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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...
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...
Enzyme Kinetics01:19

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...

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Related Experiment Video

Updated: May 13, 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

Correlation profiling for determining kinase-substrate relationships.

Fiona E McAllister1, Steven P Gygi

  • 1Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.

Methods (San Diego, Calif.)
|March 26, 2013
PubMed
Summary
This summary is machine-generated.

Determining kinase-substrate relationships is crucial. Kinase Activity-Abundance Correlation (KAAC) profiling links substrate activity to kinase abundance, identifying potential kinases responsible for phosphorylation events.

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Related Experiment Videos

Last Updated: May 13, 2026

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

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Published on: August 29, 2015

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

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Published on: February 21, 2019

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
11:23

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Area of Science:

  • Biochemistry
  • Proteomics
  • Cell Biology

Background:

  • Identifying kinase-substrate relationships is a critical challenge in phosphorylation research.
  • Kinase Activity-Abundance Correlation (KAAC) profiling offers a method to infer kinase involvement in specific phosphorylation events.

Purpose of the Study:

  • To demonstrate the utility of KAAC profiling for identifying kinase-substrate pairs.
  • To investigate potential kinases responsible for phosphorylating peptides upregulated during mitosis.

Main Methods:

  • KAAC profiling involves separating cell lysates at the protein level.
  • Analyzing fractions to generate substrate peptide activity profiles.
  • Correlating substrate activity profiles with kinase abundance profiles obtained via shotgun proteomics.

Main Results:

  • Successfully identified potential kinase-substrate pairs for six mitosis-upregulated peptides.
  • Evaluated the use of stable isotope labeling to enhance quantification in a subset of fractions.

Conclusions:

  • KAAC profiling is an effective technique for predicting kinase-substrate relationships.
  • The method is applicable to studying phosphorylation dynamics, such as those occurring during mitosis.