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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.
This volume explores the latest methods used to study and define serpin molecular structure, basic protease inhibition, serpin targets, and the roles of serpin in biology and disease using animal models. The chapters in this book cover topics such as crystallography and phage display, peptide design, phospholipid binding, and thrombus formation to microbiome analysis and development. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Cutting edge and authoritative, Serpins: Methods and Protocols is a valuable resource for researchers and scientists interested in learning more about this evolving field.
The book provides an comprehensive overview on biology, genetics and cellular functions of serpins (serine protease inhibitors) in health and disease. With over 1000 members serpins are the most diverse family of protease inhibitors. Latest groundbreaking research findings are presented and broaden the understanding on inhibitory and non-inhibitory serpins, not only in mammalian organisms but also in insects, worms, plants and viruses.
The chemistry, biochemistry and pharmacology of heparin and heparan sulfate have been and continue to be a major scientific undertaking - heparin and its derivative remain important drugs in clinical practice. Chemistry and Biology of Heparin and Heparan Sulfate provides readers with an insight into the chemistry, biology and clinical applications of heparin and heparan sulfate and examines their function in various physiological and pathological conditions. Providing a wealth of useful information, no other tome covers the diversity of topics in the field. Students, doctors, chemists, biochemists, and research scientists will find this book an invaluable source for updating their current knowledge of developments in this area. Comprehensively reviews all aspects of heparin and heparan sulfate research Uniquely describes the chemistry, biology and clinical application of heparins and heparan sulfates in one work Provides an invaluable source of knowledge of current developments for chemists, biochemists, medical doctors, researchers, students and practitioners
A NATO Advanced Research Workshop was held on the topic of the possible roles and regulation of serine proteases and their high molecular weight inhibitors, the serpins, in the nervous system. Some of the topics covered in this workshop include: Biochemistry and cell biology; Thrombin structural regions in determining bioregulatory functions; Main components of the fibrinolytic system (i.e. plasmin); Inhibitors of the fibrinolytic system; Regulation and control of physiological fibrinolysis; A key molecule dictating and regulating surface plasmin formation; Regulation of tissue plasminogen activator secretion from human endothelial cells, Thrombin disintegrates cell surface urokinase focal adhesion plaques and decreases cell extension; The heparin binding site and activation of protease nexin 1; Peptide hydrolases; Fibroblasts accelerate the inactivation of thrombin by PNI; Fibroblasts block the ability of PNI to inactivate urokinase and plasmin; Use of protein chemistry and molecular biology to determine interaction areas between proteases and their inhibitors; Signal transduction chains involved in the control of the fibrinolytic enzyme cascade; Structure of the human protease nexin gene and expression of recombinant forms of PNI; Serine proteases in the nervous system; and Serpins in degenerative and malignant neurologic diseases.
This book is an accessible resource offering practical information not found in more database-oriented resources. The first chapter lists acronyms with definitions, and a glossary of terms and subjects used in biochemistry, molecular biology, biotechnology, proteomics, genomics, and systems biology. There follows chapters on chemicals employed in biochemistry and molecular biology, complete with properties and structure drawings. Researchers will find this book to be a valuable tool that will save them time, as well as provide essential links to the roots of their science. Key selling features: Contains an extensive list of commonly used acronyms with definitions Offers a highly readable glossary for systems and techniques Provides comprehensive information for the validation of biotechnology assays and manufacturing processes Includes a list of Log P values, water solubility, and molecular weight for selected chemicals Gives a detailed listing of protease inhibitors and cocktails, as well as a list of buffers
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.