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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...

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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

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Clinical and technical phosphoproteomic research.

Elena López1, Isabel López, Antonio Ferreira

  • 1Inflammatory core, Centro de Investigación i+12 del Hospital Universitario 12 de Octubre, Avda de Córdoba s/n 28041, Madrid, Spain. elena.lopez.villar@gmail.com.

Proteome Science
|June 4, 2011
PubMed
Summary

Identifying phosphorylated proteins is key for diagnosing and treating immunological diseases like cancer. Advanced techniques like mass spectrometry are crucial for monitoring signaling pathways and developing targeted therapies.

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Area of Science:

  • Proteomics and Immunology
  • Biochemistry and Molecular Biology

Background:

  • Protein phosphorylation regulates immune responses and is crucial in cancer.
  • Signaling networks control vital cellular processes including proliferation and apoptosis.
  • Understanding kinase signaling pathways is essential for numerous immunological pathologies.

Purpose of the Study:

  • To detail current techniques for clinical phosphoproteomic studies.
  • To aid in immunology and cancer research through advanced protein analysis.
  • To highlight methods for isolating and studying phosphorylated proteins.

Main Methods:

  • Phosphoproteomic analysis using immunoproteomic techniques and mass spectrometry (MS).
  • Phosphopeptide enrichment from biological samples (tissue, bodily fluids).
  • Quantitative techniques for identifying and quantifying protein phosphorylation sites.

Main Results:

  • Enables identification and quantification of protein phosphorylation sites.
  • Facilitates pharmacodynamic readouts of disease states and drug responses.
  • Aims to improve phosphopeptide recovery and study phospho-regulation.

Conclusions:

  • Phosphoproteomics offers a promising approach for diagnosing and treating immunological diseases, including cancer.
  • Combining enrichment and quantitative techniques is vital for robust phosphoproteomic studies.
  • This field advances clinical research by providing insights into cellular signaling and drug efficacy.