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Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

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Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
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Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.
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Characterizing citrullination by mass spectrometry-based proteomics.

A S Rebak1, I A Hendriks1, M L Nielsen1

  • 1Proteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|October 1, 2023
PubMed
Summary
This summary is machine-generated.

Citrullination, a key protein modification, is crucial in immunity and stem cell function but poorly understood. Mass spectrometry (MS) proteomics can identify citrullination sites and improve understanding of these networks.

Keywords:
citrullinationmass spectrometrypost-translational modificationsproteomics

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Area of Science:

  • Biochemistry
  • Proteomics
  • Molecular Biology

Background:

  • Citrullination is a post-translational modification (PTM) of arginine with roles in autoimmune disorders, immunity, and stem cell potency.
  • Compared to other PTMs like phosphorylation, citrullination is less understood.
  • High-resolution mass spectrometry (MS)-based proteomics is a powerful tool for unbiased study of citrullination.

Purpose of the Study:

  • To outline contemporary MS methods for studying citrullination.
  • To discuss current challenges in citrullination research.
  • To explore the potential of novel MS-based proteomics approaches for understanding citrullination networks.

Main Methods:

  • High-resolution mass spectrometry (MS)-based proteomics.
  • Identification of citrullination modification sites.
  • Distinguishing citrullination from deamidation events.
  • Analysis of synovial fluids from rheumatoid arthritis patients.

Main Results:

  • MS has provided insights into peptidyl arginine deaminase targeting.
  • Site-specific citrullination information has been obtained, e.g., in rheumatoid arthritis patient synovial fluids.
  • There is significant unrealized potential for proteome-wide investigations using MS.

Conclusions:

  • MS-based proteomics offers a valuable, unbiased approach to study citrullination.
  • Further development of citrullination-specific MS methods is needed.
  • Enhanced understanding of citrullination networks can be achieved through advanced MS techniques.