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Related Concept Videos

Proteomics01:33

Proteomics

7.3K
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...
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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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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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Related Experiment Video

Updated: Jul 8, 2025

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

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Recent progress in quantitative phosphoproteomics.

Katharina Zittlau1, Payal Nashier1, Claudia Cavarischia-Rega1

  • 1Quantitative Proteomics, Interfaculty Institute of Cell Biology, University of Tuebingen, Tuebingen , Germany.

Expert Review of Proteomics
|December 20, 2023
PubMed
Summary

Quantitative phosphoproteomics uses advanced labeling techniques for precise analysis of protein phosphorylation. Optimizing methods to reduce sample needs is crucial for broader application, especially in clinical settings.

Keywords:
DIAIsobaric labelingLC-MShotspot thermal profilingphosphopeptide enrichmentprotein phosphorylationquantitative phosphoproteomicsstable isotope labeling

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Area of Science:

  • Proteomics
  • Post-translational modifications
  • Cellular signaling

Background:

  • Protein phosphorylation regulates key cellular processes, including signal transduction and enzyme activity.
  • Understanding dynamic phosphorylation changes is vital for biological and disease research.
  • Liquid chromatography-tandem mass spectrometry (LC-MS/MS) with quantitative proteomics is a powerful tool for studying phosphorylation.

Purpose of the Study:

  • To review current quantification methods in phosphoproteomics.
  • To discuss strategies for optimizing quantitative phosphoproteomics.
  • To highlight the importance of reducing sample input for wider implementation.

Main Methods:

  • Stable isotope labeling techniques.
  • Isobaric labeling techniques.
  • Liquid chromatography-tandem mass spectrometry (LC-MS/MS).

Main Results:

  • Current labeling techniques offer precise and accurate quantification of phosphorylation events.
  • Optimization can enhance analytic depth, dynamic range, site localization, and data integrity.
  • Reducing input material is essential for broader adoption, particularly for clinical samples.

Conclusions:

  • Quantitative phosphoproteomics is a rapidly advancing field with significant potential.
  • Challenges remain in achieving deeper and more comprehensive analyses, especially at single-cell levels.
  • Further optimization is needed for clinical diagnostics and advanced research applications.