Antibody Fc

Antibody Fc
  • Author : Margaret Ackerman
  • Publsiher : Academic Press
  • Release : 06 August 2013
  • ISBN : 0123948185
  • Pages : 358 pages
  • Rating : 4/5 from 21 ratings
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Summary:
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 protection for numerous vaccines and are the most rapidly growing class of drugs, with applications ranging from cancer and infectious disease to autoimmunity. Researchers have long understood the variable domain of antibodies, which are responsible for antigen recognition, and can provide protection by blocking the function of their target antigen. However, recent developments in our understanding of the protection mediated by antibodies have highlighted the critical nature of the antibody constant, or Fc domain, in the biological activity of antibodies. The Fc domain allows antibodies to link the adaptive and innate immune systems, providing specificity to a wide range of innate effector cells. In addition, they provide a feedback loop to regulate the character of the immune response via interactions with B cells and antigen-presenting cells. Clarifies the different mechanisms of IgG activity at the level of the different model systems used, including human genetic, mouse, and in vitro Covers the role of antibodies in cancer, infectious disease, and autoimmunity and in the setting of monoclonal antibody therapy as well as naturally raised antibodies Color illustrations enhance explanations of the immune system


Antibody Fc:

Antibody Fc:
  • Author : Margaret Ackerman,Falk Nimmerjahn
  • Publisher : Academic Press
  • Release : 06 August 2013
GET THIS BOOKAntibody Fc:

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

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Antibody Fc

Antibody Fc
  • Author : Stefan S. Weber,Annette Oxenius
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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In humans and mice there exist a multitude of Fcγ receptors (FcγRs) with different affinities and specificities for the different IgG subclasses. Engagement of FcRs on cells usually results in the initiation of an activating or inhibitory signaling cascade that can lead to multiple effector functions, including phagocytosis of opsonized pathogens or immune complexes. In this chapter, we discuss phagocytic cell types and their respective FcγRs that they utilize to phagocytize IgG-coated particles/pathogens. Furthermore, we discuss downstream

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Therapeutic Monoclonal Antibodies

Therapeutic Monoclonal Antibodies
  • Author : Zhiqiang An
  • Publisher : John Wiley & Sons
  • Release : 20 September 2011
GET THIS BOOKTherapeutic Monoclonal Antibodies

70-chapter authoritative reference that covers therapeutic monoclonal antibody discovery, development, and clinical applications while incorporating principles, experimental data, and methodologies. First book to address the discovery and development of antibody therapeutics in their entirety. Most chapters contain experimental data to illustrate the principles described in them. Authors provide detailed methodologies that readers can take away with them and use in their own laboratories.

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Approaches to the Purification, Analysis and Characterization of Antibody-Based Therapeutics

Approaches to the Purification, Analysis and Characterization of Antibody-Based Therapeutics
  • Author : Allan Matte
  • Publisher : Elsevier
  • Release : 07 September 2020
GET THIS BOOKApproaches to the Purification, Analysis and Characterization of Antibody-Based Therapeutics

Approaches to the Purification, Analysis and Characterization of Antibody-Based Therapeutics provides the interested and informed reader with an overview of current approaches, strategies and considerations relating to the purification, analytics and characterization of therapeutic antibodies and related molecules. While there are obviously other books published in and around this subject area, they seem to be either older (c.a. year 2000 publication date) or are more limited in scope. The book will include an extensive bibliography of the published literature in

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Therapeutic Antibody Engineering

Therapeutic Antibody Engineering
  • Author : William R Strohl,Lila M Strohl
  • Publisher : Elsevier
  • Release : 16 October 2012
GET THIS BOOKTherapeutic Antibody Engineering

The field of antibody engineering has become a vital and integral part of making new, improved next generation therapeutic monoclonal antibodies, of which there are currently more than 300 in clinical trials across several therapeutic areas. Therapeutic antibody engineering examines all aspects of engineering monoclonal antibodies and analyses the effect that various genetic engineering approaches will have on future candidates. Chapters in the first part of the book provide an introduction to monoclonal antibodies, their discovery and development and the fundamental

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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

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Antibody Fc

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

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Antibody Fc

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

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Antibody Fc

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

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