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The thrombin E192Q–BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin
TLDR
The crystal structure of human thrombin mutant E192Q has been solved in complex with BPTI at 2.3 Å resolution and it is shown that the 60‐insertion loop is a rigid moiety that partially occludes the active site, and Thrombin can undergo major structural reorganization upon strong ligand binding. Expand
Crystallographic Evidence That the F2 Kringle Catalytic Domain Linker of Prothrombin Does Not Cover the Fibrinogen Recognition Exosite (*)
TLDR
The 2.6-Å x-ray crystal structure of bovine α-thrombin in complex with rhodniin, a protein inhibitor isolated from the bug Rhodnius prolixus, has been solved and refined and the N-terminal part of the 49-residue A-chain is traced for the first time. Expand
CU-2010—A Novel Small Molecule Protease Inhibitor with Antifibrinolytic and Anticoagulant Properties
TLDR
These findings suggest that CU-2010 has similar antifibrinolytic potency compared to aprotinin, is more potent than tranexamic acid, and possesses some anticoagulant effects. Expand
Structure-based Design of a Potent Chimeric Thrombin Inhibitor*
TLDR
These results confirm the significance of the restricted active site cleft of thrombin in determining its high cleavage specificity and demonstrate that sufficient binding energy at the fibrinogen recognition exosite can forceThrombin to accept otherwise unfavorable residues in the active site Cleft. Expand
Use of IHC and newly designed matriptase inhibitors to elucidate the role of matriptase in pancreatic ductal adenocarcinoma.
TLDR
It is demonstrated for the first time that matriptase may be involved in the progression of pancreatic ductal adenocarcinoma and thatMatriptase inhibition may contribute to preventing the progressionof this devastating disease. Expand
Time‐domain in vivo near infrared fluorescence imaging for evaluation of matriptase as a potential target for the development of novel, inhibitor‐based tumor therapies
TLDR
It is clearly demonstrated that matriptase is proteolytically active in vitro as well as in vivo in tumor‐bearing mice, and that application of synthetic active‐site inhibitors having high affinity and selectivity toward matriptases can efficiently inhibit its proteolytic activity for at least 24 hr. Expand
Effects of novel synthetic serine protease inhibitors on postoperative blood loss, coagulation parameters, and vascular relaxation after cardiac surgery.
TLDR
Cou-2010 and CU-2020 significantly reduced blood loss after cardiac surgery, with prolonged partial thromboplastin and activated clotting times, demonstrating improved antithrombotic profile. Expand
Analysis of highly potent amidine containing inhibitors of serine proteases and their N-hydroxylated prodrugs (amidoximes)
TLDR
Two HPLC-based separation methods of serine protease inhibitors and their N-hydroxylated prodrugs have been developed and characterised and are suitable for the separation of most amidoxime-prodrugs currently in clinical or preclinical development. Expand
The novel synthetic serine protease inhibitor CU-2010 dose-dependently reduces postoperative blood loss and improves postischemic recovery after cardiac surgery in a canine model.
TLDR
The novel serine protease inhibitor CU-2010 significantly reduced blood loss after cardiac surgery comparable with aprotinin and led to a significantly improved postischemic recovery of myocardial and endothelial function. Expand
Metabolism and distribution of two highly potent and selective peptidomimetic inhibitors of matriptase
TLDR
This work clarifies both the metabolism and distribution of two new matriptase inhibitors and demonstrates important metabolic differences between human enzymes and those from commonly used laboratory animals. Expand
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