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Methodologies for the characterization, identification and quantification of S-nitrosylated proteins.

Publication ,  Journal Article
Foster, MW
Published in: Biochim Biophys Acta
June 2012

BACKGROUND: Protein S-nitrosylation plays a central role in signal transduction by nitric oxide (NO), and aberrant S-nitrosylation of specific proteins is increasingly implicated in disease. SCOPE OF REVIEW: Here, methodologies for the characterization, identification and quantification of SNO-proteins are reviewed, focusing on techniques suitable for the structural characterization and absolute quantification of isolated SNO-proteins, the identification and relative quantification of SNO-proteins from complex mixtures as well as the mass spectrometry-based identification and relative quantification of sites of S-nitrosylation (SNO-sites) in proteins. MAJOR CONCLUSIONS: Structural characterization of SNO-proteins by X-ray crystallography is increasingly being utilized to understand both the relationships between protein structure and Cys thiol reactivity as well as the consequences of S-nitrosylation on protein structure and function. New methods for the proteomic identification and quantification of SNO-proteins and SNO-sites have greatly impacted the ability to study protein S-nitrosylation in complex biological systems. GENERAL SIGNIFICANCE: The ability to identify and quantify SNO-proteins has long been rate-determining for scientific advances in the field of protein S-nitrosylation. Therefore, it is critical that investigators in the field have a good understand the utility and limitations of modern analytical techniques for SNO-protein analysis. This article is part of a Special Issue entitled: Regulation of cellular processes by S-nitrosylation.

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Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

June 2012

Volume

1820

Issue

6

Start / End Page

675 / 683

Location

Netherlands

Related Subject Headings

  • Signal Transduction
  • S-Nitrosothiols
  • Proteomics
  • Proteins
  • Protein Structure, Secondary
  • Nitrosation
  • Nitric Oxide
  • Mass Spectrometry
  • Intracellular Signaling Peptides and Proteins
  • Crystallography, X-Ray
 

Citation

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ICMJE
MLA
NLM
Foster, M. W. (2012). Methodologies for the characterization, identification and quantification of S-nitrosylated proteins. Biochim Biophys Acta, 1820(6), 675–683. https://doi.org/10.1016/j.bbagen.2011.03.013
Foster, Matthew W. “Methodologies for the characterization, identification and quantification of S-nitrosylated proteins.Biochim Biophys Acta 1820, no. 6 (June 2012): 675–83. https://doi.org/10.1016/j.bbagen.2011.03.013.
Foster, Matthew W. “Methodologies for the characterization, identification and quantification of S-nitrosylated proteins.Biochim Biophys Acta, vol. 1820, no. 6, June 2012, pp. 675–83. Pubmed, doi:10.1016/j.bbagen.2011.03.013.

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

June 2012

Volume

1820

Issue

6

Start / End Page

675 / 683

Location

Netherlands

Related Subject Headings

  • Signal Transduction
  • S-Nitrosothiols
  • Proteomics
  • Proteins
  • Protein Structure, Secondary
  • Nitrosation
  • Nitric Oxide
  • Mass Spectrometry
  • Intracellular Signaling Peptides and Proteins
  • Crystallography, X-Ray