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State-of-the-Art Research on C1q and the Classical Complement Pathway
C1q is the target recognition protein of the classical complement pathway and a major connecting link between innate and acquired immunity. As a charge pattern recognition molecule of innate immunity, C1q can engage a broad range of ligands derived from self, non-self and altered self via its heterotrimeric globular (gC1q) domain and thus trigger the classical complement pathway. The trimeric gC1q signature domain has been identified in a variety of non-complement proteins that can be grouped together as a C1q family. C1q circulates in serum as part of the C1 complex, in association with a catalytic tetrameric assembly of two homologous yet distinct serine proteases, C1r and C1s. Binding of ...
Structural Biology of the Complement System
Of recent, the structure of the complement system has received considerable attention, including the publication of several three-dimensional structures of complement proteins. This has led to the need for an authoritative resource to provide a complete overview of the basics, as well as an explanation of the cutting-edge work being accomplished in this emerging science. Structural Biology of the Complement System is devoted to the full exploration of structural aspects of the complement system, with special consideration of the links between molecular structure and function. Containing the work of leading authorities across the disciplines of immunology and structural biology, the book serv...
Advances in Immunology
Advances in Immunology
The Collectin Protein Family and Its Multiple Biological Activities
The topic of this book, Collectins, is a family of proteins whose major function is in innate immunity, where Collectins act as pattern recognition receptors (PRRs). In general they recognize targets such as microbial surfaces and apoptotic cells, and once bound to a target, Collectins promote the clearance of microorganisms and damaged host tissue. New cell-surface proteins and glycoproteins, which act as Collectin receptors, are currently being identified. Some Collectins, particularly MBL, activate the complement system, which enhances the ability of antibodies to fight pathogens, via three MBL-associated proteases, the MASPs. Additionally, recent research has begun to show wider-ranging ...
The Role of Pentraxins: From Inflammation, Tissue Repair and Immunity to Biomarkers
We acknowledge the initiation and support of this Research Topic by the International Union of Immunological Societies (IUIS). We hereby state publicly that the IUIS has had no editorial input in articles included in this Research Topic, thus ensuring that all aspects of this Research Topic are evaluated objectively, unbiased by any specific policy or opinion of the IUIS.
The Complement FactsBook
The Complement FactsBook, Second Edition, provides in-depth insights and an overview of the components of the complement system. This new edition highlights the use of newly recommended complement nomenclature, covering new pathways and proteins and adding information on mouse homologs. It is a completely revised and updated edition containing entries on all components of the complement system, and is an excellent source of one-stop shopping for complement information and references. It is the most convenient compilation of biochemical, biological and molecular biology for complementologists and those new in the field. This new edition is expanded to include relevant updates and topics that ...
Handbook of Proteolytic Enzymes
Extensively revised and updated, the new edition of the highly regarded Handbook of Proteolytic Enzymes is an essential reference for biochemists, biotechnologists and molecular biologists. Edited by world-renowned experts in the field, this comprehensive work provides detailed information on all known proteolytic enzymes to date. This two-volume set unveils new developments on proteolytic enzymes which are being investigatedin pharmaceutical research for such diseases as HIV, Hepatitis C, and the common cold. Volume I covers aspartic and metallo petidases while Volume II examines peptidases of cysteine, serine, threonine and unknown catalytic type. A CD-ROM accompanies the book containing f...
