ArticleThe journal of physical chemistry. C, Nanomaterials and interfaces2017
Investigating State Restriction in Fluorescent Protein FRET Using Time-Resolved Fluorescence and Anisotropy.
Article in The journal of physical chemistry. C, Nanomaterials and interfaces, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
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Who cites it
6 citing papers in PubMed.
- Targeting lysosomal pH restores mitochondrial quality control in GBA1-mutant Parkinson's disease.Translational neurodegeneration · 2026Article
- Redox-dependent binding and conformational equilibria govern the fluorescence decay of NAD(P)H in living cells.FEBS letters · 2025Article
- Principles and Applications of Resonance Energy Transfer Involving Noble Metallic Nanoparticles.Materials (Basel, Switzerland) · 2023Review
- NAD(P)H binding configurations revealed by time-resolved fluorescence and two-photon absorption.Biophysical journal · 2023Article
- Polarized Two-Photon Absorption and Heterogeneous Fluorescence Dynamics in NAD(P)H.The journal of physical chemistry. B · 2019Article
- Long-Range Energy Transfer in Protein Megamolecules.Journal of the American Chemical Society · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Most fluorescent proteins exhibit multiexponential fluorescence decays, indicating a heterogeneous excited state population. FRET between fluorescent proteins should therefore involve multiple energy transfer pathways. We recently demonstrated the FRET pathways between EGFP and mCherry (mC), upon the dimerization of 3-phosphoinositide dependent protein kinase 1 (PDK1), to be highly restricted. A mechanism for FRET restriction based on a highly unfavorable κ
Identifiers
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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.