Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. This volume in the Methods in Enzymology series comprehensively covers this topic. With an international board of authors, this volume covers subjects such as Crystallography of serpins and serpin complexes, Serpins as hormone transporters, and Production of serpins using cell free systems. This volume in the Methods in Enzymology series comprehensively covers the topic of serpins With an international board of authors, this volume covers subjects such as Crystallography of serpins and serpin complexes, Serpins as hormone transporters, and Production of serpins using cell free systems

Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases. This volume of Methods in Ezymology is split into 2 parts and comprehensively covers the subject.

Proceedings of an International Symposium held in Chapel Hill, North Carolina, April 13-16, 1996

Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. This volume in the Methods in Enzymology series comprehensively covers this topic. With an international board of authors, this volume covers subjects such as Crystallography of serpins and serpin complexes, Serpins as hormone transporters, and Production of serpins using cell free systems. This volume in the Methods in Enzymology series comprehensively covers the topic of serpins With an international board of authors, this volume covers subjects such as Crystallography of serpins and serpin complexes, Serpins as hormone transporters, and Production of serpins using cell free systems

Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases. This volume of Methods in Ezymology is split into 2 parts and comprehensively covers the subject.

Serpins constitute a superfamily of proteins that possess a unique tertiary structure and mechanism of proteinase inhibition. In humans, serpins constitute 10% of the plasma proteins and are best known as critical regulators of both the thrombotic and fibrinolytic systems. Serpins also participate in the regulation of the complement cascade, angiogenesis, tumor metastasis, apoptosis and innate immunity. Considering the importance of these molecules in regulating proteolytic cascades, it is not surprising to find that loss- and gain-of-function mutations result in significant human diseases. Massive thrombosis or bleeding, hereditary angioedema, Alzheimer''s disease, diabetic angiopathy and tumor invasion are some of the human diseases associated with serpins. In addition, mutations that alter serpin conformations (the serpinopathies) lead to lung disease, cirrhosis and a form of familial dementia. The goal of this text is to present the current knowledge on the molecular and cellular basis of serpins and their diseases.

Proteases occur naturally in all organisms. They are enzymes that are involved in many physiological reactions such as digestion of food and blood clotting. This volume reviews their role in health and disease and presents the latest research and developments. Discusses new discoveries, approaches, and ideas Contributions from leading scholars and industry experts Reference guide for researchers involved in molecular biology and related fields