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Lectins: Analytical Technologies covers both analytical and biological aspects of lectins (functional carbohydrate (complex sugar) recognition proteins) and provides researchers in the field with a resource containing background information and 'look-up' tables detailing lectin specificity and structures. Also included are methods and practical tips for designing new lectins from existing non-lectin proteins, automated approaches to lectin proteomics and high resolution mass spectrometry techniques. This book will be of interest to both novice and advanced researchers in biom

Lectins. --- Immunoglobulins. --- Antibodies --- Immune globulins --- Immune serum globulin --- Blood proteins --- Globulins --- Plasma cells --- Antibody diversity --- Antigens --- Bacterial immunoglobulin-binding proteins --- Protectins --- Receptor-specific proteins --- Hemagglutinin --- Immunoglobulins

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This is the second edition of our little red book Lectins published in 1989. In the intervening years well over 10,000 articles have appeared with lectins as the main subject, and more than twice as many in which they were touched upon, as well as around 20 books. In particular, great strides have been made in several areas of lectin research, about which little was known until the late 1980s. One prominent example is animal lectins, many of which have been discovered only during the last decade and the functions of several of which have been clarified, especially as to their key role in innate immunity. Another is the structure of lectins and of their combining sites. Thus, whereas at that time the three-dimensional structures of just three lectins and a few of their complexes with sugars had been elucidated, their numbers have increased to about 160 and over 200, respectively, and continue to grow unabated. Updating the information on these and other topics resulted in a marked expansion of the book, which is now nearly four times as long as the first edition, with 226 figures and 39 tables. Still, a few topics, such as carbohydrate-binding cytokines or bacterial toxins that are sometimes considered as lectins, have been dealt with only in passing. Similarly to the first edition, Lectins II starts with an overview of the history of lectin research.

Lectins. --- Biochemistry, general. --- Lectins --- Protectins --- Receptor-specific proteins --- Life sciences. --- Medical microbiology. --- Biochemistry. --- Life Sciences. --- Medical Microbiology. --- Hemagglutinin --- Immunoglobulins --- Microbiology. --- Microbial biology --- Biology --- Microorganisms --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Chemistry --- Medical sciences --- Composition

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The influenza virus poses a threat to human health and is responsible for global epidemics every year. In addition to seasonal infections, influenza can cause occasional pandemics of great consequence when novel viruses are introduced into humans. Despite the implementation of comprehensive vaccination programs, influenza viruses continue to pose an important and unpredictable global public health threat. They are one of the most significant causes of morbidity and mortality each year and have a significant economic impact. In recent years, research has been conducted to find alternative approaches to influenza vaccine development, including the generation of universal vaccines. Notably, significant progress in the field of influenza infection, transmission, and immunity have contributed to our understanding of influenza biology, and to expanding the technological approaches for the generation of more efficient strategies against influenza infections. Moreover, highly remarkable developments have been made in the implementation of new methodologies to evaluate the efficiency of vaccines and improve them for use on domestic animals such as poultry, horses, dogs or pigs. This enables us to decrease the exposure of humans to potentially pandemic viruses. The articles in this Special Issue will address the importance of influenza to human health and the advances in influenza research that have led to the development of better therapeutics and vaccination strategies.

heterosubtypic immunity of influenza --- master donor virus --- imprinting --- hemagglutinin --- universal vaccines --- pandemic --- adaptive immunity --- pregnant women --- innate immunity --- antibodies --- Influenza vaccine --- ARDS --- influenza A virus --- humoral response --- influenza vaccine --- original antigenic sin “OAS” --- germinal centers --- immunogenicity --- lung --- epitopes --- Influenza virus --- single nucleotide polymorphisms (SNPs) --- influenza virus --- protein microarray assay --- “universal” influenza vaccine --- vaccination --- influenza --- multiple dimensional assay (MDA) --- infection --- tissue resident --- memory --- vaccines --- CD4 T cell --- broad neutralizing antibody(bnAb) --- hemagglutinin (HA) of influenza virus --- original antigenic sin --- immune response --- morbidity --- T cell --- mPLEX-Flu assay --- Influenza A virus (IAV) --- virus–host interaction --- hemagglutin stalk --- memory B cells --- vaccine safety --- protection efficacy --- live attenuated influenza vaccine --- pediatrics --- vaccination rate

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Animal Lectins: Form, Function and Clinical Applications presents up-to-date knowledge of animal lectins. Detailed descriptions on biological activities, tissue and/or subcellular distribution, molecular structure, gene organization, possible functions, clinical applications, lectin-ligand interactions and their intervention for therapeutic purposes are provided. The recently discovered C-type lectins as well as further novel super-families of this group of molecules are described in detail. Furthermore, the clinical significance of animal lectins in inflammatory diseases, defects of immune defense and autoimmunity are described and their application as drugs and therapeutic targets is discussed. With the increasing interest in lectins in biomedical research and their therapeutic applications, this book on animal lectins and associated proteins is a must have for researchers in the area.

Cardiovascular system -- Diseases -- Treatment. --- High density lipoproteins -- Metabolism. --- Lectins. --- Lectins --- Chemistry --- Human Anatomy & Physiology --- Physical Sciences & Mathematics --- Health & Biological Sciences --- Biochemistry --- Animal Biochemistry --- Biochemistry. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Protectins --- Receptor-specific proteins --- Composition --- Life sciences. --- Immunology. --- Proteins. --- Life Sciences. --- Protein-Ligand Interactions. --- Protein Science. --- Biochemistry, general. --- Biology --- Medical sciences --- Hemagglutinin --- Immunoglobulins --- RNA-ligand interactions. --- Immunobiology --- Life sciences --- Serology --- Proteins . --- Proteids --- Biomolecules --- Polypeptides --- Proteomics

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Zinc-dependent matrix metalloproteinases (MMPs) belong to metzincins that comprise not only 23 human MMPs but also other metalloproteinases, such as 21 human ADAMs (a disintegrin and metalloproteinase domain) and 19 secreted ADAMTSs (a disintegrin and metalloproteinase thrombospondin domain). The many setbacks from the clinical trials of broad-spectrum MMP inhibitors for cancer indications in the late 1990s emphasized the extreme complexity of the participation of these proteolytic enzymes in biology. This editorial mini-review summarizes the Special Issue, which includes four review articles and 10 original articles that highlight the versatile roles of MMPs, ADAMs, and ADAMTSs, in normal physiology as well as in neoplastic and destructive processes in tissue. In addition, we briefly discuss the unambiguous involvement of MMPs in wound healing.

hemagglutinin-B --- transwell co-cultures --- matrix metalloproteinases --- TNF-α --- matrix metalloproteinase --- peritoneal mesothelial cell --- gastric cancer --- metastatic dissemination --- MT4-MMP --- cancer --- diseases --- aggrecan --- aggrecanase --- ADAMTS --- cartilage --- arthritis --- MMP-2 --- MMP-9 --- inhibitor --- allodynia --- caspase-3 --- neuropathic --- pain --- dorsal root ganglion --- spinal nerve ligation --- tuberculosis --- tuberculous meningitis --- HIV-TB-associated IRIS --- extracellular matrix breakdown --- adult --- pediatric --- lung --- central nervous system --- matrix-metalloproteinase --- monocytes --- inflammation --- phagocytosis --- apoptosis --- blood sampling --- anticoagulants --- high-molecular-weight heparin --- IL-16 --- sICAM-1 --- IL-8 --- T cells --- a disintegrin and metalloproteinase --- EMMPRIN --- CD147 --- ectodomain shedding --- MMPs --- PTMs --- glycosylation --- phosphorylation --- glycosaminoglycans --- interleukin --- IL-6 --- IL-11 --- trans-signaling --- metalloproteases --- ADAM --- MMP --- meprin --- matrix metalloproteinases (MMPs) --- protease --- signaling --- invasion --- chemokine --- cytokine --- proteomics --- interferon --- Agkistrodon venom --- metalloproteinase --- fibrinogen --- antithrombotic --- metabolomics --- extracellular matrix --- cytokines --- proteinases --- interstitial collagens --- wound healing