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Acetylation of Prostaglandin H(2) Synthases by Aspirin is Inhibited by Redox Cycling of the Peroxidase
Aspirin exerts its unique pharmacological effects by irreversibly acetylating a serine residue in the cyclooxygenase site of prostaglandin-H(2)-synthases (PGHSs). Despite the irreversibility of the inhibition, the potency of aspirin varies remarkably between cell types, suggesting that molecular det...
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| Main Authors: | , , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2007
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2693035/ https://ncbi.nlm.nih.gov/pubmed/18242581 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bcp.2007.12.005 |
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