Publication

Measurement of protein S-nitrosylation during cell signaling

Mannick, Joan B.
Schonhoff, Christopher M.
Citations
Altmetric:
Student Authors
Faculty Advisor
Academic Program
Document Type
Journal Article
Publication Date
2008-04-22
Keywords
Subject Area
Embargo Expiration Date
Abstract

S-Nitrosylation, the modification of a cysteine thiol by a nitric oxide (NO) group, has emerged as an important posttranslational modification of signaling proteins. An impediment to studying the regulation of cell signaling by S-nitrosylation has been the technical challenge of detecting endogenously S-nitrosylated proteins. Detection of S-nitrosylated proteins is difficult because the S-NO bond is labile and therefore can be lost or gained artifactually during sample preparation. Nevertheless, several methods have been developed to measure endogenous protein S-nitrosylation, including the biotin switch assay and the chemical reduction/chemiluminescence assay. This chapter describes these two methods and provides examples of how they have been used successfully to elucidate the role of protein S-nitrosylation in cell physiology and pathophysiology.

Source

Methods Enzymol. 2008;440:231-42. Link to article on publisher's site

Year of Medical School at Time of Visit
Sponsors
Dates of Travel
DOI
10.1016/S0076-6879(07)00814-2
PubMed ID
18423221
Other Identifiers
Notes
Funding and Acknowledgements
Corresponding Author
Related Resources
Related Resources
Repository Citation
Rights
Distribution License