<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kanzler CR</submitter><funding>NICHD NIH HHS</funding><funding>National Institutes of Health</funding><funding>National Institute of General Medical Sciences</funding><funding>NIGMS NIH HHS</funding><funding>National Institute of Child Health and Human Development</funding><pagination>133-138</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9643680</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>492</volume><pubmed_abstract>BioID is a proximity labeling strategy whose goal is to identify in vivo protein-protein interactions. The central components of this strategy are modified biotin ligase enzymes that promiscuously add biotin groups to proteins in close proximity. The transferred biotin group provides a powerful tag for purification and thus identification of interacting proteins. While a variety of modified biotin ligases were created for BioID, the original enzymes were inefficient, required long incubation times, and high intracellular biotin concentrations for protein labeling. These limitations hinder the application of BioID in contexts such as developing embryos where processes such as cell division and cell fate decisions occur rapidly. Recently, a new biotin ligase called TurboID was developed that</pubmed_abstract><journal>Developmental biology</journal><pubmed_title>TurboID functions as an efficient biotin ligase for BioID applications in Xenopus embryos.</pubmed_title><pmcid>PMC9643680</pmcid><funding_grant_id>R01HD091921</funding_grant_id><funding_grant_id>T32GM135066</funding_grant_id><funding_grant_id>T32 GM135066</funding_grant_id><funding_grant_id>T32 GM008349</funding_grant_id><funding_grant_id>R01 HD091921</funding_grant_id><funding_grant_id>T32GM008349</funding_grant_id><pubmed_authors>Kanzler CR</pubmed_authors><pubmed_authors>Sheets MD</pubmed_authors><pubmed_authors>Dowdle ME</pubmed_authors><pubmed_authors>Donohue M</pubmed_authors></additional><is_claimable>false</is_claimable><name>TurboID functions as an efficient biotin ligase for BioID applications in Xenopus embryos.</name><description>BioID is a proximity labeling strategy whose goal is to identify in vivo protein-protein interactions. The central components of this strategy are modified biotin ligase enzymes that promiscuously add biotin groups to proteins in close proximity. The transferred biotin group provides a powerful tag for purification and thus identification of interacting proteins. While a variety of modified biotin ligases were created for BioID, the original enzymes were inefficient, required long incubation times, and high intracellular biotin concentrations for protein labeling. These limitations hinder the application of BioID in contexts such as developing embryos where processes such as cell division and cell fate decisions occur rapidly. Recently, a new biotin ligase called TurboID was developed that</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Dec</publication><modification>2025-04-26T09:40:15.361Z</modification><creation>2025-04-06T13:08:54.062Z</creation></dates><accession>S-EPMC9643680</accession><cross_references><pubmed>36270327</pubmed><doi>10.1016/j.ydbio.2022.10.005</doi></cross_references></HashMap>