ReviewCurrent opinion in chemical biology2011
Split-protein systems: beyond binary protein-protein interactions.
Review in Current opinion in chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 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
94 citing papers in PubMed, 216 citations in OpenAlex.
- Astrocytes viewed through the lens of their proteomes and subproteomes.Nature reviews. Neuroscience · 2026Review
- SplitSeek-Pro: accurate prediction of splittable sites on protein structures.Nature communications · 2026Article
- Magneto-Photonic Gene Circuit for Minimally Invasive Control of Gene Expression in Mammalian Cells.ACS omega · 2026Article
- Magneto-Photonic Gene Circuit for Minimally Invasive Control of Gene Expression in Mammalian Cells.bioRxiv : the preprint server for biology · 2025Article
- Engineering a new tripartite split-ccGFP system from Corynactis californica for detecting protein-protein interactions.Scientific reports · 2025Article
- Programmable protein ligation on cell surfaces.Nature · 2025Article
- Reconfigurable Nucleic Acid Nanoparticles with Therapeutic RNAi Responses to Intracellular Disease Markers.Advanced functional materials · 2025Article
- Methods for Controlling Small GTPase Activity.Chembiochem : a European journal of chemical biology · 2025Review
- Split genetically encoded calcium indicators for interorganellar junctions.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Principles and Design of Molecular Tools for Sensing and Perturbing Cell Surface Receptor Activity.Chemical reviews · 2025Review
- Biosensor Technology: Advances and Applications in Livestock Infectious Disease Diagnosis.Veterinary sciences · 2025Review
- Emerging RNA-centric technologies to probe RNA-protein interactions: importance in decoding the life cycle of positive sense single strand RNA viruses and antiviral discovery.Frontiers in cellular and infection microbiology · 2025Review
- Review
- Standardized Parts for Activation of Small GTPase Signaling in Living Cells.Angewandte Chemie (International ed. in English) · 2024Article
- Imaging interorganelle contacts at a glance.Journal of cell science · 2024Review
- Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation.Journal of visualized experiments : JoVE · 2024Article
- Exploiting protein domain modularity to enable synthetic control of engineered cells.Current opinion in biomedical engineering · 2024Article
- Comprehensive Overview of Bottom-Up Proteomics Using Mass Spectrometry.ACS measurement science au · 2024Review
- Irreversible light-activated SpyLigation mediates split-protein assembly in 4D.Nature protocols · 2024Review
- A single-component, light-assisted uncaging switch for endoproteolytic release.Nature chemical biology · 2024Article
34 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
It has been estimated that 650,000 protein-protein interactions exist in the human interactome (Stumpf et al., 2008), a subset of all possible macromolecular partnerships that dictate life. Thus there is a continued need for the development of sensitive and user-friendly methods for cataloguing biomacromolecules in complex environments and for detecting their interactions, modifications, and cellular location. Such methods also allow for establishing differences in the interactome between a normal and diseased cellular state and for quantifying the outcome of therapeutic intervention. A promising approach for deconvoluting the role of macromolecular partnerships is split-protein reassembly, also called protein fragment complementation. This approach relies on the appropriate fragmentation of protein reporters, such as the green fluorescent protein or firefly luciferase, which when attached to possible interacting partners can reassemble and regain function, thereby confirming the partnership. Split-protein methods have been effectively utilized for detecting protein-protein interactions in cell-free systems, Escherichia coli, yeast, mammalian cells, plants, and live animals. Herein, we present recent advances in engineering split-protein systems that allow for the rapid detection of ternary protein complexes, small molecule inhibitors, as well as a variety of macromolecules including nucleic acids, poly(ADP) ribose, and iron sulfur clusters. We also present advances that combine split-protein systems with chemical inducers of dimerization strategies that allow for regulating the activity of orthogonal split-proteases as well as aid in identifying enzyme inhibitors. Finally, we discuss autoinhibition strategies leading to turn-on sensors as well as future directions in split-protein methodology including possible therapeutic approaches.
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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.