{"doi":"10.1016/j.biotechadv.2013.12.001","title":"Challenges and opportunities in the purification of recombinant tagged proteins","abstract":null,"journal":"Biotechnology Advances","year":2014,"id":591021,"datarank":5.1418739283407255,"base_score":5.087596335232384,"endowment":5.087596335232384,"self_citation_contribution":0.7631394502848576,"citation_network_contribution":4.378734478055868,"self_endowment_contribution":0.7631394502848576,"citer_contribution":4.378734478055868,"corpus_percentile":null,"corpus_rank":null,"citation_count":161,"citer_count":154,"citers_with_citation_signal":121,"citers_with_endowment":121,"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":1512116,"name":"Christopher R. Lowe","orcid":null,"position":1,"is_corresponding":false},{"id":1512117,"name":"Ana Cecília A. Roque","orcid":null,"position":2,"is_corresponding":false},{"id":1512115,"name":"Ana Sofia Pina","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Challenges and opportunities in the purification of recombinant tagged proteins","abstract":"The purification of recombinant proteins by affinity chromatography is one of the most efficient strategies due to the high recovery yields and purity achieved. However, this is dependent on the availability of specific affinity adsorbents for each particular target protein. The diversity of proteins to be purified augments the complexity and number of specific affinity adsorbents needed, and therefore generic platforms for the purification of recombinant proteins are appealing strategies. This justifies why genetically encoded affinity tags became so popular for recombinant protein purification, as these systems only require specific ligands for the capture of the fusion protein through a pre-defined affinity tag tail. There is a wide range of available affinity pairs \"tag-ligand\" combining biological or structural affinity ligands with the respective binding tags. This review gives a general overview of the well-established \"tag-ligand\" systems available for fusion protein purification and also explores current unconventional strategies under development.","is_dataset_classified":null,"base_score":5.087596335232384,"endowment":5.087596335232384,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"24334194","pmcid":"PMC7125906","openalex_id":"https://openalex.org/W2095373397","authors":[],"funders":[{"funder_name":"Fundação para a Ciência e a Tecnologia","grant_id":"PEst-C/EQB/LA0006/2011","title":null},{"funder_name":"Fundação para a Ciência e a Tecnologia","grant_id":"PTDC/BIO/65383/2006,/EBB-BIO/102163/2008","title":null},{"funder_name":"Fundação para a Ciência e a Tecnologia","grant_id":"PTDC/EBB-BIO/098961/2008","title":null},{"funder_name":"Fundação para a Ciência e a Tecnologia","grant_id":"PTDC/EBB-BIO/118317/2010","title":null},{"funder_name":"A.S.P.","grant_id":"SFRH/BD/48804/2008","title":null}],"total_grants":5,"fwci":4.7843,"citation_percentile":0.95054494,"influential_citations":0,"citation_trend":[{"year":2014,"count":2},{"year":2015,"count":6},{"year":2016,"count":12},{"year":2017,"count":7},{"year":2018,"count":34},{"year":2019,"count":9},{"year":2020,"count":15},{"year":2021,"count":10},{"year":2022,"count":7},{"year":2023,"count":17},{"year":2024,"count":14},{"year":2025,"count":19},{"year":2026,"count":9}],"oa_status":"green","license":"https://www.elsevier.com/tdm/userlicense/1.0/","oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/7125906","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/7125906","host_type":"repository"},{"url":"https://api.elsevier.com/content/article/PII:S0734975013002176?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0734975013002176?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.biotechadv.2013.12.001","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/24334194","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC7125906","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC7125906?pdf=render","host_type":"Europe_PMC"}],"fields_of_study":["Monoclonal and Polyclonal Antibodies Research","Protein purification and stability","Peptidase Inhibition and Analysis","Animals","Chromatography, Affinity","Humans","Ligands","Mice","Recombinant Fusion Proteins"],"mesh_terms":["Animals","Chromatography, Affinity","Humans","Ligands","Recombinant Fusion Proteins","Mice"],"keywords":["Tandem affinity purification","Recombinant DNA","Affinity chromatography","FLAG-tag","Fusion protein","Myc-tag","Ligand (biochemistry)","Protein purification","Target protein","Protein tag","Computational biology","Biochemistry","Chemistry","Biology","Chromatography","Receptor","Enzyme","Gene","Fusion proteins","Affinity ligands","Recombinant Proteins","Affinity Tags"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-25T13:47:09.691328Z","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":[]}