Protein posttranslational modification

James L Hougland, Joseph Darling, Susan Flynn

Research output: Chapter in Book/Report/Conference proceedingChapter

5 Citations (Scopus)

Abstract

Proteins play central and essential roles in the vast majority of biological processes. Protein function is transduced through molecular interactions involving amino acid side chains. This chapter focuses on the protein modifications that occur due to reactive species generated during oxidative stress. It presents an overview of the modifications that can occur at each amino acid due to oxidative stress and a survey of the methods currently in use to detect oxidative stress‐related posttranslational modifications (PTMs). Among the array of methods that have been used to identify oxidative PTMs, mass spectrometry and chemoselective modifications have proven to be the most robust and specific tools for identifying these modifications within the proteome. A section provides an overview of the current state of both techniques, with more detailed descriptions. The chapter concludes with a discussion on the role of PTMs in cellular redox signaling.

Original languageEnglish (US)
Title of host publicationMolecular Basis of Oxidative Stress
Subtitle of host publicationChemistry, Mechanisms, and Disease Pathogenesis
PublisherWiley
Pages71-92
Number of pages22
ISBN (Electronic)9780470572184
ISBN (Print)9781118355886
DOIs
StatePublished - Jan 1 2013

Fingerprint

Post Translational Protein Processing
Oxidative stress
Proteins
Oxidative Stress
Biological Phenomena
Amino acids
Amino Acids
Molecular interactions
Proteome
Oxidation-Reduction
Mass spectrometry
Mass Spectrometry

Keywords

  • Amino acid modification
  • Cellular redox signaling
  • Posttranslational modifications (PTMs)
  • Protein posttranslational modification

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Hougland, J. L., Darling, J., & Flynn, S. (2013). Protein posttranslational modification. In Molecular Basis of Oxidative Stress: Chemistry, Mechanisms, and Disease Pathogenesis (pp. 71-92). Wiley. https://doi.org/10.1002/9781118355886.ch3

Protein posttranslational modification. / Hougland, James L; Darling, Joseph; Flynn, Susan.

Molecular Basis of Oxidative Stress: Chemistry, Mechanisms, and Disease Pathogenesis. Wiley, 2013. p. 71-92.

Research output: Chapter in Book/Report/Conference proceedingChapter

Hougland, JL, Darling, J & Flynn, S 2013, Protein posttranslational modification. in Molecular Basis of Oxidative Stress: Chemistry, Mechanisms, and Disease Pathogenesis. Wiley, pp. 71-92. https://doi.org/10.1002/9781118355886.ch3
Hougland JL, Darling J, Flynn S. Protein posttranslational modification. In Molecular Basis of Oxidative Stress: Chemistry, Mechanisms, and Disease Pathogenesis. Wiley. 2013. p. 71-92 https://doi.org/10.1002/9781118355886.ch3
Hougland, James L ; Darling, Joseph ; Flynn, Susan. / Protein posttranslational modification. Molecular Basis of Oxidative Stress: Chemistry, Mechanisms, and Disease Pathogenesis. Wiley, 2013. pp. 71-92
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