ArticleBiopolymers2014
Sequence context and crosslinking mechanism affect the efficiency of in vivo capture of a protein-protein interaction.
Article in Biopolymers, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 18 citations in OpenAlex.
- BPTF Target Engagement by Acetylated H2A.Z Photoaffinity Probes.Biochemistry · 2025Article
- Photoactivatable O-GlcNAc Transferase Library Enables Covalent Chemical Capture of Solvent-Exposed TPR Domain Interactions.Chembiochem : a European journal of chemical biology · 2025Article
- Synthetic Biology Meets CaCells · 2024Review
- Yeast Display Enables Identification of Covalent Single-Domain Antibodies against Botulinum Neurotoxin Light Chain A.ACS chemical biology · 2022Article
- Chemical Biology Tools for Examining the Bacterial Cell Wall.Cell chemical biology · 2020Review
- Genetic code expansion and photocross-linking identify different β-arrestin binding modes to the angiotensin II type 1 receptor.The Journal of biological chemistry · 2019Article
- Article
- Chemoproteomic profiling reveals that cathepsin D off-target activity drives ocular toxicity of β-secretase inhibitors.Nature communications · 2016Article
- Discovery of Enzymatic Targets of Transcriptional Activators via in Vivo Covalent Chemical Capture.Journal of the American Chemical Society · 2016Article
- A Novel SRP Recognition Sequence in the Homeostatic Control Region of Heat Shock Transcription Factor σ32.Scientific reports · 2016Article
- Binding of the Covalent Flavin Assembly Factor to the Flavoprotein Subunit of Complex II.The Journal of biological chemistry · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Protein-protein interactions (PPIs) are essential for implementing cellular processes and thus methods for the discovery and study of PPIs are highly desirable. An emerging method for capturing PPIs in their native cellular environment is in vivo covalent chemical capture, a method that uses nonsense suppression to site specifically incorporate photoactivable unnatural amino acids (UAAs) in living cells. However, in one study we found that this method did not capture a PPI for which there was abundant functional evidence, a complex formed between the transcriptional activator Gal4 and its repressor protein Gal80. Here we describe the factors that influence the success of covalent chemical capture and show that the innate reactivity of the two UAAs utilized, (p-benzoylphenylalanine (pBpa) and p-azidophenylalanine (pAzpa)), plays a profound role in the capture of Gal80 by Gal4. Based upon these data, guidelines are outlined for the successful use of in vivo photo-crosslinking to capture novel PPIs and to characterize the interfaces.
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.