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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...
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...
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...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...

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Related Experiment Video

Updated: May 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

What general conclusions can we draw from kinase profiling data sets?

Jeffrey J Sutherland1, Cen Gao, Suntara Cahya

  • 1Eli Lilly and Company, Lilly Research Laboratories, Lilly Corporate Center, DC 1930, Indianapolis, IN 46285, USA.

Biochimica Et Biophysica Acta
|January 22, 2013
PubMed
Summary
This summary is machine-generated.

Assessing kinase inhibitor activity across different assay panels reveals low agreement for active compounds, though inactive compound data is more consistent. This highlights challenges in drawing broad conclusions about kinase selectivity and inhibitor profiles.

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Related Experiment Videos

Last Updated: May 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

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Published on: October 23, 2019

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
  • Pharmacology
  • Drug Discovery

Background:

  • Understanding kinase selectivity trends is crucial for drug development, influencing target selection, compound prioritization, and patient tailoring.
  • Recent studies have characterized kinase inhibitors using large assay panels, leading to generalizations that shape research directions.
  • Overlapping compound-kinase data across different reports necessitates evaluating the concordance of results from various assay technologies.

Purpose of the Study:

  • To evaluate the concordance of kinase inhibitor activity results across four distinct biochemical assay data sources.
  • To assess agreement in determining compound activity, target promiscuity, and pharmacological similarity.
  • To investigate the consistency of kinase inhibitor promiscuity across different profiling panels.

Main Methods:

  • Comparative analysis of compound-kinase activity data from four independent sources utilizing different biochemical assay technologies.
  • Evaluation of result concordance for active and inactive compounds, as well as target and inhibitor promiscuity.
  • Assessment of selectivity differences between type I and type II inhibitors and kinase space similarity.

Main Results:

  • Overall agreement across all results was 77% within a 3-fold range or qualitatively similar.
  • Agreement for active compounds was significantly lower at 37%, suggesting panels are better at identifying lack of activity.
  • Low concordance was observed for kinase target promiscuity and pharmacological similarity, while inhibitor promiscuity was consistent across sources.

Conclusions:

  • Different kinase profiling panels exhibit better agreement in identifying inactive compounds than quantifying the degree of activity.
  • Drawing general conclusions about kinase selectivity and inhibitor profiles from current data is challenging due to low concordance.
  • No significant selectivity difference was found between type I and type II inhibitors, and kinase space similarity was limited and consistent across sources.