Proteolytically cleaved mutant antithrombin-Hamilton has high stability to denaturation characteristic of wild type inhibitor serpins
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(94)00568-0/fullpdf
Reference39 articles.
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2. HUMAN PLASMA PROTEINASE INHIBITORS
3. α1-Antitrypsin and the serpins: variation and countervariation
4. R.W. Carrell D.R. Boswell A.J. Barrett G. Salvesen Proteinase Inhibitors 1986 Elsevier Biomedical Press Amsterdam 405 419
5. Ligand binding: proteinase-protein inhibitor interactions
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1. Serpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization;Journal of Amino Acids;2011-05-24
2. A protein family under 'stress' - serpin stability, folding and misfolding;Frontiers in Bioscience;2005
3. The Functional Integrity of the Serpin Domain of C1-inhibitor Depends on the Unique N-terminal Domain, as Revealed by a Pathological Mutant;Journal of Biological Chemistry;2003-08
4. Distribution of serpins in the tissues of the tobacco hornworm (Manduca sexta) larvae;Journal of Insect Physiology;2001-07
5. Engineering an Anion-Binding Cavity in Antichymotrypsin Modulates the “Spring-Loaded” Serpin−Protease Interaction;Biochemistry;1998-02-18
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