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Related Concept Videos

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...
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...
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...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...

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Related Experiment Video

Updated: Jun 8, 2026

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
15:41

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae

Published on: October 12, 2009

Phosphoproteomics.

Nurhan Ozlu1,2, Bikem Akten1,3,4, Wiebke Timm1,5,6

  • 1Proteomics Center at Children's Hospital Boston, Boston, MA, USA.

Wiley Interdisciplinary Reviews. Systems Biology and Medicine
|September 14, 2010
PubMed
Summary
This summary is machine-generated.

Protein phosphorylation, a key post-translational modification, regulates vital cellular functions across all life. This review covers advanced proteomics technologies for studying phosphorylation, noting recent quantitative analysis advancements.

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Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis
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Last Updated: Jun 8, 2026

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
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Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae

Published on: October 12, 2009

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein phosphorylation is the most common and evolutionarily conserved post-translational modification (PTM).
  • Its reversible nature is crucial for signal transduction, controlling diverse cellular functions from bacteria to humans.
  • Phosphorylation impacts protein stability, localization, activity, and complex formation, enabling precise regulation of cell cycle and growth.

Purpose of the Study:

  • To review state-of-the-art proteomics technologies for studying protein phosphorylation.
  • To highlight advancements in quantitative global phosphorylation analyses.
  • To identify limitations and caveats in current experimental approaches.

Main Methods:

  • Review of current proteomics technologies.
  • Analysis of recent advancements in quantitative global proteomics.
  • Discussion of experimental design and data interpretation challenges.

Main Results:

  • Significant progress in proteomics enables quantitative, global analysis of phosphorylation.
  • New technologies offer deeper insights into phosphorylation-dependent signaling pathways.
  • Experimental caveats require careful consideration for accurate interpretation.

Conclusions:

  • Proteomics technologies have greatly advanced the study of protein phosphorylation.
  • Quantitative global analyses are now feasible, providing comprehensive insights.
  • Careful experimental design and awareness of limitations are crucial for reliable phosphorylation research.