Distribution of the Native Strain in Human α1-Antitrypsin and Its Association with Protease Inhibitor Function
Open Access
- 1 June 2000
- journal article
- Published by Elsevier
- Vol. 275 (22) , 16904-16909
- https://doi.org/10.1074/jbc.m001006200
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- The native strains in the hydrophobic core and flexible reactive loop of a serine protease inhibitor: crystal structure of an uncleaved α1-antitrypsin at 2.7 åStructure, 1996
- The serpin PAI-1 inhibits cell migration by blocking integrin αvβ3 binding to vitronectinNature, 1996
- Probing the native strain in α1-antitrypsinNature Structural & Molecular Biology, 1996
- Divining the serpin inhibition mechanism: a suicide substrate ‘springe’?Trends in Biotechnology, 1995
- The Inhibition Mechanism of SerpinsPublished by Elsevier ,1995
- Serpin-Protease Complexes Are Trapped as Stable Acyl-Enzyme IntermediatesPublished by Elsevier ,1995
- Structural basis for serpin inhibitor activityProteins-Structure Function and Bioinformatics, 1995
- Amyloid-associated proteins α1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filamentsNature, 1994
- Mechanism of serpin action: evidence that C1 inhibitor functions as a suicide substrateBiochemistry, 1991
- Implications of the three-dimensional structure of .alpha.1-antitrypsin for structure and function of serpinsBiochemistry, 1989