The Light Chain Allosterically Enhances the Protease Activity of Murine Urokinase-Type Plasminogen Activator-Reference-Cited by-同舟云学术

The Light Chain Allosterically Enhances the Protease Activity of Murine Urokinase-Type Plasminogen Activator

Published:2024-05-23 Issue:11 Volume:63 Page:1434-1444
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Torres-Paris Constanza¹,Song Harriet J.¹,Engelberger Felipe²³,Ramírez-Sarmiento César A.²³,Komives Elizabeth A.¹^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry, Mail Code 0309, University of California San Diego, 9325 S Scholars Dr, La Jolla, California 92161, United States

2. Institute for Biological and Medical Engineering, Schools of Engineering, Medicine and Biological Sciences, Pontificia Universidad Católica de Chile, Santiago 7820436, Chile

3. ANID - Millennium Science Initiative Program - Millennium Institute for Integrative Biology (iBio), Santiago 8331150, Chile

Funder

National Heart, Lung, and Blood Institute

American Heart Association

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.4c00071

Reference41 articles.

1. Regulation of cell signalling by uPAR

2. Structure of Human Urokinase Plasminogen Activator in Complex with Its Receptor

3. Crystal structures of two human vitronectin, urokinase and urokinase receptor complexes

4. The kringle stabilizes urokinase binding to the urokinase receptor

5. Direct interaction of the kringle domain of urokinase-type plasminogen activator (uPA) and integrin αvβ3 induces signal transduction and enhances plasminogen activation

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