ArticleOrganic letters2007
Photochemically-activated probes of protein-protein interactions.
Article in Organic letters, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed.
- Targeting collagen strands by photo-triggered triple-helix hybridization.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Light-activated regulation of cofilin dynamics using a photocaged hydrogen peroxide generator.Journal of the American Chemical Society · 2010Article
- Light-mediated remote control of signaling pathways.Biochimica et biophysica acta · 2010Review
- Simultaneous fluorescent monitoring of proteasomal subunit catalysis.Journal of the American Chemical Society · 2010Article
- Illuminating the chemistry of life: design, synthesis, and applications of "caged" and related photoresponsive compounds.ACS chemical biology · 2009Review
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.
Funding
Abstract
The activity of light-activatable ("caged") compounds can be temporally and spatially controlled, thereby providing a means to interrogate intracellular biochemical pathways as a function of time and space. Nearly all caged peptides contain photocleavable groups positioned on the side chains of key residues. We describe an alternative active site targeted strategy that disrupts the interaction between the protein target (SH2 domain, kinase, and proteinase) and a critical amide NH moiety of the peptide probe.
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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.