ReviewCurrent opinion in chemical biology2008
Understanding and exploiting substrate recognition by protein kinases.
Review in Current opinion in chemical biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 55 citations in OpenAlex.
- Kinase Inhibitors for Targeted Cancer Therapy.Current topics in medicinal chemistry · 2026Review
- The prospect of substrate-based kinase inhibitors to improve target selectivity and overcome drug resistance.Chemical science · 2024Review
- Structural Insights into Protein Regulation by Phosphorylation and Substrate Recognition of Protein Kinases/Phosphatases.Life (Basel, Switzerland) · 2021Review
- Recognition of physiological phosphorylation sites by p21-activated kinase 4.Journal of structural biology · 2020Article
- Global phosphoproteomic analysis identifies SRMS-regulated secondary signaling intermediates.Proteome science · 2018Article
- Enzyme Activity Assays for Protein Kinases: Strategies to Identify Active Substrates.Current drug discovery technologies · 2016Review
- Article
- Small Molecule Inhibition of the Autophagy Kinase ULK1 and Identification of ULK1 Substrates.Molecular cell · 2015Article
- Exploiting holistic approaches to model specificity in protein phosphorylation.Frontiers in genetics · 2014Review
- Navigating cancer network attractors for tumor-specific therapy.Nature biotechnology · 2012Article
- MMFPh: a maximal motif finder for phosphoproteomics datasets.Bioinformatics (Oxford, England) · 2012Article
- Discovery of cellular substrates for protein kinase A using a peptide array screening protocol.The Biochemical journal · 2011Article
- Regulation and function of protein kinases and phosphatases.Enzyme research · 2011Article
- Computational prediction and experimental verification of new MAP kinase docking sites and substrates including Gli transcription factors.PLoS computational biology · 2010Article
- Analysis of serine-threonine kinase specificity using arrayed positional scanning peptide libraries.Current protocols in molecular biology · 2010Article
- Deciphering protein kinase specificity through large-scale analysis of yeast phosphorylation site motifs.Science signaling · 2010Article
- Tyrosine phosphorylation: thirty years and counting.Current opinion in cell biology · 2009Review
- Recognition-domain focused chemosensors: versatile and efficient reporters of protein kinase activity.Journal of the American Chemical Society · 2008Article
- 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
1 author at 1 institution in 1 country.
Funding
Abstract
Protein kinases play a virtually universal role in cellular regulation and are emerging as an important class of new drug targets, yet the cellular functions of most human kinases largely remain obscure. Aspects of substrate recognition common to all kinases in the ATP nucleotide binding site have been exploited in the generation of analog-specific mutants for exploring kinase function and discovering novel protein substrates. Likewise, understanding interactions with the protein substrate, which differ substantially between kinases, can also help to identify substrates and to produce tools for studying kinase pathways, including fluorescent biosensors. Principles of kinase substrate recognition are particularly valuable in guiding bioinformatics and phosphoproteomics approaches that impact our understanding of signaling pathways and networks on a global scale.
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.