{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T20:29:53Z","timestamp":1791318593652,"version":"4.3.1"},"reference-count":128,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2014,11,1]],"date-time":"2014-11-01T00:00:00Z","timestamp":1414800000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2014,11,1]],"date-time":"2014-11-01T00:00:00Z","timestamp":1414800000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"name":"National Kidney Foundation Young Investigator"},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["K24 DK094872"],"award-info":[{"award-number":["K24 DK094872"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000011","name":"Howard Hughes Medical Institute","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000011","id-type":"DOI","asserted-by":"publisher"}]},{"name":"American Diabetes Association Junior Faculty Award"}],"content-domain":{"domain":["ajkd.org","clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["American Journal of Kidney Diseases"],"published-print":{"date-parts":[[2014,11]]},"DOI":"10.1053\/j.ajkd.2014.04.034","type":"journal-article","created":{"date-parts":[[2014,7,16]],"date-time":"2014-07-16T07:16:30Z","timestamp":1405494990000},"page":"793-803","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":122,"title":["Protein Carbamylation in Kidney Disease: Pathogenesis and Clinical Implications"],"prefix":"10.1053","volume":"64","clinical-trial-number":[{"clinical-trial-number":"nct01612429","registry":"10.18810\/clinical-trials-gov"}],"author":[{"given":"Sahir","family":"Kalim","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S. Ananth","family":"Karumanchi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ravi I.","family":"Thadhani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anders H.","family":"Berg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1053\/j.ajkd.2014.04.034_bib1","doi-asserted-by":"crossref","first-page":"1927","DOI":"10.2215\/CJN.04310413","article-title":"Carbamylation of serum albumin and erythropoietin resistance in end stage kidney disease","volume":"8","author":"Kalim","year":"2013","journal-title":"Clin J Am Soc Nephrol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib2","doi-asserted-by":"crossref","first-page":"175ra29","DOI":"10.1126\/scitranslmed.3005218","article-title":"Carbamylation of serum albumin as a risk factor for mortality in patients with kidney failure","volume":"5","author":"Berg","year":"2013","journal-title":"Sci Transl Med"},{"key":"10.1053\/j.ajkd.2014.04.034_bib3","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1002\/andp.18280870206","article-title":"Ueber k\u00fcnstliche Bildung des Harnstoffs","volume":"87","author":"W\u00f6hler","year":"1828","journal-title":"Ann Phys"},{"key":"10.1053\/j.ajkd.2014.04.034_bib4","first-page":"746","article-title":"Transformation of ammonium cyanate into urea","volume":"67","author":"Walker","year":"1895","journal-title":"J\u00a0Chem Soc"},{"key":"10.1053\/j.ajkd.2014.04.034_bib5","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1007\/BF02174423","article-title":"Cyanate","volume":"5","author":"Shutz","year":"1949","journal-title":"Experientia"},{"key":"10.1053\/j.ajkd.2014.04.034_bib6","doi-asserted-by":"crossref","first-page":"3177","DOI":"10.1016\/S0021-9258(20)81332-5","article-title":"Reaction of the cyanate present in aqueous urea with amino acids and proteins","volume":"235","author":"Stark","year":"1960","journal-title":"J\u00a0Biol Chem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib7","doi-asserted-by":"crossref","first-page":"1411","DOI":"10.1016\/S0021-9258(18)91330-X","article-title":"On the reversible reaction of cyanate with sulfhydryl groups and the determination of NH2-terminal cysteine and cystine in proteins","volume":"239","author":"Stark","year":"1964","journal-title":"J\u00a0Biol Chem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib8","doi-asserted-by":"crossref","first-page":"1030","DOI":"10.1021\/bi00882a008","article-title":"Reactions of cyanate with functional groups of proteins. 3. Reactions with amino and carboxyl groups","volume":"4","author":"Stark","year":"1965","journal-title":"Biochemistry"},{"key":"10.1053\/j.ajkd.2014.04.034_bib9","doi-asserted-by":"crossref","first-page":"1382","DOI":"10.1021\/ja01198a042","article-title":"Synthesis of orotic acid from aspartic acid","volume":"69","author":"Nyc","year":"1947","journal-title":"J\u00a0Am Chem Soc"},{"key":"10.1053\/j.ajkd.2014.04.034_bib10","doi-asserted-by":"crossref","first-page":"1579","DOI":"10.1016\/S0021-9258(18)96131-4","article-title":"Carbamylation of amino and tyrosine hydroxyl groups. Preparation of an inhibitor of oxytocin with no intrinsic activity on the isolated uterus","volume":"242","author":"Smyth","year":"1967","journal-title":"J\u00a0Biol Chem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib11","doi-asserted-by":"crossref","first-page":"3033","DOI":"10.1093\/ndt\/gfn342","article-title":"\u2018O\u2019, erythropoietin carbamoylation versus carbamylation","volume":"23","author":"Jelkmann","year":"2008","journal-title":"Nephrol Dial Transplant"},{"key":"10.1053\/j.ajkd.2014.04.034_bib12","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1373\/clinchem.2011.163188","article-title":"Carbamylation-derived products: bioactive compounds and potential biomarkers in chronic kidney failure and atherosclerosis","volume":"57","author":"Jaisson","year":"2011","journal-title":"Clin Chem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib13","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/S0076-6879(72)25057-1","article-title":"Modification of proteins with cyanate","volume":"25","author":"Stark","year":"1972","journal-title":"Methods Enzymol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib14","doi-asserted-by":"crossref","first-page":"3679","DOI":"10.1021\/jo062586z","article-title":"Nucleophilicities of primary and secondary amines in water","volume":"72","author":"Brotzel","year":"2007","journal-title":"J\u00a0Org Chem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib15","doi-asserted-by":"crossref","first-page":"e82655","DOI":"10.1371\/journal.pone.0082655","article-title":"Endogenous carbamylation of kidney medullary proteins","volume":"8","author":"Claxton","year":"2014","journal-title":"PLoS One"},{"key":"10.1053\/j.ajkd.2014.04.034_bib16","series-title":"The Urea Cycle","first-page":"501","article-title":"Physiological and clinical implications of protein carbamylation","author":"Carreras","year":"1976"},{"key":"10.1053\/j.ajkd.2014.04.034_bib17","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1042\/bj0420628","article-title":"The isomeric transformation of urea into ammonium cyanate in aqueous solutions","volume":"42","author":"Dirnhuber","year":"1948","journal-title":"Biochem J"},{"key":"10.1053\/j.ajkd.2014.04.034_bib18","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":"10.1053\/j.ajkd.2014.04.034_bib19","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1093\/clinchem\/42.3.482","article-title":"Plasma cyanate concentrations in chronic kidney failure","volume":"42","author":"Nilsson","year":"1996","journal-title":"Clin Chem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib20","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/S0022-2143(98)90143-3","article-title":"Essential carbamoyl-amino acids formed in\u00a0vivo in patients with end-stage kidney disease managed by continuous ambulatory peritoneal dialysis: isolation, identification, and quantitation","volume":"131","author":"Kraus","year":"1998","journal-title":"J\u00a0Lab Clin Med"},{"key":"10.1053\/j.ajkd.2014.04.034_bib21","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/0003-2697(71)90094-7","article-title":"Gel isoelectric focusing for following the successive carbamylations of amino groups in chymotrypsinogen A","volume":"40","author":"Bobb","year":"1971","journal-title":"Anal Biochem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib22","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/0006-291X(68)90425-7","article-title":"Enzyme regulation by substrate; rapid inactivation of glutamate dehydrogenase by carbamyl phosphate","volume":"32","author":"Grisolia","year":"1968","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1053\/j.ajkd.2014.04.034_bib23","doi-asserted-by":"crossref","first-page":"3566","DOI":"10.1016\/S0021-9258(19)34178-X","article-title":"Carbamylation of pepsinogen and pepsin","volume":"243","author":"Rimon","year":"1968","journal-title":"J\u00a0Biol Chem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib24","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.chembiol.2005.11.005","article-title":"Impact of carbamylation on type I collagen conformational structure and its ability to activate human polymorphonuclear neutrophils","volume":"13","author":"Jaisson","year":"2006","journal-title":"Chem Biol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib25","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1016\/j.matbio.2006.10.008","article-title":"Carbamylation differentially alters type I collagen sensitivity to various collagenases","volume":"26","author":"Jaisson","year":"2007","journal-title":"Matrix Biol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib26","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1159\/000014403","article-title":"Impaired biological activity of erythropoietin by cyanate carbamylation","volume":"18","author":"Mun","year":"2000","journal-title":"Blood Purif"},{"key":"10.1053\/j.ajkd.2014.04.034_bib27","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1126\/science.1098313","article-title":"Derivatives of erythropoietin that are tissue protective but not erythropoietic","volume":"305","author":"Leist","year":"2004","journal-title":"Science"},{"key":"10.1053\/j.ajkd.2014.04.034_bib28","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1080\/00365590310006291","article-title":"Inhibition of erythropoietin activity by cyanate","volume":"38","author":"Park","year":"2004","journal-title":"Scand J Urol Nephrol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib29","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1111\/j.1365-2796.2008.02024.x","article-title":"Erythropoietin-mediated tissue protection: reducing collateral damage from the primary injury response","volume":"264","author":"Brines","year":"2008","journal-title":"J\u00a0Intern Med"},{"key":"10.1053\/j.ajkd.2014.04.034_bib30","first-page":"605","article-title":"Modifications du point isoelectrique de la chaine-alpha de l'hemoglobine sous l'action de l'uree, du cyanate de sodium, de l'anhydride succinique ou de l'anhydride diethylene triamine pentaacetique","volume":"46","author":"Legendre","year":"1998","journal-title":"Pathol Biol (Paris)"},{"key":"10.1053\/j.ajkd.2014.04.034_bib31","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1111\/j.1399-3011.1981.tb02039.x","article-title":"Modification of lysine 69 reactivity in bovine growth hormone by carbamylation of its N-terminal\u00a0group","volume":"18","author":"Nowicki","year":"1981","journal-title":"Int J Pept Protein Res"},{"key":"10.1053\/j.ajkd.2014.04.034_bib32","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1016\/S0014-4835(87)80067-2","article-title":"High-molecular-weight crystallin aggregate formation resulting from non-enzymic carbamylation of lens crystallins: relevance to cataract formation","volume":"45","author":"Beswick","year":"1987","journal-title":"Exp Eye Res"},{"key":"10.1053\/j.ajkd.2014.04.034_bib33","first-page":"807","article-title":"Changes in protein stability upon chemical modification of lysine residues of bovine serum albumin by different reagents","volume":"31","author":"Fazili","year":"1993","journal-title":"Biochem Mol Biol Int"},{"key":"10.1053\/j.ajkd.2014.04.034_bib34","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1016\/S0021-9258(18)51734-8","article-title":"Inactivation of chymotrypsin by cyanate","volume":"239","author":"Shaw","year":"1964","journal-title":"J\u00a0Biol Chem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib35","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1172\/JCI106845","article-title":"The effects of cyanate in\u00a0vitro on red blood cell metabolism and function in sickle cell anemia","volume":"51","author":"De Furia","year":"1972","journal-title":"J\u00a0Clin Invest"},{"key":"10.1053\/j.ajkd.2014.04.034_bib36","doi-asserted-by":"crossref","first-page":"2107","DOI":"10.1093\/clinchem\/32.11.2107a","article-title":"Carbamylation of apo-aspartate aminotransferase: a possible mechanism for enzyme inactivation in uremic patients","volume":"32","author":"Van Lente","year":"1986","journal-title":"Clin Chem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib37","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1016\/S0021-9258(19)45671-8","article-title":"Inactivation of bovine glutamate dehydrogenase by carbamyl phosphate and cyanate","volume":"247","author":"Veronese","year":"1972","journal-title":"J\u00a0Biol Chem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib38","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1159\/000184303","article-title":"Carbamylation of insulin and its biological activity","volume":"46","author":"Oimomi","year":"1987","journal-title":"Nephron"},{"key":"10.1053\/j.ajkd.2014.04.034_bib39","doi-asserted-by":"crossref","first-page":"9053","DOI":"10.1016\/S0021-9258(17)34284-9","article-title":"Role of lysine residues of plasma lipoproteins in high affinity binding to cell surface receptors on human fibroblasts","volume":"253","author":"Weisgraber","year":"1978","journal-title":"J\u00a0Biol Chem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib40","doi-asserted-by":"crossref","first-page":"4570","DOI":"10.1016\/S0021-9258(19)69473-1","article-title":"Allosteric properties of carbamylated hemoglobins","volume":"256","author":"Lee","year":"1981","journal-title":"J\u00a0Biol Chem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib41","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1007\/BF02285090","article-title":"Albumin binding in uraemia: quantitative assessment of inhibition by endogenous ligands and carbamylation of albumin","volume":"43","author":"Dengler","year":"1992","journal-title":"Eur J Clin Pharmacol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib42","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1038\/clpt.1980.87","article-title":"Plasma protein carbamylation and decreased acidic drug protein binding in uremia","volume":"27","author":"Erill","year":"1980","journal-title":"Clin Pharmacol Ther"},{"key":"10.1053\/j.ajkd.2014.04.034_bib43","first-page":"275","article-title":"Carbamylated albumin stimulates microRNA-146, which is increased in human kidney cell carcinoma","volume":"3","author":"Ha","year":"2010","journal-title":"Mol Med Rep"},{"key":"10.1053\/j.ajkd.2014.04.034_bib44","doi-asserted-by":"crossref","first-page":"1509","DOI":"10.1016\/j.febslet.2007.03.008","article-title":"Carbamylated albumin is a potent inhibitor of polymorphonuclear neutrophil respiratory burst","volume":"581","author":"Jaisson","year":"2007","journal-title":"FEBS Lett"},{"key":"10.1053\/j.ajkd.2014.04.034_bib45","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1681\/ASN.V72275","article-title":"Urea induces the heat shock response in human neuroblastoma cells","volume":"7","author":"Maddock","year":"1996","journal-title":"J\u00a0Am Soc Nephrol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib46","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1046\/j.1523-1755.1998.00777.x","article-title":"Carbamylated hemoglobin and carbamylated plasma protein in hemodialyzed patients","volume":"53","author":"Balion","year":"1998","journal-title":"Kidney Int"},{"key":"10.1053\/j.ajkd.2014.04.034_bib47","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1182\/blood.V47.6.909.909","article-title":"Decreased life span and membrane damage of carbamylated erythrocytes in\u00a0vitro","volume":"47","author":"Lane","year":"1976","journal-title":"Blood"},{"key":"10.1053\/j.ajkd.2014.04.034_bib48","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/S0014-5793(04)00233-9","article-title":"Enhanced activation of and increased production of matrix metalloproteinase-9\u00a0by\u00a0human blood monocytes upon adhering to carbamylated collagen","volume":"563","author":"Garnotel","year":"2004","journal-title":"FEBS Lett"},{"key":"10.1053\/j.ajkd.2014.04.034_bib49","doi-asserted-by":"crossref","first-page":"F476","DOI":"10.1152\/ajprenal.00342.2010","article-title":"Glycated and carbamylated albumin is more \u201cnephrotoxic\u201d than unmodified albumin in the amphibian kidney","volume":"301","author":"Gross","year":"2011","journal-title":"Am J Physiol Kidney Physiol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib50","doi-asserted-by":"crossref","first-page":"e82506","DOI":"10.1371\/journal.pone.0082506","article-title":"Chronic increase of urea leads to carbamylated proteins accumulation in tissues in a mouse model of CKD","volume":"8","author":"Pietrement","year":"2013","journal-title":"PloS One"},{"key":"10.1053\/j.ajkd.2014.04.034_bib51","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.semnephrol.2005.09.006","article-title":"Amino acid and protein kinetics in kidney failure: an integrated approach","volume":"26","author":"Raj","year":"2006","journal-title":"Semin Nephrol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib52","first-page":"77","article-title":"Etiology of the protein-energy wasting syndrome in chronic kidney disease: a consensus statement from the International Society of Kidney Nutrition and Metabolism (ISRNM)","volume":"23","author":"Carrero","year":"2013","journal-title":"J\u00a0Ren Nutr"},{"key":"10.1053\/j.ajkd.2014.04.034_bib53","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1038\/nrneph.2011.60","article-title":"Diets and enteral supplements for improving outcomes in chronic kidney disease","volume":"7","author":"Kalantar-Zadeh","year":"2011","journal-title":"Nat Rev Nephrol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib54","doi-asserted-by":"crossref","first-page":"772","DOI":"10.1016\/j.biochi.2011.01.007","article-title":"S-Carbamoylation impairs the oxidant scavenging activity of cysteine: its possible impact on increased LDL modification in uraemia","volume":"93","author":"Schreier","year":"2011","journal-title":"Biochimie"},{"key":"10.1053\/j.ajkd.2014.04.034_bib55","doi-asserted-by":"crossref","first-page":"1601","DOI":"10.1177\/0960327110394225","article-title":"The effect of uremic toxin cyanate (OCN\u2212) on anaerobic sulfur metabolism and prooxidative processes in the rat kidney: a protective role of lipoate","volume":"30","author":"Iciek","year":"2010","journal-title":"Hum Exp Toxicol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib56","doi-asserted-by":"crossref","first-page":"473","DOI":"10.3109\/15376516.2011.556155","article-title":"The effect of the uremic toxin cyanate (CNO(-)) on anaerobic cysteine metabolism and oxidative processes in the rat liver: a protective effect of lipoate","volume":"21","author":"Sokolowska","year":"2011","journal-title":"Toxicol Mech Methods"},{"key":"10.1053\/j.ajkd.2014.04.034_bib57","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1016\/j.freeradbiomed.2010.11.029","article-title":"Cysteine\/cystine redox signaling in cardiovascular disease","volume":"50","author":"Go","year":"2012","journal-title":"Free Radic Biol Med"},{"key":"10.1053\/j.ajkd.2014.04.034_bib58","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1007\/s11255-011-9905-1","article-title":"Total, free, and protein-bound thiols in plasma of peritoneal dialysis and predialysis patients","volume":"43","author":"Przemyslaw","year":"2011","journal-title":"Int Urol Nephrol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib59","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1080\/00365510410002869","article-title":"Protein thiol oxidation and lipid peroxidation in patients with uraemia","volume":"64","author":"Prakash","year":"2004","journal-title":"Scand J Clin Lab Invest"},{"key":"10.1053\/j.ajkd.2014.04.034_bib60","doi-asserted-by":"crossref","first-page":"2571","DOI":"10.1046\/j.1523-1755.2000.00443.x","article-title":"Plasma protein thiol oxidation and carbonyl formation in chronic kidney failure","volume":"58","author":"Himmelfarb","year":"2000","journal-title":"Kidney Int"},{"key":"10.1053\/j.ajkd.2014.04.034_bib61","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.mcna.2011.11.005","article-title":"Atherosclerosis in chronic kidney disease: lessons learned from glycation in diabetes","volume":"96","author":"Mohar","year":"2012","journal-title":"Med Clin North Am"},{"key":"10.1053\/j.ajkd.2014.04.034_bib62","doi-asserted-by":"crossref","first-page":"1176","DOI":"10.1038\/nm1637","article-title":"Protein carbamylation links inflammation, smoking, uremia and atherogenesis","volume":"13","author":"Wang","year":"2007","journal-title":"Nat Med"},{"key":"10.1053\/j.ajkd.2014.04.034_bib63","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/0026-0495(93)90030-R","article-title":"Catabolism of low-density lipoprotein is altered in experimental chronic kidney failure","volume":"42","author":"Shapiro","year":"1993","journal-title":"Metabolism"},{"key":"10.1053\/j.ajkd.2014.04.034_bib64","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1038\/ki.1992.179","article-title":"Carbamylation-induced alterations in low-density lipoprotein metabolism","volume":"41","author":"Horkko","year":"1992","journal-title":"Kidney Int"},{"key":"10.1053\/j.ajkd.2014.04.034_bib65","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1111\/j.1365-2362.1994.tb00974.x","article-title":"Decreased clearance of uraemic and mildly carbamylated low-density lipoprotein","volume":"24","author":"Horkko","year":"1994","journal-title":"Eur J Clin Invest"},{"key":"10.1053\/j.ajkd.2014.04.034_bib66","doi-asserted-by":"crossref","first-page":"1732","DOI":"10.1038\/ki.1995.239","article-title":"Decreased clearance of low-density lipoprotein in uremic patients under dialysis treatment","volume":"47","author":"Horkko","year":"1995","journal-title":"Kidney Int"},{"key":"10.1053\/j.ajkd.2014.04.034_bib67","doi-asserted-by":"crossref","first-page":"1852","DOI":"10.1681\/ASN.2010040365","article-title":"Chronic uremia stimulates LDL carbamylation and atherosclerosis","volume":"21","author":"Apostolov","year":"2010","journal-title":"J\u00a0Am Soc Nephrol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib68","first-page":"65","article-title":"Novel mechanisms in accelerated atherosclerosis in kidney disease","volume":"18","author":"Shah","year":"2008","journal-title":"J\u00a0Ren Nutr"},{"key":"10.1053\/j.ajkd.2014.04.034_bib69","doi-asserted-by":"crossref","first-page":"1622","DOI":"10.1161\/ATVBAHA.109.189795","article-title":"Scavenger receptors of endothelial cells mediate the uptake and cellular proatherogenic effects of carbamylated LDL","volume":"29","author":"Apostolov","year":"2009","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib70","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1161\/01.ATV.0000258795.75121.8a","article-title":"Carbamylated low-density lipoprotein induces monocyte adhesion to endothelial cells through intercellular adhesion molecule-1 and vascular cell adhesion molecule-1","volume":"27","author":"Apostolov","year":"2007","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib71","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1111\/j.1523-1755.2005.00391.x","article-title":"Carbamylated low-density lipoprotein induces death of endothelial cells: a link to atherosclerosis in patients with kidney disease","volume":"68","author":"Ok","year":"2005","journal-title":"Kidney Int"},{"key":"10.1053\/j.ajkd.2014.04.034_bib72","doi-asserted-by":"crossref","first-page":"H1836","DOI":"10.1152\/ajpheart.01079.2006","article-title":"Modified LDLs induce proliferation-mediated death of human vascular endothelial cells through MAPK pathway","volume":"292","author":"Apostolov","year":"2007","journal-title":"Am J Physiol Heart Circ Physiol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib73","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1111\/j.1440-1797.2008.00948.x","article-title":"Carbamylated low-density lipoprotein induces proliferation and increases adhesion molecule expression of human coronary artery smooth muscle cells","volume":"13","author":"Asci","year":"2008","journal-title":"Nephrology (Carlton)"},{"key":"10.1053\/j.ajkd.2014.04.034_bib74","doi-asserted-by":"crossref","first-page":"2337","DOI":"10.1089\/ars.2010.3640","article-title":"Protein carbamylation renders high-density lipoprotein dysfunctional","volume":"14","author":"Holzer","year":"2011","journal-title":"Antioxid Redox Signal"},{"key":"10.1053\/j.ajkd.2014.04.034_bib75","doi-asserted-by":"crossref","first-page":"F989","DOI":"10.1152\/ajprenal.2001.280.6.F989","article-title":"Uremic levels of urea inhibit L-arginine transport in cultured endothelial cells","volume":"280","author":"Xiao","year":"2001","journal-title":"Am J Physiol Kidney Physiol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib76","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1089\/ars.2011.4090","article-title":"Cyanate is a novel inducer of endothelial ICAM-1 expression","volume":"16","author":"El-Gamal","year":"2011","journal-title":"Antioxid Redox Signal"},{"key":"10.1053\/j.ajkd.2014.04.034_bib77","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1681\/ASN.2012030254","article-title":"Protein carbamylation predicts mortality in ESRD","volume":"24","author":"Koeth","year":"2013","journal-title":"J\u00a0Am Soc Nephrol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib78","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1093\/milmed\/137.6.215","article-title":"Sickle cell disease: clinical advances by the Murayama molecular hypothesis","volume":"137","author":"Nalbandian","year":"1972","journal-title":"Mil Med"},{"key":"10.1053\/j.ajkd.2014.04.034_bib79","doi-asserted-by":"crossref","first-page":"752","DOI":"10.1056\/NEJM197810052991405","article-title":"Sickle-cell anemia: molecular and cellular bases of therapeutic approaches (first of three parts)","volume":"299","author":"Dean","year":"1978","journal-title":"N\u00a0Engl J Med"},{"key":"10.1053\/j.ajkd.2014.04.034_bib80","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1093\/clinchem\/18.9.961","article-title":"Urea, urease, cyanate, and the sickling of hemoglobin S","volume":"18","author":"Nalbandian","year":"1972","journal-title":"Clin Chem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib81","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1056\/NEJM197403212901204","article-title":"Sodium cyanate as a potential treatment for sickle-cell disease","volume":"290","author":"Gillette","year":"1974","journal-title":"N\u00a0Engl J Med"},{"key":"10.1053\/j.ajkd.2014.04.034_bib82","first-page":"157","article-title":"Clinical evaluation of cyanate in sickle cell anemia","volume":"9","author":"Harkness","year":"1975","journal-title":"Prog Hematol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib83","doi-asserted-by":"crossref","first-page":"6611","DOI":"10.1016\/S0021-9258(19)42200-X","article-title":"Studies on the mechanism of action of cyanate in sickle cell disease. Oxygen affinity and gelling properties of hemoglobin S carbamylated on specific chains","volume":"249","author":"Nigen","year":"1974","journal-title":"J\u00a0Biol Chem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib84","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1001\/archopht.1976.03910030465005","article-title":"Cyanate-induced cataracts in patients with sickle-cell hemoglobinopathies","volume":"94","author":"Nicholson","year":"1976","journal-title":"Arch Ophthalmol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib85","doi-asserted-by":"crossref","first-page":"1130","DOI":"10.1110\/ps.40901","article-title":"In\u00a0vivo carbamylation and acetylation of water-soluble human lens alphaB-crystallin lysine 92","volume":"10","author":"Lapko","year":"2001","journal-title":"Protein Sci"},{"key":"10.1053\/j.ajkd.2014.04.034_bib86","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1042\/bj2230221","article-title":"Conformational changes induced in bovine lens alpha-crystallin by carbamylation. Relevance to cataract","volume":"223","author":"Beswick","year":"1984","journal-title":"Biochem J"},{"key":"10.1053\/j.ajkd.2014.04.034_bib87","first-page":"104","article-title":"Identification of the preferentially targeted proteins by carbamylation during whole lens incubation by using radio-labelled potassium cyanate and mass spectrometry","volume":"3","author":"Yan","year":"2010","journal-title":"Int J Ophthalmol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib88","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1080\/02713680802455959","article-title":"Identification of the primary targets of carbamylation in bovine lens proteins by mass spectrometry","volume":"33","author":"Zhang","year":"2008","journal-title":"Curr Eye Res"},{"key":"10.1053\/j.ajkd.2014.04.034_bib89","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1016\/S1350-9462(98)00030-5","article-title":"Alpha-crystallin as a molecular chaperone","volume":"18","author":"Derham","year":"1999","journal-title":"Prog Retin Eye Res"},{"key":"10.1053\/j.ajkd.2014.04.034_bib90","first-page":"136","article-title":"Carbamylation of human lens gamma-crystallins: relevance to cataract formation","volume":"9","author":"Liu","year":"1993","journal-title":"Yan Ke Xue Bao"},{"key":"10.1053\/j.ajkd.2014.04.034_bib91","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1016\/S0014-4835(80)80015-7","article-title":"Carbamylation of lens proteins: a possible factor in cataractogenesis in some tropical countries","volume":"31","author":"Harding","year":"1980","journal-title":"Exp Eye Res"},{"key":"10.1053\/j.ajkd.2014.04.034_bib92","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/S0022-3565(25)30735-4","article-title":"Sodium cyanate-induced ocular lesions in the beagle","volume":"200","author":"Kern","year":"1977","journal-title":"J\u00a0Pharmacol Exp Ther"},{"key":"10.1053\/j.ajkd.2014.04.034_bib93","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1016\/S0022-2275(20)37720-8","article-title":"Immunogenicity of homologous low density lipoprotein after methylation, ethylation, acetylation, or carbamylation: generation of antibodies specific for derivatized lysine","volume":"25","author":"Steinbrecher","year":"1984","journal-title":"J\u00a0Lipid Res"},{"key":"10.1053\/j.ajkd.2014.04.034_bib94","doi-asserted-by":"crossref","first-page":"6882","DOI":"10.4049\/jimmunol.1000075","article-title":"Carbamylation-dependent activation of T cells: a novel mechanism in the pathogenesis of autoimmune arthritis","volume":"184","author":"Mydel","year":"2010","journal-title":"J\u00a0Immunol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib95","doi-asserted-by":"crossref","first-page":"17372","DOI":"10.1073\/pnas.1114465108","article-title":"Autoantibodies recognizing carbamylated proteins are present in sera of patients with rheumatoid arthritis and predict joint damage","volume":"108","author":"Shi","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1053\/j.ajkd.2014.04.034_bib96","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1089\/ars.2012.4535","article-title":"Carbamyl adducts on low-density lipoprotein induce IgG response in LDLR\u2212\/\u2212 mice and bind plasma autoantibodies in humans under enhanced carbamylation","volume":"19","author":"Kummu","year":"2013","journal-title":"Antioxid Redox Signal"},{"key":"10.1053\/j.ajkd.2014.04.034_bib97","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/j.autrev.2013.10.008","article-title":"Carbamylation and antibodies against carbamylated proteins in autoimmunity and other pathologies","volume":"13","author":"Shi","year":"2014","journal-title":"Autoimmun Rev"},{"key":"10.1053\/j.ajkd.2014.04.034_bib98","doi-asserted-by":"crossref","first-page":"2053","DOI":"10.1136\/annrheumdis-2013-203650","article-title":"Anticarbamylated protein (anti-CarP) antibodies are present in sera of juvenile idiopathic arthritis (JIA) patients","volume":"72","author":"Muller","year":"2013","journal-title":"Ann Rheum Dis"},{"key":"10.1053\/j.ajkd.2014.04.034_bib99","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1016\/S0022-2143(99)90086-0","article-title":"Carbamylated proteins activate glomerular mesangial cells and stimulate collagen deposition","volume":"133","author":"Shaykh","year":"1999","journal-title":"J\u00a0Lab Clin Med"},{"key":"10.1053\/j.ajkd.2014.04.034_bib100","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1023\/A:1006838626730","article-title":"Immunological characterization of epitopes on tau of Alzheimer's type and chemically modified tau","volume":"168","author":"Farias","year":"1997","journal-title":"Mol Cell Biochem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib101","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1006\/bbrc.1995.2395","article-title":"Carbamylation inhibits the ferroxidase activity of caeruloplasmin","volume":"214","author":"Roxborough","year":"1995","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1053\/j.ajkd.2014.04.034_bib102","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1186\/2193-1801-2-647","article-title":"Carbamoylation correlates of cyanate neuropathy and cyanide poisoning: relevance to the biomarkers of cassava cyanogenesis and motor system toxicity","volume":"2","author":"Kimani","year":"2013","journal-title":"Springerplus"},{"key":"10.1053\/j.ajkd.2014.04.034_bib103","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1007\/s11011-013-9459-2","article-title":"Memory deficits associated with sublethal cyanide poisoning relative to cyanate toxicity in rodents","volume":"29","author":"Kimani","year":"2014","journal-title":"Metab Brain Dis"},{"key":"10.1053\/j.ajkd.2014.04.034_bib104","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1016\/j.fct.2010.05.080","article-title":"On the biomarkers and mechanisms of konzo, a distinct upper motor neuron disease associated with food (cassava) cyanogenic exposure","volume":"49","author":"Kassa","year":"2010","journal-title":"Food Chem Toxicol"},{"key":"10.1053\/j.ajkd.2014.04.034_bib105","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1093\/toxsci\/50.2.228","article-title":"Bioactivation of cyanide to cyanate in sulfur amino acid deficiency: relevance to neurological disease in humans subsisting on cassava","volume":"50","author":"Tor-Agbidye","year":"1999","journal-title":"Toxicol Sci"},{"key":"10.1053\/j.ajkd.2014.04.034_bib106","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1056\/NEJM198104023041406","article-title":"Hemoglobin carbamylation in uremia","volume":"304","author":"Fluckiger","year":"1981","journal-title":"N\u00a0Engl J Med"},{"issue":"pt 2","key":"10.1053\/j.ajkd.2014.04.034_bib107","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1177\/000456329202900215","article-title":"Carbamylated haemoglobin in normal, diabetic and uraemic patients","volume":"29","author":"Kwan","year":"1992","journal-title":"Ann Clin Biochem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib108","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1093\/ndt\/8.6.565","article-title":"Carbamylated haemoglobin\u2014a retrospective index of time-averaged urea concentration","volume":"8","author":"Kwan","year":"1993","journal-title":"Nephrol Dial Transplant"},{"key":"10.1053\/j.ajkd.2014.04.034_bib109","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1093\/ndt\/6.1.38","article-title":"Carbamylated haemoglobin, urea kinetic modelling and adequacy of dialysis in haemodialysis patients","volume":"6","author":"Kwan","year":"1991","journal-title":"Nephrol Dial Transplant"},{"key":"10.1053\/j.ajkd.2014.04.034_bib110","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/S0272-6386(97)90280-8","article-title":"Carbamylated hemoglobin in hemodialysis patients","volume":"30","author":"Tarif","year":"1997","journal-title":"Am J Kidney Dis"},{"key":"10.1053\/j.ajkd.2014.04.034_bib111","doi-asserted-by":"crossref","first-page":"1344","DOI":"10.1038\/ki.1996.447","article-title":"Carbamylated hemoglobin: a potential marker for the adequacy of hemodialysis therapy in end-stage kidney failure","volume":"50","author":"Davenport","year":"1996","journal-title":"Kidney Int"},{"key":"10.1053\/j.ajkd.2014.04.034_bib112","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1159\/000058397","article-title":"Carbamylated hemoglobin as a therapeutic marker in hemodialysis","volume":"91","author":"Hasuike","year":"2002","journal-title":"Nephron"},{"key":"10.1053\/j.ajkd.2014.04.034_bib113","doi-asserted-by":"crossref","first-page":"1732","DOI":"10.2337\/diacare.21.10.1732","article-title":"Abnormally decreased HbA1c can be assessed with erythrocyte creatine in patients with a shortened erythrocyte age","volume":"21","author":"Jiao","year":"1998","journal-title":"Diabetes Care"},{"key":"10.1053\/j.ajkd.2014.04.034_bib114","doi-asserted-by":"crossref","first-page":"826","DOI":"10.2169\/internalmedicine.37.826","article-title":"Influence of erythropoietin treatment on hemoglobin A1c levels in patients with chronic kidney failure on hemodialysis","volume":"37","author":"Nakao","year":"1998","journal-title":"Intern Med"},{"key":"10.1053\/j.ajkd.2014.04.034_bib115","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1007\/BF03347514","article-title":"Hemoglobin A1c levels in non-diabetic patients with end-stage kidney disease (ESRD) receiving hemodialysis","volume":"27","author":"Wang","year":"2004","journal-title":"J\u00a0Endocrinol Invest"},{"key":"10.1053\/j.ajkd.2014.04.034_bib116","doi-asserted-by":"crossref","first-page":"1621","DOI":"10.2337\/dc12-0027","article-title":"A\u00a0critical evaluation of glycated protein parameters in advanced nephropathy: a matter of life or death: time to dispense with the hemoglobin A1c in end-stage kidney disease","volume":"35","author":"Freedman","year":"2012","journal-title":"Diabetes Care"},{"key":"10.1053\/j.ajkd.2014.04.034_bib117","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1038\/ki.1995.454","article-title":"Factors determining hemoglobin carbamylation in kidney failure","volume":"48","author":"Stim","year":"1995","journal-title":"Kidney Int"},{"key":"10.1053\/j.ajkd.2014.04.034_bib118","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1093\/clinchem\/36.4.607","article-title":"Determination of carbamylated hemoglobin by high-performance liquid chromatography","volume":"36","author":"Kwan","year":"1990","journal-title":"Clin Chem"},{"key":"10.1053\/j.ajkd.2014.04.034_bib119","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1093\/ndt\/15.8.1183","article-title":"Kinetics of carbamylated haemoglobin in acute kidney failure","volume":"15","author":"Wynckel","year":"2000","journal-title":"Nephrol Dial Transplant"},{"key":"10.1053\/j.ajkd.2014.04.034_bib120","doi-asserted-by":"crossref","first-page":"1614","DOI":"10.1016\/0140-6736(93)90757-8","article-title":"Differentiation of acute from chronic kidney impairment by detection of carbamylated haemoglobin","volume":"341","author":"Davenport","year":"1993","journal-title":"Lancet"},{"key":"10.1053\/j.ajkd.2014.04.034_bib121","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/S0272-6386(97)90562-X","article-title":"Temporal changes and reversibility of carbamylated hemoglobin in kidney failure","volume":"30","author":"Han","year":"1997","journal-title":"Am J Kidney Dis"},{"key":"10.1053\/j.ajkd.2014.04.034_bib122","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.cardfail.2013.02.001","article-title":"Protein carbamylation in chronic systolic heart failure: relationship with kidney impairment and adverse long-term outcomes","volume":"19","author":"Tang","year":"2013","journal-title":"J\u00a0Card Fail"},{"key":"10.1053\/j.ajkd.2014.04.034_bib123","doi-asserted-by":"crossref","first-page":"E136","DOI":"10.1152\/ajpendo.00352.2003","article-title":"Protein turnover and amino acid transport kinetics in end-stage kidney disease","volume":"286","author":"Raj","year":"2004","journal-title":"Am J Physiol Endocrinol Metab"},{"key":"10.1053\/j.ajkd.2014.04.034_bib124","doi-asserted-by":"crossref","first-page":"1963","DOI":"10.1093\/ndt\/gft215","article-title":"Do we need another Kt\/V?","volume":"28","author":"Tattersall","year":"2013","journal-title":"Nephrol Dial Transplant"},{"key":"10.1053\/j.ajkd.2014.04.034_bib125","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/S0272-6386(97)90278-X","article-title":"Methodological limitations of the ESRD Core Indicators Project: an ESRD network's experience with implementing an ESRD quality survey. Medical Review Board of the ESRD Network of New England","volume":"30","author":"Owen","year":"1997","journal-title":"Am J Kidney Dis"},{"key":"10.1053\/j.ajkd.2014.04.034_bib126","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1089\/ars.2011.4403","article-title":"Myeloperoxidase-derived chlorinating species induce protein carbamylation through decomposition of thiocyanate and urea: novel pathways generating dysfunctional high-density lipoprotein","volume":"17","author":"Holzer","year":"2012","journal-title":"Antioxid Redox Signal"},{"key":"10.1053\/j.ajkd.2014.04.034_bib127","first-page":"323","article-title":"Serum thiocyanate levels in smokers, passive smokers and never smokers","volume":"56","author":"Zil","year":"2006","journal-title":"J\u00a0Pak Med Assoc"},{"key":"10.1053\/j.ajkd.2014.04.034_bib128","doi-asserted-by":"crossref","first-page":"1314","DOI":"10.1096\/fj.10-173377","article-title":"Carbamylated low-density lipoprotein induces oxidative stress and accelerated senescence in human endothelial progenitor cells","volume":"25","author":"Carracedo","year":"2011","journal-title":"FASEB J"}],"container-title":["American Journal of Kidney Diseases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0272638614009652?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0272638614009652?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,3]],"date-time":"2025-10-03T02:24:30Z","timestamp":1759458270000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0272638614009652"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,11]]},"references-count":128,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2014,11]]}},"alternative-id":["S0272638614009652"],"URL":"https:\/\/doi.org\/10.1053\/j.ajkd.2014.04.034","relation":{},"ISSN":["0272-6386"],"issn-type":[{"value":"0272-6386","type":"print"}],"subject":[],"published":{"date-parts":[[2014,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Protein Carbamylation in Kidney Disease: Pathogenesis and Clinical Implications","name":"articletitle","label":"Article Title"},{"value":"American Journal of Kidney Diseases","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1053\/j.ajkd.2014.04.034","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2014 National Kidney Foundation, Inc. Published by Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}