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2012 ; 3
(12
): 929-33
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SNObase, a database for S-nitrosation modification
#MMPMID23129220
Zhang X
; Huang B
; Zhang L
; Zhang Y
; Zhao Y
; Guo X
; Qiao X
; Chen C
Protein Cell
2012[Dec]; 3
(12
): 929-33
PMID23129220
show ga
S-Nitros(yl)ation is a ubiquitous redox-based post-translational modification of
protein cysteine thiols by nitric oxide or its derivatives, which transduces the
bioactivity of nitric oxide (NO) by regulation of protein conformation, activity,
stability, localization and protein-protein interactions. These years, more and
more S-nitrosated proteins were identified in physiological and pathological
processes and the number is still growing. Here we developed a database named
SNObase ( http://www.nitrosation.org ), which collected S-nitrosation targets
extracted from literatures up to June 1st, 2012. SNObase contained 2561
instances, and provided information about S-nitrosation targets, sites,
biological model, related diseases, trends of S-nitrosation level and effects of
S-nitrosation on protein function. With SNObase, we did functional analysis for
all the SNO targets: In the gene ontology (GO) biological process category, some
processes were discovered to be related to S-nitrosation ("response to drug",
"regulation of cell motion") besides the previously reported related processes.
In the GO cellular component category, cytosol and mitochondrion were both
enriched. From the KEGG pathway enrichment results, we found SNO targets were
enriched in different diseases, which suggests possible significant roles of
S-nitrosation in the progress of these diseases. This SNObase means to be a
database with precise, comprehensive and easily accessible information, an
environment to help researchers integrate data with comparison and relevancy
analysis between different groups or works, and also an SNO knowledgebase
offering feasibility for systemic and global analysis of S-nitrosation in
interdisciplinary studies.
free
free
free
