Chapter 22. Fc receptor structure and the design of anti-inflammatories: New therapeutics for autoimmune disease

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• Publication year

  2002

• Venue

  Annual Reports in Medicinal Chemistry

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/S0065-7743(02)37023-4
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

• Fc receptor biology.

  2003cited by this paper
• The Structure of a Human Type III Fcγ Receptor in Complex with Fc*

  2001cited by this paper
• IgG Fc receptors.

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• The structure of the IgE Cɛ2 domain and its role in stabilizing the complex with its high-affinity receptor FcɛRIα

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• The Interaction of FcαRI with IgA and Its Implications for Ligand Binding by Immunoreceptors of the Leukocyte Receptor Cluster1

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• The IgG Fc Contains Distinct Fc Receptor (FcR) Binding Sites: The Leukocyte Receptors FcγRI and FcγRIIa Bind to a Region in the Fc Distinct from That Recognized by Neonatal FcR and Protein A1

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• Structure of the Fc fragment of human IgE bound to its high-affinity receptor FcεRIα

  2000cited by this paper
• The 3.2-Å crystal structure of the human IgG1 Fc fragment–FcγRIII complex

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• Inhibition of IgE-receptor interactions.

  2000cited by this paper
• Conformation of the isolated cepsilon3 domain of IgE and its complex with the high-affinity receptor, FcepsilonRI.

  2000cited by this paper
• Crystal structure of the extracellular domain of a human Fc gamma RIII.

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• Convergence of Fcγ Receptor IIA and Fcγ Receptor IIIB Signaling Pathways in Human Neutrophils1

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• Crystal structure of the soluble form of the human Fcγ‐receptor IIb: a new member of the immunoglobulin superfamily at 1.7 Å resolution

  1999cited by this paper
• Biochemical analysis and crystallisation of FcγRIIa, the low affinity receptor for IgG

  1999cited by this paper
• Characterization and crystallization of soluble human Fc gamma receptor II (CD32) isoforms produced in insect cells.

  1999cited by this paper
• The role of the human Fc receptor Fc gamma RIIA in the immune clearance of platelets: a transgenic mouse model.

  1999cited by this paper
• Fine Structure Analysis of Interaction of FcεRI with IgE*

  1999cited by this paper
• Crystal structure of the human leukocyte Fc receptor, FcγRIIa.

  1999cited by this paper
• The second and third extracellular domains of FcgammaRI (CD64) confer the unique high affinity binding of IgG2a.

  1998cited by this paper
• Crystal structure of the human high-affinity IgE receptor.

  1998cited by this paper
• Human IgG Fc receptors.

  1997cited by this paper
• Multiple Regions of Human FcγRII (CD32) Contribute to the Binding of IgG (*)

  1995cited by this paper
• Molecular basis of Fc receptor function.

  1994cited by this paper
• Identification of the IgG binding site of the human low affinity receptor for IgG Fc gamma RII. Enhancement and ablation of binding by site-directed mutagenesis.

  1994cited by this paper
• Chimeric Fc receptors identify immunoglobulin‐binding regions in human FcγRII and FcϵRI

  1993cited by this paper
• Recombinant soluble human Fc gamma RII: production, characterization, and inhibition of the Arthus reaction

  1993cited by this paper
• Transmembrane signaling: the joy of aggregation.

  1992cited by this paper
• Chimeric Fc receptors identify functional domains of the murine high affinity receptor for IgG.

  1991cited by this paper
• Structure of the mouse beta Fc gamma receptor II gene.

  1991cited by this paper
• Molecular cloning and expression of the mouse high affinity Fc receptor for IgG.

  1990cited by this paper

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  2009cites this paper
• Epitope Mapping of Fc gamma RIIa Monoclonal Antibodies

  2008cites this paper
• FcγRII and multi-system autoimmune disease

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• Past, present and future drug treatment for rheumatoid arthritis and systemic lupus erythematosus

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• The role of FcγRIIa as an inflammatory mediator in rheumatoid arthritis and systemic lupus erythematosus

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• Fc receptors are major mediators of antibody based inflammation in autoimmunity.

  2002cites this paper