Related Experiment Video

Updated: Jun 8, 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 in cancer

H C Harsha1, Akhilesh Pandey

  • 1Institute of Bioinformatics, International Technology Park, Bangalore, India. harsha@ibioinformatics.org

Molecular Oncology
|October 13, 2010
PubMed

Insights

This review covers advanced methods for analyzing protein phosphorylation, crucial for understanding cellular processes and cancer development. It highlights techniques for mapping thousands of phosphorylation sites and identifying drug targets.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Reversible protein phosphorylation regulates cellular functions.
  • Dysregulated kinase signaling pathways are linked to cancer.
  • Phosphorylation analysis is vital for understanding oncogenesis.

Purpose of the Study:

  • To review phosphoproteomic analysis approaches.
  • To highlight protein kinase characterization methods.
  • To summarize key cancer phosphoproteomic studies.

Main Methods:

  • Phosphoprotein/phosphopeptide enrichment strategies.
  • Quantitative mass spectrometry for global phosphoproteomics.
  • Chemical proteomic strategies for target identification.

Main Results:

  • High-throughput characterization of site-specific phosphorylation is possible.
  • Thousands of proteins can be profiled in a single experiment.
  • Kinase inhibitor targets can be identified using chemical proteomics.

Conclusions:

  • Phosphoproteomics offers powerful insights into cancer signaling.
  • Advanced analytical techniques enable comprehensive phosphorylation profiling.
  • This field is crucial for developing targeted cancer therapies.

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