ArticleCommunications biology2019
A high-throughput integrated microfluidics method enables tyrosine autophosphorylation discovery.
Article in Communications biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Peptide Arrays as Tools for Unraveling Tumor Microenvironments and Drug Discovery in Oncology.Cells · 2026Review
- Versatile Microfluidics Platform for Enhanced Multitarget Super-Resolution Microscopy.ACS nano · 2026Article
- Affinity microfluidics enables high-throughput protein degradation analysis in cell-free extracts.Communications biology · 2022Article
- Photoactivation of Cell-Free Expressed Archaerhodopsin-3 in a Model Cell Membrane.International journal of molecular sciences · 2021Article
- Heterozygous Recurrent Mutations Inducing Dysfunction ofFrontiers in cell and developmental biology · 2021Article
- Cell-free protein synthesis andRSC advances · 2020Article
- Protein and Proteome Measurements with Microfluidic Chips.Analytical chemistry · 2020Review
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Autophosphorylation of receptor and non-receptor tyrosine kinases is a common molecular switch with broad implications for pathogeneses and therapy of cancer and other human diseases. Technologies for large-scale discovery and analysis of autophosphorylation are limited by the inherent difficulty to distinguish between phosphorylation and autophosphorylation in vivo and by the complexity associated with functional assays of receptors kinases in vitro. Here, we report a method for the direct detection and analysis of tyrosine autophosphorylation using integrated microfluidics and freshly synthesized protein arrays. We demonstrate the efficacy of our platform in detecting autophosphorylation activity of soluble and transmembrane tyrosine kinases, and the dependency of in vitro autophosphorylation assays on membranes. Our method, Integrated Microfluidics for Autophosphorylation Discovery (IMAD), is high-throughput, requires low reaction volumes and can be applied in basic and translational research settings. To our knowledge, it is the first demonstration of posttranslational modification analysis of membrane protein arrays.
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Registered trials
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