Titlebook: Serine Proteases and Their Serpin Inhibitors in the Nervous System; Regulation in Develo Barry W. Festoff (Director),Daniel Hantaï Book 199

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Structure and Function of Tissue-Type Plasminogen Activatort in the structure and function relationships of this molecule. Many studies have been performed both to understand the fundamental molecular mechanisms of plasminogen activation by t-PA and to develop derivatives of the molecule with improved . thrombolytic properties. It was found that t-PA can be

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The Heparin Binding Site and Activation of Protease Nexin Ited by cultured human foreskin fibroblasts and some other non-vascular cells.. In the presence of optimal concentrations of the glycosaminoglycan — heparin, the association constant for the formation of the PNI-thrombin complex increases by a factor of 500-fold;. giving a rate constant for the react

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calamity

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Use of Protein Chemistry and Molecular Biology to Determine Interaction Areas Between Proteases and ino acids (preferably arginine) Thrombin, however, exhibits a narrower specificity than trypsin with respect to the peptide bonds that it will cleave. This narrower specificity of thrombin is partly due to the presence on thrombin of secondary binding sites and this article will concentrate on the c

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Rodent Serpins : Accelerated Evolution and Novel Specificitiesmed to be appropriate model systems in the study of human biology and diseases. In many cases, direct comparisons are valid and valuable. However, recently several disappointing results have been reported using the mouse as a model for studying human diseases. The deletion by homologous recombinatio

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