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The second and third extracellular domains of FcgammaRI (CD64) confer the unique high affinity binding of IgG2a

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The second and third extracellular domains of FcgammaRI (CD64) confer the unique high affinity binding of IgG2a (English)

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M D Hulett

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P M Hogarth

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2

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language of work or name

English

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publication date

October 1998

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published in

Molecular Immunology

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volume

35

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issue

14-15

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page(s)

989-96

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cites work

Isolation and expression of functional high-affinity Fc receptor complementary DNAs

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Phagocytosis mediated by three distinct Fc gamma receptor classes on human leukocytes

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Recombinant immune interferon increases immunoglobulin G Fc receptors on cultured human mononuclear phagocytes

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Antigen targeting to myeloid-specific human Fc gamma RI/CD64 triggers enhanced antibody responses in transgenic mice

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Molecular basis of Fc receptor function

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Multiple regions of human Fc gamma RII (CD32) contribute to the binding of IgG.

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Structure based design and characterization of peptides that inhibit IgE binding to its high-affinity receptor

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The IgG binding site of human FcgammaRIIIB receptor involves CC' and FG loops of the membrane-proximal domain

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Structure and function of human and murine receptors for IgG.

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Biology of Human Immunoglobulin G Fc Receptors

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Identifiers

DOI

10.1016/S0161-5890(98)00069-8

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PubMed publication ID

9881694

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(Q28293321)

The second and third extracellular domains of FcgammaRI (CD64) confer the unique high affinity binding of IgG2a

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