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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,...
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...
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...

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Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer
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Quantitative phosphoproteomics to characterize signaling networks.

Kristoffer T G Rigbolt1, Blagoy Blagoev

  • 1Center for Experimental BioInformatics, Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, 5230 Odense M, Denmark. kristoffer.rigbolt@frias.uni-freiburg.de

Seminars in Cell & Developmental Biology
|June 9, 2012
PubMed
Summary

Quantitative phosphoproteomics enables system-wide analysis of cellular signaling networks by identifying and quantifying protein phosphorylation. This review highlights technological advances, applications, and future challenges in the field.

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Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
15:41

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae

Published on: October 12, 2009

Area of Science:

  • Cellular Biology
  • Biochemistry
  • Proteomics

Background:

  • Reversible protein phosphorylation regulates crucial cellular processes through signal transduction pathways.
  • Quantitative phosphoproteomics has emerged as a powerful tool for system-wide analysis of protein phosphorylation.
  • This technology is essential for comprehensive characterization of cellular signaling networks.

Purpose of the Study:

  • To review the technological advancements in quantitative phosphoproteomics.
  • To showcase recent system-wide applications of phosphoproteomics in diverse biological processes.
  • To discuss current limitations and future challenges in the field.

Main Methods:

  • Highly optimized procedures for sample preparation.
  • Advanced mass spectrometry techniques.
  • Sophisticated data analysis algorithms for identification and quantification of phosphorylations.

Main Results:

  • Identification and quantification of thousands of phosphorylation sites.
  • System-wide overviews of cellular signaling networks.
  • Applications in diverse fields like immunology, stem cell biology, and DNA damage response.

Conclusions:

  • Quantitative phosphoproteomics is a versatile platform for studying signaling networks.
  • Technological progress has enabled broad applications across biological research.
  • Ongoing challenges require further development for deeper insights into cellular signaling.