α1-Proteinase Inhibitor Forms Initial Non-covalent and Final Covalent Complexes with Elastase Analogously to Other Serpin-Proteinase Pairs, Suggesting a Common Mechanism of Inhibition-Reference-Cited by-同舟云学术

α1-Proteinase Inhibitor Forms Initial Non-covalent and Final Covalent Complexes with Elastase Analogously to Other Serpin-Proteinase Pairs, Suggesting a Common Mechanism of Inhibition

Published:2004-03 Issue:10 Volume:279 Page:9264-9269
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Dobó József,Gettins Peter G.W.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference30 articles.

1. Serpin Structure, Mechanism, and Function

2. Mechanism of serpin action: evidence that C1 inhibitor functions as a suicide substrate

3. Antichymotrypsin interaction with chymotrypsin. Partitioning of the complex.

4. Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition.

5. Serpin-Protease Complexes Are Trapped as Stable Acyl-Enzyme Intermediates

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