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Related Concept Videos

Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
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...
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...

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Related Experiment Video

Updated: Jun 20, 2026

Pre-clinical Evaluation of Tyrosine Kinase Inhibitors for Treatment of Acute Leukemia
10:49

Pre-clinical Evaluation of Tyrosine Kinase Inhibitors for Treatment of Acute Leukemia

Published on: September 18, 2013

Bacterial tyrosine-kinases: structure-function analysis and therapeutic potential.

Christophe Grangeasse1, Raphaël Terreux, Sylvie Nessler

  • 1Institut de Biologie et Chimie des Protéines, UMR 5086, CNRS, Université de Lyon, 7, passage du Vercors, 69367 Lyon cedex 07, France. c.grangeasse@ibcp.fr

Biochimica Et Biophysica Acta
|September 1, 2009
PubMed
Summary

Bacteria utilize BY-kinases, a unique class of tyrosine-kinases, to regulate essential cellular processes like polysaccharide synthesis. These enzymes represent promising targets for developing novel antibiotics against bacterial pathogens.

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Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays
07:42

Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays

Published on: September 19, 2018

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Last Updated: Jun 20, 2026

Pre-clinical Evaluation of Tyrosine Kinase Inhibitors for Treatment of Acute Leukemia
10:49

Pre-clinical Evaluation of Tyrosine Kinase Inhibitors for Treatment of Acute Leukemia

Published on: September 18, 2013

Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays
07:42

Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays

Published on: September 19, 2018

Area of Science:

  • Bacterial physiology and molecular biology
  • Enzymology and protein phosphorylation
  • Antimicrobial drug discovery

Background:

  • Serine/threonine-kinases and tyrosine-kinases play crucial roles in bacterial physiology.
  • Bacteria possess unique tyrosine-kinases (BY-kinases) distinct from eukaryotic counterparts.
  • BY-kinases are ATP-binding proteins with Walker motifs, grouped into a specific family.

Purpose of the Study:

  • To review current knowledge on bacterial BY-kinases.
  • To discuss the potential of BY-kinases as targets for new antibiotic development.
  • To highlight the role of BY-kinases in bacterial cellular processes.

Main Methods:

  • Characterization of bacterial kinase genes.
  • Structural analysis of BY-kinases.
  • Phosphoproteome analysis to identify cellular roles.
  • Literature review of BY-kinase functions and potential.

Main Results:

  • BY-kinases are involved in diverse bacterial cellular processes.
  • The best-characterized role of BY-kinases is regulating extracellular polysaccharide synthesis.
  • Crystal structures of two BY-kinases have been determined.
  • BY-kinases are implicated in bacterial virulence.

Conclusions:

  • BY-kinases are essential bacterial enzymes with significant roles in physiology and virulence.
  • Targeting BY-kinases offers a promising strategy for developing novel antibiotics.
  • Further research into BY-kinases could lead to new therapeutic interventions against bacterial infections.