Conformational properties of serine proteinase inhibitors (serpins) confer multiple pathophysiological roles
- 1 March 2001
- journal article
- review article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
- Vol. 1535 (3) , 221-235
- https://doi.org/10.1016/s0925-4439(01)00025-4
Abstract
No abstract availableKeywords
This publication has 140 references indexed in Scilit:
- Novel Functions of Human α1-Protease Inhibitor after S-Nitrosylation: Inhibition of Cysteine Protease and Antibacterial ActivityBiochemical and Biophysical Research Communications, 2000
- Conformational changes in serpins: I. the native and cleaved conformations of α 1 -antitrypsin 1 1Edited by J. M. ThorntonJournal of Molecular Biology, 2000
- Oxidation of α1-Proteinase Inhibitor by the Myeloperoxidase–Hydrogen Peroxidase System Promotes Binding to Immunoglobulin ABiochemical and Biophysical Research Communications, 1999
- A point mutation in exon 7 of the C1-inhibitor gene causing type I hereditary angioedemaHuman Genetics, 1996
- Gene Structure, Chromosomal Localization, and Expression of the Murine Homologue of Human Proteinase Inhibitor 6 (PI-6) Suggests Divergence of PI-6 from the Ovalbumin SerpinsPublished by Elsevier ,1995
- Serum glycoproteins and severity of coronary atherosclerosisAmerican Heart Journal, 1995
- Tissue Destruction by NeutrophilsNew England Journal of Medicine, 1989
- Tumors: Wounds That Do Not HealNew England Journal of Medicine, 1986
- Isolation and properties of oxidized alpha-1-proteinase inhibitor from human rheumatoid synovial fluidBiochemical and Biophysical Research Communications, 1980
- A surprising new protein superfamily containing ovalbumin, antithrombin-III, and alpha1-proteinase inhibitorBiochemical and Biophysical Research Communications, 1980