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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...
Dipeptidyl Peptidase 4 Inhibitors01:23

Dipeptidyl Peptidase 4 Inhibitors

Dipeptidyl peptidase 4 (DPP-4) is a serine protease widely distributed in the body. It's involved in the inactivation of GLP-1 and GIP hormones, which are crucial for insulin regulation. DPP-4 inhibitors, such as sitagliptin (Januvia), saxagliptin (Onglyza), linagliptin (Tradjenta), alogliptin (Nesina), and vildagliptin (Galvus), help increase the proportion of active GLP-1, enhancing insulin secretion. These inhibitors work by competitively binding to DPP-4. This binding causes a significant...
Inhibitors of Bacterial DNA Synthesis01:28

Inhibitors of Bacterial DNA Synthesis

Bacterial pathogens depend on precise and efficient DNA replication to sustain infection. Two type II topoisomerases—DNA gyrase and topoisomerase IV—are critical to this process, as they resolve DNA supercoiling and unlink chromosomes during replication. Fluoroquinolones, synthetic derivatives of quinolones, exploit this mechanism by stabilizing the transient DNA–enzyme cleavage complex, preventing strand religation, and causing lethal double-strand breaks. These antibiotics are selectively...
Inhibitors of Viral Protein Synthesis01:30

Inhibitors of Viral Protein Synthesis

Protein synthesis is indispensable for viral replication, as viruses lack the cellular machinery required for this process and must hijack the host's translational apparatus. In response, host cells deploy a critical innate immune defense involving interferons, specialized cytokines that play a central role in inhibiting viral propagation.Upon viral detection, infected cells release interferons that bind to receptors on adjacent uninfected cells, activating the JAK-STAT signaling pathway and...

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Related Experiment Video

Updated: May 20, 2026

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

[Kinase inhibitors].

Takao Yamori1, Dexin Kong

  • 1Division of Molecular Pharmacology, Cancer Chemotherapy Center, Japanese Foundation for Cancer Research.

Nihon Rinsho. Japanese Journal of Clinical Medicine
|June 12, 2010
PubMed
Summary
This summary is machine-generated.

Kinases regulate cell functions, and their dysregulation drives cancer. Kinase inhibitors are crucial therapeutic targets, with ongoing development offering promising cancer treatment strategies.

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Last Updated: May 20, 2026

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
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Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Kinases are enzymes that regulate cellular functions through phosphorylation.
  • Dysregulation of kinases involved in cell growth signaling is a key factor in cancer development.
  • Kinases represent critical therapeutic targets in oncology.

Purpose of the Study:

  • To review the current landscape of kinase inhibitors in cancer therapy.
  • To discuss the future perspectives and ongoing developments in kinase inhibitor research.

Main Methods:

  • Literature review of kinase inhibitor research.
  • Analysis of the role of kinases in carcinogenesis.
  • Discussion of therapeutic strategies involving kinase inhibitors.

Main Results:

  • Kinase inhibitors have emerged as a significant area of cancer drug development.
  • The dysregulation of kinases is directly linked to the induction of malignant phenotypes.
  • Targeting kinases offers a promising approach for cancer treatment.

Conclusions:

  • Kinase inhibitors are highly promising therapeutic agents for cancer treatment.
  • Continued research and development in kinase inhibitors are essential for advancing cancer therapy.
  • Understanding kinase function and dysregulation is key to developing effective cancer treatments.