{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T10:34:23Z","timestamp":1790505263922,"version":"4.1.0"},"reference-count":87,"publisher":"Springer Science and Business Media LLC","issue":"3","license":[{"start":{"date-parts":[[2018,2,14]],"date-time":"2018-02-14T00:00:00Z","timestamp":1518566400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Chem Biol"],"published-print":{"date-parts":[[2018,3]]},"DOI":"10.1038\/nchembio.2575","type":"journal-article","created":{"date-parts":[[2018,2,14]],"date-time":"2018-02-14T19:02:14Z","timestamp":1518634934000},"page":"244-252","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":167,"title":["Features and regulation of non-enzymatic post-translational modifications"],"prefix":"10.1038","volume":"14","author":[{"given":"Robert","family":"Harmel","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dorothea","family":"Fiedler","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2018,2,14]]},"reference":[{"key":"BFnchembio2575_CR1","doi-asserted-by":"publisher","first-page":"7342","DOI":"10.1002\/anie.200501023","volume":"44","author":"CT Walsh","year":"2005","unstructured":"Walsh, C.T., Garneau-Tsodikova, S. & Gatto, G.J. Jr. Protein posttranslational modifications: the chemistry of proteome diversifications. Angew. Chem. Int. Ed. Engl. 44, 7342\u20137372 (2005).","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"BFnchembio2575_CR2","unstructured":"UniProt Consortium. Controlled vocabulary of posttranslational modifications (PTM). UniProt http:\/\/www.uniprot.org\/docs\/ptmlist (2017)."},{"key":"BFnchembio2575_CR3","doi-asserted-by":"publisher","first-page":"823","DOI":"10.1016\/j.cell.2007.05.009","volume":"129","author":"A Barski","year":"2007","unstructured":"Barski, A. et al. High-resolution profiling of histone methylations in the human genome. Cell 129, 823\u2013837 (2007).","journal-title":"Cell"},{"key":"BFnchembio2575_CR4","doi-asserted-by":"publisher","first-page":"4566","DOI":"10.1021\/pr800468j","volume":"7","author":"D Meierhofer","year":"2008","unstructured":"Meierhofer, D., Wang, X., Huang, L. & Kaiser, P. Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J. Proteome Res. 7, 4566\u20134576 (2008).","journal-title":"J. Proteome Res."},{"key":"BFnchembio2575_CR5","doi-asserted-by":"publisher","first-page":"153","DOI":"10.1016\/j.copbio.2014.12.020","volume":"34","author":"MA Keller","year":"2015","unstructured":"Keller, M.A., Piedrafita, G. & Ralser, M. The widespread role of non-enzymatic reactions in cellular metabolism. Curr. Opin. Biotechnol. 34, 153\u2013161 (2015).","journal-title":"Curr. Opin. Biotechnol."},{"key":"BFnchembio2575_CR6","doi-asserted-by":"publisher","first-page":"530","DOI":"10.1038\/nrm2203","volume":"8","author":"JA Ubersax","year":"2007","unstructured":"Ubersax, J.A. & Ferrell, J.E. Jr. Mechanisms of specificity in protein phosphorylation. Nat. Rev. Mol. Cell Biol. 8, 530\u2013541 (2007).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"BFnchembio2575_CR7","doi-asserted-by":"publisher","first-page":"1912","DOI":"10.1126\/science.1075762","volume":"298","author":"G Manning","year":"2002","unstructured":"Manning, G., Whyte, D.B., Martinez, R., Hunter, T. & Sudarsanam, S. The protein kinase complement of the human genome. Science 298, 1912\u20131934 (2002).","journal-title":"Science"},{"key":"BFnchembio2575_CR8","doi-asserted-by":"publisher","first-page":"529","DOI":"10.1016\/j.redox.2014.02.005","volume":"2","author":"R Bret\u00f3n-Romero","year":"2014","unstructured":"Bret\u00f3n-Romero, R. & Lamas, S. Hydrogen peroxide signaling in vascular endothelial cells. Redox Biol. 2, 529\u2013534 (2014).","journal-title":"Redox Biol."},{"key":"BFnchembio2575_CR9","doi-asserted-by":"publisher","first-page":"15407","DOI":"10.1021\/bi992025k","volume":"38","author":"A Claiborne","year":"1999","unstructured":"Claiborne, A. et al. Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry 38, 15407\u201315416 (1999).","journal-title":"Biochemistry"},{"key":"BFnchembio2575_CR10","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1016\/j.diabres.2004.09.004","volume":"67","author":"N Ahmed","year":"2005","unstructured":"Ahmed, N. Advanced glycation endproducts\u2014role in pathology of diabetic complications. Diabetes Res. Clin. Pract. 67, 3\u201321 (2005).","journal-title":"Diabetes Res. Clin. Pract."},{"key":"BFnchembio2575_CR11","doi-asserted-by":"publisher","first-page":"488","DOI":"10.1111\/j.1749-6632.2002.tb04690.x","volume":"973","author":"DA Dickinson","year":"2002","unstructured":"Dickinson, D.A. & Forman, H.J.A.Y. Glutathione in defense and signaling: lessons from a small thiol. Ann. NY Acad. Sci. 973, 488\u2013504 (2002).","journal-title":"Ann. NY Acad. Sci."},{"key":"BFnchembio2575_CR12","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1016\/j.yjmcc.2014.01.018","volume":"73","author":"HJ Forman","year":"2014","unstructured":"Forman, H.J., Ursini, F. & Maiorino, M. An overview of mechanisms of redox signaling. J. Mol. Cell. Cardiol. 73, 2\u20139 (2014).","journal-title":"J. Mol. Cell. Cardiol."},{"key":"BFnchembio2575_CR13","doi-asserted-by":"publisher","first-page":"1401","DOI":"10.1373\/clinchem.2010.145201","volume":"56","author":"S Jaisson","year":"2010","unstructured":"Jaisson, S. & Gillery, P. Evaluation of nonenzymatic posttranslational modification-derived products as biomarkers of molecular aging of proteins. Clin. Chem. 56, 1401\u20131412 (2010).","journal-title":"Clin. Chem."},{"key":"BFnchembio2575_CR14","doi-asserted-by":"publisher","first-page":"981","DOI":"10.1016\/j.cellsig.2012.01.008","volume":"24","author":"PD Ray","year":"2012","unstructured":"Ray, P.D., Huang, B.-W. & Tsuji, Y. Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling. Cell. Signal. 24, 981\u2013990 (2012).","journal-title":"Cell. Signal."},{"key":"BFnchembio2575_CR15","doi-asserted-by":"publisher","first-page":"1250","DOI":"10.1080\/10715760600918142","volume":"40","author":"ER Stadtman","year":"2006","unstructured":"Stadtman, E.R. Protein oxidation and aging. Free Radic. Res. 40, 1250\u20131258 (2006).","journal-title":"Free Radic. Res."},{"key":"BFnchembio2575_CR16","doi-asserted-by":"publisher","first-page":"129","DOI":"10.1007\/s001250051591","volume":"44","author":"R Singh","year":"2001","unstructured":"Singh, R., Barden, A., Mori, T. & Beilin, L. Advanced glycation end-products: a review. Diabetologia 44, 129\u2013146 (2001).","journal-title":"Diabetologia"},{"key":"BFnchembio2575_CR17","doi-asserted-by":"publisher","first-page":"474","DOI":"10.1038\/ki.2015.166","volume":"88","author":"FH Verbrugge","year":"2015","unstructured":"Verbrugge, F.H., Tang, W.H.W. & Hazen, S.L. Protein carbamylation and cardiovascular disease. Kidney Int. 88, 474\u2013478 (2015).","journal-title":"Kidney Int."},{"key":"BFnchembio2575_CR18","doi-asserted-by":"publisher","first-page":"169","DOI":"10.1016\/S1471-4914(03)00031-5","volume":"9","author":"I Dalle-Donne","year":"2003","unstructured":"Dalle-Donne, I., Giustarini, D., Colombo, R., Rossi, R. & Milzani, A. Protein carbonylation in human diseases. Trends Mol. Med. 9, 169\u2013176 (2003).","journal-title":"Trends Mol. Med."},{"key":"BFnchembio2575_CR19","doi-asserted-by":"publisher","first-page":"101","DOI":"10.3109\/10715762.2010.524643","volume":"45","author":"N Frizzell","year":"2011","unstructured":"Frizzell, N., Lima, M. & Baynes, J.W. Succination of proteins in diabetes. Free Radic. Res. 45, 101\u2013109 (2011).","journal-title":"Free Radic. Res."},{"key":"BFnchembio2575_CR20","doi-asserted-by":"publisher","first-page":"793","DOI":"10.1053\/j.ajkd.2014.04.034","volume":"64","author":"S Kalim","year":"2014","unstructured":"Kalim, S., Karumanchi, S.A., Thadhani, R.I. & Berg, A.H. Protein carbamylation in kidney disease: pathogenesis and clinical implications. Am. J. Kidney Dis. 64, 793\u2013803 (2014).","journal-title":"Am. J. Kidney Dis."},{"key":"BFnchembio2575_CR21","doi-asserted-by":"publisher","first-page":"1","DOI":"10.2337\/diabetes.48.1.1","volume":"48","author":"JW Baynes","year":"1999","unstructured":"Baynes, J.W. & Thorpe, S.R. Role of oxidative stress in diabetic complications: a new perspective on an old paradigm. Diabetes 48, 1\u20139 (1999).","journal-title":"Diabetes"},{"key":"BFnchembio2575_CR22","doi-asserted-by":"publisher","first-page":"1277","DOI":"10.1016\/S0891-5849(96)00495-9","volume":"22","author":"HP Ciolino","year":"1997","unstructured":"Ciolino, H.P. & Levine, R.L. Modification of proteins in endothelial cell death during oxidative stress. Free Radic. Biol. Med. 22, 1277\u20131282 (1997).","journal-title":"Free Radic. Biol. Med."},{"key":"BFnchembio2575_CR23","doi-asserted-by":"publisher","first-page":"504","DOI":"10.1038\/nchembio.607","volume":"7","author":"BC Dickinson","year":"2011","unstructured":"Dickinson, B.C. & Chang, C.J. Chemistry and biology of reactive oxygen species in signaling or stress responses. Nat. Chem. Biol. 7, 504\u2013511 (2011).","journal-title":"Nat. Chem. Biol."},{"key":"BFnchembio2575_CR24","doi-asserted-by":"publisher","first-page":"3766","DOI":"10.1021\/pr1002609","volume":"9","author":"AG Madian","year":"2010","unstructured":"Madian, A.G. & Regnier, F.E. Proteomic identification of carbonylated proteins and their oxidation sites. J. Proteome Res. 9, 3766\u20133780 (2010).","journal-title":"J. Proteome Res."},{"key":"BFnchembio2575_CR25","doi-asserted-by":"publisher","first-page":"2159","DOI":"10.1021\/pr060021d","volume":"5","author":"H Mirzaei","year":"2006","unstructured":"Mirzaei, H. & Regnier, F. Creation of allotypic active sites during oxidative stress. J. Proteome Res. 5, 2159\u20132168 (2006).","journal-title":"J. Proteome Res."},{"key":"BFnchembio2575_CR26","doi-asserted-by":"publisher","first-page":"1354","DOI":"10.1016\/j.freeradbiomed.2010.07.010","volume":"49","author":"E Thomson","year":"2010","unstructured":"Thomson, E. et al. Identifying peroxidases and their oxidants in the early pathology of cystic fibrosis. Free Radic. Biol. Med. 49, 1354\u20131360 (2010).","journal-title":"Free Radic. Biol. Med."},{"key":"BFnchembio2575_CR27","doi-asserted-by":"publisher","first-page":"895","DOI":"10.1021\/tx960181b","volume":"10","author":"DP Hartley","year":"1997","unstructured":"Hartley, D.P., Kroll, D.J. & Petersen, D.R. Prooxidant-initiated lipid peroxidation in isolated rat hepatocytes: detection of 4-hydroxynonenal- and malondialdehyde-protein adducts. Chem. Res. Toxicol. 10, 895\u2013905 (1997).","journal-title":"Chem. Res. Toxicol."},{"key":"BFnchembio2575_CR28","doi-asserted-by":"publisher","first-page":"490","DOI":"10.1164\/rccm.2110101","volume":"166","author":"I Rahman","year":"2002","unstructured":"Rahman, I. et al. 4-Hydroxy-2-nonenal, a specific lipid peroxidation product, is elevated in lungs of patients with chronic obstructive pulmonary disease. Am. J. Respir. Crit. Care Med. 166, 490\u2013495 (2002).","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"BFnchembio2575_CR29","doi-asserted-by":"publisher","first-page":"373","DOI":"10.1016\/S0306-4522(00)00580-7","volume":"103","author":"MY Aksenov","year":"2001","unstructured":"Aksenov, M.Y., Aksenova, M.V., Butterfield, D.A., Geddes, J.W. & Markesbery, W.R. Protein oxidation in the brain in Alzheimer's disease. Neuroscience 103, 373\u2013383 (2001).","journal-title":"Neuroscience"},{"key":"BFnchembio2575_CR30","doi-asserted-by":"publisher","first-page":"9982","DOI":"10.1074\/jbc.271.17.9982","volume":"271","author":"M-X Fu","year":"1996","unstructured":"Fu, M.-X. et al. The advanced glycation end product, Ne-(carboxymethyl)lysine, is a product of both lipid peroxidation and glycoxidation reactions. J. Biol. Chem. 271, 9982\u20139986 (1996).","journal-title":"J. Biol. Chem."},{"key":"BFnchembio2575_CR31","doi-asserted-by":"crossref","first-page":"32299","DOI":"10.1016\/S0021-9258(18)31635-1","volume":"269","author":"TW Lo","year":"1994","unstructured":"Lo, T.W., Westwood, M.E., McLellan, A.C., Selwood, T. & Thornalley, P.J. Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N \u03b1-acetylarginine, N \u03b1-acetylcysteine, and N \u03b1-acetyllysine, and bovine serum albumin. J. Biol. Chem. 269, 32299\u201332305 (1994).","journal-title":"J. Biol. Chem."},{"key":"BFnchembio2575_CR32","doi-asserted-by":"publisher","first-page":"1828","DOI":"10.1016\/j.carres.2006.03.027","volume":"341","author":"P Manini","year":"2006","unstructured":"Manini, P., La Pietra, P., Panzella, L., Napolitano, A. & d'Ischia, M. Glyoxal formation by Fenton-induced degradation of carbohydrates and related compounds. Carbohydr. Res. 341, 1828\u20131833 (2006).","journal-title":"Carbohydr. Res."},{"key":"BFnchembio2575_CR33","doi-asserted-by":"publisher","first-page":"10017","DOI":"10.1074\/jbc.270.17.10017","volume":"270","author":"MA Glomb","year":"1995","unstructured":"Glomb, M.A. & Monnier, V.M. Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction. J. Biol. Chem. 270, 10017\u201310026 (1995).","journal-title":"J. Biol. Chem."},{"key":"BFnchembio2575_CR34","doi-asserted-by":"publisher","first-page":"581","DOI":"10.1042\/bj20030763","volume":"375","author":"PJ Thornalley","year":"2003","unstructured":"Thornalley, P.J. et al. Quantitative screening of advanced glycation endproducts in cellular and extracellular proteins by tandem mass spectrometry. Biochem. J. 375, 581\u2013592 (2003).","journal-title":"Biochem. J."},{"key":"BFnchembio2575_CR35","doi-asserted-by":"publisher","first-page":"2463","DOI":"10.1172\/JCI116481","volume":"91","author":"DG Dyer","year":"1993","unstructured":"Dyer, D.G. et al. Accumulation of Maillard reaction products in skin collagen in diabetes and aging. J. Clin. Invest. 91, 2463\u20132469 (1993).","journal-title":"J. Clin. Invest."},{"key":"BFnchembio2575_CR36","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.abb.2006.03.005","volume":"450","author":"NL Alderson","year":"2006","unstructured":"Alderson, N.L. et al. S-(2-Succinyl)cysteine: a novel chemical modification of tissue proteins by a Krebs cycle intermediate. Arch. Biochem. Biophys. 450, 1\u20138 (2006).","journal-title":"Arch. Biochem. Biophys."},{"key":"BFnchembio2575_CR37","doi-asserted-by":"publisher","first-page":"272","DOI":"10.1196\/annals.1433.047","volume":"1126","author":"M Blatnik","year":"2008","unstructured":"Blatnik, M., Thorpe, S.R. & Baynes, J.W. Succination of proteins by fumarate: mechanism of inactivation of glyceraldehyde-3-phosphate dehydrogenase in diabetes. Ann. NY Acad. Sci. 1126, 272\u2013275 (2008).","journal-title":"Ann. NY Acad. Sci."},{"key":"BFnchembio2575_CR38","doi-asserted-by":"publisher","first-page":"2547","DOI":"10.1038\/onc.2013.222","volume":"33","author":"J Adam","year":"2014","unstructured":"Adam, J., Yang, M., Soga, T. & Pollard, P.J. Rare insights into cancer biology. Oncogene 33, 2547\u20132556 (2014).","journal-title":"Oncogene"},{"key":"BFnchembio2575_CR39","doi-asserted-by":"publisher","first-page":"4","DOI":"10.1002\/path.2932","volume":"225","author":"C Bardella","year":"2011","unstructured":"Bardella, C. et al. Aberrant succination of proteins in fumarate hydratase-deficient mice and HLRCC patients is a robust biomarker of mutation status. J. Pathol. 225, 4\u201311 (2011).","journal-title":"J. Pathol."},{"key":"BFnchembio2575_CR40","doi-asserted-by":"publisher","first-page":"524","DOI":"10.1016\/j.ccr.2011.09.006","volume":"20","author":"J Adam","year":"2011","unstructured":"Adam, J. et al. Renal cyst formation in Fh1-deficient mice is independent of the Hif\/Phd pathway: roles for fumarate in KEAP1 succination and Nrf2 signaling. Cancer Cell 20, 524\u2013537 (2011).","journal-title":"Cancer Cell"},{"key":"BFnchembio2575_CR41","doi-asserted-by":"publisher","first-page":"1303","DOI":"10.1158\/0008-5472.CAN-07-5003","volume":"68","author":"T Ohta","year":"2008","unstructured":"Ohta, T. et al. Loss of Keap1 function activates Nrf2 and provides advantages for lung cancer cell growth. Cancer Res. 68, 1303\u20131309 (2008).","journal-title":"Cancer Res."},{"key":"BFnchembio2575_CR42","doi-asserted-by":"publisher","first-page":"S102","DOI":"10.1046\/j.1523-1755.2001.59780102.x","volume":"78","author":"LM Kraus","year":"2001","unstructured":"Kraus, L.M. & Kraus, A.P. Jr. Carbamoylation of amino acids and proteins in uremia. Kidney Int. Suppl. 78, S102\u2013S107 (2001).","journal-title":"Kidney Int. Suppl."},{"key":"BFnchembio2575_CR43","doi-asserted-by":"publisher","first-page":"1176","DOI":"10.1038\/nm1637","volume":"13","author":"Z Wang","year":"2007","unstructured":"Wang, Z. et al. Protein carbamylation links inflammation, smoking, uremia and atherogenesis. Nat. Med. 13, 1176\u20131184 (2007).","journal-title":"Nat. Med."},{"key":"BFnchembio2575_CR44","doi-asserted-by":"publisher","first-page":"389","DOI":"10.1111\/j.1582-4934.2006.tb00407.x","volume":"10","author":"I Dalle-Donne","year":"2006","unstructured":"Dalle-Donne, I. et al. Protein carbonylation, cellular dysfunction, and disease progression. J. Cell. Mol. Med. 10, 389\u2013406 (2006).","journal-title":"J. Cell. Mol. Med."},{"key":"BFnchembio2575_CR45","doi-asserted-by":"publisher","first-page":"27257","DOI":"10.1074\/jbc.M401586200","volume":"279","author":"T Koeck","year":"2004","unstructured":"Koeck, T. et al. Rapid and selective oxygen-regulated protein tyrosine denitration and nitration in mitochondria. J. Biol. Chem. 279, 27257\u201327262 (2004).","journal-title":"J. Biol. Chem."},{"key":"BFnchembio2575_CR46","doi-asserted-by":"publisher","first-page":"H30","DOI":"10.1152\/ajpheart.00743.2003","volume":"286","author":"KS Aulak","year":"2004","unstructured":"Aulak, K.S., Koeck, T., Crabb, J.W. & Stuehr, D.J. Dynamics of protein nitration in cells and mitochondria. Am. J. Physiol. Heart Circ. Physiol. 286, H30\u2013H38 (2004).","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"BFnchembio2575_CR47","first-page":"1","volume":"1","author":"S Sengupta","year":"2016","unstructured":"Sengupta, S. & Bhattacharjee, A. Dynamics of protein tyrosine nitration and denitration. RE:view 1, 1\u201313 (2016).","journal-title":"RE:view"},{"key":"BFnchembio2575_CR48","doi-asserted-by":"publisher","first-page":"H687","DOI":"10.1152\/ajpheart.00876.2012","volume":"305","author":"RS Deeb","year":"2013","unstructured":"Deeb, R.S. et al. Characterization of a cellular denitrase activity that reverses nitration of cyclooxygenase. Am. J. Physiol. Heart Circ. Physiol. 305, H687\u2013H698 (2013).","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"BFnchembio2575_CR49","doi-asserted-by":"publisher","first-page":"1055","DOI":"10.1091\/mbc.e03-08-0629","volume":"15","author":"H-Y Kim","year":"2004","unstructured":"Kim, H.-Y. & Gladyshev, V.N. Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases. Mol. Biol. Cell 15, 1055\u20131064 (2004).","journal-title":"Mol. Biol. Cell"},{"key":"BFnchembio2575_CR50","doi-asserted-by":"publisher","first-page":"1367","DOI":"10.1016\/j.bbapap.2014.01.001","volume":"1844","author":"A Drazic","year":"2014","unstructured":"Drazic, A. & Winter, J. The physiological role of reversible methionine oxidation. Biochim. Biophys. Acta 1844, 1367\u20131382 (2014).","journal-title":"Biochim. Biophys. Acta"},{"key":"BFnchembio2575_CR51","doi-asserted-by":"publisher","first-page":"814","DOI":"10.1089\/ars.2015.6385","volume":"23","author":"A Kaya","year":"2015","unstructured":"Kaya, A., Lee, B.C. & Gladyshev, V.N. Regulation of protein function by reversible methionine oxidation and the role of selenoprotein MsrB1. Antioxid. Redox Signal. 23, 814\u2013822 (2015).","journal-title":"Antioxid. Redox Signal."},{"key":"BFnchembio2575_CR52","doi-asserted-by":"publisher","first-page":"9493","DOI":"10.1073\/pnas.1300578110","volume":"110","author":"A Drazic","year":"2013","unstructured":"Drazic, A. et al. Methionine oxidation activates a transcription factor in response to oxidative stress. Proc. Natl. Acad. Sci. USA 110, 9493\u20139498 (2013).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnchembio2575_CR53","doi-asserted-by":"publisher","first-page":"4633","DOI":"10.1021\/cr300163e","volume":"113","author":"CE Paulsen","year":"2013","unstructured":"Paulsen, C.E. & Carroll, K.S. Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery. Chem. Rev. 113, 4633\u20134679 (2013).","journal-title":"Chem. Rev."},{"key":"BFnchembio2575_CR54","doi-asserted-by":"publisher","first-page":"382","DOI":"10.1161\/CIRCRESAHA.112.268680","volume":"112","author":"HS Chung","year":"2013","unstructured":"Chung, H.S., Wang, S.-B., Venkatraman, V., Murray, C.I. & Van Eyk, J.E. Cysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system. Circ. Res. 112, 382\u2013392 (2013).","journal-title":"Circ. Res."},{"key":"BFnchembio2575_CR55","doi-asserted-by":"publisher","first-page":"1998","DOI":"10.1128\/MCB.22.7.1998-2010.2002","volume":"22","author":"DA Buckley","year":"2002","unstructured":"Buckley, D.A., Cheng, A., Kiely, P.A., Tremblay, M.L. & O'Connor, R. Regulation of insulin-like growth factor type I (IGF-I) receptor kinase activity by protein tyrosine phosphatase 1B (PTP-1B) and enhanced IGF-I-mediated suppression of apoptosis and motility in PTP-1B-deficient fibroblasts. Mol. Cell. Biol. 22, 1998\u20132010 (2002).","journal-title":"Mol. Cell. Biol."},{"key":"BFnchembio2575_CR56","doi-asserted-by":"publisher","first-page":"21938","DOI":"10.1074\/jbc.C100109200","volume":"276","author":"K Mahadev","year":"2001","unstructured":"Mahadev, K., Zilbering, A., Zhu, L. & Goldstein, B.J. Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade. J. Biol. Chem. 276, 21938\u201321942 (2001).","journal-title":"J. Biol. Chem."},{"key":"BFnchembio2575_CR57","doi-asserted-by":"publisher","first-page":"15366","DOI":"10.1074\/jbc.273.25.15366","volume":"273","author":"S-R Lee","year":"1998","unstructured":"Lee, S.-R., Kwon, K.-S., Kim, S.-R. & Rhee, S.G. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J. Biol. Chem. 273, 15366\u201315372 (1998).","journal-title":"J. Biol. Chem."},{"key":"BFnchembio2575_CR58","doi-asserted-by":"publisher","first-page":"769","DOI":"10.1038\/nature01680","volume":"423","author":"A Salmeen","year":"2003","unstructured":"Salmeen, A. et al. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423, 769\u2013773 (2003).","journal-title":"Nature"},{"key":"BFnchembio2575_CR59","doi-asserted-by":"publisher","first-page":"773","DOI":"10.1038\/nature01681","volume":"423","author":"RLM van Montfort","year":"2003","unstructured":"van Montfort, R.L.M., Congreve, M., Tisi, D., Carr, R. & Jhoti, H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423, 773\u2013777 (2003).","journal-title":"Nature"},{"key":"BFnchembio2575_CR60","doi-asserted-by":"publisher","first-page":"5633","DOI":"10.1021\/bi973035t","volume":"37","author":"JM Denu","year":"1998","unstructured":"Denu, J.M. & Tanner, K.G. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37, 5633\u20135642 (1998).","journal-title":"Biochemistry"},{"key":"BFnchembio2575_CR61","doi-asserted-by":"publisher","first-page":"549","DOI":"10.1126\/science.1238327","volume":"341","author":"RE Moellering","year":"2013","unstructured":"Moellering, R.E. & Cravatt, B.F. Functional lysine modification by an intrinsically reactive primary glycolytic metabolite. Science 341, 549\u2013553 (2013).","journal-title":"Science"},{"key":"BFnchembio2575_CR62","doi-asserted-by":"publisher","first-page":"947","DOI":"10.1021\/cb3001793","volume":"7","author":"H Lin","year":"2012","unstructured":"Lin, H., Su, X. & He, B. Protein lysine acylation and cysteine succination by intermediates of energy metabolism. ACS Chem. Biol. 7, 947\u2013960 (2012).","journal-title":"ACS Chem. Biol."},{"key":"BFnchembio2575_CR63","doi-asserted-by":"publisher","first-page":"58","DOI":"10.1038\/nchembio.495","volume":"7","author":"Z Zhang","year":"2011","unstructured":"Zhang, Z. et al. Identification of lysine succinylation as a new post-translational modification. Nat. Chem. Biol. 7, 58\u201363 (2011).","journal-title":"Nat. Chem. Biol."},{"key":"BFnchembio2575_CR64","doi-asserted-by":"publisher","first-page":"122","DOI":"10.1021\/cb500848p","volume":"10","author":"J Baeza","year":"2015","unstructured":"Baeza, J., Smallegan, M.J. & Denu, J.M. Site-specific reactivity of nonenzymatic lysine acetylation. ACS Chem. Biol. 10, 122\u2013128 (2015).","journal-title":"ACS Chem. Biol."},{"key":"BFnchembio2575_CR65","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1016\/j.chembiol.2017.01.002","volume":"24","author":"RA Kulkarni","year":"2017","unstructured":"Kulkarni, R.A. et al. Discovering targets of non-enzymatic acylation by thioester reactivity profiling. Cell Chem. Biol. 24, 231\u2013242 (2017).","journal-title":"Cell Chem. Biol."},{"key":"BFnchembio2575_CR66","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1016\/j.molcel.2014.03.027","volume":"54","author":"GR Wagner","year":"2014","unstructured":"Wagner, G.R. & Hirschey, M.D. Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases. Mol. Cell 54, 5\u201316 (2014).","journal-title":"Mol. Cell"},{"key":"BFnchembio2575_CR67","doi-asserted-by":"publisher","first-page":"605","DOI":"10.1016\/j.cmet.2014.03.014","volume":"19","author":"M Tan","year":"2014","unstructured":"Tan, M. et al. Lysine glutarylation is a protein posttranslational modification regulated by SIRT5. Cell Metab. 19, 605\u2013617 (2014).","journal-title":"Cell Metab."},{"key":"BFnchembio2575_CR68","doi-asserted-by":"publisher","first-page":"806","DOI":"10.1126\/science.1207861","volume":"334","author":"J Du","year":"2011","unstructured":"Du, J. et al. Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase. Science 334, 806\u2013809 (2011).","journal-title":"Science"},{"key":"BFnchembio2575_CR69","doi-asserted-by":"publisher","first-page":"29036","DOI":"10.1074\/jbc.M113.486753","volume":"288","author":"GR Wagner","year":"2013","unstructured":"Wagner, G.R. & Payne, R.M. Widespread and enzyme-independent Ne-acetylation and Ne-succinylation of proteins in the chemical conditions of the mitochondrial matrix. J. Biol. Chem. 288, 29036\u201329045 (2013).","journal-title":"J. Biol. Chem."},{"key":"BFnchembio2575_CR70","doi-asserted-by":"publisher","first-page":"823","DOI":"10.1016\/j.cmet.2017.03.006","volume":"25","author":"GR Wagner","year":"2017","unstructured":"Wagner, G.R. et al. A class of reactive acyl-CoA species reveals the non-enzymatic origins of protein acylation. Cell Metab. 25, 823\u2013837.e8 (2017).","journal-title":"Cell Metab."},{"key":"BFnchembio2575_CR71","doi-asserted-by":"publisher","first-page":"2793","DOI":"10.1128\/jb.175.10.2793-2798.1993","volume":"175","author":"WR McCleary","year":"1993","unstructured":"McCleary, W.R., Stock, J.B. & Ninfa, A.J. Is acetyl phosphate a global signal in Escherichia coli? J. Bacteriol. 175, 2793\u20132798 (1993).","journal-title":"J. Bacteriol."},{"key":"BFnchembio2575_CR72","doi-asserted-by":"publisher","first-page":"5574","DOI":"10.1128\/JB.00564-07","volume":"189","author":"AH Klein","year":"2007","unstructured":"Klein, A.H., Shulla, A., Reimann, S.A., Keating, D.H. & Wolfe, A.J. The intracellular concentration of acetyl phosphate in Escherichia coli is sufficient for direct phosphorylation of two-component response regulators. J. Bacteriol. 189, 5574\u20135581 (2007).","journal-title":"J. Bacteriol."},{"key":"BFnchembio2575_CR73","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1016\/j.molcel.2015.02.010","volume":"58","author":"C Azevedo","year":"2015","unstructured":"Azevedo, C., Livermore, T. & Saiardi, A. Protein polyphosphorylation of lysine residues by inorganic polyphosphate. Mol. Cell 58, 71\u201382 (2015).","journal-title":"Mol. Cell"},{"key":"BFnchembio2575_CR74","doi-asserted-by":"publisher","first-page":"897","DOI":"10.1016\/j.cell.2010.11.032","volume":"143","author":"A Chakraborty","year":"2010","unstructured":"Chakraborty, A. et al. Inositol pyrophosphates inhibit Akt signaling, thereby regulating insulin sensitivity and weight gain. Cell 143, 897\u2013910 (2010).","journal-title":"Cell"},{"key":"BFnchembio2575_CR75","doi-asserted-by":"publisher","first-page":"1911","DOI":"10.1073\/pnas.0409322102","volume":"102","author":"A Saiardi","year":"2005","unstructured":"Saiardi, A., Resnick, A.C., Snowman, A.M., Wendland, B. & Snyder, S.H. Inositol pyrophosphates regulate cell death and telomere length through phosphoinositide 3-kinase-related protein kinases. Proc. Natl. Acad. Sci. USA 102, 1911\u20131914 (2005).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnchembio2575_CR76","doi-asserted-by":"publisher","first-page":"21161","DOI":"10.1073\/pnas.0909176106","volume":"106","author":"C Azevedo","year":"2009","unstructured":"Azevedo, C., Burton, A., Ruiz-Mateos, E., Marsh, M. & Saiardi, A. Inositol pyrophosphate mediated pyrophosphorylation of AP3B1 regulates HIV-1 Gag release. Proc. Natl. Acad. Sci. USA 106, 21161\u201321166 (2009).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnchembio2575_CR77","doi-asserted-by":"publisher","first-page":"3031","DOI":"10.1042\/BCJ20160610","volume":"473","author":"M Chanduri","year":"2016","unstructured":"Chanduri, M. et al. Inositol hexakisphosphate kinase 1 (IP6K1) activity is required for cytoplasmic dynein-driven transport. Biochem. J. 473, 3031\u20133047 (2016).","journal-title":"Biochem. J."},{"key":"BFnchembio2575_CR78","doi-asserted-by":"publisher","first-page":"3672","DOI":"10.1021\/acs.analchem.6b05095","volume":"89","author":"M Penkert","year":"2017","unstructured":"Penkert, M. et al. Unambiguous identification of serine and threonine pyrophosphorylation using neutral-loss-triggered electron-transfer\/higher-energy collision dissociation. Anal. Chem. 89, 3672\u20133680 (2017).","journal-title":"Anal. Chem."},{"key":"BFnchembio2575_CR79","doi-asserted-by":"publisher","first-page":"2101","DOI":"10.1126\/science.1103344","volume":"306","author":"A Saiardi","year":"2004","unstructured":"Saiardi, A., Bhandari, R., Resnick, A.C., Snowman, A.M. & Snyder, S.H. Phosphorylation of proteins by inositol pyrophosphates. Science 306, 2101\u20132105 (2004).","journal-title":"Science"},{"key":"BFnchembio2575_CR80","doi-asserted-by":"publisher","first-page":"15305","DOI":"10.1073\/pnas.0707338104","volume":"104","author":"R Bhandari","year":"2007","unstructured":"Bhandari, R. et al. Protein pyrophosphorylation by inositol pyrophosphates is a posttranslational event. Proc. Natl. Acad. Sci. USA 104, 15305\u201315310 (2007).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnchembio2575_CR81","doi-asserted-by":"publisher","first-page":"7192","DOI":"10.1002\/anie.201402905","volume":"53","author":"M Wu","year":"2014","unstructured":"Wu, M. et al. Elucidating diphosphoinositol polyphosphate function with nonhydrolyzable analogues. Angew. Chem. Int. Ed. Engl. 53, 7192\u20137197 (2014).","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"BFnchembio2575_CR82","doi-asserted-by":"publisher","first-page":"12406","DOI":"10.1002\/chem.201601754","volume":"22","author":"A Hager","year":"2016","unstructured":"Hager, A. et al. Cellular cations control conformational switching of inositol pyrophosphate analogues. Chemistry 22, 12406\u201312414 (2016).","journal-title":"Chemistry"},{"key":"BFnchembio2575_CR83","doi-asserted-by":"publisher","first-page":"415","DOI":"10.1002\/cbic.201402589","volume":"16","author":"LM Yates","year":"2015","unstructured":"Yates, L.M. & Fiedler, D. Establishing the stability and reversibility of protein pyrophosphorylation with synthetic peptides. ChemBioChem 16, 415\u2013423 (2015).","journal-title":"ChemBioChem"},{"key":"BFnchembio2575_CR84","doi-asserted-by":"publisher","first-page":"714","DOI":"10.1002\/msb.201304521","volume":"9","author":"P Beltrao","year":"2013","unstructured":"Beltrao, P., Bork, P., Krogan, N.J. & van Noort, V. Evolution and functional cross-talk of protein post-translational modifications. Mol. Syst. Biol. 9, 714 (2013).","journal-title":"Mol. Syst. Biol."},{"key":"BFnchembio2575_CR85","doi-asserted-by":"publisher","first-page":"596","DOI":"10.1038\/nchembio821","volume":"2","author":"T Yoshida","year":"2006","unstructured":"Yoshida, T. et al. Nitric oxide activates TRP channels by cysteine S-nitrosylation. Nat. Chem. Biol. 2, 596\u2013607 (2006).","journal-title":"Nat. Chem. Biol."},{"key":"BFnchembio2575_CR86","first-page":"ra72","volume":"2","author":"AK Mustafa","year":"2009","unstructured":"Mustafa, A.K. et al. H2S signals through protein S-sulfhydration. Sci. Signal. 2, ra72 (2009).","journal-title":"Sci. Signal."},{"key":"BFnchembio2575_CR87","doi-asserted-by":"publisher","first-page":"334","DOI":"10.1038\/s41467-017-02655-1","volume":"9","author":"RS Kathayat","year":"2018","unstructured":"Kathayat, R.S. et al. Active and dynamic mitochondrial S-depalmitoylation revealed by targeted fluorescent probes. Nat. Commun. 9, 334 (2018).","journal-title":"Nat. Commun."}],"container-title":["Nature Chemical Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nchembio.2575.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nchembio.2575","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/doifinder\/10.1038\/nchembio.2575","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"},{"URL":"http:\/\/www.nature.com\/articles\/nchembio.2575.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T19:47:09Z","timestamp":1684439229000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nchembio.2575"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,2,14]]},"references-count":87,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2018,3]]}},"alternative-id":["BFnchembio2575"],"URL":"https:\/\/doi.org\/10.1038\/nchembio.2575","relation":{},"ISSN":["1552-4450","1552-4469"],"issn-type":[{"value":"1552-4450","type":"print"},{"value":"1552-4469","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,2,14]]},"assertion":[{"value":"21 June 2017","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"12 January 2018","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"14 February 2018","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing financial interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}