Aspirin — now we can see it
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Biochemistry, Genetics and Molecular Biology,General Medicine
Link
http://www.nature.com/articles/nm0995-882.pdf
Reference9 articles.
1. Loll, P.J., Picot, D. & Garavito, R.M. The structural basis of aspirin activity inferred from the crystal structure of inactivated prostaglandin H2 synthase. Nature struct. Biol. 2, 637–643 (1995).
2. Vane, J.R. Inhibition of prostaglandin synthesis as a mechanism of action for aspirin-like drugs. Nature New Biol. 231, 232–235 (1971).
3. Smith, W.L., Eling, T.E., Kulmacz, R.J., Marnett, L.J. & Tsai, A.-L. Tyrosyl radicals and their role in hydroperoxide-dependent activation and inactivation of prostaglandin endoperoxide synthase. Biochemistry 31, 3–7 (1992).
4. Vane, J. Towards a better aspirin. Nature 367, 215–216 (1994).
5. Meade, E.A., Smith, W.L. & DeWitt, D.L. Differential inhibition of prostaglandin endoperoxide synthase (cyclooxygenase) isozymes by aspirin and other non-steroidal anti-inflammatory drugs. J. biol. Chem. 268, 6610–6614 (1993).
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