ArticleNature communications2017
Split-BioID a conditional proteomics approach to monitor the composition of spatiotemporally defined protein complexes.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.
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Who cites it
116 citing papers in PubMed, 187 citations in OpenAlex.
- Chemically stabilized long antisense oligonucleotides perturb RNA exosome function.Nucleic acids research · 2026Article
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- Best practices for biotin ligase-based proximity labeling proteomics in plant systems.The Plant cell · 2026Review
- A guide to mapping ubiquitin and ubiquitin-like E3 ligases to their substrates.The FEBS journal · 2026Review
- Light-Controlled Assembly and Disassembly of Covalent RNA-Protein Conjugates to Control RNA Base Editing.Molecules (Basel, Switzerland) · 2026Article
- Proteomic investigation of signaling dynamics: from static maps to network rewiring.Bioscience reports · 2026Review
- Astrocytes viewed through the lens of their proteomes and subproteomes.Nature reviews. Neuroscience · 2026Review
- Detection of Protein-Protein Interactions in Escherichia coli With Single Molecule Sensitivity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Post-transcriptional regulatory networks: The dynamic interplay of RNA-binding proteins.The FEBS journal · 2026Review
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- Proximity Labeling Reveals RNA-Binding Proteins Associating with the Human Mitochondrial Import Receptor TOMM20.Journal of proteome research · 2026Article
- STUPPIT is a proximity labeling tool for labeling intermediary proteins that bridge two non-interacting proteins.PLoS biology · 2025Article
- A brief guide to analyzing TurboID-based proximity labeling-mass spectrometry in plants.Molecules and cells · 2025Review
- Review
- Characterizing host-microbe interactions with bacterial effector proteins using proximity-dependent biotin identification (BioID).Communications biology · 2025Review
- Identification of E3 Ubiquitin Ligase Substrates Using Biotin Ligase-Based Proximity Labeling Approaches.Biomedicines · 2025Review
- A subcellular map of translational machinery composition and regulation at the single-molecule level.Science (New York, N.Y.) · 2025Article
- Proximity proteomics reveals a mechanism of fatty acid transfer at lipid droplet-mitochondria- endoplasmic reticulum contact sites.Nature communications · 2025Article
- RNA Helicase DDX3 Interacts with the Capsid Protein of Hepatitis E Virus and Plays a Vital Role in the Viral Replication.Pathogens (Basel, Switzerland) · 2025Article
56 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding the function of the thousands of cellular proteins is a central question in molecular cell biology. As proteins are typically part of multiple dynamic and often overlapping macromolecular complexes exerting distinct functions, the identification of protein-protein interactions (PPI) and their assignment to specific complexes is a crucial but challenging task. We present a protein fragments complementation assay integrated with the proximity-dependent biotinylation technique BioID. Activated on the interaction of two proteins, split-BioID is a conditional proteomics approach that allows in a single and simple assay to both experimentally validate binary PPI and to unbiasedly identify additional interacting factors. Applying our method to the miRNA-mediated silencing pathway, we can probe the proteomes of two distinct functional complexes containing the Ago2 protein and uncover the protein GIGYF2 as a regulator of miRNA-mediated translation repression. Hence, we provide a novel tool to study dynamic spatiotemporally defined protein complexes in their native cellular environment.
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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.