{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,26]],"date-time":"2026-10-26T20:30:02Z","timestamp":1793046602561,"version":"4.5.0"},"reference-count":68,"publisher":"Oxford University Press (OUP)","issue":"11","license":[{"start":{"date-parts":[[2011,11,1]],"date-time":"2011-11-01T00:00:00Z","timestamp":1320105600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2011,11,1]]},"abstract":"<jats:sec><jats:title>BACKGROUND<\/jats:title><jats:p>Carbamylation is a posttranslational modification of proteins resulting from the nonenzymatic reaction between isocyanic acid and specific free functional groups. This reaction alters protein structural and functional properties and thus contributes to molecular ageing. Many studies have shown the involvement of carbamylated proteins in diseases, especially in chronic renal failure and atherosclerosis.<\/jats:p><\/jats:sec><jats:sec><jats:title>CONTENT<\/jats:title><jats:p>In this review we describe the biochemical basis of the carbamylation process and its role in protein molecular ageing. We summarize the current evidence of protein carbamylation involvement in disease, identify available biomarkers of the carbamylation process and their related analytical methods, and discuss the practical relevance of these biomarkers.<\/jats:p><\/jats:sec><jats:sec><jats:title>SUMMARY<\/jats:title><jats:p>Carbamylation-induced protein alterations are involved in the progression of various diseases, because carbamylation-derived products (CDPs) are bioactive compounds that trigger specific and inappropriate cellular responses. For instance, carbamylation may promote hormone and enzyme inactivation, and carbamylated proteins, as diverse as collagen or LDLs, induce characteristic biochemical events of atherosclerosis progression. CDPs are potential biomarkers to monitor diseases characterized by an increased rate of carbamylation (e.g., chronic renal failure and atherosclerosis). Different methods (e.g., liquid chromatography\u2013tandem mass spectrometry and immunoassays) to measure specific carbamylated proteins or general markers of carbamylation, such as protein-bound homocitrulline, have been described. Their use in clinical practice must still be validated by appropriate clinical studies.<\/jats:p><\/jats:sec>","DOI":"10.1373\/clinchem.2011.163188","type":"journal-article","created":{"date-parts":[[2011,7,19]],"date-time":"2011-07-19T02:51:45Z","timestamp":1311043905000},"page":"1499-1505","source":"Crossref","is-referenced-by-count":146,"title":["Carbamylation-Derived Products: Bioactive Compounds and Potential Biomarkers in Chronic Renal Failure and Atherosclerosis"],"prefix":"10.1093","volume":"57","author":[{"given":"St\u00e9phane","family":"Jaisson","sequence":"first","affiliation":[{"name":"Laboratory of Pediatric Biology and Research and"},{"name":"Laboratory of Biochemistry and Molecular Biology, Faculty of Medicine, Reims, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christine","family":"Pietrement","sequence":"first","affiliation":[{"name":"Department of Pediatrics (Nephrology Unit), American Memorial Hospital, University Hospital of Reims, France"},{"name":"Laboratory of Biochemistry and Molecular Biology, Faculty of Medicine, Reims, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philippe","family":"Gillery","sequence":"first","affiliation":[{"name":"Laboratory of Pediatric Biology and Research and"},{"name":"Laboratory of Biochemistry and Molecular Biology, Faculty of Medicine, Reims, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2011,11,1]]},"reference":[{"key":"2020022705035194100_B1","doi-asserted-by":"crossref","first-page":"1401","DOI":"10.1373\/clinchem.2010.145201","article-title":"Evaluation of nonenzymatic posttranslational modification-derived products as biomarkers of molecular aging of proteins","volume":"56","author":"Jaisson","year":"2010","journal-title":"Clin Chem"},{"key":"2020022705035194100_B2","doi-asserted-by":"crossref","first-page":"1116","DOI":"10.1373\/clinchem.2004.034645","article-title":"The clinical chemome: a tool for the diagnosis and management of chronic disease","volume":"50","author":"Baynes","year":"2004","journal-title":"Clin Chem"},{"key":"2020022705035194100_B3","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1097\/MED.0b013e328327728d","article-title":"HbA1c: how do we measure it and what does it mean?","volume":"16","author":"Little","year":"2009","journal-title":"Curr Opin Endocrinol Diabetes Obes"},{"key":"2020022705035194100_B4","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.atherosclerosis.2007.07.025","article-title":"Receptor for advanced glycation endproducts and atherosclerosis: from basic mechanisms to clinical implications","volume":"196","author":"Basta","year":"2008","journal-title":"Atherosclerosis"},{"key":"2020022705035194100_B5","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1161\/CIRCULATIONAHA.106.621854","article-title":"Advanced glycation end products: sparking the development of diabetic vascular injury","volume":"114","author":"Goldin","year":"2006","journal-title":"Circulation"},{"key":"2020022705035194100_B6","doi-asserted-by":"crossref","first-page":"S102","DOI":"10.1046\/j.1523-1755.2001.59780102.x","article-title":"Carbamoylation of amino acids and proteins in uremia","volume":"78","author":"Kraus","year":"2001","journal-title":"Kidney Int Suppl"},{"key":"2020022705035194100_B7","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1053\/j.jrn.2007.10.014","article-title":"Novel mechanisms in accelerated atherosclerosis in kidney disease","volume":"18","author":"Shah","year":"2008","journal-title":"J Ren Nutr"},{"key":"2020022705035194100_B8","first-page":"271","article-title":"Carbamylation of glutamate dehydrogenase and other mitochondrial proteins by biosynthetic carbamyl phosphate","volume":"7","author":"Gonzalez","year":"1975","journal-title":"Physiol Chem Phys"},{"key":"2020022705035194100_B9","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/0014-5793(71)80378-2","article-title":"Homocitrulline formation following carbamylation of histones with carbamyl phosphate","volume":"16","author":"Ramponi","year":"1971","journal-title":"FEBS Lett"},{"key":"2020022705035194100_B10","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1016\/S0076-6879(67)11074-4","article-title":"Modification of proteins with cyanate","volume":"11","author":"Stark","year":"1967","journal-title":"Methods Enzymol"},{"key":"2020022705035194100_B11","unstructured":"IUPAC, Commission on Nomenclature of Organic Chemistry. 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