{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,22]],"date-time":"2026-01-22T01:26:36Z","timestamp":1769045196544,"version":"3.49.0"},"reference-count":69,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,10,1]],"date-time":"2018-10-01T00:00:00Z","timestamp":1538352000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,10,1]],"date-time":"2018-10-01T00:00:00Z","timestamp":1538352000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100012232","name":"National Key Clinical Specialty Discipline Construction Program of China","doi-asserted-by":"publisher","award":["2017YFA0505200"],"award-info":[{"award-number":["2017YFA0505200"]}],"id":[{"id":"10.13039\/501100012232","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["bmn.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Current Opinion in Chemical Biology"],"published-print":{"date-parts":[[2018,10]]},"DOI":"10.1016\/j.cbpa.2018.03.018","type":"journal-article","created":{"date-parts":[[2018,4,11]],"date-time":"2018-04-11T13:04:52Z","timestamp":1523451892000},"page":"33-40","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":38,"special_numbering":"C","title":["Acyl donors for native chemical ligation"],"prefix":"10.1016","volume":"46","author":[{"given":"Bingjia","family":"Yan","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Weiwei","family":"Shi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Linzhi","family":"Ye","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lei","family":"Liu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.cbpa.2018.03.018_bib0350","doi-asserted-by":"crossref","first-page":"6705","DOI":"10.1073\/pnas.95.12.6705","article-title":"Expressed protein ligation: a general method for protein engineering","volume":"95","author":"Muir","year":"1998","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.cbpa.2018.03.018_sbref0355","doi-asserted-by":"crossref","first-page":"776","DOI":"10.1126\/science.7973629","article-title":"Synthesis of proteins by native chemical ligation","volume":"266","author":"Dawson","year":"1994","journal-title":"Science"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0360","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1039\/B700141J","article-title":"Total chemical synthesis of proteins","volume":"38","author":"Kent","year":"2009","journal-title":"Chem Soc Rev"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0365","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s11426-016-0381-1","article-title":"Recent advances in the preparation of Fmoc-SPPS-based peptide thioester and its surrogates for NCL-type reactions","volume":"60","author":"Li","year":"2017","journal-title":"Sci China Chem"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0370","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1093\/nsr\/nwv072","article-title":"Chemical synthesis of proteins using hydrazide intermediates","volume":"3","author":"Huang","year":"2016","journal-title":"Natl Sci Rev"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0375","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.cbpa.2014.09.021","article-title":"Recent extensions to native chemical ligation for the chemical synthesis of peptides and proteins","volume":"22","author":"Malins","year":"2014","journal-title":"Curr Opin Chem Biol"},{"key":"10.1016\/j.cbpa.2018.03.018_sbref0380","doi-asserted-by":"crossref","first-page":"14011","DOI":"10.1021\/jacs.5b07237","article-title":"Rapid additive-free selenocysteine\u2013selenoester peptide ligation","volume":"137","author":"Mitchell","year":"2015","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0385","doi-asserted-by":"crossref","first-page":"11684","DOI":"10.1021\/ja992881j","article-title":"Fmoc-based synthesis of peptide-\u03b1-thioesters: application to the total chemical synthesis of a glycoprotein by native chemical ligation","volume":"121","author":"Shin","year":"1999","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0390","doi-asserted-by":"crossref","first-page":"8337","DOI":"10.1021\/ja001763p","article-title":"Semisynthesis of hyperphosphorylated type I TGF\u03b2 receptor: addressing the mechanism of kinase activation","volume":"122","author":"Huse","year":"2000","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0395","doi-asserted-by":"crossref","first-page":"8669","DOI":"10.1016\/S0040-4039(98)01868-1","article-title":"Direct preparation of peptide thioesters using an Fmoc solid-phase method","volume":"39","author":"Li","year":"1998","journal-title":"Tetrahedron Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0400","doi-asserted-by":"crossref","first-page":"6237","DOI":"10.1016\/S0040-4039(97)01434-2","article-title":"Preparation of peptide thioesters using Fmoc-solid-phase peptide synthesis and its application to the construction of a template-assembled synthetic protein (TASP)","volume":"38","author":"Futaki","year":"1997","journal-title":"Tetrahedron Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0405","doi-asserted-by":"crossref","first-page":"11369","DOI":"10.1021\/ja992668n","article-title":"Solid phase synthesis of peptide C-terminal thioesters by Fmoc\/t-Bu chemistry","volume":"121","author":"Ingenito","year":"1999","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0410","doi-asserted-by":"crossref","first-page":"3620","DOI":"10.1002\/chem.200701978","article-title":"Solid-phase synthesis of peptide and glycopeptide thioesters through side-chain anchoring strategies","volume":"14","author":"Ficht","year":"2008","journal-title":"Chem Eur J"},{"key":"10.1016\/j.cbpa.2018.03.018_sbref0415","doi-asserted-by":"crossref","first-page":"6851","DOI":"10.1002\/anie.200705471","article-title":"An efficient Fmoc-SPPS approach for the generation of thioester peptide precursors for use in native chemical ligation","volume":"47","author":"Blanco-Canosa","year":"2008","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0420","doi-asserted-by":"crossref","first-page":"2488","DOI":"10.1002\/cbic.201100472","article-title":"A reversible protection strategy to improve Fmoc-SPPS of peptide thioesters by the N-acylurea approach","volume":"12","author":"Mahto","year":"2011","journal-title":"ChemBioChem"},{"key":"10.1016\/j.cbpa.2018.03.018_sbref0425","doi-asserted-by":"crossref","first-page":"7197","DOI":"10.1021\/jacs.5b03504","article-title":"Chemical protein synthesis using a second-generation N-acylurea linker for the preparation of peptide-thioester precursors","volume":"137","author":"Blanco-Canosa","year":"2015","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2018.03.018_sbref0430","doi-asserted-by":"crossref","first-page":"7645","DOI":"10.1002\/anie.201100996","article-title":"Protein chemical synthesis by ligation of peptide hydrazides","volume":"50","author":"Fang","year":"2011","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0435","doi-asserted-by":"crossref","first-page":"5713","DOI":"10.1002\/anie.201500051","article-title":"An efficient one-pot four-segment condensation method for protein chemical synthesis","volume":"54","author":"Tang","year":"2015","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0440","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1007\/s11426-016-0386-4","article-title":"Chemical synthesis of histone H2A with methylation at Gln104","volume":"60","author":"He","year":"2017","journal-title":"Sci China Chem"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0445","doi-asserted-by":"crossref","first-page":"3695","DOI":"10.1021\/ja500222u","article-title":"Expedient total synthesis of small to medium-sized membrane proteins via Fmoc chemistry","volume":"136","author":"Zheng","year":"2014","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0450","doi-asserted-by":"crossref","first-page":"7429","DOI":"10.1021\/jacs.6b04031","article-title":"Quasi-racemic X-ray structures of K27-linked ubiquitin chains prepared by total chemical synthesis","volume":"138","author":"Pan","year":"2016","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0455","doi-asserted-by":"crossref","first-page":"14497","DOI":"10.1021\/jacs.6b09545","article-title":"Monomer\/Oligomer quasi-racemic protein crystallography","volume":"138","author":"Gao","year":"2016","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0460","doi-asserted-by":"crossref","first-page":"2222","DOI":"10.1002\/ange.201408078","article-title":"Peptide o-aminoanilides as crypto-thioesters for protein chemical synthesis","volume":"127","author":"Wang","year":"2015","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0465","first-page":"1","article-title":"Chemical synthesis of a two-photon-activatable chemokine and photon-guided lymphocyte migration in vivo","volume":"6","author":"Chen","year":"2015","journal-title":"Nat Commun"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0470","doi-asserted-by":"crossref","first-page":"11760","DOI":"10.1002\/anie.201506225","article-title":"Blocking of the PD-1\/PD-L1 interaction by a D-peptide antagonist for cancer immunotherapy","volume":"54","author":"Chang","year":"2015","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0475","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1038\/nchem.2517","article-title":"A synthetic molecular system capable of mirror-image genetic replication and transcription","volume":"8","author":"Wang","year":"2016","journal-title":"Nat Chem"},{"key":"10.1016\/j.cbpa.2018.03.018_sbref0480","doi-asserted-by":"crossref","first-page":"4861","DOI":"10.1021\/ol0481028","article-title":"Native chemical ligation through in situ O to S acyl shift","volume":"6","author":"Botti","year":"2004","journal-title":"Org Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0485","doi-asserted-by":"crossref","first-page":"4914","DOI":"10.1021\/ja711126e","article-title":"Cyclic peptide inhibitors of staphylococcal virulence prepared by Fmoc-based thiolactone peptide synthesis","volume":"130","author":"George","year":"2008","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0490","doi-asserted-by":"crossref","first-page":"9848","DOI":"10.1021\/jo4015112","article-title":"An Fmoc compatible. O to S shift-mediated procedure for the preparation of the C-terminal thioester peptides","volume":"78","author":"Liu","year":"2013","journal-title":"J Org Chem"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0495","doi-asserted-by":"crossref","first-page":"2610","DOI":"10.1021\/ol2007204","article-title":"Acid-catalyzed tandem thiol switch for preparing peptide thioesters from mercaptoethyl esters","volume":"13","author":"Eom","year":"2011","journal-title":"Org Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0500","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1002\/cbic.200900789","article-title":"Chemical protein synthesis by kinetically controlled ligation of peptide O-esters","volume":"11","author":"Zheng","year":"2010","journal-title":"ChemBioChem"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0505","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1007\/s11426-011-4434-4","article-title":"Chemical synthesis of a cyclotide via intramolecular cyclization of peptide O-esters","volume":"55","author":"Zheng","year":"2012","journal-title":"Sci China Chem"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0510","doi-asserted-by":"crossref","first-page":"6576","DOI":"10.1021\/ja0491836","article-title":"Toward fully synthetic glycoproteins by ultimately convergent routes: a solution to a long-standing problem","volume":"126","author":"Warren","year":"2004","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0515","doi-asserted-by":"crossref","first-page":"7383","DOI":"10.1002\/anie.200702865","article-title":"Development of efficient methods for accomplishing cysteine-free peptide and glycopeptide coupling","volume":"46","author":"Chen","year":"2007","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0520","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1246\/cl.2007.76","article-title":"Peptide ligation using a building block having a cysteinyl prolyl ester (CPE) autoactivating unit at the carboxy terminus","volume":"36","author":"Kawakami","year":"2006","journal-title":"Chem Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0525","doi-asserted-by":"crossref","first-page":"1903","DOI":"10.1016\/j.tetlet.2007.01.086","article-title":"Sequential peptide ligation by using a controlled cysteinyl prolyl ester (CPE) autoactivating unit","volume":"48","author":"Kawakami","year":"2007","journal-title":"Tetrahedron Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0530","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.tetlet.2006.11.034","article-title":"N-alkyl cysteine-assisted thioesterification of peptides","volume":"48","author":"Hojo","year":"2007","journal-title":"Tetrahedron Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0535","doi-asserted-by":"crossref","first-page":"1370","DOI":"10.1016\/j.tetlet.2015.01.095","article-title":"Peptidyl N-alkylcysteine as a peptide thioester surrogate in the native chemical ligation","volume":"56","author":"Asahina","year":"2015","journal-title":"Tetrahedron Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0540","doi-asserted-by":"crossref","first-page":"8226","DOI":"10.1002\/anie.201501847","article-title":"Chemical synthesis of O-glycosylated human interleukin-2 by the reverse polarity protection strategy","volume":"54","author":"Asahina","year":"2015","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2018.03.018_sbref0545","doi-asserted-by":"crossref","first-page":"2114","DOI":"10.1039\/C6CC10243C","article-title":"One-pot native chemical ligation by combination of two orthogonal thioester precursors","volume":"53","author":"Asahina","year":"2017","journal-title":"Chem Commun"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0550","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1039\/C5SC02630J","article-title":"A straightforward method for automated Fmoc-based synthesis of bio-inspired peptide crypto-thioesters","volume":"7","author":"Terrier","year":"2016","journal-title":"Chem Sci"},{"key":"10.1016\/j.cbpa.2018.03.018_sbref0555","doi-asserted-by":"crossref","first-page":"5238","DOI":"10.1021\/ol102273u","article-title":"Bis (2-sulfanylethyl) amino native peptide ligation","volume":"12","author":"Ollivier","year":"2010","journal-title":"Org Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0560","doi-asserted-by":"crossref","first-page":"7211","DOI":"10.1039\/C6OB01079B","article-title":"Insight into the SEA amide thioester equilibrium. Application to the synthesis of thioesters at neutral pH","volume":"14","author":"Pira","year":"2016","journal-title":"Org Biomol Chem"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0565","doi-asserted-by":"crossref","first-page":"3842","DOI":"10.1021\/acs.orglett.6b01847","article-title":"Kinetically controlled chemoselective cyclization simplifies the access to cyclic and branched peptides","volume":"18","author":"Boll","year":"2016","journal-title":"Org Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0570","doi-asserted-by":"crossref","first-page":"3194","DOI":"10.1021\/jo200029e","article-title":"Synthesis of peptide alkylthioesters using the intramolecular N,S-acyl shift properties of bis (2-sulfanylethyl) amino peptides","volume":"76","author":"Dheur","year":"2011","journal-title":"J Org Chem"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0575","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1021\/ol8028093","article-title":"N\u2192S acyl-transfer-mediated synthesis of peptide thioesters using anilide derivatives","volume":"11","author":"Tsuda","year":"2009","journal-title":"Org Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0580","doi-asserted-by":"crossref","first-page":"1840","DOI":"10.1002\/cbic.201100241","article-title":"N-sulfanylethylanilide peptide as a crypto-thioester peptide","volume":"12","author":"Sato","year":"2011","journal-title":"ChemBioChem"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0585","doi-asserted-by":"crossref","first-page":"5940","DOI":"10.1021\/acs.orglett.6b03055","article-title":"N-sulfanylethylaminooxybutyramide (SEAoxy): a crypto-thioester compatible with Fmoc solid-phase peptide synthesis","volume":"18","author":"Tsuda","year":"2016","journal-title":"Org Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0590","doi-asserted-by":"crossref","first-page":"4416","DOI":"10.1021\/acs.orglett.6b02207","article-title":"Development of an anilide-type scaffold for the thioester precursor N-sulfanylethylcoumarinyl amide","volume":"18","author":"Eto","year":"2016","journal-title":"Org Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0595","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1039\/C3SC52140K","article-title":"In situ thioester formation for protein ligation using \u03b1-methylcysteine","volume":"5","author":"Burlina","year":"2014","journal-title":"Chem Sci"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0600","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1021\/ol102735k","article-title":"Peptidyl N,N-bis (2-mercaptoethyl)-amides as thioester precursors for native chemical ligation","volume":"13","author":"Hou","year":"2010","journal-title":"Org Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0605","doi-asserted-by":"crossref","first-page":"2491","DOI":"10.1039\/C7OB00103G","article-title":"Peptide Weinreb amide derivatives as thioester precursors for native chemical ligation","volume":"15","author":"Rao","year":"2017","journal-title":"Org Biomol Chem"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0610","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1002\/psc.1164","article-title":"Synthesis of peptide thioester via an N\u2013S acyl shift reaction under mild acidic conditions on an N-4,5-dimethoxy-2-mercaptobenzyl auxiliary group","volume":"15","author":"Nakamura","year":"2009","journal-title":"J Pept Sci"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0615","doi-asserted-by":"crossref","first-page":"4465","DOI":"10.1021\/ol0616034","article-title":"Efficient microwave-assisted tandem N-to S-acyl transfer and thioester exchange for the preparation of a glycosylated peptide thioester","volume":"8","author":"Nagaike","year":"2006","journal-title":"Org Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0620","doi-asserted-by":"crossref","first-page":"5176","DOI":"10.1021\/ol202047q","article-title":"Tandem thiol switch synthesis of peptide thioesters via N\u2013S acyl shift on thiazolidine","volume":"13","author":"Sharma","year":"2011","journal-title":"Org Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0625","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1021\/ol052755m","article-title":"Cysteine-derived S-protected oxazolidinones: potential chemical devices for the preparation of peptide thioesters","volume":"8","author":"Ohta","year":"2006","journal-title":"Org Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0630","doi-asserted-by":"crossref","first-page":"2620","DOI":"10.1021\/ol400801k","article-title":"A thioethylalkylamide (TEA) thioester surrogate in the synthesis of a cyclic peptide via a tandem acyl shift","volume":"15","author":"Taichi","year":"2013","journal-title":"Org Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0635","doi-asserted-by":"crossref","first-page":"2647","DOI":"10.1021\/ol050776a","article-title":"Fmoc solid-phase synthesis of peptide thioesters using an intramolecular N,S-acyl shift","volume":"7","author":"Ollivier","year":"2005","journal-title":"Org Lett"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0640","doi-asserted-by":"crossref","first-page":"3946","DOI":"10.1021\/jacs.6b13271","article-title":"A facile N-mercaptoethoxyglycinamide (MEGA) linker approach to peptide thioesterification and cyclization","volume":"139","author":"Shelton","year":"2017","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0645","doi-asserted-by":"crossref","first-page":"4890","DOI":"10.1021\/jacs.6b01202","article-title":"Internal activation of peptidyl prolyl thioesters in native chemical ligation","volume":"138","author":"Gui","year":"2016","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0650","doi-asserted-by":"crossref","first-page":"1940","DOI":"10.1039\/C7SC04148A","article-title":"Traceless \u03b2-mercaptan-assisted activation of valinyl benzimidazolinones in peptide ligation","volume":"9","author":"Wang","year":"2018","journal-title":"Chem Sci"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0655","doi-asserted-by":"crossref","first-page":"3473","DOI":"10.1016\/j.bmc.2013.03.076","article-title":"Solid phase synthesis of peptide-selenoesters","volume":"21","author":"Ghassemian","year":"2013","journal-title":"Bioorgan Med Chem"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0660","doi-asserted-by":"crossref","first-page":"2657","DOI":"10.1039\/C5SC03459K","article-title":"Accelerating chemoselective peptide bond formation using bis (2-selenylethyl)amido peptide selenoester surrogates","volume":"7","author":"Raibaut","year":"2016","journal-title":"Chem Sci"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0665","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1002\/psc.2581","article-title":"Peptide ligation chemistry at selenol amino acids","volume":"20","author":"Malins","year":"2014","journal-title":"J Pept Sci"},{"key":"10.1016\/j.cbpa.2018.03.018_sbref0670","doi-asserted-by":"crossref","first-page":"12042","DOI":"10.1002\/anie.201105512","article-title":"Preformed selenoesters enable rapid native chemical ligation at intractable sites","volume":"50","author":"Durek","year":"2011","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0675","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1002\/psc.2469","article-title":"Investigation of peptide thioester formation via N\u2192Se acyl transfer","volume":"19","author":"Adams","year":"2013","journal-title":"J Pept Sci"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0680","doi-asserted-by":"crossref","first-page":"15914","DOI":"10.1002\/ange.201709418","article-title":"One-pot four-segment ligation using seleno-and thioesters: synthesis of superoxide dismutase","volume":"129","author":"Takei","year":"2017","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2018.03.018_bib0685","doi-asserted-by":"crossref","first-page":"5424","DOI":"10.1039\/C7CC00823F","article-title":"Solid-phase synthesis of peptide selenoesters via a side-chain anchoring strategy","volume":"53","author":"Hanna","year":"2017","journal-title":"Chem Commun"},{"key":"10.1016\/j.cbpa.2018.03.018_sbref0690","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1039\/C7SC02736B","article-title":"Peptide nucleic acid-templated selenocysteine\u2013selenoester ligation enables rapid miRNA detection","volume":"9","author":"Sayers","year":"2018","journal-title":"Chem Sci"}],"container-title":["Current Opinion in Chemical Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1367593117302272?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1367593117302272?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,24]],"date-time":"2025-10-24T02:40:14Z","timestamp":1761273614000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1367593117302272"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,10]]},"references-count":69,"alternative-id":["S1367593117302272"],"URL":"https:\/\/doi.org\/10.1016\/j.cbpa.2018.03.018","relation":{},"ISSN":["1367-5931"],"issn-type":[{"value":"1367-5931","type":"print"}],"subject":[],"published":{"date-parts":[[2018,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Acyl donors for native chemical ligation","name":"articletitle","label":"Article Title"},{"value":"Current Opinion in Chemical Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cbpa.2018.03.018","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}