SNObase, a database for S-nitrosation modification

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.

Research methods of anti-HIV-1 inhibitors targeting at Vif-APOBEC3G axis / 中国中药杂志

The mammalian APOBEC3G protein (apolipoprotein B mRNA-editing enzyme catalytic polypeptide 3 protein G, APOBEC3G) is an important component of the cellular innate immune response to retroviral infection. APOBEC3G can extinguish HIV-1 (human immunodeficiency virus type 1) infectivity by its incorporation into virus particles and subsequent cytosine deaminase activity to block replication of HIV-1. HIV-1 Vif (viral infectivity factor) suppresses various APOBEC3 proteins through a common mechanism which induces the degradation of target proteins. Therefore, the interrelation of Vif-APOBEC3G has been extensively studied, which represents attractive targets for the development of novel inhibitors. We summarize the papers in which the detection technique and methods have been developed to assay the anti-HIV activity and its mechanism, such as western-blotting, co-immunoprecipitation, pulse-chase experiments, bioluminescence resonance energy transfer, biomolecular interaction analysis. This review is towards developing therapeutics aimed at the Vif-APOBEC3G axis.