ArticleJournal of the American Chemical Society2011
Thermodynamics, kinetics, and photochemistry of β-strand association and dissociation in a split-GFP system.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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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
24 citing papers in PubMed.
- Key challenges and recommendations for defining organelle membrane contact sites.Nature reviews. Molecular cell biology · 2025Review
- Dynamic assessment of PI4P metabolism using split GFP based sensors.Scientific reports · 2025Article
- Challenges and Solutions for Leave-One-Out Biosensor Design in the Context of a Rugged Fitness Landscape.Sensors (Basel, Switzerland) · 2024Article
- FAST, a method based on split-GFP for the detection in solution of proteins synthesized in cell-free expression systems.Scientific reports · 2024Article
- Chemical control of excited-state reactivity of the anionic green fluorescent protein chromophore.Communications chemistry · 2024Article
- Simulation-guided engineering of split GFPs with efficient β-strand photodissociation.Nature communications · 2023Article
- Aptamer-Array-Guided Protein Assembly Enhances Synthetic mRNA Switch Performance.Angewandte Chemie (International ed. in English) · 2022Article
- Substitutional landscape of a split fluorescent protein fragment using high-density peptide microarrays.PloS one · 2021Article
- A Novel Proximity Biotinylation Assay Based on the Self-Associating Split GFP1-10/11.Proteomes · 2020Article
- Unified Model for Photophysical and Electro-Optical Properties of Green Fluorescent Proteins.Journal of the American Chemical Society · 2019Article
- Split Green Fluorescent Proteins: Scope, Limitations, and Outlook.Annual review of biophysics · 2019Review
- Designing a Green Fluorogenic Protease Reporter by Flipping a Beta Strand of GFP for Imaging Apoptosis in Animals.Journal of the American Chemical Society · 2019Article
- Chromophore pre-maturation for improved speed and sensitivity of split-GFP monitoring of protein secretion.Scientific reports · 2019Article
- Structural Insight into the Photochemistry of Split Green Fluorescent Proteins: A Unique Role for a His-Tag.Journal of the American Chemical Society · 2018Article
- Mechanism and bottlenecks in strand photodissociation of split green fluorescent proteins (GFPs).Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Mispacking and the Fitness Landscape of the Green Fluorescent Protein Chromophore Milieu.Biochemistry · 2017Article
- Techniques for the Analysis of Protein-Protein Interactions in Vivo.Plant physiology · 2016Review
- Specific cell surface labeling of GPCRs using split GFP.Scientific reports · 2016Article
- Toward Computationally Designed Self-Reporting Biosensors Using Leave-One-Out Green Fluorescent Protein.Biochemistry · 2015Article
- Short Hydrogen Bonds and Proton Delocalization in Green Fluorescent Protein (GFP).ACS central science · 2015Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Truncated green fluorescent protein (GFP) that is refolded after removing the 10th β-strand can readily bind to a synthetic strand to recover the absorbance and fluorescence of the whole protein. This allows rigorous experimental determination of thermodynamic and kinetic parameters of the split system including the equilibrium constant and the association/dissociation rates, which enables residue-specific analysis of peptide-protein interactions. The dissociation rate of the noncovalently bound strand is observed by strand exchange that is accompanied by a color change, and surprisingly, the rate is greatly enhanced by light irradiation. This peptide-protein photodissociation is a very unusual phenomenon and can potentially be useful for introducing spatially and temporally well-defined perturbations to biological systems as a genetically encoded caged protein.
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Registered trials
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