Distortion of the Catalytic Domain of Tissue-type Plasminogen Activator by Plasminogen Activator Inhibitor-1 Coincides with the Formation of Stable Serpin-Proteinase Complexes-Reference-Cited by-同舟云学术

Distortion of the Catalytic Domain of Tissue-type Plasminogen Activator by Plasminogen Activator Inhibitor-1 Coincides with the Formation of Stable Serpin-Proteinase Complexes

Published:2003-11 Issue:48 Volume:278 Page:48197-48203
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Perron Michel J.,Blouse Grant E.,Shore Joseph D.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference35 articles.

1. The Molecular Basis for Anti-Proteolytic and Non-Proteolytic Functions of Plasminogen Activator Inhibitor Type-1: Roles of the Reactive Centre Loop, the Shutter Region, the Flexible Joint Region and the Small Serpin Fragment

2. Divining the serpin inhibition mechanism: a suicide substrate ‘springe’?

3. Structure of a serpin–protease complex shows inhibition by deformation

4. Intrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibition

5. Insight into the Mechanism of Serpin−Proteinase Inhibition from 2D [1H-15N] NMR Studies of the 69 kDa α1-Proteinase Inhibitor Pittsburgh−Trypsin Covalent Complex

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