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The Journal of Biological Chemistry|July 21, 2012
Meizothrombin is an unexpectedly zymogen-like variant of thrombinHarlan N Bradford, Sriram Krishnaswamy
The Journal of Biological Chemistry|March 26, 2016
The Fragment 1 Region of Prothrombin Facilitates the Favored Binding of Fragment 12 to Zymogen and Enforces Zymogen-like Character in the ProteinaseHarlan N Bradford, Sriram Krishnaswamy
The Journal of Biological Chemistry|December 23, 2018
Occlusion of anion-binding exosite 2 in meizothrombin explains its impaired ability to activate factor VHarlan N Bradford, Sriram Krishnaswamy
The Journal of Biological Chemistry|August 14, 2013
Membrane binding by prothrombin mediates its constrained presentation to prothrombinase for cleavageHarlan N Bradford, Steven J Orcutt, Sriram Krishnaswamy
The Journal of Biological Chemistry|October 28, 2009
Regulated cleavage of prothrombin by prothrombinase: repositioning a cleavage site reveals the unique kinetic behavior of the action of prothrombinase on its compound substrateHarlan N Bradford, Joseph A Micucci, Sriram Krishnaswamy
Thrombosis and Haemostasis|November 5, 2005
Domain 5 of cleaved high molecular weight kininogen inhibits endothelial cell migration through AktVaibhav Katkade, Abigail A Soyombo, Irma Isordia-Salas, et al.
Arteriosclerosis, Thrombosis, and Vascular Biology|August 12, 2006
High-molecular-weight kininogen fragments stimulate the secretion of cytokines and chemokines through uPAR, Mac-1, and gC1qR in monocytesMohammad M Khan, Harlan N Bradford, Irma Isordia-Salas, et al.
American Journal of Physiology. Heart and Circulatory Physiology|February 13, 2007
Antithrombotic activity of kininogen is mediated by inhibitory effects of domain 3 during arterial injury in vivoSarmina Hassan, Irma M Sainz, Mohammad M Khan, et al.
Blood|May 27, 2004
Inhibition of tumor angiogenesis in vivo by a monoclonal antibody targeted to domain 5 of high molecular weight kininogenJames S Song, Irma M Sainz, Stephen C Cosenza, et al.
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