ArticleiScience2018
2C-BioID: An Advanced Two Component BioID System for Precision Mapping of Protein Interactomes.
Article in iScience, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed.
- 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
- Leveraging a self-cleaving peptide for tailored control in proximity labeling proteomics.Cell reports methods · 2024Article
- Chemical and Biological Strategies for Profiling Protein-Protein Interactions in Living Cells.Chemistry, an Asian journal · 2023Review
- Impact of inherent biases built into proteomic techniques: Proximity labeling and affinity capture compared.The Journal of biological chemistry · 2023Article
- Native lamin A/C proteomes and novel partners from heart and skeletal muscle in a mouse chronic inflammation model of human frailty.Frontiers in cell and developmental biology · 2023Article
- Analyzing Protein Interactions by MAC-Tag Approaches.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Identification of STAU1 as a regulator of HBV replication by TurboID-based proximity labeling.iScience · 2022Article
- Advances in enzyme-mediated proximity labeling and its potential for plant research.Plant physiology · 2022Article
- Off-the-shelf proximity biotinylation for interaction proteomics.Nature communications · 2021Article
- Disrupting the LINC complex by AAV mediated gene transduction prevents progression of Lamin induced cardiomyopathy.Nature communications · 2021Article
- Review
- Visualizing protein-protein interactions in plants by rapamycin-dependent delocalization.The Plant cell · 2021Article
- Mapping the micro-proteome of the nuclear lamina and lamina-associated domains.Life science alliance · 2021Article
- Article
- A Novel Proximity Biotinylation Assay Based on the Self-Associating Split GFP1-10/11.Proteomes · 2020Article
- Insight into the Interactome of Intramitochondrial PKA Using Biotinylation-Proximity Labeling.International journal of molecular sciences · 2020Article
- Combined proximity labeling and affinity purification-mass spectrometry workflow for mapping and visualizing protein interaction networks.Nature protocols · 2020Article
- Review
- Proximity Dependent Biotinylation: Key Enzymes and Adaptation to Proteomics Approaches.Molecular & cellular proteomics : MCP · 2020Review
- Probing the Environment of Emerin by Enhanced Ascorbate Peroxidase 2 (APEX2)-Mediated Proximity Labeling.Cells · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The modulation of protein-protein interactions (PPIs) is an essential regulatory activity defining diverse cell functions in development and disease. BioID is an unbiased proximity-dependent biotinylation method making use of a biotin-protein ligase fused to a protein of interest and has become an important tool for mapping of PPIs within cellular contexts. We devised an advanced method, 2C-BioID, in which the biotin-protein ligase is kept separate from the protein of interest, until the two are induced to associate by the addition of a dimerizing agent. As proof of principle, we compared the interactomes of lamina-associated polypeptide 2β (LAP2β) with those of lamins A and C, using 2C- and conventional BioID. 2C-BioID greatly enhanced data robustness by facilitating the in silico elimination of non-specific interactors as well as overcoming the problems associated with aberrant protein localization. 2C-BioID therefore significantly strengthens the specificity and reliability of BioID-based interactome analysis, by the more stringent exclusion of false-positives and more efficient intracellular targeting.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.