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Related Concept Videos

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...
MAPK Signaling Cascades01:07

MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
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...
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...

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Related Experiment Video

Updated: Jul 15, 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

Structural insights into multitargeting Mycobacterium tuberculosis Pkn kinases.

Angelika Pölläniemi1, Ya Miao1, Lotta Laitila1

  • 1Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.

Microbiology Spectrum
|July 14, 2026
PubMed
Summary

New kinase inhibitors show promise against drug-resistant tuberculosis. This study identifies compounds targeting essential Mycobacterium tuberculosis kinases, offering a potential strategy to overcome treatment challenges posed by resistant bacterial strains.

Keywords:
Pkn kinasesX-ray crystallographyantimycobacterialdrug discovery

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Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

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Related Experiment Videos

Last Updated: Jul 15, 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 Inhibitor Screening In Self-assembled Human Protein Microarrays
13:22

Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

Published on: October 23, 2019

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

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

Area of Science:

  • Biochemistry
  • Microbiology
  • Drug Discovery

Background:

  • Tuberculosis (TB) is a major global health issue, exacerbated by multidrug-resistant (MDR-TB) and extensively drug-resistant (XDR-TB) strains.
  • Protein kinases (PknA, PknB, PknG) are crucial for Mycobacterium tuberculosis survival, virulence, and persistence.
  • Existing treatments for resistant TB are limited and often toxic, necessitating novel therapeutic approaches.

Purpose of the Study:

  • To screen for and identify novel kinase inhibitors targeting essential Mycobacterium tuberculosis kinases.
  • To evaluate the efficacy of identified compounds against M. tuberculosis growth.
  • To elucidate the structural and biophysical interactions of these inhibitors with their targets.

Main Methods:

  • Screening of an in-house kinase inhibitor library against M. tuberculosis kinases.
  • In vitro inhibition assays and M. tuberculosis growth inhibition assays.
  • X-ray crystallography, molecular docking, and isothermal titration calorimetry for structural and biophysical characterization.

Main Results:

  • Four structurally diverse compounds were identified that inhibit PknA, PknB, and PknG in vitro.
  • These compounds demonstrated efficacy in inhibiting M. tuberculosis growth.
  • Structural and biophysical analyses provided insights into the binding mechanisms of the inhibitors.

Conclusions:

  • The identified compounds provide a structural framework for developing multitargeting kinase inhibitors.
  • This multitargeting approach offers a potential strategy to combat drug-resistant M. tuberculosis.
  • The findings advance rational drug design for next-generation antitubercular therapies.