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We also demonstrate that the biotinylation range of BioID2 can be considerably modulated using flexible linkers, thus enabling application-specific adjustment of the biotin-labeling radius.</jats:p>","journal":"Molecular Biology of the Cell","year":2016,"id":679066,"datarank":1.0252776879220953,"base_score":6.835184586147301,"endowment":6.835184586147301,"self_citation_contribution":1.0252776879220953,"citation_network_contribution":0.0,"self_endowment_contribution":1.0252776879220953,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":929,"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":1774270,"name":"Samuel C. 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Here we report improvements to the BioID method centered on BioID2, a substantially smaller promiscuous biotin ligase. BioID2 enables more-selective targeting of fusion proteins, requires less biotin supplementation, and exhibits enhanced labeling of proximate proteins. Thus BioID2 improves the efficiency of screening for protein–protein associations. 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