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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...
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: May 12, 2026

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer
12:23

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

Published on: August 2, 2018

Phosphoproteomics--more than meets the eye.

Stefan Loroch1, Clarissa Dickhut, René P Zahedi

  • 1Leibniz-Institut für Analytische Wissenschaften - ISAS - e.V, Dortmund, Germany.

Electrophoresis
|April 12, 2013
PubMed
Summary

Post-translational modifications, particularly protein phosphorylation, are crucial for cellular adaptation. This review highlights advancements in mass spectrometry (MS) for studying phosphorylation and discusses common research pitfalls.

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Last Updated: May 12, 2026

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Proteomics

Background:

  • Post-translational modifications (PTMs) are vital for cellular responses to stimuli.
  • Protein phosphorylation is a key PTM regulating cellular processes and protein interactions.
  • Recent advancements in mass spectrometry (MS) have significantly improved the study of phosphorylation.

Purpose of the Study:

  • To review current knowledge on protein phosphorylation, including O- and N-phosphorylation.
  • To highlight the impact of MS-based approaches on phosphorylation research.
  • To discuss challenges and pitfalls in phosphorylation studies.

Main Methods:

  • Mass spectrometry (MS)-based proteomics.
  • Phosphopeptide enrichment strategies.
  • Literature review of phosphorylation research.

Main Results:

  • MS and enrichment strategies have yielded new insights into phosphorylation.
  • O-phosphorylation remains the primary focus, but N-phosphorylation's relevance is increasingly recognized.
  • Common pitfalls exist in sample preparation, LC-MS analysis, and data interpretation.

Conclusions:

  • Advanced MS techniques are revolutionizing phosphorylation research.
  • Addressing methodological challenges is crucial for reliable and comparable phosphorylation studies.
  • Further research into N-phosphorylation is warranted.