Post-Translational Protein Modifications in Oxidative Stress
A special issue of Antioxidants (ISSN 2076-3921).
Deadline for manuscript submissions: closed (31 March 2019) | Viewed by 7548
Special Issue Editor
Special Issue Information
Dear Colleagues,
Numerous post translational protein modifications play crucial roles in the cellular redox balance and are known to be implicated in many diseases. Some of the most well-known modifications are induced by reactive oxygen and nitrogen species, which generates a wide range of adducts that preferentially target cysteine thiols. Oxygen derived modifications include sulfenylation (SOH), formation of sulfinic acid (SO2H) and sulfonic acid (SO3H) while S-nitrosylation covers thiol adduct formation by nitrogen oxide. In addition, there are many more modifications, i.e., S- and N-homocysteinylation, S-glutathionylation, including protein carbonylation, which are known either to deregulate redox state or to be of importance for maintaining cellular homeostasis. Not only endogenous radicals and compounds cause protein modifications associated with oxidative stress, but also exogenous compounds from food products such as sulfites can potentially play a significant role.
In this Special Edition of Antioxidants, we invite you to submit your most recent research findings or a review article. The aim of this Issue is to consolidate up-to-date research and knowledge on post-translational modifications associated with oxidative stress. Of interest are the development of new approaches and applications of already well-known methods to determine the role and significance of these modifications in disease.
Dr. Klaus Klarskov
Guest Editor
Manuscript Submission Information
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