Antibody Fc

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  • Author : Peter Sun
  • Publisher : Elsevier Inc. Chapters
  • Pages : 358 pages
  • ISBN : 012806028X
  • Rating : /5 from reviews
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Download or Read online Antibody Fc full in PDF, ePub and kindle. this book written by Peter Sun and published by Elsevier Inc. Chapters which was released on 06 August 2013 with total page 358 pages. We cannot guarantee that Antibody Fc book is available in the library, click Get Book button and read full online book in your kindle, tablet, IPAD, PC or mobile whenever and wherever You Like. Molecular mechanisms of antibody-mediated Fc receptor activation have long been an interest in both Fc receptor biology and antibody therapeutics. The structural efforts to elucidate antibody recognition by Fc receptors have led to the generation of several crystal structures of antibody Fc fragments complexed with Fc receptors. Collectively, these structures revealed a conserved receptor binding mode for IgG and IgE, distinct from those for the neonatal Fc receptor (FcRn), protein A, and protein G. Fcγ receptor recognition in the lower hinge region allows enhanced antigen recognition through dimeric Fabs but obligates immune-complex formation for receptor activation. It also provides the basis for Fcγ receptors to differentiate among IgG subclasses. More recently, pentraxins have also been shown to bind and activate Fc receptors, and structural efforts to elucidate pentraxin Fcγ receptor recognition have revealed surprising similarities between pentraxins and immunoglobulins in Fc receptor recognition. This review summarizes the structural findings that formed the basis of modern antibody–Fc receptor biology and recent advances of shared Fc receptor recognition by innate pentraxins.

Antibody Fc

Antibody Fc
  • Author : Peter Sun
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
GET THIS BOOK Antibody Fc

Molecular mechanisms of antibody-mediated Fc receptor activation have long been an interest in both Fc receptor biology and antibody therapeutics. The structural efforts to elucidate antibody recognition by Fc receptors have led to the generation of several crystal structures of antibody Fc fragments complexed with Fc receptors. Collectively, these structures revealed a conserved receptor binding mode for IgG and IgE, distinct from those for the neonatal Fc receptor (FcRn), protein A, and protein G. Fcγ receptor recognition in the lower

Antibody Fc

Antibody Fc
  • Author : Xiaojie Yu,Kavitha Baruah,Christopher N. Scanlan,Max Crispin
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
GET THIS BOOK Antibody Fc

The antibody Fc region is posttranslationally modified by N-linked glycosylation. In immunoglobulin G (IgG), the processing of the glycans is restricted by the presence of extensive interaction with the protein surface. The resulting set of antibody glycoforms exhibit a range of effector functions. In this chapter, we outline the impact of glycosylation on the immune function of antibodies and discuss the implications for monoclonal antibody and intravenous immunoglobulin therapies.

Antibody Fc

Antibody Fc
  • Author : Victor Raúl Gómez Román,Joseph C. Murray,Louis M. Weiner
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
GET THIS BOOK Antibody Fc

Antibody-dependent cellular cytotoxicity (ADCC), also called antibody-dependent cell-mediated cytotoxicity, is an immune mechanism through which Fc receptor-bearing effector cells can recognize and kill antibody-coated target cells expressing tumor- or pathogen-derived antigens on their surface. Numerous associations between ADCC activity, Fc receptor polymorphisms, and clinical outcomes have been observed in both the settings of vaccination and monoclonal antibody therapy. Here, the effector cells and receptors involved in ADCC are introduced, followed by a description of the four main stages and mechanisms

Antibody Fc

Antibody Fc
  • Author : Theo Rispens,Gestur Vidarsson
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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Immunoglobulins are a group of closely related glycoproteins composed of 82 to 96% protein and 4 to 18% carbohydrate. In humans, there are five classes of immunoglobulins, which differ in heavy-chain structure. Immunoglobulin G (IgG) is the major class of immunoglobulins in blood and can be further subdivided in subclasses. The four subclasses of IgG were discovered in the 1960s following extensive studies using specific rabbit antisera against human IgG myeloma proteins.1 They are designated IgG1, IgG2, IgG3, and IgG4, in order of decreasing

Antibody Fc

Antibody Fc
  • Author : Marije B. Overdijk,Sandra Verploegen,Wim K. Bleeker,Paul W.H.I. Parren
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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Historically, lack of specificity for cancer cells has been a major problem in cancer treatment; however, the development of monoclonal antibodies (mAbs), which combine high specificity with multiple mechanisms of action (MoAs), started a revolution in anti-cancer treatment options which continues to date. As of January 2013, 15 major antibody products were being marketed for cancer treatment in various countries around the globe, 10 of which are unmodified mAbs, which generally have multiple potential MoAs and may act via direct, Fab-domain-related effects or

Antibody Fc

Antibody Fc
  • Author : Roy Jefferis
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
GET THIS BOOK Antibody Fc

Diversity of antigen-binding specificity may be considered the hallmark of antibodies; however, the human IgG-Fc region also exhibits binding specificity for multiple ligands. Evolution of the IgG-Fc has resulted in the generation of interaction sites for endogenous (self) ligands that recruit and activate mechanisms facilitating the removal and destruction of antibody–pathogen immune complexes. However, pathogens (bacteria and virus) have co-evolved to elaborate IgG-Fc binding proteins that seek to subvert these protective mechanisms. The four human IgG subclasses exhibit differential

Antibody Fc

Antibody Fc
  • Author : Robert M. Anthony
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
GET THIS BOOK Antibody Fc

IgG antibodies are highly potent molecules, with the unique ability to link foreign particles to innate immune cells. IgG antibodies recognize antigens with high affinity and bind cellular Fc receptors with low affinity individually. These interactions occur in the form of immune complexes, resulting in high-avidity interactions. In fact, the effector functions triggered by IgG antibodies are highly dependent on the type of Fc receptor that is bound; however, many aspects can influence Fc receptor binding by IgG antibodies, including

Antibody Fc

Antibody Fc
  • Author : Margaret Ackerman,Falk Nimmerjahn
  • Publisher : Academic Press
  • Release : 06 August 2013
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Antibody Fc is the first single text to synthesize the literature on the mechanisms underlying the dramatic variability of antibodies to influence the immune response. The book demonstrates the importance of the Fc domain, including protective mechanisms, effector cell types, genetic data, and variability in Fc domain function. This volume is a critical single-source reference for researchers in vaccine discovery, immunologists, microbiologists, oncologists and protein engineers as well as graduate students in immunology and vaccinology. Antibodies represent the correlate of

Antibody Fc

Antibody Fc
  • Author : Joseph U. Igietseme,Xiaoping Zhu,Carolyn M. Black
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
GET THIS BOOK Antibody Fc

Fc receptor (FcR)-dependent effector functions of antibodies contribute significantly to protective immunity against microbial pathogens and tumors. Therefore, FcR-mediated immunological processes constitute a key component of the immune system’s defense armamentaria for maintaining the biological and physiological integrity of the mammalian host who is yoked with frequent encounters with infections and neoplasia. The direct effector functions that result from FcR triggering are phagocytosis, antibody-dependent cellular cytotoxicity, and induction of inflammation; also, FcR-mediated processes provide immunoregulation and immunomodulation that

Antibody Fc

Antibody Fc
  • Author : Falk Nimmerjahn
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
GET THIS BOOK Antibody Fc

Autoimmune disorders are characterized by the destruction of self-tissues by the immune system. Multiple checkpoints are in place to prevent autoreactivity under normal circumstances. Co-expression of activating and inhibitory Fc receptors (FcRs) represents such a checkpoint by establishing a threshold for immune cell activation. In many human autoimmune diseases, however, balanced FcR expression is disturbed. Analysis of murine model systems provides strong evidence that aberrant FcR expression can result in uncontrolled immune responses and the initiation of autoimmune disease. This

Engineering Antibody Fc Domains for Improved Therapeutic Function

Engineering Antibody Fc Domains for Improved Therapeutic Function
  • Author : William James Kelton
  • Publisher : Unknown
  • Release : 18 October 2021
GET THIS BOOK Engineering Antibody Fc Domains for Improved Therapeutic Function

Therapeutic antibodies have achieved exceptional clinical success in the treatment of cancer and other human diseases. Now, new approaches are required to enhance the potency of antibodies to further increase the number of patients responding to therapy. By engineering the antibody Fc domain through mutation of the amino acid sequence, binding affinity to activating or inhibitory Fc receptors on effector cells can be increased to modulate the cellular immune response. However, attaining selectivity for closely related Fc receptors has proved

Antibody Fc

Antibody Fc
  • Author : George J. Weiner
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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Monoclonal antibodies (mAbs), including rituximab, are now a mainstay in the therapy of cancer. Despite their undeniable therapeutic value, there is much we do not fully understand about the mechanisms of action responsible for their anti-tumor effects. These mechanisms are often studied in isolation. In this chapter, we will review the mechanisms of action of anti-cancer mAbs and discuss how they interact. The focus of this discussion will be on rituximab, but similar conclusions can be reached with other mAbs.

Antibody Fc

Antibody Fc
  • Author : Scott B. Halstead
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
GET THIS BOOK Antibody Fc

While the benefits of antibody responses are widely known, pathogens are also able to exploit antibodies to facilitate cell entry and potentially alter the cellular response via interactions with Fc receptors. This phenomenon, known as antibody-dependent enhancement (ADE) of disease, is a factor in numerous human and veterinary diseases. It is thought to result from innate cellular responses to Fcγ receptor-facilitated entry of infectious microbial immune complexes, and paradoxically results in increased production of pathogenic organisms. ADE has been described