ArticleCurrent protocols in molecular biology2010
Analysis of serine-threonine kinase specificity using arrayed positional scanning peptide libraries.
Article in Current protocols in molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 16 citations in OpenAlex.
- Proximity-Based Phospho-Interactome (Prob-PhI) Characterization Reveals Distinct Signaling Activities of MEK1 and MEK2.Analytical chemistry · 2026Article
- Identification of CryAB as a target of NUAK kinase activity in Drosophila muscle tissue.Genetics · 2023Article
- Fluorescence Lifetime Imaging Probes for Cell-Based Measurements of Enzyme Activity.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Global substrate specificity profiling of post-translational modifying enzymes.Protein science : a publication of the Protein Society · 2018Review
- Phosphoproteomics-Based Profiling of Kinase Activities in Cancer Cells.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Article
- Phosphoproteomic analysis identifies the tumor suppressor PDCD4 as a RSK substrate negatively regulated by 14-3-3.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Toward a systems-level view of dynamic phosphorylation networks.Frontiers in genetics · 2014Review
- Deciphering post-translational modification codes.FEBS letters · 2013Review
- Bivalent inhibitors of protein kinases.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Protein kinases vary substantially in their consensus phosphorylation motifs, the residues that are either preferred or deselected by the kinase at specific positions surrounding the phosphorylation site. The protocol described here is used to rapidly determine phosphorylation motifs for serine-threonine kinases. The procedure involves screening an arrayed combinatorial peptide library consisting of 198 biotinylated substrates. Peptides are phosphorylated by the kinase of interest in the presence of radiolabeled ATP and then captured on streptavidin membrane. The membrane is subsequently washed, dried, and exposed to a phosphor screen to visualize and quantify incorporation of radiolabel into the peptides. The phosphorylation motif is thereby derived from the relative extent of phosphorylation of each peptide in the array.
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.