ArticleMethods in molecular biology (Clifton, N.J.)2016
Identifying Protein-Protein Associations at the Nuclear Envelope with BioID.
Article in Methods in molecular biology (Clifton, N.J.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Proximity proteomics reveals a role for IFI16 during human coronavirus infection.bioRxiv : the preprint server for biology · 2026Article
- A BioID-based approach uncovers the interactome of hexose-6-phosphate dehydrogenase in breast cancer cells and identifies anterior gradient protein 2 as an interacting partner.Cell & bioscience · 2025Article
- Proximity Proteomics Reveals USP44 Forms a Complex with BRCA2 in Neuroblastoma Cells and Is Required to Prevent Chromosome Breakage.Biomedicines · 2024Article
- RESC14 and RESC8 cooperate to mediate RESC function and dynamics during trypanosome RNA editing.Nucleic acids research · 2024Article
- Cell surface protein-protein interaction profiling for biological network analysis and novel target discovery.Life medicine · 2024Review
- Centralspindlin proteins Pavarotti and Tumbleweed along with WASH regulate nuclear envelope budding.The Journal of cell biology · 2023Article
- Proximity Mapping of CCP6 Reveals Its Association with Centrosome Organization and Cilium Assembly.International journal of molecular sciences · 2023Article
- Oncohistone interactome profiling uncovers contrasting oncogenic mechanisms and identifies potential therapeutic targets in high grade glioma.Acta neuropathologica · 2022Article
- The Nuclear Lamina.Cold Spring Harbor perspectives in biology · 2022Review
- Proximity-dependent biotinylation detects associations between SARS coronavirus nonstructural protein 1 and stress granule-associated proteins.The Journal of biological chemistry · 2021Article
- Mapping the micro-proteome of the nuclear lamina and lamina-associated domains.Life science alliance · 2021Article
- Article
- Mass spectrometry-based protein-protein interaction networks for the study of human diseases.Molecular systems biology · 2021Review
- BioID Performed on Golgi Enriched Fractions Identify C10orf76 as a GBF1 Binding Protein Essential for Golgi Maintenance and Secretion.Molecular & cellular proteomics : MCP · 2019Article
- Proximity labeling to detect RNA-protein interactions in live cells.FEBS open bio · 2019Article
- A proximity-tagging system to identify membrane protein-protein interactions.Nature methods · 2018Article
- Review
- Article
- Analysis of K-Ras Interactions by Biotin Ligase Tagging.Cancer genomics & proteomicsArticle
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The nuclear envelope (NE) is a critical cellular structure whose constituents and roles in a myriad of cellular processes seem ever expanding. To determine the underlying mechanisms by which the NE constituents participate in various cellular events, it is necessary to understand the nature of their protein-protein associations. BioID (proximity-dependent biotin identification) is a recently established method to generate a history of protein-protein associations as they occur over time in living cells. BioID is based on fusion of a bait protein to a promiscuous biotin ligase. Expression of the BioID fusion protein in a relevant cellular environment enables biotinylation of vicinal and interacting proteins of the bait protein, permitting isolation and identification by conventional biotin-affinity capture and mass-spec analysis. In this way, BioID provides unique capabilities to identify protein-protein associations at the NE. In this chapter we provide a detailed protocol for the application of BioID to the study of NE proteins.
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