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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

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Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Protein kinase substrate identification on functional protein arrays.

Lihao Meng1, Gregory A Michaud, Janie S Merkel

  • 1Invitrogen Corp,, Protein Array Center, 688 East Main Street, Branford, CT 06405, USA. lihao.meng@invitrogen.com

BMC Biotechnology
|March 1, 2008
PubMed
Summary

Researchers optimized protein arrays for identifying kinase substrates, a crucial step in understanding cell signaling and developing new therapeutics. This multiplex method accelerates the discovery of novel protein kinase substrates and their functions.

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Last Updated: Jul 7, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
11:11

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Systems Biology

Background:

  • Kinases are key therapeutic targets for various diseases.
  • Systems biology necessitates high-throughput methods for studying protein phosphorylation.
  • Functional protein arrays offer a multiplex approach for kinase substrate identification.

Purpose of the Study:

  • To characterize factors influencing protein array-based kinase substrate identification.
  • To optimize the protein array method for efficiency and accuracy.
  • To compare protein array results with standard solution-based assays.

Main Methods:

  • Utilized functional protein arrays with immobilized proteins and kinases in solution.
  • Employed radioactive detection and hit identification algorithms.
  • Investigated effects of time, buffer composition, and protein concentration.
  • Developed and applied a pooling-deconvolution strategy.

Main Results:

  • Detailed characterization of optimal conditions for protein array-based kinase substrate identification.
  • Achieved over 80% correlation with standard solution-based phosphorylation assays.
  • Successfully identified novel protein kinase substrates from arrays of thousands of proteins.
  • Demonstrated enhanced characterization of kinase-substrate relationships and reduced reagent consumption via pooling-deconvolution.

Conclusions:

  • Functional protein microarrays are a valuable tool for multiplex analysis of protein phosphorylation.
  • This technology enables rapid identification of novel kinase substrates.
  • Integration with systems biology approaches will advance understanding of cell signaling pathways and kinase function.