{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T00:52:28Z","timestamp":1792457548390,"version":"4.5.0"},"reference-count":29,"publisher":"Elsevier BV","issue":"24","license":[{"start":{"date-parts":[[2019,12,1]],"date-time":"2019-12-01T00:00:00Z","timestamp":1575158400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,12,1]],"date-time":"2019-12-01T00:00:00Z","timestamp":1575158400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100008530","name":"European Regional Development Fund","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100008530","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic &amp; Medicinal Chemistry"],"published-print":{"date-parts":[[2019,12]]},"DOI":"10.1016\/j.bmc.2019.115177","type":"journal-article","created":{"date-parts":[[2019,11,2]],"date-time":"2019-11-02T23:15:02Z","timestamp":1572736502000},"page":"115177","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":9,"title":["Exploration of zinc-binding groups for the design of inhibitors for the oxytocinase subfamily of M1 aminopeptidases"],"prefix":"10.1016","volume":"27","author":[{"given":"Sofia","family":"Tsoukalidou","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Magdalini","family":"Kakou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ioannis","family":"Mavridis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Despoina","family":"Koumantou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vito","family":"Calderone","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marco","family":"Fragai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Efstratios","family":"Stratikos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Athanasios","family":"Papakyriakou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dionisios","family":"Vourloumis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bmc.2019.115177_b0005","doi-asserted-by":"crossref","first-page":"6468","DOI":"10.1021\/acs.jmedchem.7b00782","article-title":"Design of aminopeptidase n inhibitors as anti-cancer agents","volume":"61","author":"Amin","year":"2018","journal-title":"J Med Chem"},{"key":"10.1016\/j.bmc.2019.115177_b0010","doi-asserted-by":"crossref","first-page":"3656","DOI":"10.2174\/138161209789271816","article-title":"A new role for zn(ii) aminopeptidases: antigenic peptide generation and destruction","volume":"15","author":"Evnouchidou","year":"2009","journal-title":"Curr Pharm Des"},{"key":"10.1016\/j.bmc.2019.115177_b0015","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.bbapap.2004.09.011","article-title":"The oxytocinase subfamily of m1 aminopeptidases","volume":"1751","author":"Tsujimoto","year":"2005","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.bmc.2019.115177_h0020","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.coi.2012.10.001","article-title":"Peptidases trimming mhc class i ligands","volume":"25","author":"Weimershaus","year":"2012","journal-title":"Curr Opin Immunol"},{"key":"10.1016\/j.bmc.2019.115177_h0025","doi-asserted-by":"crossref","first-page":"946","DOI":"10.3389\/fimmu.2017.00946","article-title":"The role of conformational dynamics in antigen trimming by intracellular aminopeptidases","volume":"8","author":"Papakyriakou","year":"2017","journal-title":"Front Immunol"},{"key":"10.1016\/j.bmc.2019.115177_h0030","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.cbpa.2014.08.007","article-title":"Regulating adaptive immune responses using small molecule modulators of aminopeptidases that process antigenic peptides","volume":"23C","author":"Stratikos","year":"2014","journal-title":"Curr Opin Chem Biol"},{"key":"10.1016\/j.bmc.2019.115177_h0035","first-page":"1","article-title":"Inhibitors of er aminopeptidase 1 and 2: from design to clinical application","volume":"25","author":"Georgiadis","year":"2018","journal-title":"Curr Med Chem"},{"key":"10.1016\/j.bmc.2019.115177_h0040","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1093\/jb\/mvt066","article-title":"Endoplasmic reticulum aminopeptidases: Biochemistry, physiology and pathology","volume":"154","author":"Hattori","year":"2013","journal-title":"J Biochem"},{"key":"10.1016\/j.bmc.2019.115177_h0045","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1358\/dnp.2009.22.3.1325032","article-title":"Targeting the insulin-regulated aminopeptidase\/at4 receptor for cognitive disorders","volume":"22","author":"Hallberg","year":"2009","journal-title":"Drug News Perspect"},{"key":"10.1016\/j.bmc.2019.115177_h0050","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.1016\/j.molcel.2015.04.008","article-title":"Erp44 exerts redox-dependent control of blood pressure at the er","volume":"58","author":"Hisatsune","year":"2015","journal-title":"Mol Cell"},{"key":"10.1016\/j.bmc.2019.115177_h0055","doi-asserted-by":"crossref","first-page":"4443","DOI":"10.4049\/jimmunol.1300935","article-title":"Tlr-mediated secretion of endoplasmic reticulum aminopeptidase 1 from macrophages","volume":"192","author":"Goto","year":"2014","journal-title":"J Immunol"},{"key":"10.1016\/j.bmc.2019.115177_b0035","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1021\/acschemneuro.6b00146","article-title":"Aryl sulfonamide inhibitors of insulin-regulated aminopeptidase enhance spine density in primary hippocampal neuron cultures","volume":"7","author":"Diwakarla","year":"2016","journal-title":"ACS Chem Neurosci"},{"key":"10.1016\/j.bmc.2019.115177_h0065","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1021\/acsmedchemlett.6b00505","article-title":"Crystal structures of erap2 complexed with inhibitors reveal pharmacophore requirements for optimizing inhibitor potency","volume":"8","author":"Mpakali","year":"2017","journal-title":"ACS Med Chem Lett"},{"key":"10.1016\/j.bmc.2019.115177_h0070","doi-asserted-by":"crossref","first-page":"4832","DOI":"10.1016\/j.bmcl.2013.07.024","article-title":"Novel selective inhibitors of aminopeptidases that generate antigenic peptides","volume":"23","author":"Papakyriakou","year":"2013","journal-title":"Bioorg Med Chem Lett"},{"key":"10.1016\/j.bmc.2019.115177_h0075","doi-asserted-by":"crossref","first-page":"1524","DOI":"10.1021\/jm501867s","article-title":"3,4-diaminobenzoic acid derivatives as inhibitors of the oxytocinase subfamily of m1 aminopeptidases with immune-regulating properties","volume":"58","author":"Papakyriakou","year":"2015","journal-title":"J Med Chem"},{"key":"10.1016\/j.bmc.2019.115177_h0080","doi-asserted-by":"crossref","first-page":"3156","DOI":"10.1021\/ja057957s","article-title":"A new role for old ligands: Discerning chelators for zinc metalloproteinases","volume":"128","author":"Jacobsen","year":"2006","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.bmc.2019.115177_h0085","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.bbamcr.2009.08.006","article-title":"To bind zinc or not to bind zinc: An examination of innovative approaches to improved metalloproteinase inhibition","volume":"1803","author":"Jacobsen","year":"2010","journal-title":"Biochim Biophys Acta Mol Cell Res"},{"key":"10.1016\/j.bmc.2019.115177_h0090","doi-asserted-by":"crossref","first-page":"3423","DOI":"10.1021\/ic026029g","article-title":"Examination of novel zinc-binding groups for use in matrix metalloproteinase inhibitors","volume":"42","author":"Puerta","year":"2003","journal-title":"Inorg Chem"},{"key":"10.1016\/j.bmc.2019.115177_h0095","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1007\/s00775-005-0053-x","article-title":"Heterocyclic zinc-binding groups for use in next-generation matrix metalloproteinase inhibitors: Potency, toxicity, and reactivity","volume":"11","author":"Puerta","year":"2006","journal-title":"J Biol Inorg Chem"},{"key":"10.1016\/j.bmc.2019.115177_h0100","doi-asserted-by":"crossref","first-page":"8388","DOI":"10.1021\/ja0485513","article-title":"New beginnings for matrix metalloproteinase inhibitors: Identification of high-affinity zinc-binding groups","volume":"126","author":"Puerta","year":"2004","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.bmc.2019.115177_b0050","doi-asserted-by":"crossref","first-page":"3492","DOI":"10.1021\/jm301769u","article-title":"3-hydroxypyridin-2-thione as novel zinc binding group for selective histone deacetylase inhibition","volume":"56","author":"Patil","year":"2013","journal-title":"J Med Chem"},{"key":"10.1016\/j.bmc.2019.115177_b0055","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1021\/acsmedchemlett.9b00002","article-title":"High-resolution crystal structure of endoplasmic reticulum aminopeptidase 1 with bound phosphinic transition-state analogue inhibitor","volume":"10","author":"Giastas","year":"2019","journal-title":"ACS Med Chem Lett"},{"key":"10.1016\/j.bmc.2019.115177_b0060","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.1021\/jm00168a033","article-title":"Novel 3-hydroxy-2(1h)-pyridinones. Synthesis, iron(iii)-chelating properties, and biological activity","volume":"33","author":"Streater","year":"1990","journal-title":"J Med Chem"},{"key":"10.1016\/j.bmc.2019.115177_b0065","doi-asserted-by":"crossref","first-page":"3267","DOI":"10.1016\/S0040-4020(01)00196-X","article-title":"Practical syntheses of b disaccharide and linear b type 2 trisaccharide - non-primate epitope markers recognized by human anti-\u03b1-gal antibodies causing hyperacute rejection of xenotransplants","volume":"57","author":"Hanessian","year":"2001","journal-title":"Tetrahedron"},{"key":"10.1016\/j.bmc.2019.115177_b0070","article-title":"Applications of lawesson's reagent in organic and organometallic syntheses","volume":"1929\u20131958","author":"Jesberger","year":"2003","journal-title":"Synthesis"},{"key":"10.1016\/j.bmc.2019.115177_b0075","doi-asserted-by":"crossref","first-page":"5334","DOI":"10.1073\/pnas.0407106102","article-title":"Conformational variability of matrix metalloproteinases: beyond a single 3d structure","volume":"102","author":"Bertini","year":"2005","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.bmc.2019.115177_b0080","doi-asserted-by":"crossref","first-page":"7392","DOI":"10.1016\/j.bmc.2006.07.028","article-title":"Synthesis of bicyclic molecular scaffolds (btaa): an investigation towards new selective mmp-12 inhibitors","volume":"14","author":"Mannino","year":"2006","journal-title":"Bioorg Med Chem"},{"key":"10.1016\/j.bmc.2019.115177_b0085","doi-asserted-by":"crossref","first-page":"W441","DOI":"10.1093\/nar\/gkp253","article-title":"Ic50-to-ki: a web-based tool for converting ic50 to ki values for inhibitors of enzyme activity and ligand binding","volume":"37","author":"Cer","year":"2009","journal-title":"Nucl Acids Res"},{"key":"10.1016\/j.bmc.2019.115177_b0090","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.1021\/acs.biochem.6b01170","article-title":"Critical role of interdomain interactions in the conformational change and catalytic mechanism of endoplasmic reticulum aminopeptidase 1","volume":"56","author":"Stamogiannos","year":"2017","journal-title":"Biochemistry"}],"container-title":["Bioorganic &amp; Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968089619311150?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968089619311150?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,19]],"date-time":"2025-10-19T01:04:23Z","timestamp":1760835863000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0968089619311150"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,12]]},"references-count":29,"journal-issue":{"issue":"24","published-print":{"date-parts":[[2019,12]]}},"alternative-id":["S0968089619311150"],"URL":"https:\/\/doi.org\/10.1016\/j.bmc.2019.115177","relation":{},"ISSN":["0968-0896"],"issn-type":[{"value":"0968-0896","type":"print"}],"subject":[],"published":{"date-parts":[[2019,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Exploration of zinc-binding groups for the design of inhibitors for the oxytocinase subfamily of M1 aminopeptidases","name":"articletitle","label":"Article Title"},{"value":"Bioorganic & Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bmc.2019.115177","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"115177"}}