Dynamic Mechanism for the Serpin Loop Insertion as Revealed by Quantitative Kinetics
- 29 April 2005
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 348 (2) , 409-418
- https://doi.org/10.1016/j.jmb.2005.02.054
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Different Conformational Changes within the F-Helix Occur during Serpin Folding, Polymerization, and Proteinase InhibitionBiochemistry, 2004
- Serpin Polymerization Is Prevented by a Hydrogen Bond Network That Is Centered on His-334 and Stabilized by GlycerolJournal of Biological Chemistry, 2003
- Serpinopathies and the conformational dementiasNature Reviews Genetics, 2002
- Probing the serpin structural-transition mechanism in ovalbumin mutant R339T by proteolytic-cleavage kinetics of the reactive-centre loopBiochemical Journal, 2002
- Biological implications of a 3 å structure of dimeric antithrombinStructure, 1994
- Engineering Plasminogen Activator Inhibitor 1 Mutants with Increased Functional StabilityBiochemistry, 1994
- Structural basis of latency in plasminogen activator inhibitor-1Nature, 1992
- MOLSCRIPT: a program to produce both detailed and schematic plots of protein structuresJournal of Applied Crystallography, 1991
- Crystal structure of plakalbumin, a proteolytically nicked form of ovalbuminJournal of Molecular Biology, 1990
- A surprising new protein superfamily containing ovalbumin, antithrombin-III, and alpha1-proteinase inhibitorBiochemical and Biophysical Research Communications, 1980