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Related Concept Videos

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...

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Related Experiment Video

Updated: May 21, 2026

Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays
07:42

Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays

Published on: September 19, 2018

Toward quantitative phosphotyrosine profiling in vivo.

Hannah Johnson1, Forest M White

  • 1Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, United States.

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

Advances in mass spectrometry (MS) and enrichment methods enable sensitive detection and quantification of tyrosine phosphorylation. These techniques are crucial for understanding cell signaling in health and disease.

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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

Published on: August 2, 2018

Related Experiment Videos

Last Updated: May 21, 2026

Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays
07:42

Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays

Published on: September 19, 2018

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

Area of Science:

  • Cell Biology
  • Biochemistry
  • Proteomics

Background:

  • Tyrosine phosphorylation is a critical post-translational modification regulating cell biology.
  • Understanding its role requires identifying phosphorylation sites and quantifying their levels under physiological conditions.

Purpose of the Study:

  • To review advancements in mass spectrometry (MS) and phosphotyrosine enrichment methods.
  • To discuss computational and manual approaches for phosphopeptide identification and site localization.
  • To cover methods for relative quantification of phosphorylation sites.

Main Methods:

  • Mass spectrometry (MS) for phosphotyrosine identification and characterization.
  • Phosphotyrosine enrichment techniques for detecting low-level phosphorylation.
  • Computational and manual analysis for phosphopeptide sequencing and site localization.
  • Quantitative MS for relative phosphorylation site analysis.

Main Results:

  • Recent advances facilitate the identification of low-level tyrosine phosphorylation events.
  • Methods are available for confident phosphopeptide identification and site localization.
  • Techniques enable relative quantification of numerous phosphorylation sites.

Conclusions:

  • New MS and enrichment technologies allow for detailed characterization of tyrosine phosphorylation signaling.
  • Quantitative MS-based analysis provides biological insights into signaling networks.
  • These approaches are vital for understanding signal transduction in health and disease.