ArticleJournal of the American Chemical Society2011
Construction of a photoactivatable profluorescent enzyme via propinquity labeling.
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 7 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
7 citing papers in PubMed, 30 citations in OpenAlex.
- Deactivatable Bisubstrate Inhibitors of Protein Kinases.Molecules (Basel, Switzerland) · 2022Article
- The Development and Application of Opto-Chemical Tools in the Zebrafish.Molecules (Basel, Switzerland) · 2022Review
- Optochemical Control of Biological Processes in Cells and Animals.Angewandte Chemie (International ed. in English) · 2018Review
- Total chemical synthesis of photoactivatable proteins for light-controlled manipulation of antigen-antibody interactions.Chemical science · 2016Article
- Vitamin B12: a tunable, long wavelength, light-responsive platform for launching therapeutic agents.Accounts of chemical research · 2015Article
- Merging of confocal and caging technologies: selective three-color communication with profluorescent reporters.Angewandte Chemie (International ed. in English) · 2012Article
- Chemical tools for studying directed cell migration.ACS chemical biology · 2011Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A strategy for the construction of a profluorescent caged enzyme is described. An active site-directed peptide-based affinity label was designed, synthesized, and employed to covalently label a nonactive site residue in the cAMP-dependent protein kinase. The modified kinase displays minimal catalytic activity and low fluorescence. Photolysis results in partial cleavage of the enzyme-bound affinity label, restoration of enzymatic activity (60-80%) and a strong fluorescent response (10-20 fold). The caged kinase displays analogous behavior in living cells, inducing a light-dependent loss of stress fibers that is characteristic of cAMP action. This strategy furnishes molecularly engineered enzymes that can be remotely controlled in time, space, and total activity.
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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.