Allostery involves coupling of conformational changes between two widely separated
binding sites. The common view holds that allosteric proteins are symmetric oligomers, with …

Following initiation of coagulation as part of the hemostatic response to injury, thrombin is
generated from its inactive precursor prothrombin by factor Xa as part of the prothrombinase …

Thrombin is the key enzyme of the entire hemostatic process since it is able to exert both
procoagulant and anticoagulant functions; therefore, it represents an attractive target for the …

The endothelial cell protein C receptor (EPCR) functions as an important regulator of the
protein C anticoagulant pathway by binding protein C and enhancing activation by the …

The specificity of blood coagulation proteinases for substrate, inhibitor, and effector
recognition is mediated by exosites on the surfaces of the catalytic domains, physically …

Arterial and venous thrombosis are major causes of morbidity and mortality. Arterial
thrombosis is the most common cause of myocardial infarction, stroke, and limb gangrene …

Aptamers are synthetic nucleic acids that are developed to target with high affinity and
specificity chemical entities ranging from single ions to macromolecules and present a wide …

Animal Lectins: Form, Function and Clinical Applications presents up-to-date knowledge of
animal lectins. Detailed descriptions on biological activities, tissue and/or subcellular …

Antithrombin I (fibrin) is an important inhibitor of thrombin generation that functions by
sequestering thrombin in the forming fibrin clot, and also by reducing the catalytic activity of …

Aptamers directed against human thrombin can selectively bind to two different exosites on
the protein surface. The simultaneous use of two DNA aptamers, HD1 and HD22, directed to …