{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,31]],"date-time":"2026-07-31T00:26:32Z","timestamp":1785457592810,"version":"3.56.0"},"reference-count":44,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31872600"],"award-info":[{"award-number":["31872600"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31572660"],"award-info":[{"award-number":["31572660"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100009666","name":"Salt Science Research Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100009666","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002367","name":"Chinese Academy of Sciences","doi-asserted-by":"publisher","award":["XDB0730200"],"award-info":[{"award-number":["XDB0730200"]}],"id":[{"id":"10.13039\/501100002367","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100010870","name":"Qingdao Municipal Science and Technology Bureau","doi-asserted-by":"publisher","award":["18-1-2-12-zhc"],"award-info":[{"award-number":["18-1-2-12-zhc"]}],"id":[{"id":"10.13039\/501100010870","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemical and Biophysical Research Communications"],"published-print":{"date-parts":[[2025,5]]},"DOI":"10.1016\/j.bbrc.2025.151683","type":"journal-article","created":{"date-parts":[[2025,3,22]],"date-time":"2025-03-22T17:08:47Z","timestamp":1742663327000},"page":"151683","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":3,"special_numbering":"C","title":["Structural insight into ligand interactions of thymidylate synthase from white spot syndrome virus"],"prefix":"10.1016","volume":"759","author":[{"given":"Changshui","family":"Liu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7109-9154","authenticated-orcid":false,"given":"Kun","family":"Zang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qingjun","family":"Ma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrc.2025.151683_bib1","series-title":"A Handbook of Shrimp Pathology and Diagnostic Procedures for Diseases of Cultured Penaeid Shrimp","author":"Lightner","year":"1996"},{"key":"10.1016\/j.bbrc.2025.151683_bib2","doi-asserted-by":"crossref","first-page":"822","DOI":"10.1111\/raq.12352","article-title":"Causative agent, diagnosis and management of white spot disease in shrimp: a review","volume":"12","author":"Dey","year":"2020","journal-title":"Rev. Aquacult."},{"key":"10.1016\/j.bbrc.2025.151683_bib3","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/j.jip.2012.03.013","article-title":"Disease will limit future food supply from the global crustacean fishery and aquaculture sectors","volume":"110","author":"Stentiford","year":"2012","journal-title":"J. Invertebr. Pathol."},{"key":"10.1016\/j.bbrc.2025.151683_bib4","doi-asserted-by":"crossref","first-page":"2633","DOI":"10.1007\/s00705-021-05156-1","article-title":"Changes to virus taxonomy and to the international code of virus classification and nomenclature ratified by the international committee on taxonomy of viruses (2021)","volume":"166","author":"Walker","year":"2021","journal-title":"Arch. Virol."},{"key":"10.1016\/j.bbrc.2025.151683_bib5","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1006\/viro.2001.1002","article-title":"The white spot syndrome virus DNA genome sequence","volume":"286","author":"van Hulten","year":"2001","journal-title":"Virology"},{"key":"10.1016\/j.bbrc.2025.151683_bib6","doi-asserted-by":"crossref","first-page":"11811","DOI":"10.1128\/JVI.75.23.11811-11820.2001","article-title":"Complete genome sequence of the shrimp white spot bacilliform virus","volume":"75","author":"Yang","year":"2001","journal-title":"J. Virol."},{"key":"10.1016\/j.bbrc.2025.151683_bib7","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.virusres.2005.01.003","article-title":"Identification and function of a shrimp white spot syndrome virus (WSSV) gene that encodes a dUTPase","volume":"110","author":"Liu","year":"2005","journal-title":"Virus Res."},{"key":"10.1016\/j.bbrc.2025.151683_bib8","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1074\/jbc.M117.815266","article-title":"The dUTPase of white spot syndrome virus assembles its active sites in a noncanonical manner","volume":"293","author":"Zang","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2025.151683_bib9","doi-asserted-by":"crossref","first-page":"2035","DOI":"10.1099\/vir.0.80048-0","article-title":"Identification of the thymidylate synthase within the genome of white spot syndrome virus","volume":"85","author":"Qin","year":"2004","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.bbrc.2025.151683_bib10","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1006\/viro.2000.0597","article-title":"Identification and characterization of a shrimp white spot syndrome virus (WSSV) gene that encodes a novel chimeric polypeptide of cellular-type thymidine kinase and thymidylate kinase","volume":"277","author":"Tsai","year":"2000","journal-title":"Virology"},{"key":"10.1016\/j.bbrc.2025.151683_bib11","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1007\/s10126-013-9529-9","article-title":"Protection of shrimp Penaeus monodon from WSSV infection using antisense constructs","volume":"16","author":"Ahanger","year":"2014","journal-title":"Mar. Biotechnol."},{"key":"10.1016\/j.bbrc.2025.151683_bib12","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1146\/annurev.bi.64.070195.003445","article-title":"The catalytic mechanism and structure of thymidylate synthase","volume":"64","author":"Carreras","year":"1995","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bbrc.2025.151683_bib13","doi-asserted-by":"crossref","first-page":"2241","DOI":"10.2174\/0929867054864868","article-title":"Thymidylate synthase structure, function and implication in drug discovery","volume":"12","author":"Costi","year":"2005","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.bbrc.2025.151683_bib14","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1038\/nrclinonc.2014.51","article-title":"Standing the test of time: targeting thymidylate biosynthesis in cancer therapy","volume":"11","author":"Wilson","year":"2014","journal-title":"Nat. Rev. Clin. Oncol."},{"key":"10.1016\/j.bbrc.2025.151683_bib15","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1021\/bi9815896","article-title":"Structure-based design of inhibitors specific for bacterial thymidylate synthase","volume":"38","author":"Stout","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2025.151683_bib16","doi-asserted-by":"crossref","first-page":"1148","DOI":"10.1021\/ml400208v","article-title":"Discovery of potent and selective inhibitors of Toxoplasma gondii thymidylate synthase for opportunistic infections","volume":"4","author":"Zaware","year":"2013","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.bbrc.2025.151683_bib17","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1016\/j.ejmech.2016.07.066","article-title":"X-ray crystal structures of Enterococcus faecalis thymidylate synthase with folate binding site inhibitors","volume":"123","author":"Catalano","year":"2016","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bbrc.2025.151683_bib18","doi-asserted-by":"crossref","first-page":"2069","DOI":"10.1002\/1873-3468.13474","article-title":"Understanding the structural basis of species selective, stereospecific inhibition for Cryptosporidium and human thymidylate synthase","volume":"593","author":"Czyzyk","year":"2019","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbrc.2025.151683_bib19","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1016\/j.cbpc.2009.06.008","article-title":"Functional identity of the active sites of crustacean and viral thymidylate synthases","volume":"150","author":"Arvizu-Flores","year":"2009","journal-title":"Comp. Biochem. Physiol. C Toxicol. Pharmacol."},{"key":"10.1016\/j.bbrc.2025.151683_bib20","doi-asserted-by":"crossref","first-page":"1891","DOI":"10.1007\/s00343-019-9184-8","article-title":"Structural analysis of a shrimp thymidylate synthase reveals species-specific interactions with dUMP and raltitrexed","volume":"38","author":"Liu","year":"2020","journal-title":"J. Ocean. Limnol."},{"key":"10.1016\/j.bbrc.2025.151683_bib21","doi-asserted-by":"crossref","first-page":"6069","DOI":"10.1093\/nar\/18.20.6069","article-title":"Ligation-independent cloning of PCR products (LIC-PCR)","volume":"18","author":"Aslanidis","year":"1990","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbrc.2025.151683_bib22","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1007\/s41365-019-0683-2","article-title":"The protein complex crystallography beamline (BL19U1) at the Shanghai Synchrotron Radiation Facility","volume":"30","author":"Zhang","year":"2019","journal-title":"Nucl. Sci. Tech."},{"key":"10.1016\/j.bbrc.2025.151683_bib23","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1107\/S0907444911007773","article-title":"Data processing and analysis with the autoPROC toolbox","volume":"67","author":"Vonrhein","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.bbrc.2025.151683_bib24","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"Xds","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.bbrc.2025.151683_bib25","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.1107\/S0907444913000061","article-title":"How good are my data and what is the resolution?","volume":"69","author":"Evans","year":"2013","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.bbrc.2025.151683_bib26","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.bbrc.2025.151683_bib27","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP4 suite and current developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.bbrc.2025.151683_bib28","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1107\/S0907444911056058","article-title":"Exploiting structure similarity in refinement: automated NCS and target-structure restraints in BUSTER","volume":"68","author":"Smart","year":"2012","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.bbrc.2025.151683_bib29","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1107\/S0907444912001308","article-title":"Towards automated crystallographic structure refinement with phenix.refine","volume":"68","author":"Afonine","year":"2012","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.bbrc.2025.151683_bib30","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.bbrc.2025.151683_bib31","doi-asserted-by":"crossref","first-page":"2731","DOI":"10.1093\/molbev\/msr121","article-title":"MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods","volume":"28","author":"Tamura","year":"2011","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.bbrc.2025.151683_bib32","doi-asserted-by":"crossref","first-page":"W320","DOI":"10.1093\/nar\/gku316","article-title":"Deciphering key features in protein structures with the new ENDscript server","volume":"42","author":"Robert","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbrc.2025.151683_bib33","doi-asserted-by":"crossref","first-page":"13449","DOI":"10.1074\/jbc.M117.787267","article-title":"Structural analyses of human thymidylate synthase reveal a site that may control conformational switching between active and inactive states","volume":"292","author":"Chen","year":"2017","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2025.151683_bib34","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.bioorg.2013.11.003","article-title":"Crystal structure of phosphoramide-phosphorylated thymidylate synthase reveals pSer127, reflecting probably pHis to pSer phosphotransfer","volume":"52","author":"Wilk","year":"2014","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bbrc.2025.151683_bib35","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.jmgm.2017.08.008","article-title":"Crystal structures of nematode (parasitic T. spiralis and free living C. elegans), compared to mammalian, thymidylate synthases (TS). Molecular docking and molecular dynamics simulations in search for nematode-specific inhibitors of TS","volume":"77","author":"Jarmu\u0142a","year":"2017","journal-title":"J. Mol. Graph. Model."},{"key":"10.1016\/j.bbrc.2025.151683_bib36","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1006\/jmbi.1993.1463","article-title":"Refined structures of substrate-bound and phosphate-bound thymidylate synthase from Lactobacillus casei","volume":"232","author":"Finer-Moore","year":"1993","journal-title":"J. Mol. Biol."},{"issue":"24","key":"10.1016\/j.bbrc.2025.151683_bib37","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.3390\/molecules24071257","article-title":"Structural comparison of Enterococcus faecalis and human thymidylate synthase complexes with the substrate dUMP and its analogue FdUMP provides hints about enzyme conformational variabilities","author":"Pozzi","year":"2019","journal-title":"Molecules"},{"key":"10.1016\/j.bbrc.2025.151683_bib38","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1016\/S0969-2126(98)00086-0","article-title":"The additivity of substrate fragments in enzyme\u2013ligand binding","volume":"6","author":"Stout","year":"1998","journal-title":"Structure"},{"key":"10.1016\/j.bbrc.2025.151683_bib39","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0143947","article-title":"Structure of the varicella zoster virus thymidylate synthase establishes functional and structural similarities as the human enzyme and potentiates itself as a target of brivudine","volume":"10","author":"Hew","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.bbrc.2025.151683_bib40","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0168019","article-title":"Structural analysis of thymidylate synthase from kaposi's sarcoma-associated herpesvirus with the anticancer drug raltitrexed","volume":"11","author":"Choi","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.bbrc.2025.151683_bib41","doi-asserted-by":"crossref","first-page":"2939","DOI":"10.1021\/bi200066k","article-title":"A survey of aspartate-phenylalanine and glutamate-phenylalanine interactions in the protein data bank: searching for anion-\u03c0 pairs","volume":"50","author":"Philip","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2025.151683_bib42","doi-asserted-by":"crossref","first-page":"1168","DOI":"10.1016\/j.ijbiomac.2020.11.071","article-title":"Structure analysis of thymidylate synthase from white spot syndrome virus reveals WSSV-specific structural elements","volume":"167","author":"Panchal","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bbrc.2025.151683_bib43","doi-asserted-by":"crossref","first-page":"E542","DOI":"10.1073\/pnas.1104829108","article-title":"Protein-protein interface-binding peptides inhibit the cancer therapy target human thymidylate synthase","volume":"108","author":"Cardinale","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.bbrc.2025.151683_bib44","doi-asserted-by":"crossref","first-page":"1745","DOI":"10.1111\/raq.12670","article-title":"Structural insights into proteins from white spot syndrome virus: perspectives on structure-based anti-viral strategies","volume":"14","author":"Datta","year":"2022","journal-title":"Rev. Aquacult."}],"container-title":["Biochemical and Biophysical Research Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X25003973?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X25003973?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T14:51:48Z","timestamp":1762095108000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006291X25003973"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,5]]},"references-count":44,"alternative-id":["S0006291X25003973"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrc.2025.151683","relation":{},"ISSN":["0006-291X"],"issn-type":[{"value":"0006-291X","type":"print"}],"subject":[],"published":{"date-parts":[[2025,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural insight into ligand interactions of thymidylate synthase from white spot syndrome virus","name":"articletitle","label":"Article Title"},{"value":"Biochemical and Biophysical Research Communications","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbrc.2025.151683","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"151683"}}