Abstract:
:Reactive nitrogen species are formed during a variety of disease states and have been shown to modify several amino acids on proteins. To date, the majority of research in this area has focused on the nitration of tyrosine residues to form 3-nitrotyrosine. However, emerging evidence suggests that another modification, nitration of tryptophan residues, to form nitrotryptophan (NO(2)-Trp), may also play a significant role in the biology of nitrosative stress. This review takes an in-depth look at NO(2)-Trp, presenting the current research about its formation, prevalence and biological significance, as well as the methods used to identify NO(2)-Trp-modified proteins. Although more research is needed to understand the full biological role of NO(2)-Trp, the data presented herein suggest a contribution to nitrosative stress-induced cell dysregulation and perhaps even in physiological cell processes.
journal_name
J Proteomicsjournal_title
Journal of proteomicsauthors
Nuriel T,Hansler A,Gross SSdoi
10.1016/j.jprot.2011.05.032subject
Has Abstractpub_date
2011-10-19 00:00:00pages
2300-12issue
11eissn
1874-3919issn
1876-7737pii
S1874-3919(11)00246-6journal_volume
74pub_type
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