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Related Concept Videos

Proteomics01:33

Proteomics

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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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Capillary Electrophoresis Mass Spectrometry Approaches for Characterization of the Protein and Metabolite Corona Acquired by Nanomaterials
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CETSA in integrated proteomics studies of cellular processes.

Nayana Prabhu1, Lingyun Dai2, Pär Nordlund3

  • 1School of Biological Sciences, Nanyang Technological University, 637551, Singapore; Institute of Molecular and Cell Biology, A*STAR, 138673, Singapore.

Current Opinion in Chemical Biology
|December 16, 2019
PubMed
Summary

Cellular Thermal Shift Assay (CETSA) monitors protein interactions in cells. Integrating mass spectrometry-CETSA with other proteomics methods offers deeper insights into cellular processes and drug effects.

Keywords:
Cell statesCellular thermal shift assay (CETSA)Drug responseMass spectrometryProtein interaction states (PRINTS)Proteomics

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Area of Science:

  • Biochemistry
  • Proteomics
  • Cellular Biology

Background:

  • The Cellular Thermal Shift Assay (CETSA) is a method to monitor protein interactions.
  • Mass spectrometry-coupled CETSA (MS-CETSA) provides proteome-wide data on protein interactions.
  • Understanding CETSA shifts requires deeper mechanistic insights.

Purpose of the Study:

  • To expand mechanistic understanding of CETSA shifts.
  • To complement existing CETSA experimental data.
  • To propose an integrated proteomics platform for studying in situ proteome modulation.

Main Methods:

  • Utilizing mass spectrometry-coupled CETSA (MS-CETSA).
  • Integrating MS-CETSA with other proteomics techniques.
  • Analyzing functional modulations of protein interactions in intact cells and tissues.

Main Results:

  • MS-CETSA generates robust data on diverse protein interaction classes.
  • CETSA is suitable for studying protein interactions in cellular processes and drug actions.
  • Integration of MS-CETSA with other proteomics methods enhances mechanistic insights.

Conclusions:

  • Integrating MS-CETSA with other proteomics techniques provides a powerful platform.
  • This integrated approach allows for detailed, comprehensive, and interactive studies of proteome modulation in situ.
  • The proposed platform expands mechanistic insight into CETSA shifts and protein interactions.