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Related Concept Videos

Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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...
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...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Related Experiment Video

Updated: May 26, 2026

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
07:28

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

Published on: October 19, 2021

Modeling signaling networks using high-throughput phospho-proteomics.

Camille Terfve1, Julio Saez-Rodriguez

  • 1European Bioinformatics Institute (EMBL-EBI), Wellcome Trust Genome Campus, Cambridge CB10 1SD, UK. terfve@ebi.ac.uk

Advances in Experimental Medicine and Biology
|December 14, 2011
PubMed
Summary
This summary is machine-generated.

Mathematical modeling aids understanding complex cellular signaling networks. This review covers data acquisition (antibody-based, mass spectrometry) and computational analysis methods for phosphoproteomics data.

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Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis
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Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis

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JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
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Published on: June 25, 2020

Area of Science:

  • Systems Biology
  • Computational Biology
  • Biochemistry

Background:

  • Cellular communication relies on complex signaling networks.
  • Mathematical modeling is crucial for deciphering network complexity.
  • Phosphoproteomics data provides key insights into signaling pathways.

Purpose of the Study:

  • To review recent advancements in data acquisition for cellular signaling.
  • To explore various computational model formalisms for analyzing phosphoproteomics data.
  • To bridge the gap between experimental data and mechanistic understanding of signaling networks.

Main Methods:

  • Antibody-based technologies and mass spectrometry (MS) for phosphoproteomics data acquisition.
  • Review of computational approaches including clustering, data mining, and mechanistic models.
  • Discussion of rule-based, logic-based, Bayesian network inference, and linear regression models.

Main Results:

  • Comparison of antibody-based and MS techniques, highlighting their strengths and limitations.
  • Overview of diverse modeling formalisms applicable to high-throughput phosphoproteomics data.
  • Demonstration of how different models capture various aspects of signaling network dynamics.

Conclusions:

  • Accurate data acquisition and appropriate model formalisms are essential for understanding cellular signaling.
  • A range of computational tools are available for analyzing complex phosphoproteomics datasets.
  • Integrating experimental data with mathematical models enhances our comprehension of cellular information processing.