{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T01:17:30Z","timestamp":1759540650258,"version":"3.44.0"},"reference-count":25,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100003141","name":"Consejo Nacional de Ciencia y Tecnolog\u00eda","doi-asserted-by":"publisher","award":["FORDECYT-PRONACES 840801"],"award-info":[{"award-number":["FORDECYT-PRONACES 840801"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Chemico-Biological Interactions"],"published-print":{"date-parts":[[2021,8]]},"DOI":"10.1016\/j.cbi.2021.109524","type":"journal-article","created":{"date-parts":[[2021,5,19]],"date-time":"2021-05-19T21:38:37Z","timestamp":1621460317000},"page":"109524","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"special_numbering":"C","title":["DAEH N-terminal sequence of avian serum albumins as catalytic center of Cu (II)-dependent organophosphorus hydrolyzing A-esterase activity"],"prefix":"10.1016","volume":"345","author":[{"given":"Antonio","family":"Monroy-Noyola","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Miguel Angel","family":"Sogorb","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Damianys","family":"Almenares-Lopez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0877-0953","authenticated-orcid":false,"given":"Eugenio","family":"Vilanova","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.cbi.2021.109524_bib1","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/0048-3575(87)90021-6","article-title":"Interaction of some unsustituted phosphoramidate analogs of methamidophos (O, S dimethyl phosphorothioamidate) with acetylcholinesterase and neuropathy target esterase of hen brain","volume":"28","author":"Vilanova","year":"1987","journal-title":"Pestic. Biochem. Physiol."},{"key":"10.1016\/j.cbi.2021.109524_bib2","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/0300-483X(89)90081-4","article-title":"Biochemical clinical tests of the delayed neuropathic potential of some O-alkyl o-dichlorophenyl phosphoramidate analogues of methamidophos (O, S-dimethyl phosphorothioamidate)","volume":"54","author":"Johnson","year":"1989","journal-title":"Toxicology"},{"key":"10.1016\/j.cbi.2021.109524_bib3","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/S0378-4274(97)00084-2","article-title":"Inhibition and aging of neuropathytarget esterase by the stereoisomers of a phosphoramidate related to methamidophos","volume":"93","author":"Sogorb","year":"1997","journal-title":"Toxicol. Lett."},{"key":"10.1016\/j.cbi.2021.109524_bib4","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/0378-4347(93)80264-5","article-title":"Chiral high-performance liquid chromatography and gas chromatography of the isomers of O-hexyl, O-2,5-dichlorophenyl phosphoramidate","volume":"622","author":"D\u00edaz-Alejo","year":"1993","journal-title":"J. Chromatogr."},{"key":"10.1016\/j.cbi.2021.109524_bib5","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/S0009-2797(97)00106-3","article-title":"A stereospecific phosphotriesterase in hen liver and brain","volume":"108","author":"D\u00edaz-Alejo","year":"1998","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2021.109524_bib6","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/S0009-2797(99)00035-6","article-title":"Dichlorophenyl phosphoramidates as substrates for avian and mammalian liver phosphotriesterases: activity levels, calcium dependence and stereospecificity","volume":"119\u2013120","author":"Monroy-Noyola","year":"1999","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2021.109524_bib7","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1016\/S0887-2333(99)00066-1","article-title":"Enzyme concentration as an important factor in the in vitro testing of the stereospecificity of the enzymatic hydrolysis of organophosphorus compounds","volume":"4\u20135","author":"Monroy-Noyola","year":"1999","journal-title":"Toxicol. Vitro"},{"key":"10.1016\/j.cbi.2021.109524_bib8","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.toxlet.2007.03.002","article-title":"Stereospecific hydrolysis of a phosphoramidate as a model to understand the role of biotransformation in the neurotoxicity of chiral organophosphorus compounds","volume":"170","author":"Monroy-Noyola","year":"2007","journal-title":"Toxicol. Lett."},{"key":"10.1016\/j.cbi.2021.109524_bib9","doi-asserted-by":"crossref","first-page":"1801","DOI":"10.1007\/s00204-014-1327-2","article-title":"Stereospecific hydrolysis of a phosphoramidate used as an OPIDP model by human sera with PON1 192 alloforms","volume":"89","author":"Monroy-Noyola","year":"2015","journal-title":"Arch. Toxicol."},{"key":"10.1016\/j.cbi.2021.109524_bib10","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/j.fct.2017.05.055","article-title":"Copper activation of organophosporus compounds detoxication by chicken serum","volume":"106","author":"Monroy-Noyola","year":"2017","journal-title":"Food Chem. Toxicol."},{"key":"10.1016\/j.cbi.2021.109524_bib11","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1016\/j.fct.2018.07.047","article-title":"Albumin, the responsible protein of the Cu2+-dependent hydrolysis of O-hexyl O-2, 5-dichlorophenyl phosphoramidate (HDCP) by chicken serum \"antagonistic stereoselectivity","volume":"120","author":"Monroy-Noyola","year":"2018","journal-title":"Food Chem. Toxicol."},{"key":"10.1016\/j.cbi.2021.109524_bib12","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1042\/bj2870211","article-title":"Further characterization of the N-terminal copper(II)- and nickel(II)-binding motif of proteins Studies of metal binding to chicken serum albumin and the native sequence peptide","volume":"287","author":"Predki","year":"1992","journal-title":"Biochem. J."},{"key":"10.1016\/j.cbi.2021.109524_bib13","series-title":"Documentation of NCBI's Annotation Process","article-title":"Definition predicted: Meleagris gallopavo serum albumin-like (LOC100546796)","author":"Ncbi","year":"2016"},{"key":"10.1016\/j.cbi.2021.109524_bib14","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1016\/j.cbi.2019.05.039","article-title":"Copper (II)-dependent hydrolysis of trichloronate by Turkey serum albumin","volume":"308","author":"Almenares-L\u00f3pez","year":"2019","journal-title":"Chem. Biol. Interact."},{"year":"1991","series-title":"GeneBank Database Accession # 63740","author":"Cassady","key":"10.1016\/j.cbi.2021.109524_bib15"},{"key":"10.1016\/j.cbi.2021.109524_bib16","series-title":"All about Albumin; Biochemistry, Genetics and Medical Applications","first-page":"432","author":"Peters","year":"1996"},{"issue":"6","key":"10.1016\/j.cbi.2021.109524_bib17","doi-asserted-by":"crossref","first-page":"2677","DOI":"10.1007\/s00216-010-4076-y","article-title":"Matrix-assisted laser desorption\/ionization time-of-flight mass spectrometry (MALDI-TOF MS) for detection and identification of albumin phosphylation by organophosphorus pesticides and G- and V-type nerve agents","volume":"398","author":"John","year":"2010","journal-title":"Anal. Bioanal. Chem."},{"issue":"4","key":"10.1016\/j.cbi.2021.109524_bib18","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1007\/s002040050492","article-title":"Phosphotriesterase activity identified in purified serum albumins","volume":"72","author":"Sogorb","year":"1998","journal-title":"Arch. Toxicol."},{"issue":"12","key":"10.1016\/j.cbi.2021.109524_bib19","doi-asserted-by":"crossref","first-page":"1441","DOI":"10.1021\/tx980015z","article-title":"Chicken serum albumin hydrolyzes dichlorophenyl phosphoramidates by a mechanism based on transient phosphorylation","volume":"11","author":"Sogorb","year":"1998","journal-title":"Chem. Res. Toxicol."},{"issue":"2","key":"10.1016\/j.cbi.2021.109524_bib20","doi-asserted-by":"crossref","first-page":"178","DOI":"10.2144\/000112528","article-title":"Serum albumin leads to false-positive results in the XTT and the MTT assay","volume":"43","author":"Funk","year":"2007","journal-title":"Biotechniques"},{"issue":"2","key":"10.1016\/j.cbi.2021.109524_bib21","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/0009-8981(83)90124-9","article-title":"A modification of the 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) method for the determination of the sulphhydryl content of human serum albumin","volume":"130","author":"Ghiggeri","year":"1983","journal-title":"Clin. Chim. Acta"},{"issue":"2","key":"10.1016\/j.cbi.2021.109524_bib22","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1016\/0005-2795(81)90025-8","article-title":"High yield coupling of peptides to protein carriers","volume":"670","author":"Atassi","year":"1981","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.cbi.2021.109524_bib23","first-page":"227","article-title":"Appearance of new N-terminal residues upon treatment of human and bovine serum albumin with N-bromosuccinimide","volume":"31","author":"Peters","year":"1959","journal-title":"C. R. Trav. Lab. Carlsberg"},{"issue":"12","key":"10.1016\/j.cbi.2021.109524_bib24","doi-asserted-by":"crossref","first-page":"5444","DOI":"10.1016\/j.bbagen.2013.06.018","article-title":"Binding of transition metal ions to albumin: sites, affinities and rates","volume":"1830","author":"Bal","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.cbi.2021.109524_bib25","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/j.ijbiomac.2018.11.120","article-title":"The effect of the stoichiometric ratio of zinc towards the fibrillation of Bovine Serum Albumin (BSA): a mechanistic insight","volume":"123","author":"Roy","year":"2019","journal-title":"Int. J. Biol. Macromol."}],"container-title":["Chemico-Biological Interactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279721001605?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279721001605?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,14]],"date-time":"2025-09-14T14:03:07Z","timestamp":1757858587000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0009279721001605"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,8]]},"references-count":25,"alternative-id":["S0009279721001605"],"URL":"https:\/\/doi.org\/10.1016\/j.cbi.2021.109524","relation":{},"ISSN":["0009-2797"],"issn-type":[{"type":"print","value":"0009-2797"}],"subject":[],"published":{"date-parts":[[2021,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"DAEH N-terminal sequence of avian serum albumins as catalytic center of Cu (II)-dependent organophosphorus hydrolyzing A-esterase activity","name":"articletitle","label":"Article Title"},{"value":"Chemico-Biological Interactions","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cbi.2021.109524","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"109524"}}