ArticleCurrent protocols in chemical biology2014
Quantification of protein kinase enzymatic activity in unfractionated cell lysates using CSox-based sensors.
Article in Current protocols in chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Let the peptides shine: SOX (Sulfonamido-OXine)-labelled peptides for direct kinase and phosphatase monitoring.RSC chemical biology · 2026Review
- Un-LOK-ing a New Approach for Conformational Selective Targeting of STK10 (LOK).ACS medicinal chemistry letters · 2025Article
- Phosphorylation-Assisted Luciferase Complementation Assay Designed to Monitor Kinase Activity and Kinase-Domain-Mediated Protein-Protein Binding.International journal of molecular sciences · 2023Article
- Inhibitors of the Hippo Pathway Kinases STK3/MST2 and STK4/MST1 Have Utility for the Treatment of Acute Myeloid Leukemia.Journal of medicinal chemistry · 2022Article
- Design, Synthesis, and Biochemical Evaluation of New Triazole Derivatives as Aurora-A Kinase Inhibitors.Molecules (Basel, Switzerland) · 2021Article
- A fluorescent probe for monitoring PTP-PEST enzymatic activity.The Analyst · 2020Article
- A Panel of Protein Kinase Chemosensors Distinguishes Different Types of Fatty Liver Disease.Biochemistry · 2019Article
- Quantification of Cell Signaling Networks Using Kinase Activity Chemosensors.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Temporal Analysis of PP2A Phosphatase Activity During Insulin Stimulation Using a Direct Activity Probe.ACS chemical biology · 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
4 authors at 2 institutions in 1 country.
Funding
Abstract
Defining perturbations in protein kinase activity within biological samples can provide insight into disease mechanisms as well as potential targets for drug development. In this article, we present a method that utilizes a phosphorylation-sensitive amino acid, termed CSox, to afford kinase-selective biosensors capable of reporting on enzymatic activity directly in biological samples. These sensors produce an increase in fluorescence in response to phosphorylation of an amino acid residue adjacent to CSox. Probes can be designed for either serine/threonine or tyrosine kinases, and analysis can be performed using standard fluorescence equipment. The procedures provided herein represent our optimized protocols for the design, validation, and application of CSox-based protein kinase activity sensors.
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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.