The Mechanism of α1-Antitrypsin Polymerization Probed by Fluorescence Spectroscopy
- 1 August 1998
- journal article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 356 (2) , 296-300
- https://doi.org/10.1006/abbi.1998.0751
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site 1 1Edited by R. HuberJournal of Molecular Biology, 1997
- Inhibitory mechanism of serpins. Identification of steps involving the active-site serine residue of the proteaseJournal of Molecular Biology, 1997
- Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpinsProtein Science, 1997
- α1-Antitrypsin DeficiencyChest, 1996
- ReviewBiological Chemistry Hoppe-Seyler, 1996
- α1-Antitrypsin Mmalton (Phe52-deleted) Forms Loop-Sheet Polymers in Vivo.Published by Elsevier ,1995
- What do dysfunctional serpins tell us about molecular mobility and disease?Nature Structural & Molecular Biology, 1995
- Biological implications of a 3 å structure of dimeric antithrombinStructure, 1994
- Structural basis of latency in plasminogen activator inhibitor-1Nature, 1992
- Crystal structure of ovalbumin as a model for the reactive centre of serpinsNature, 1990