{"doi":"10.5936/csbj.201303009","title":"THE ALBUMIN-BINDING DOMAIN AS A SCAFFOLD FOR PROTEIN ENGINEERING","abstract":null,"journal":"Computational and Structural Biotechnology Journal","year":2013,"id":592994,"datarank":3.8498402445503714,"base_score":4.74493212836325,"endowment":4.74493212836325,"self_citation_contribution":0.7117398192544876,"citation_network_contribution":3.138100425295884,"self_endowment_contribution":0.7117398192544876,"citer_contribution":3.138100425295884,"corpus_percentile":null,"corpus_rank":null,"citation_count":114,"citer_count":96,"citers_with_citation_signal":85,"citers_with_endowment":85,"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":1022336,"name":"Sophia Hober","orcid":"0000-0003-0605-8417","position":1,"is_corresponding":false},{"id":809228,"name":"Johan Nilvebrant","orcid":"0000-0002-6104-6446","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"THE ALBUMIN-BINDING DOMAIN AS A SCAFFOLD FOR PROTEIN ENGINEERING","abstract":"The albumin-binding domain is a small, three-helical protein domain found in various surface proteins expressed by gram-positive bacteria. Albumin binding is important in bacterial pathogenesis and several homologous domains have been identified. Such albumin-binding regions have been used for protein purification or immobilization. Moreover, improvement of the pharmacokinetics, through the non-covalent association to albumin, by fusing such domains to therapeutic proteins has been shown to be successful. Domains derived from streptococcal protein G and protein PAB from Finegoldia magna, which share a common origin and therefore represent an interesting evolutionary system, have been thoroughly studied structurally and functionally. Their albumin-binding sites have been mapped and these domains form the basis for a wide range of protein engineering approaches. By substitution-mutagenesis they have been engineered to achieve a broader specificity, an increased stability or an improved binding affinity, respectively. Furthermore, novel binding sites have been incorporated either by replacing the original albumin-binding surface, or by complementing it with a novel interaction interface. Combinatorial protein libraries, where several residues have been randomized simultaneously, have generated a large number of new variants with desired binding characteristics. The albumin-binding domain has also been utilized to explore the relationship between three-dimensional structure and amino acid sequence. Proteins with latent structural information built into their sequence, where a single amino acid substitution shifts the equilibrium in favor of a different fold with a new function, have been designed. Altogether, these examples illustrate the versatility of the albumin-binding domain as a scaffold for protein engineering.","is_dataset_classified":null,"base_score":4.74493212836325,"endowment":4.74493212836325,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"24688717","pmcid":"PMC3962080","openalex_id":"https://openalex.org/W2020558940","authors":[],"funders":[],"total_grants":0,"fwci":3.1098,"citation_percentile":0.90715491,"influential_citations":0,"citation_trend":[{"year":2014,"count":3},{"year":2015,"count":3},{"year":2016,"count":7},{"year":2017,"count":6},{"year":2018,"count":12},{"year":2019,"count":8},{"year":2020,"count":13},{"year":2021,"count":14},{"year":2022,"count":14},{"year":2023,"count":7},{"year":2024,"count":7},{"year":2025,"count":12},{"year":2026,"count":8}],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://doi.org/10.5936/csbj.201303009","host_type":"journal"},{"url":"https://doi.org/10.5936/csbj.201303009","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S2001037014601185?httpAccept=text/plain","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S2001037014601185?httpAccept=text/xml","host_type":"publisher"},{"url":"https://spj.science.org/doi/pdf/10.5936/csbj.201303009","host_type":"publisher"},{"url":"https://pubmed.ncbi.nlm.nih.gov/24688717","host_type":"repository"},{"url":"https://doaj.org/article/a6eb4cc7ac8a411396798012c597c993","host_type":"repository"},{"url":"http://europepmc.org/articles/PMC3962080","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3962080","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC3962080","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC3962080?pdf=render","host_type":"Europe_PMC"}],"fields_of_study":["Monoclonal and Polyclonal Antibodies Research","Biochemical and Structural Characterization","Glycosylation and Glycoproteins Research"],"mesh_terms":[],"keywords":["Protein engineering","Plasma protein binding","Albumin","Binding domain","Biochemistry","Mutagenesis","Protein structure","Amino acid","Protein domain","Binding site","Chemistry","Computational biology","Biophysics","Biology","Gene","Mutation","Specificity","Bispecific","Affinity maturation","Affinity Protein"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"uniprot"},{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-26T16:36:04.300258Z","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":[]}