4.5 Review

The SNO-proteome: causation and classifications

Journal

CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 15, Issue 1, Pages 129-136

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2010.10.012

Keywords

-

Funding

  1. National Institutes of Health [RO1 HL096673, RO1 HL095463, RO1 HL059130]
  2. DARPA [N66001-10-C-2015]

Ask authors/readers for more resources

Cell signaling is a complex and highly regulated process. Posttranslational modifications of proteins serve to sense and transduce cellular signals in a precisely coordinated manner. It is increasingly recognized that protein S-nitrosylation, the addition of a nitric oxide group to cysteine thiols, serves an important role in a wide range of signaling pathways. In spite of the large number of SNO-proteins now identified (similar to 1000), the observed specificity of S-nitrosylation in terms of target proteins and specific cysteines within modified proteins is incompletely understood. Here we review the progress made in S-nitrosylation detection methods that have facilitated the study of the SNO-proteome under physiological and pathophysiological conditions, and some factors important in determining the SNO-proteome. Classification schemes for emergent denitrosylases and prospective 'protein S-nitrosylases' are provided.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available