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Related Concept Videos

Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...

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Related Experiment Video

Updated: May 26, 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

An integrated Bayesian framework for identifying phosphorylation networks in stimulated cells.

Tapesh Santra1, Boris Kholodenko, Walter Kolch

  • 1Systems Biology Ireland, Conway Institute, University College Dublin (UCD), Belfield, Dublin 4, Ireland. tapesh.santra@ucd.ie

Advances in Experimental Medicine and Biology
|December 14, 2011
PubMed
Summary

We developed a Bayesian framework to infer cell signaling pathways by analyzing protein phosphorylation events. This method accurately predicts phosphorylation networks using diverse data types for better understanding of cellular mechanisms.

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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Related Experiment Videos

Last Updated: May 26, 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

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Area of Science:

  • Molecular Biology
  • Systems Biology
  • Bioinformatics

Background:

  • Protein phosphorylation is a key mechanism in cellular signal transduction pathways.
  • Understanding phosphorylation events is crucial for deciphering cellular signaling mechanisms.
  • Ligand stimulation triggers specific phosphorylation cascades leading to cellular responses like transcription.

Purpose of the Study:

  • To develop a computational framework for inferring protein phosphorylation networks.
  • To enhance the accuracy of predicting signaling pathways using integrated data.
  • To provide a tool for a deeper understanding of cell signaling.

Main Methods:

  • Developed a Bayesian inference framework to model phosphorylation networks.
  • Utilized time-series phosphosite concentration data upon ligand stimulation.
  • Integrated diverse data sources including sequence, genomic, experimental, pathway, and literature data.

Main Results:

  • Successfully inferred phosphorylation networks from time-series data.
  • Achieved high prediction accuracy by integrating multiple data types.
  • Validated results against publicly available biological data.

Conclusions:

  • The Bayesian framework provides an accurate method for predicting phosphorylation networks.
  • Integration of diverse data significantly improves the prediction of signaling mechanisms.
  • This approach advances the understanding of cellular signal transduction pathways.