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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...
Enzymes02:34

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Induced-fit Model01:13

Induced-fit Model

Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

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Updated: Jun 4, 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

Kinase substrate interactions.

Michael G Smith1, Jason Ptacek, Michael Snyder

  • 1Illumina, Inc., San Diego, CA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|March 4, 2011
PubMed
Summary
This summary is machine-generated.

Functional protein microarrays enable high-throughput identification of kinase phosphorylation targets. This multiplex tool offers a sensitive and robust alternative to traditional methods for studying kinase-substrate interactions.

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Last Updated: Jun 4, 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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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
  • Molecular Biology
  • Proteomics

Background:

  • Kinases are key targets in cancer therapy due to their roles in cell cycle and tumor growth.
  • High-throughput screening requires advanced tools for studying kinase-substrate interactions.
  • Traditional methods like mass spectroscopy are lower-throughput.

Purpose of the Study:

  • To apply functional protein microarrays for identifying kinase phosphorylation targets.
  • To develop a multiplex tool for kinase-substrate interaction studies.
  • To offer a sensitive and robust alternative to existing assays.

Main Methods:

  • Utilized functional protein microarrays with immobilized proteins.
  • Employed highly sensitive radioactive detection.
  • Applied robust informatics algorithms for data analysis.

Main Results:

  • Successfully identified phosphorylation targets of individual protein kinases.
  • Demonstrated the efficacy of protein microarrays in kinase research.
  • Validated the use of radioactive detection and informatics for kinase target identification.

Conclusions:

  • Functional protein microarrays are effective for identifying kinase phosphorylation substrates.
  • This approach enhances high-throughput screening for kinase-targeted drug discovery.
  • Offers a sensitive, robust, and multiplex method for kinase research.