Interactions of Plasminogen Activator Inhibitor-1 with Vitronectin Involve an Extensive Binding Surface and Induce Mutual Conformational Rearrangements-Reference-Cited by-同舟云学术

Interactions of Plasminogen Activator Inhibitor-1 with Vitronectin Involve an Extensive Binding Surface and Induce Mutual Conformational Rearrangements

Published:2009-02-04 Issue:8 Volume:48 Page:1723-1735
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Blouse Grant E.¹,Dupont Daniel M.¹,Schar Christine R.¹,Jensen Jan K.¹,Minor Kenneth H.¹,Anagli John Y.¹,Gårdsvoll Henrik¹,Ploug Michael¹,Peterson Cynthia B.¹,Andreasen Peter A.¹

Affiliation:

1. Laboratory of Cellular Protein Science, Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Århus C, Denmark, Department of Biochemistry, Cellular, and Molecular Biology and Center of Excellence in Structural Biology, University of Tennessee, Knoxville, Tennessee 37996, Finsen Laboratory 3735, Rigshospitalet, Copenhagen Biocenter, Ole Maaløes Vej 5, DK-2200 Copenhagen N, Denmark, Department of Pathology, Henry Ford Health System, Detroit, Michigan 48202, and Department of...

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi8017015

Reference76 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. Plasminogen activator inhibitor-1 and tumour growth, invasion, and metastasis

3. Plasminogen Activator Inhibitor 1 (PAI-1) in Plasma: Its Role in Thrombotic Disease

4. Serpin Structure, Mechanism, and Function

5. Phylogeny of the Serpin Superfamily: Implications of Patterns of Amino Acid Conservation for Structure and Function

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