrinogen-structural variants and functional sites. Thromb Haemost 70:42\u201347","journal-title":"Thromb Haemost"},{"key":"1574_CR29","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":"1574_CR30","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1016\/0003-2697(66)90209-0","volume":"17","author":"JA Uerre","year":"1966","unstructured":"Uerre JA, Miller CH (1966) Preparation of L-homocysteine from L-homocysteine thiolactone. Anal Biochem 17:310\u2013315","journal-title":"Anal Biochem"},{"key":"1574_CR31","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/0006-2944(82)90027-8","volume":"27","author":"NP Dudman","year":"1982","unstructured":"Dudman NP, Wilcken DE (1982) Homocysteine thiolactone and experimental homocysteinemia. Biochem Med 27:244\u2013253","journal-title":"Biochem Med"},{"key":"1574_CR32","doi-asserted-by":"crossref","first-page":"22485","DOI":"10.1074\/jbc.M603656200","volume":"281","author":"J Zimny","year":"2006","unstructured":"Zimny J, Sikora M, Guranowski A, Jakubowski H (2006) Protective mechanisms against homocysteine toxicity: the role of bleomycin hydrolase. J Biol Chem 281:22485\u201322492","journal-title":"J Biol Chem"},{"key":"1574_CR33","doi-asserted-by":"crossref","first-page":"1177","DOI":"10.3233\/JAD-2010-1311","volume":"19","author":"J Suszynska","year":"2010","unstructured":"Suszynska J, Tisonczyk J, Lee H, Smith MA, Jakubowski H (2010) Reduced homocysteine-thiolactonase activity in Alzheimer\u2019s disease. J Alzheimer\u2019s Dis 19:1177\u20131183","journal-title":"J Alzheimer\u2019s Dis"},{"key":"1574_CR34","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) Cell biology and metabolism: metabolism of homocysteine thiolactone in human cell cultures : possible mechanism for pathological consequences of elevated metabolism of homocysteine thiolactone in human cell cultures. J Biol Chem 272:1935\u20131942","journal-title":"J Biol Chem"},{"key":"1574_CR35","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1161\/01.ATV.11.3.663","volume":"11","author":"NPB Dudman","year":"1991","unstructured":"Dudman NPB, Hicks C, Lynch JF, Wilcken DEL, Wang J (1991) Homocysteine thiolactone disposal by human arterial endothelial cells and serum in vitro. Arterioscler Thromb 11:663\u2013670","journal-title":"Arterioscler Thromb"},{"key":"1574_CR36","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1002\/rcm.681","volume":"16","author":"CE Hop","year":"2002","unstructured":"Hop CE, Bakhtiar R (2002) Homocysteine thiolactone and protein homocysteinylation: mechanistic studies with model peptides and proteins. Rapid Commun Mass Spectrom 16:1049\u20131053","journal-title":"Rapid Commun Mass Spectrom"},{"key":"1574_CR37","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/j.ab.2004.11.035","volume":"337","author":"G Chwatko","year":"2005","unstructured":"Chwatko G, Jakubowski H (2005) The determination of homocysteine-thiolactone in human plasma. Anal Biochem 337:271\u2013277","journal-title":"Anal Biochem"},{"key":"1574_CR38","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1007\/s11239-014-1063-8","volume":"38","author":"V Genoud","year":"2014","unstructured":"Genoud V, Lauricella AM, Kordich LC, Quintana I (2014) Impact of homocysteine-thiolactone on plasma fibrin networks. J Thromb Thrombolysis 38:540\u2013545","journal-title":"J Thromb Thrombolysis"}],"container-title":["Journal of Thrombosis and Thrombolysis"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s11239-017-1574-1\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11239-017-1574-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11239-017-1574-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,8,5]],"date-time":"2022-08-05T15:03:44Z","timestamp":1659711824000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s11239-017-1574-1"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,10,26]]},"references-count":38,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2018,1]]}},"alternative-id":["1574"],"URL":"https:\/\/doi.org\/10.1007\/s11239-017-1574-1","relation":{},"ISSN":["0929-5305","1573-742X"],"issn-type":[{"value":"0929-5305","type":"print"},{"value":"1573-742X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,10,26]]}}}