{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T22:02:01Z","timestamp":1791151321364,"version":"4.1.0"},"reference-count":74,"publisher":"Springer Science and Business Media LLC","issue":"7","license":[{"start":{"date-parts":[[2015,3,24]],"date-time":"2015-03-24T00:00:00Z","timestamp":1427155200000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Amino Acids"],"published-print":{"date-parts":[[2015,7]]},"DOI":"10.1007\/s00726-015-1956-7","type":"journal-article","created":{"date-parts":[[2015,3,23]],"date-time":"2015-03-23T14:06:07Z","timestamp":1427119567000},"page":"1319-1339","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":92,"title":["Homocysteine thiolactone and N-homocysteinylated protein induce pro-atherogenic changes in gene expression in human vascular endothelial cells"],"prefix":"10.1007","volume":"47","author":[{"given":"Dorota","family":"Gurda","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luiza","family":"Handschuh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Weronika","family":"Kotkowiak","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hieronim","family":"Jakubowski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2015,3,24]]},"reference":[{"key":"1956_CR1","doi-asserted-by":"crossref","first-page":"F1462","DOI":"10.1152\/ajprenal.00623.2013","volume":"306","author":"N Akahoshi","year":"2014","unstructured":"Akahoshi N et al (2014) Neutral aminoaciduria in cystathionine beta-synthase-deficient mice; an animal model of homocystinuria. Am J Physiol Renal Physiol 306:F1462\u2013F1476. doi: 10.1152\/ajprenal.00623.2013","journal-title":"Am J Physiol Renal Physiol"},{"key":"1956_CR2","doi-asserted-by":"crossref","first-page":"664","DOI":"10.18632\/aging.100491","volume":"4","author":"E Albertini","year":"2012","unstructured":"Albertini E, Koziel R, Durr A, Neuhaus M, Jansen-Durr P (2012) Cystathionine beta synthase modulates senescence of human endothelial cells. Aging 4:664\u2013673","journal-title":"Aging"},{"key":"1956_CR3","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1111\/j.2517-6161.1995.tb02031.x","volume":"57","author":"Y Benjamini","year":"1995","unstructured":"Benjamini Y, Hochberg Y (1995) Controlling the false discovery rate\u2014a practical and powerful approach to multiple testing. J R Stat Soc B Met 57:289\u2013300","journal-title":"J R Stat Soc B Met"},{"key":"1956_CR4","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1007\/s00109-005-0679-8","volume":"83","author":"R Castro","year":"2005","unstructured":"Castro R et al (2005) Intracellular S-adenosylhomocysteine increased levels are associated with DNA hypomethylation in HUVEC. J Mol Med 83:831\u2013836. doi: 10.1007\/s00109-005-0679-8","journal-title":"J Mol Med"},{"key":"1956_CR5","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1152\/physiolgenomics.00168.2013","volume":"46","author":"P Chaturvedi","year":"2014","unstructured":"Chaturvedi P, Kalani A, Givvimani S, Kamat PK, Familtseva A, Tyagi SC (2014) Differential regulation of DNA methylation versus histone acetylation in cardiomyocytes during HHcy in vitro and in vivo: an epigenetic mechanism. Physiol Genomics 46:245\u2013255. doi: 10.1152\/physiolgenomics.00168.2013","journal-title":"Physiol Genomics"},{"key":"1956_CR6","doi-asserted-by":"crossref","first-page":"1707","DOI":"10.1096\/fj.06-7435com","volume":"21","author":"G Chwatko","year":"2007","unstructured":"Chwatko G, Boers GH, Strauss KA, Shih DM, Jakubowski H (2007) Mutations in methylenetetrahydrofolate reductase or cystathionine beta-synthase gene, or a high-methionine diet, increase homocysteine thiolactone levels in humans and mice. Faseb J 21:1707\u20131713","journal-title":"Faseb J"},{"key":"1956_CR7","doi-asserted-by":"crossref","first-page":"9769","DOI":"10.1074\/jbc.C400557200","volume":"280","author":"MN Corradetti","year":"2005","unstructured":"Corradetti MN, Inoki K, Guan KL (2005) The stress-inducted proteins RTP801 and RTP801L are negative regulators of the mammalian target of rapamycin pathway. J Biol Chem 280:9769\u20139772. doi: 10.1074\/jbc.C400557200","journal-title":"J Biol Chem"},{"key":"1956_CR8","doi-asserted-by":"crossref","first-page":"1830","DOI":"10.1161\/01.ATV.0000142366.69080.c3","volume":"24","author":"C Cuaz-Perolin","year":"2004","unstructured":"Cuaz-Perolin C et al (2004) REDD2 gene is upregulated by modified LDL or hypoxia and mediates human macrophage cell death. Arterioscler Thromb Vasc Biol 24:1830\u20131835. doi: 10.1161\/01.ATV.0000142366.69080.c3","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"1956_CR9","doi-asserted-by":"crossref","first-page":"1596","DOI":"10.1161\/ATVBAHA.108.166421","volume":"28","author":"S Dayal","year":"2008","unstructured":"Dayal S, Lentz SR (2008) Murine models of hyperhomocysteinemia and their vascular phenotypes. Arterioscler Thromb Vasc Biol 28:1596\u20131605. doi: 10.1161\/ATVBAHA.108.166421","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"1956_CR10","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1111\/j.1538-7836.2005.01141.x","volume":"3","author":"M Heijer Den","year":"2005","unstructured":"Den Heijer M, Lewington S, Clarke R (2005) Homocysteine, MTHFR and risk of venous thrombosis: a meta-analysis of published epidemiological studies. J Thromb Haemost 3:292\u2013299. doi: 10.1111\/j.1538-7836.2005.01141.x","journal-title":"J Thromb Haemost"},{"key":"1956_CR11","doi-asserted-by":"crossref","first-page":"25506","DOI":"10.1074\/jbc.M504815200","volume":"280","author":"AM Devlin","year":"2005","unstructured":"Devlin AM, Bottiglieri T, Domann FE, Lentz SR (2005) Tissue-specific changes in H19 methylation and expression in mice with hyperhomocysteinemia. J Biol Chem 280:25506\u201325511","journal-title":"J Biol Chem"},{"key":"1956_CR12","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1074\/mcp.M900406-MCP200","volume":"9","author":"PM DiBello","year":"2010","unstructured":"DiBello PM, Dayal S, Kaveti S, Zhang D, Kinter M, Lentz SR, Jacobsen DW (2010) The nutrigenetics of hyperhomocysteinemia: quantitative proteomics reveals differences in the methionine cycle enzymes of gene-induced versus diet-induced hyperhomocysteinemia. Mol Cell Proteomics MCP 9:471\u2013485. doi: 10.1074\/mcp.M900406-MCP200","journal-title":"Mol Cell Proteomics MCP"},{"key":"1956_CR13","doi-asserted-by":"crossref","first-page":"4676","DOI":"10.1073\/pnas.0700529104","volume":"104","author":"E Dong","year":"2007","unstructured":"Dong E, Guidotti A, Grayson DR, Costa E (2007) Histone hyperacetylation induces demethylation of reelin and 67-kDa glutamic acid decarboxylase promoters. Proc Natl Acad Sci USA 104:4676\u20134681. doi: 10.1073\/pnas.0700529104","journal-title":"Proc Natl Acad Sci USA"},{"key":"1956_CR14","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":"1956_CR15","first-page":"4899","volume":"54","author":"T Fiskerstrand","year":"1994","unstructured":"Fiskerstrand T, Christensen B, Tysnes OB, Ueland PM, Refsum H (1994) Development and reversion of methionine dependence in a human glioma cell line: relation to homocysteine remethylation and cobalamin status. Cancer Res 54:4899\u20134906","journal-title":"Cancer Res"},{"key":"1956_CR16","doi-asserted-by":"crossref","first-page":"10864","DOI":"10.1074\/jbc.M313268200","volume":"279","author":"R Glowacki","year":"2004","unstructured":"Glowacki R, Jakubowski H (2004) Cross-talk between Cys34 and lysine residues in human serum albumin revealed by N-homocysteinylation. J Biol Chem 279:10864\u201310871","journal-title":"J Biol Chem"},{"key":"1956_CR17","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/S0022-2275(20)33292-2","volume":"39","author":"PJ Gough","year":"1998","unstructured":"Gough PJ, Greaves DR, Gordon S (1998) A naturally occurring isoform of the human macrophage scavenger receptor (SR-A) gene generated by alternative splicing blocks modified LDL uptake. J Lipid Res 39:531\u2013543","journal-title":"J Lipid Res"},{"key":"1956_CR18","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1016\/j.cell.2012.02.044","volume":"149","author":"JM Han","year":"2012","unstructured":"Han JM et al (2012) Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway. Cell 149:410\u2013424. doi: 10.1016\/j.cell.2012.02.044","journal-title":"Cell"},{"key":"1956_CR19","doi-asserted-by":"crossref","first-page":"2145","DOI":"10.1161\/CIRCULATIONAHA.110.956839","volume":"123","author":"DE Handy","year":"2011","unstructured":"Handy DE, Castro R, Loscalzo J (2011) Epigenetic modifications: basic mechanisms and role in cardiovascular disease. Circulation 123:2145\u20132156. doi: 10.1161\/CIRCULATIONAHA.110.956839","journal-title":"Circulation"},{"key":"1956_CR20","doi-asserted-by":"crossref","first-page":"2258","DOI":"10.1373\/clinchem.2006.074302","volume":"52","author":"GL Hortin","year":"2006","unstructured":"Hortin GL, Seam N, Hoehn GT (2006) Bound homocysteine, cysteine, and cysteinylglycine distribution between albumin and globulins. Clin Chem 52:2258\u20132264. doi: 10.1373\/clinchem.2006.074302","journal-title":"Clin Chem"},{"key":"1956_CR21","doi-asserted-by":"crossref","first-page":"1693","DOI":"10.1016\/S0140-6736(03)13372-7","volume":"361","author":"D Ingrosso","year":"2003","unstructured":"Ingrosso D et al (2003) Folate treatment and unbalanced methylation and changes of allelic expression induced by hyperhomocysteinaemia in patients with uraemia. Lancet 361:1693\u20131699","journal-title":"Lancet"},{"key":"1956_CR22","first-page":"3384","volume":"119","author":"AT Jacovina","year":"2009","unstructured":"Jacovina AT et al (2009) Homocysteine inhibits neoangiogenesis in mice through blockade of annexin A2-dependent fibrinolysis. J Clin Investig 119:3384\u20133394. doi: 10.1172\/JCI39591","journal-title":"J Clin Investig"},{"key":"1956_CR23","doi-asserted-by":"crossref","first-page":"17672","DOI":"10.1074\/jbc.270.30.17672","volume":"270","author":"H Jakubowski","year":"1995","unstructured":"Jakubowski H (1995) Proofreading in vivo. Editing of homocysteine by aminoacyl-tRNA synthetases in Escherichia coli. J Biol Chem 270:17672\u201317673","journal-title":"J Biol Chem"},{"key":"1956_CR24","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 (1997a) 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":"1956_CR25","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1007\/978-1-4615-5771-5_22","volume-title":"Homocysteine metabolism: from basic science to clinical medicine","author":"H Jakubowski","year":"1997","unstructured":"Jakubowski H (1997b) Synthesis of homocysteine thiolactone in normal and malignant cells. In: Rosenberg IH, Graham I, Ueland PM, Refsum H (eds) Homocysteine metabolism: from basic science to clinical medicine. Kluwer Academic Publishers, Norwell, pp 157\u2013165"},{"key":"1956_CR26","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":"1956_CR27","doi-asserted-by":"crossref","first-page":"3957","DOI":"10.1074\/jbc.275.6.3957","volume":"275","author":"H Jakubowski","year":"2000","unstructured":"Jakubowski H (2000) Calcium-dependent human serum homocysteine thiolactone hydrolase. A protective mechanism against protein N-homocysteinylation. J Biol Chem 275:3957\u20133962","journal-title":"J Biol Chem"},{"key":"1956_CR28","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/S0003-2697(02)00224-5","volume":"308","author":"H Jakubowski","year":"2002","unstructured":"Jakubowski H (2002a) The determination of homocysteine-thiolactone in biological samples. Anal Biochem 308:112\u2013119","journal-title":"Anal Biochem"},{"key":"1956_CR29","doi-asserted-by":"crossref","first-page":"30425","DOI":"10.1074\/jbc.C200267200","volume":"277","author":"H Jakubowski","year":"2002","unstructured":"Jakubowski H (2002b) 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":"1956_CR30","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"},{"issue":"Suppl 9","key":"1956_CR31","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":"1956_CR32","doi-asserted-by":"crossref","first-page":"149","DOI":"10.18388\/abp.2011_2259","volume":"58","author":"H Jakubowski","year":"2011","unstructured":"Jakubowski H (2011) Quality control in tRNA charging\u2014editing of homocysteine. Acta Biochim Pol 58:149\u2013163","journal-title":"Acta Biochim Pol"},{"key":"1956_CR33","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. doi: 10.1002\/wrna.122","journal-title":"Wiley Interdiscip Rev RNA"},{"key":"1956_CR34","doi-asserted-by":"crossref","DOI":"10.1007\/978-3-7091-1410-0","volume-title":"Homocysteine in protein structure\/function and human disease\u2014chemical biology of homocysteine-containing proteins","author":"H Jakubowski","year":"2013","unstructured":"Jakubowski H (2013) Homocysteine in protein structure\/function and human disease\u2014chemical biology of homocysteine-containing proteins. Springer, Wien"},{"key":"1956_CR35","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":"1956_CR36","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. doi: 10.1096\/fj.08-112086","journal-title":"Faseb J"},{"key":"1956_CR37","doi-asserted-by":"crossref","first-page":"1721","DOI":"10.1096\/fj.08-127548","volume":"23","author":"H Jakubowski","year":"2009","unstructured":"Jakubowski H et al (2009) Genetic or nutritional disorders in homocysteine or folate metabolism increase protein N-homocysteinylation in mice. Faseb J 23:1721\u20131727. doi: 10.1096\/fj.08-127548","journal-title":"Faseb J"},{"key":"1956_CR38","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1161\/01.RES.87.1.45","volume":"87","author":"H Jakubowski","year":"2000","unstructured":"Jakubowski H, Zhang L, Bardeguez A, Aviv A (2000) Homocysteine thiolactone and protein homocysteinylation in human endothelial cells: implications for atherosclerosis. Circ Res 87:45\u201351","journal-title":"Circ Res"},{"key":"1956_CR39","doi-asserted-by":"crossref","first-page":"3648","DOI":"10.1182\/blood-2007-06-096701","volume":"110","author":"MD Jamaluddin","year":"2007","unstructured":"Jamaluddin MD et al (2007) Homocysteine inhibits endothelial cell growth via DNA hypomethylation of the cyclin A gene. Blood 110:3648\u20133655. doi: 10.1182\/blood-2007-06-096701","journal-title":"Blood"},{"key":"1956_CR40","doi-asserted-by":"crossref","first-page":"3235","DOI":"10.3390\/nu5083235","volume":"5","author":"J Joseph","year":"2013","unstructured":"Joseph J, Loscalzo J (2013) Methoxistasis: integrating the roles of homocysteine and folic acid in cardiovascular pathobiology. Nutrients 5:3235\u20133256. doi: 10.3390\/nu5083235","journal-title":"Nutrients"},{"key":"1956_CR41","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1093\/cvr\/cvr250","volume":"92","author":"CS Kim","year":"2011","unstructured":"Kim CS et al (2011) Homocysteine promotes human endothelial cell dysfunction via site-specific epigenetic regulation of p66shc. Cardiovasc Res 92:466\u2013475. doi: 10.1093\/cvr\/cvr250","journal-title":"Cardiovasc Res"},{"key":"1956_CR42","doi-asserted-by":"crossref","first-page":"29659","DOI":"10.1074\/jbc.271.47.29659","volume":"271","author":"K Kokame","year":"1996","unstructured":"Kokame K, Kato H, Miyata T (1996) Homocysteine-respondent genes in vascular endothelial cells identified by differential display analysis. GRP78\/BiP and novel genes. J Biol Chem 271:29659\u201329665","journal-title":"J Biol Chem"},{"key":"1956_CR43","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.mehy.2014.11.016","volume":"84","author":"A Konieczna","year":"2015","unstructured":"Konieczna A, Szczepanska A, Sawiuk K, Lyzen R, Wegrzyn G (2015) Enzymes of the central carbon metabolism: are they linkers between transcription, DNA replication, and carcinogenesis? Med Hypotheses 84:58\u201367. doi: 10.1016\/j.mehy.2014.11.016","journal-title":"Med Hypotheses"},{"key":"1956_CR44","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":"1956_CR45","doi-asserted-by":"crossref","first-page":"31994","DOI":"10.1074\/jbc.M112.355172","volume":"287","author":"KN Maclean","year":"2012","unstructured":"Maclean KN et al (2012) Cystathionine protects against endoplasmic reticulum stress-induced lipid accumulation, tissue injury, and apoptotic cell death. J Biol Chem 287:31994\u201332005. doi: 10.1074\/jbc.M112.355172","journal-title":"J Biol Chem"},{"key":"1956_CR46","first-page":"1","volume":"37","author":"SH Mudd","year":"1985","unstructured":"Mudd SH et al (1985) The natural history of homocystinuria due to cystathionine beta-synthase deficiency. Am J Hum Genet 37:1\u201331","journal-title":"Am J Hum Genet"},{"key":"1956_CR47","unstructured":"Mudd SH, Levy HL, Kraus JP (2001) Disorders of transsulfuration. In: Scriver CR, Beaudet AL, Sly WS, Valle D, Childs B, Kinzler KW, Vogelstein B (eds) The metabolic and molecular bases of inherited disease,\u00a0vol 2, 8th edn. Mc Graw-Hill, New York, pp 2007\u20132056"},{"key":"1956_CR48","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1038\/emboj.2008.308","volume":"28","author":"S Nada","year":"2009","unstructured":"Nada S, Hondo A, Kasai A, Koike M, Saito K, Uchiyama Y, Okada M (2009) The novel lipid raft adaptor p 18 controls endosome dynamics by anchoring the MEK-ERK pathway to late endosomes. EMBO J 28:477\u2013489. doi: 10.1038\/emboj.2008.308","journal-title":"EMBO J"},{"key":"1956_CR49","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1016\/j.biopha.2008.04.001","volume":"62","author":"J Perla-Kajan","year":"2008","unstructured":"Perla-Kajan J et al (2008) Immunohistochemical detection of N-homocysteinylated proteins in humans and mice. Biomed Pharmacother 62:473\u2013479. doi: 10.1016\/j.biopha.2008.04.001","journal-title":"Biomed Pharmacother"},{"key":"1956_CR50","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1007\/s00726-006-0432-9","volume":"32","author":"J Perla-Kajan","year":"2007","unstructured":"Perla-Kajan J, Twardowski T, Jakubowski H (2007) Mechanisms of homocysteine toxicity in humans. Amino Acids 32:561\u2013572","journal-title":"Amino Acids"},{"key":"1956_CR51","doi-asserted-by":"crossref","first-page":"79","DOI":"10.2478\/v10019-010-0022-z","volume":"44","author":"N Plazar","year":"2010","unstructured":"Plazar N, Jurdana M (2010) Hyperhomocysteinemia and the role of B vitamins in cancer. Radiol Oncol 44:79\u201385. doi: 10.2478\/v10019-010-0022-z","journal-title":"Radiol Oncol"},{"key":"1956_CR52","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.brainres.2008.07.077","volume":"1237","author":"IP Pogribny","year":"2008","unstructured":"Pogribny IP, Karpf AR, James SR, Melnyk S, Han T, Tryndyak VP (2008) Epigenetic alterations in the brains of Fisher 344 rats induced by long-term administration of folate\/methyl-deficient diet. Brain Res 1237:25\u201334. doi: 10.1016\/j.brainres.2008.07.077","journal-title":"Brain Res"},{"key":"1956_CR53","doi-asserted-by":"crossref","first-page":"1731S","DOI":"10.1093\/jn\/136.6.1731S","volume":"136","author":"H Refsum","year":"2006","unstructured":"Refsum H et al (2006) The Hordaland Homocysteine Study: a community-based study of homocysteine, its determinants, and associations with disease. J Nutr 136:1731S\u20131740S","journal-title":"J Nutr"},{"key":"1956_CR54","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":"1956_CR55","author":"DL Sauls","year":"2011","unstructured":"Sauls DL, Warren M, Hoffman M (2011) Homocysteinylated fibrinogen forms disulfide-linked complexes with albumin. Thromb Res. doi: 10.1016\/j.thromres.2011.01.009","journal-title":"Thromb Res"},{"key":"1956_CR56","doi-asserted-by":"crossref","first-page":"573","DOI":"10.18388\/abp.2011_2227","volume":"58","author":"MT Schmidt","year":"2011","unstructured":"Schmidt MT, Handschuh L, Zyprych J, Szabelska A, Olejnik-Schmidt AK, Siatkowski I, Figlerowicz M (2011) Impact of DNA microarray data transformation on gene expression analysis\u2014comparison of two normalization methods. Acta Biochim Pol 58:573\u2013580","journal-title":"Acta Biochim Pol"},{"key":"1956_CR57","doi-asserted-by":"crossref","first-page":"1593","DOI":"10.1056\/NEJMoa011364","volume":"345","author":"G Schnyder","year":"2001","unstructured":"Schnyder G et al (2001) Decreased rate of coronary restenosis after lowering of plasma homocysteine levels. N Engl J Med 345:1593\u20131600. doi: 10.1056\/NEJMoa011364","journal-title":"N Engl J Med"},{"key":"1956_CR58","doi-asserted-by":"crossref","first-page":"30111","DOI":"10.1074\/jbc.M104324200","volume":"276","author":"S Sengupta","year":"2001","unstructured":"Sengupta S et al (2001) Albumin thiolate anion is an intermediate in the formation of albumin-S-S-homocysteine. J Biol Chem 276:30111\u201330117","journal-title":"J Biol Chem"},{"key":"1956_CR59","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/1476-511X-5-1","volume":"5","author":"P Sharma","year":"2006","unstructured":"Sharma P, Senthilkumar RD, Brahmachari V, Sundaramoorthy E, Mahajan A, Sharma A, Sengupta S (2006) Mining literature for a comprehensive pathway analysis: a case study for retrieval of homocysteine related genes for genetic and epigenetic studies. Lipids Health Dis 5:1. doi: 10.1186\/1476-511X-5-1","journal-title":"Lipids Health Dis"},{"key":"1956_CR60","doi-asserted-by":"crossref","first-page":"1858","DOI":"10.1099\/mic.0.026609-0","volume":"155","author":"M Sikora","year":"2009","unstructured":"Sikora M, Jakubowski H (2009) Homocysteine editing and growth inhibition in Escherichia coli. Microbiology 155:1858\u20131865. doi: 10.1099\/mic.0.026609-0","journal-title":"Microbiology"},{"key":"1956_CR01","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. doi: 10.1007\/s00726-013-1617-7","journal-title":"Amino Acids"},{"key":"1956_CR61","unstructured":"Smyth GK (2004) Linear models and empirical bayes methods for assessing differential expression in microarray experiments. Stat Appl Genet Mol Biol 3: Article 3. doi: 10.102202\/1544-61151027"},{"key":"1956_CR62","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S1046-2023(03)00155-5","volume":"31","author":"GK Smyth","year":"2003","unstructured":"Smyth GK, Speed T (2003) Normalization of cDNA microarray data. Methods 31:265\u2013273","journal-title":"Methods"},{"key":"1956_CR63","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.ymgme.2007.02.012","volume":"91","author":"KA Strauss","year":"2007","unstructured":"Strauss KA et al (2007) Prevention of brain disease from severe 5, 10-methylenetetrahydrofolate reductase deficiency. Mol Genet Metab 91:165\u2013175","journal-title":"Mol Genet Metab"},{"key":"1956_CR64","doi-asserted-by":"crossref","first-page":"713","DOI":"10.3233\/JAD-132033","volume":"40","author":"J Suszynska-Zajczyk","year":"2014","unstructured":"Suszynska-Zajczyk J, Luczak M, Marczak L, Jakubowski H (2014a) Hyperhomocysteinemia and bleomycin hydrolase modulate the expression of mouse brain proteins involved in neurodegeneration. J Alzheimers Dis 40:713\u2013726. doi: 10.3233\/JAD-132033","journal-title":"J Alzheimers Dis"},{"key":"1956_CR65","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1016\/j.ymgme.2014.07.011","volume":"113","author":"J Suszynska-Zajczyk","year":"2014","unstructured":"Suszynska-Zajczyk J, Sikora M, Jakubowski H (2014b) Paraoxonase 1 deficiency and hyperhomocysteinemia alter the expression of mouse kidney proteins involved in renal disease. Mol Genet Metab 113:200\u2013206. doi: 10.1016\/j.ymgme.2014.07.011","journal-title":"Mol Genet Metab"},{"key":"1956_CR66","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/j.ymgme.2014.05.010","volume":"112","author":"J Suszynska-Zajczyk","year":"2014","unstructured":"Suszynska-Zajczyk J, Utyro O, Jakubowski H (2014c) Methionine-induced hyperhomocysteinemia and bleomycin hydrolase deficiency alter the expression of mouse kidney proteins involved in renal disease. Mol Genet Metab 112:339\u2013346. doi: 10.1016\/j.ymgme.2014.05.010","journal-title":"Mol Genet Metab"},{"key":"1956_CR67","doi-asserted-by":"crossref","first-page":"1471","DOI":"10.1007\/s00726-014-1712-4","volume":"46","author":"J Suszynska-Zajczyk","year":"2014","unstructured":"Suszynska-Zajczyk J, Wroblewski J, Utyro O, Luczak M, Marczak L, Jakubowski H (2014d) Bleomycin hydrolase and hyperhomocysteinemia modulate the expression of mouse proteins involved in liver homeostasis. Amino Acids 46:1471\u20131480. doi: 10.1007\/s00726-014-1712-4","journal-title":"Amino Acids"},{"key":"1956_CR68","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1038\/nature09270","volume":"466","author":"TM Teslovich","year":"2010","unstructured":"Teslovich TM et al (2010) Biological, clinical and population relevance of 95 loci for blood lipids. Nature 466:707\u2013713. doi: 10.1038\/nature09270","journal-title":"Nature"},{"key":"1956_CR69","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1038\/nrm3890","volume":"15","author":"P Tessarz","year":"2014","unstructured":"Tessarz P, Kouzarides T (2014) Histone core modifications regulating nucleosome structure and dynamics. Nat Rev Mol Cell Biol 15:703\u2013708. doi: 10.1038\/nrm3890","journal-title":"Nat Rev Mol Cell Biol"},{"key":"1956_CR70","doi-asserted-by":"crossref","first-page":"1263","DOI":"10.1172\/JCI11596","volume":"107","author":"GH Werstuck","year":"2001","unstructured":"Werstuck GH et al (2001) Homocysteine-induced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways. J Clin Invest 107:1263\u20131273","journal-title":"J Clin Invest"},{"key":"1956_CR71","doi-asserted-by":"crossref","first-page":"e1004214","DOI":"10.1371\/journal.pgen.1004214","volume":"10","author":"SR Williams","year":"2014","unstructured":"Williams SR et al (2014) Genome-wide meta-analysis of homocysteine and methionine metabolism identifies five one carbon metabolism loci and a novel association of ALDH1L1 with ischemic stroke. PLoS Genet 10:e1004214. doi: 10.1371\/journal.pgen.1004214","journal-title":"PLoS Genet"},{"key":"1956_CR72","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1089\/dna.2007.0619","volume":"26","author":"J Yi-Deng","year":"2007","unstructured":"Yi-Deng J, Tao S, Hui-Ping Z, Jian-Tuan X, Jun C, Gui-Zhong L, Shu-Ren W (2007) Folate and ApoE DNA methylation induced by homocysteine in human monocytes. DNA Cell Biol 26:737\u2013744. doi: 10.1089\/dna.2007.0619","journal-title":"DNA Cell Biol"},{"key":"1956_CR73","author":"JY Zhao","year":"2012","unstructured":"Zhao JY et al (2012) A functional variant in the cystathionine beta-synthase gene promoter significantly reduces congenital heart disease susceptibility in a Han Chinese population. Cell Res. doi: 10.1038\/cr.2012.135","journal-title":"Cell Res"}],"container-title":["Amino Acids"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s00726-015-1956-7.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s00726-015-1956-7\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s00726-015-1956-7","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,7]],"date-time":"2024-06-07T23:55:14Z","timestamp":1717804514000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s00726-015-1956-7"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,3,24]]},"references-count":74,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2015,7]]}},"alternative-id":["1956"],"URL":"https:\/\/doi.org\/10.1007\/s00726-015-1956-7","relation":{},"ISSN":["0939-4451","1438-2199"],"issn-type":[{"value":"0939-4451","type":"print"},{"value":"1438-2199","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,3,24]]}}}