Related Experiment Video

Updated: Jul 18, 2026

Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays
13:22

Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

Published on: October 23, 2019

Protein kinase inhibition: different approaches to selective inhibitor design

Giovanna Scapin1

  • 1Department of Medicinal Chemistry, MRL, Merck & Co., Inc. PO BOX 2000, Rahway, NJ 07065, USA. giovanna_scapin@merck.com

Current Drug Targets
|November 15, 2006
PubMed

Insights

Protein kinases are key drug targets, but achieving selectivity is challenging. This review explores evolving methods for developing selective kinase inhibitors to improve therapeutic potential.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Protein kinases regulate critical cellular functions, and their dysregulation is implicated in diseases like cancer.
  • Abnormal protein kinase activity drives various pathophysiologic states, including cancer, inflammatory, autoimmune, and cardiac diseases.
  • Protein kinases are major therapeutic targets, but achieving specificity in inhibition is a significant challenge.

Purpose of the Study:

  • To review the evolution of methodologies for discovering selective kinase inhibitors.
  • To provide an overview of traditional screening methods and newer approaches.

Main Methods:

  • Review of traditional screening-based methods.
  • Exploration of chemogenomics, proteomics, and chemical genetics.
  • Discussion of evolving technologies in drug discovery.

Main Results:

  • Traditional methods face challenges in achieving target specificity.
  • Newer technologies offer improved strategies for kinase inhibitor development.
  • The quest for selective inhibitors has progressed significantly.

Conclusions:

  • Developing selective kinase inhibitors is crucial for effective therapeutic strategies.
  • Advancements in chemogenomics, proteomics, and chemical genetics are enhancing inhibitor discovery.
  • Overcoming specificity issues is key to realizing the therapeutic potential of kinase inhibitors.
  • Meta_Description:

More Related Videos

Identification of Mediators of T-cell Receptor Signaling via the Screening of Chemical Inhibitor Libraries08:49

Identification of Mediators of T-cell Receptor Signaling via the Screening of Chemical Inhibitor Libraries

Published on: January 22, 2019

Identification of Kinase-substrate Pairs Using High Throughput Screening11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Related Concept Videos

Enzyme Inhibition01:30

Enzyme Inhibition

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
Inhibition of Cdk Activity02:34

Inhibition of Cdk Activity

The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
Inhibition of CDK Activity02:34

Inhibition of CDK Activity

The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
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...
Targeted Cancer Therapies02:57

Targeted Cancer Therapies

The targeted cancer therapies, also known as “molecular targeted therapies,” take advantage of the molecular and genetic differences between the cancer cells and the normal cells. It needs a thorough understanding of the cancer cells to develop drugs that can target specific molecular aspects that drive the growth, progression, and spread of cancer cells without affecting the growth and survival of other normal cells in the body.
There are several types of targeted therapies against specific...
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...