{"doi":"10.1016/j.pep.2017.09.013","title":"High-level expression of soluble recombinant proteins in Escherichia coli using an HE-maltotriose-binding protein fusion tag","abstract":null,"journal":"Protein Expression and Purification","year":2018,"id":603866,"datarank":0.49983067652628066,"base_score":3.332204510175204,"endowment":3.332204510175204,"self_citation_contribution":0.49983067652628066,"citation_network_contribution":0.0,"self_endowment_contribution":0.49983067652628066,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":27,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1549179,"name":"Wanying Guo","orcid":null,"position":1,"is_corresponding":false},{"id":1549182,"name":"Bingqian Su","orcid":null,"position":2,"is_corresponding":false},{"id":918327,"name":"Yujie Guo","orcid":"0000-0002-0307-9266","position":3,"is_corresponding":false},{"id":115955,"name":"Jiang Wang","orcid":null,"position":4,"is_corresponding":false},{"id":1549184,"name":"Beibei Chu","orcid":null,"position":5,"is_corresponding":false},{"id":1549185,"name":"Guoyu Yang","orcid":null,"position":6,"is_corresponding":false},{"id":1549177,"name":"Yingqian Han","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"High-level expression of soluble recombinant proteins in Escherichia coli using an HE-maltotriose-binding protein fusion tag","abstract":"Recombinant proteins are commonly expressed in prokaryotic expression systems for large-scale production. The use of genetically engineered affinity and solubility enhancing fusion proteins has increased greatly in recent years, and there now exists a considerable repertoire of these that can be used to enhance the expression, stability, solubility, folding, and purification of their fusion partner. Here, a modified histidine tag (HE) used as an affinity tag was employed together with a truncated maltotriose-binding protein (MBP; consisting of residues 59-433) from Pyrococcus furiosus as a solubility enhancing tag accompanying a tobacco etch virus protease-recognition site for protein expression and purification in Escherichia coli. Various proteins tagged at the N-terminus with HE-MBP(Pyr) were expressed in E. coli BL21(DE3) cells to determine expression and solubility relative to those tagged with His6-MBP or His6-MBP(Pyr). Furthermore, four HE-MBP(Pyr)-fused proteins were purified by immobilized metal affinity chromatography to assess the affinity of HE with immobilized Ni<sup>2+</sup>. Our results showed that HE-MBP(Pyr) represents an attractive fusion protein allowing high levels of soluble expression and purification of recombinant protein in E. coli.","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"28963004","pmcid":null,"openalex_id":"https://openalex.org/W28963004","authors":[],"funders":[{"funder_name":"Ministry of Agriculture of China","grant_id":"2011-G35","title":null},{"funder_name":"Ministry of Agriculture of China","grant_id":"2014ZX0801015B","title":null}],"total_grants":2,"fwci":0.0,"citation_percentile":0.00923645,"influential_citations":0,"citation_trend":[],"oa_status":"closed","license":"https://www.elsevier.com/tdm/userlicense/1.0/","oa_locations":[{"url":"https://dialnet.unirioja.es/servlet/articulo?codigo=155257","host_type":"journal"},{"url":"https://api.elsevier.com/content/article/PII:S1046592817303959?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S1046592817303959?httpAccept=text/plain","host_type":"publisher"}],"fields_of_study":["Legal and Labor Studies","Agricultural Economics and Policy"],"mesh_terms":["Escherichia coli","Pyrococcus furiosus","Endopeptidases","Trisaccharides","Histidine","Oligopeptides","Recombinant Fusion Proteins","Chromatography, Affinity","Cloning, Molecular","Gene Expression","Protein Binding","Plasmids","Solubility","Protein Stability","Maltose-Binding Proteins"],"keywords":["Political science","Humanities","European union","Economics","Art","International trade","Recombinant protein","Histidine Tag","Soluble Protein Expression","Maltotriose Binding Protein"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Zero hunger"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-29T22:52:42.908880Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}