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dbSNO 2.0: a resource for exploring structural environment, functional and disease association and regulatory network of protein S-nitrosylation.

Chen YJ, Lu CT, Su MG, Huang KY, Ching WC, Yang HH, Liao YC, Chen YJ, Lee TY - Nucleic Acids Res. (2014)

Bottom Line: Given the increasing number of proteins reported to be regulated by S-nitrosylation (SNO), it is considered to act, in a manner analogous to phosphorylation, as a pleiotropic regulator that elicits dual effects to regulate diverse pathophysiological processes by altering protein function, stability, and conformation change in various cancers and human disorders.Additionally, the annotations of protein molecular functions, biological processes, functional domains and human diseases are integrated to explore the functional and disease associations for S-nitrosoproteome.In this update, users are allowed to search a group of interested proteins/genes and the system reconstructs the SNO regulatory network based on the information of metabolic pathways and protein-protein interactions.

View Article: PubMed Central - PubMed

Affiliation: Institute of Chemistry, Academia Sinica, Taipei 115, Taiwan.

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Disease network for human S-nitrosylated proteins.
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Figure 4: Disease network for human S-nitrosylated proteins.

Mentions: Based on the information from OMIM, KEGG and IPA database analysis, the correlation of these 720 human SNO proteins with disease-related processes and networks was also analyzed and categorized into 31 diseases. As shown in Figure 4, 370 (51%) of SNO proteins were matched to cancers, including oral, breast, gastric, colorectal, liver cancer, etc. (Supplementary Table S17). In addition to cancer, other top four diseases were described as organismal injury and abnormalities, reproductive system disease, gastrointestinal disease and neurological disease. The correlations of diseases linking with their common proteins were presented to clarify the relationship of SNO proteins and diseases. Taken together, the results showed that these SNO proteins display annotated roles in the disease regulation. The connecting information of these diseases can help users to understand whether the SNO of these proteins plays the same or different roles in correlated diseases. Most importantly, the relationship between different diseases for SNO may supply the new respect to find out the potential regulators that modulate the disease initiation, progression or suppression.


dbSNO 2.0: a resource for exploring structural environment, functional and disease association and regulatory network of protein S-nitrosylation.

Chen YJ, Lu CT, Su MG, Huang KY, Ching WC, Yang HH, Liao YC, Chen YJ, Lee TY - Nucleic Acids Res. (2014)

Disease network for human S-nitrosylated proteins.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4383970&req=5

Figure 4: Disease network for human S-nitrosylated proteins.
Mentions: Based on the information from OMIM, KEGG and IPA database analysis, the correlation of these 720 human SNO proteins with disease-related processes and networks was also analyzed and categorized into 31 diseases. As shown in Figure 4, 370 (51%) of SNO proteins were matched to cancers, including oral, breast, gastric, colorectal, liver cancer, etc. (Supplementary Table S17). In addition to cancer, other top four diseases were described as organismal injury and abnormalities, reproductive system disease, gastrointestinal disease and neurological disease. The correlations of diseases linking with their common proteins were presented to clarify the relationship of SNO proteins and diseases. Taken together, the results showed that these SNO proteins display annotated roles in the disease regulation. The connecting information of these diseases can help users to understand whether the SNO of these proteins plays the same or different roles in correlated diseases. Most importantly, the relationship between different diseases for SNO may supply the new respect to find out the potential regulators that modulate the disease initiation, progression or suppression.

Bottom Line: Given the increasing number of proteins reported to be regulated by S-nitrosylation (SNO), it is considered to act, in a manner analogous to phosphorylation, as a pleiotropic regulator that elicits dual effects to regulate diverse pathophysiological processes by altering protein function, stability, and conformation change in various cancers and human disorders.Additionally, the annotations of protein molecular functions, biological processes, functional domains and human diseases are integrated to explore the functional and disease associations for S-nitrosoproteome.In this update, users are allowed to search a group of interested proteins/genes and the system reconstructs the SNO regulatory network based on the information of metabolic pathways and protein-protein interactions.

View Article: PubMed Central - PubMed

Affiliation: Institute of Chemistry, Academia Sinica, Taipei 115, Taiwan.

Show MeSH
Related in: MedlinePlus