{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,17]],"date-time":"2026-06-17T03:34:43Z","timestamp":1781667283402,"version":"3.54.5"},"reference-count":30,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2026,2,1]],"date-time":"2026-02-01T00:00:00Z","timestamp":1769904000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,2,1]],"date-time":"2026-02-01T00:00:00Z","timestamp":1769904000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,12,19]],"date-time":"2025-12-19T00:00:00Z","timestamp":1766102400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000054","name":"National Institutes of Health National Cancer Institute","doi-asserted-by":"publisher","award":["CA233576"],"award-info":[{"award-number":["CA233576"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000054","name":"National Institutes of Health National Cancer Institute","doi-asserted-by":"publisher","award":["CA291724"],"award-info":[{"award-number":["CA291724"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2026,2]]},"DOI":"10.1016\/j.jbc.2025.111099","type":"journal-article","created":{"date-parts":[[2025,12,22]],"date-time":"2025-12-22T07:39:56Z","timestamp":1766389196000},"page":"111099","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"title":["Chaperone-assisted expression and purification of the AML-associated Src-family kinase Fgr in Escherichia coli"],"prefix":"10.1016","volume":"302","author":[{"given":"Giancarlo","family":"Gonzalez-Areizaga","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5238-3806","authenticated-orcid":false,"given":"Thomas E.","family":"Smithgall","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2025.111099_bib1","doi-asserted-by":"crossref","first-page":"7906","DOI":"10.1038\/sj.onc.1208160","article-title":"Src family kinases, key regulators of signal transduction","volume":"23","author":"Parsons","year":"2004","journal-title":"Oncogene"},{"key":"10.1016\/j.jbc.2025.111099_bib2","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/j.bbapap.2005.07.027","article-title":"Endogenous and synthetic inhibitors of the Src-family protein tyrosine kinases","volume":"1754","author":"Chong","year":"2005","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.jbc.2025.111099_bib3","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1038\/385595a0","article-title":"Three-dimensional structure of the tyrosine kinase c-Src","volume":"385","author":"Xu","year":"1997","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2025.111099_bib4","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1016\/S1097-2765(00)80356-1","article-title":"Crystal structures of c-Src reveal features of its autoinhibitory mechanism","volume":"3","author":"Xu","year":"1999","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2025.111099_bib5","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1038\/385602a0","article-title":"Crystal structure of the Src family tyrosine kinase Hck","volume":"385","author":"Sicheri","year":"1997","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2025.111099_bib6","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1016\/S1097-2765(00)80357-3","article-title":"Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor","volume":"3","author":"Schindler","year":"1999","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2025.111099_bib7","doi-asserted-by":"crossref","first-page":"2594","DOI":"10.1021\/acs.biochem.4c00323","article-title":"Cocrystallization of the Src-family kinase Hck with the ATP-Site inhibitor A-419259 stabilizes an extended activation loop conformation","volume":"63","author":"Selzer","year":"2024","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2025.111099_bib8","doi-asserted-by":"crossref","first-page":"1508","DOI":"10.1016\/j.str.2022.08.008","article-title":"ATP-site inhibitors induce unique conformations of the acute myeloid leukemia-associated Src-family kinase, Fgr","volume":"30","author":"Du","year":"2022","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2025.111099_bib9","doi-asserted-by":"crossref","first-page":"3058","DOI":"10.1007\/s00018-008-8122-2","article-title":"Structure and dynamic regulation of Src-family kinases","volume":"65","author":"Engen","year":"2008","journal-title":"Cell Mol. Life Sci."},{"key":"10.1016\/j.jbc.2025.111099_bib10","doi-asserted-by":"crossref","first-page":"eaat5916","DOI":"10.1126\/scisignal.aat5916","article-title":"The Src family kinase Fgr is a transforming oncoprotein that functions independently of SH3-SH2 domain regulation","volume":"11","author":"Shen","year":"2018","journal-title":"Sci. Signal."},{"key":"10.1016\/j.jbc.2025.111099_bib11","first-page":"2020","article-title":"SRC-Family kinases in acute myeloid leukaemia and mastocytosis","volume":"12","author":"Voisset","year":"1996","journal-title":"Cancers (Basel)"},{"key":"10.1016\/j.jbc.2025.111099_bib12","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0225887","article-title":"Expression of myeloid Src-family kinases is associated with poor prognosis in AML and influences Flt3-ITD kinase inhibitor acquired resistance","volume":"14","author":"Patel","year":"2019","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2025.111099_bib13","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/S0969-2126(96)00028-7","article-title":"Chaperone-assisted protein expression","volume":"4","author":"Cole","year":"1996","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2025.111099_bib14","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1146\/annurev-biophys-082521-113418","article-title":"Chaperonin mechanisms: multiple and (Mis)Understood?","volume":"51","author":"Horovitz","year":"2022","journal-title":"Annu. Rev. Biophys."},{"key":"10.1016\/j.jbc.2025.111099_bib15","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1007\/978-1-0716-1859-2_20","article-title":"Optimizing chaperone removal strategy from overexpressed recombinant proteins : GNE, a case Study","volume":"2406","author":"Sharma","year":"2022","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.jbc.2025.111099_bib16","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1177\/1087057106286829","article-title":"A generic, homogenous method for measuring kinase and inhibitor activity via adenosine 5'-diphosphate accumulation","volume":"11","author":"Charter","year":"2006","journal-title":"J. Biomol. Screen."},{"key":"10.1016\/j.jbc.2025.111099_bib17","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0105629","article-title":"Differential sensitivity of Src-family kinases to activation by SH3 domain displacement","volume":"9","author":"Moroco","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2025.111099_bib18","first-page":"635","article-title":"Overproduction of bacterial chaperones improves the solubility of recombinant protein tyrosine kinases in escherichia coli","volume":"40","author":"Caspers","year":"1994","journal-title":"Cell Mol. Biol. (Noisy-le-grand)"},{"key":"10.1016\/j.jbc.2025.111099_bib19","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1073\/pnas.92.4.1048","article-title":"Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL","volume":"92","author":"Amrein","year":"1995","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2025.111099_bib20","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.pep.2008.10.022","article-title":"Chaperone over-expression in escherichia coli: apparent increased yields of soluble recombinant protein kinases are due mainly to soluble aggregates","volume":"64","author":"Haacke","year":"2009","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.jbc.2025.111099_bib21","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1186\/1472-6750-7-32","article-title":"Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli","volume":"7","author":"de Marco","year":"2007","journal-title":"BMC. Biotechnol."},{"key":"10.1016\/j.jbc.2025.111099_bib22","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/j.pep.2008.04.001","article-title":"Bacterial expression and purification of interleukin-2 tyrosine kinase: single step separation of the chaperonin impurity","volume":"60","author":"Joseph","year":"2008","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.jbc.2025.111099_bib23","doi-asserted-by":"crossref","first-page":"72","DOI":"10.3389\/fcimb.2013.00072","article-title":"Engineering production of punctional scFv antibody in E. coli by co-expressing the molecule chaperone Skp","volume":"3","author":"Wang","year":"2013","journal-title":"Front. Cell Infect. Microbiol."},{"key":"10.1016\/j.jbc.2025.111099_bib24","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1016\/j.jbiosc.2010.12.015","article-title":"Effects of cytoplasmic and periplasmic chaperones on secretory production of single-chain Fv antibody in Escherichia coli","volume":"111","author":"Sonoda","year":"2011","journal-title":"J. Biosci. Bioeng."},{"key":"10.1016\/j.jbc.2025.111099_bib25","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1186\/1475-2859-9-22","article-title":"Co-expression of Skp and FkpA chaperones improves cell viability and alters the global expression of stress response genes during scFvD1.3 production","volume":"9","author":"Ow","year":"2010","journal-title":"Microb. Cell Fact."},{"key":"10.1016\/j.jbc.2025.111099_bib26","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1006\/prep.1999.1035","article-title":"Escherichia coli skp chaperone coexpression improves solubility and phage display of single-chain antibody fragments","volume":"15","author":"Hayhurst","year":"1999","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.jbc.2025.111099_bib27","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1016\/j.pep.2005.07.028","article-title":"Enhanced soluble protein expression using two new fusion tags","volume":"46","author":"Chatterjee","year":"2006","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.jbc.2025.111099_bib28","doi-asserted-by":"crossref","first-page":"4822","DOI":"10.1021\/bi300412y","article-title":"The Skp chaperone helps fold soluble proteins in vitro by inhibiting aggregation","volume":"51","author":"Entzminger","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2025.111099_bib29","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jbiotec.2012.11.007","article-title":"Engineering Escherichia coli for soluble expression and single step purification of active human lysozyme","volume":"164","author":"Lamppa","year":"2013","journal-title":"J. Biotechnol."},{"key":"10.1016\/j.jbc.2025.111099_bib30","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2024.108088","article-title":"An SH3-binding allosteric modulator stabilizes the global conformation of the AML-associated Src-family kinase, Hck","volume":"301","author":"Selzer","year":"2025","journal-title":"J. Biol. Chem."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925825029515?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925825029515?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,2,23]],"date-time":"2026-02-23T20:26:19Z","timestamp":1771878379000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925825029515"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,2]]},"references-count":30,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2026,2]]}},"alternative-id":["S0021925825029515"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2025.111099","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2026,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Chaperone-assisted expression and purification of the AML-associated Src-family kinase Fgr in Escherichia coli","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2025.111099","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"111099"}}