The role of conformational change in serpin structure and function

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1. 1Binding of thrombin to thrombomodulin accelerates inhibition of the enzyme by antithrombin III. Evidence for a heparin-independent mechanism1987 · 69 citations
2. 2Conformation of the reactive site loop of .alpha.1-proteinase inhibitor probed by limited proteolysis1992 · 198 citations
3. 3Localization of anticoagulantly active heparan sulfate proteoglycans in vascular endothelium: antithrombin binding on cultured endothelial cells and perfused rat aorta.1990 · 247 citations
4. 4Substrate properties of C1 inhibitor Ma (alanine 434—-glutamic acid). Genetic and structural evidence suggesting that the P12-region contains critical determinants of serine protease inhibitor/substrate status1991 · 146 citations
5. 5Analysis of the plasma elimination kinetics and conformational stabilities of native, proteinase-complexed and reactive site cleaved serpins: comparison of .alpha.1-proteinase inhibitor, .alpha.1-antichymotrypsin, antithrombin III, .alpha.2-antiplasmin, angiotensinogen, and ovalbumin1991 · 219 citations