ArticleNature communications2015
Modulating protein activity using tethered ligands with mutually exclusive binding sites.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 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
19 citing papers in PubMed, 47 citations in OpenAlex.
- Affinity-Activated Protein Switches for Modular and Signal-ON Detection of Small Molecules.Analytical chemistry · 2026Article
- [Applications of native mass spectrometry and ultraviolet photodissociation in protein structure and interaction analysis].Se pu = Chinese journal of chromatography · 2024Review
- A transient vesicular glue for amplification and temporal regulation of biocatalytic reaction networks.Chemical science · 2023Article
- Site-specific dual encoding and labeling of proteins via genetic code expansion.Cell chemical biology · 2023Review
- Practical Guidance for Consensus Scoring and Force Field Selection in Protein-Ligand Binding Free Energy Simulations.Journal of chemical information and modeling · 2022Article
- Deciphering the anti-filarial potential of bioactive compounds fromPharmaceutical biology · 2022Article
- Interplay of Affinity and Surface Tethering in Protein Recognition.The journal of physical chemistry letters · 2022Article
- Cystine Knot Peptides with Tuneable Activity and Mechanism.Angewandte Chemie (International ed. in English) · 2022Article
- Article
- Bioluminescent Protein-Inhibitor Pair in the Design of a Molecular Aptamer Beacon Biosensing System.Analytical chemistry · 2020Article
- iFLinkC: an iterative functional linker cloning strategy for the combinatorial assembly and recombination of linker peptides with functional domains.Nucleic acids research · 2020Article
- Development and Applications of Bioluminescent and Chemiluminescent Reporters and Biosensors.Annual review of analytical chemistry (Palo Alto, Calif.) · 2019Review
- Investigating supramolecular systems using Förster resonance energy transfer.Chemical Society reviews · 2018Review
- Luciferase-induced photoreductive uncaging of small-molecule effectors.Nature communications · 2018Article
- Designing cell function: assembly of synthetic gene circuits for cell biology applications.Nature reviews. Molecular cell biology · 2018Review
- Semisynthetic Bioluminescent Sensor Proteins for Direct Detection of Antibodies and Small Molecules in Solution.ACS sensors · 2017Article
- Dual Readout BRET/FRET Sensors for Measuring Intracellular Zinc.ACS chemical biology · 2016Article
- On-Demand Targeting: Investigating Biology with Proximity-Directed Chemistry.Journal of the American Chemical Society · 2016Article
- Imaging and manipulating proteins in live cells through covalent labeling.Nature chemical biology · 2015Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The possibility to design proteins whose activities can be switched on and off by unrelated effector molecules would enable applications in various research areas, ranging from biosensing to synthetic biology. We describe here a general method to modulate the activity of a protein in response to the concentration of a specific effector. The approach is based on synthetic ligands that possess two mutually exclusive binding sites, one for the protein of interest and one for the effector. Tethering such a ligand to the protein of interest results in an intramolecular ligand-protein interaction that can be disrupted through the presence of the effector. Specifically, we introduce a luciferase controlled by another protein, a human carbonic anhydrase whose activity can be controlled by proteins or small molecules in vitro and on living cells, and novel fluorescent and bioluminescent biosensors.
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.