The citrate ion increases the conformational stability of α1-antitrypsin
- 31 August 2000
- journal article
- Published by Elsevier BV in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1481 (1), 11-17
- https://doi.org/10.1016/s0167-4838(00)00118-7
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Conformational changes in serpins: I. the native and cleaved conformations of α1-antitrypsinJournal of Molecular Biology, 2000
- Inactive conformation of the serpin α1-antichymotrypsin indicates two-stage insertion of the reactive loop: Implications for inhibitory function and conformational diseaseProceedings of the National Academy of Sciences of the United States of America, 2000
- Genetics and respiratory disease bullet 2: Alpha1-antitrypsin deficiency, cirrhosis and emphysemaThorax, 1998
- An atlas of serpin conformationsTrends in Biochemical Sciences, 1998
- Wild-type α1-antitrypsin is in the canonical inhibitory conformationJournal of Molecular Biology, 1998
- Alpha-1-Antitrypsin DeficiencySeminars in Liver Disease, 1998
- The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding siteJournal of Molecular Biology, 1997
- Mutations Which Impede Loop/Sheet Polymerization Enhance the Secretion of Human α1-Antitrypsin Deficiency VariantsOnline Journal of Public Health Informatics, 1995
- Conformational changes in intact and papain‐modified α1‐proteinase inhibitor induced by guanidinium chlorideJBIC Journal of Biological Inorganic Chemistry, 1990
- HUMAN PLASMA PROTEINASE INHIBITORSAnnual Review of Biochemistry, 1983