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- W2898888137 abstract "Nitric oxide (NO) mediates various physiological and pathological processes, including cell proliferation, differentiation, and inflammation. Protein S-nitrosylation (SNO), a NO-mediated reversible protein modification, leads to changes in the activity and function of target proteins. Recent findings on protein-protein transnitrosylation reactions (transfer of an NO group from one protein to another) have unveiled the mechanism of NO modulation of specific signaling pathways. The intracellular level of S-nitrosoglutathione (GSNO), a major reactive NO species, is controlled by GSNO reductase (GSNOR), a major regulator of NO/SNO signaling. Increasing number of GSNOR-related studies have shown the important role that denitrosylation plays in cellular NO/SNO homeostasis and human pathophysiology. This review introduces recent evidence of GSNO-mediated NO/SNO signaling depending on GSNOR expression or activity. In addition, the applicability of GSNOR as a target for drug therapy will be discussed in this review." @default.
- W2898888137 created "2018-11-09" @default.
- W2898888137 creator A5029273980 @default.
- W2898888137 date "2018-11-01" @default.
- W2898888137 modified "2023-09-24" @default.
- W2898888137 title "Pathophysiological Role of S-Nitrosylation and Transnitrosylation Depending on S-Nitrosoglutathione Levels Regulated by S-Nitrosoglutathione Reductase" @default.
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- W2898888137 doi "https://doi.org/10.4062/biomolther.2018.179" @default.
- W2898888137 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6254642" @default.
- W2898888137 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30464072" @default.
- W2898888137 hasPublicationYear "2018" @default.
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