Recombinant soluble Fc gamma RII inhibits immune complex precipitation (Q70823403)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8536382 AND SRC:MED&resulttype=core&format=json

14 October 2019

title

Recombinant soluble Fc gamma RII inhibits immune complex precipitation (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8536382 AND SRC:MED&resulttype=core&format=json

14 October 2019

author name string

A L Gavin

1

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14 October 2019

B D Wines

2

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14 October 2019

M S Powell

3

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14 October 2019

P M Hogarth

4

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14 October 2019

publication date

1 December 1995

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Clinical and Experimental Immunology

14 October 2019

published in

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14 October 2019

volume

102

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14 October 2019

issue

3

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14 October 2019

page(s)

620-625

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Prevention of immune precipitation by purified components of the alternative pathway

14 October 2019

cites work

1 reference

12 December 2020

The role of C1, C1-inactivator and C4 in modulating immune precipitation

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Recombinant human IgG1-murine IgE chimeric Ig. Construction, expression, and binding to human Fc gamma receptors

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The role of complement and its receptor in the elimination of immune complexes

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Mechanism of human monocyte activation via the 40-kDa Fc receptor for IgG

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The cutaneous reaction to soluble antigen-antibody complexes; a comparison with the Arthus phenomenon

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IgM-RF prevents complement-mediated inhibition of immune precipitation

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Detection and quantification of secreted soluble FcγRIIA in human sera by an enzyme-linked immunosorbent assay

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Mapping epitopes of human Fc gamma RII (CDw32) with monoclonal antibodies and recombinant receptors

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IgM anti-Fc gamma R autoantibodies trigger neutrophil degranulation

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Monoclonal antibody to human IgG Fc receptors. Cross-linking of receptors induces lysosomal enzyme release and superoxide generation by neutrophils

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On the fragmentation of monoclonal IgG1, IgG2a, and IgG2b from BALB/c mice

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Human Fc gamma RI and Fc gamma RII interact with distinct but overlapping sites on human IgG

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Human epidermal Langerhans cells secrete a soluble receptor for IgG (Fc gamma RII/CD32) that inhibits the binding of immune complexes to Fc gamma R cells.

1 reference

12 December 2020

BOUND COMPLEMENT AND IMMUNOLOGIC INJURY OF BLOOD VESSELS

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A soluble form of Fc gamma RIII is present in human serum and other body fluids and is elevated at sites of inflammation

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Recombinant soluble human Fc gamma RII: production, characterization, and inhibition of the Arthus reaction

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IgG Fc receptors in sera from patients with rheumatoid arthritis and systemic lupus erythematosus

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Immunologic tissue injury mediated by neutrophilic leukocytes.

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Purification of a plasma protein that inhibits complement-mediated prevention of immune precipitation

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Complement-mediated inhibition of immune precipitation. I. Role of the classical and alternative pathways

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Fc-mediated immune precipitation. I. A new role of the Fc-portion of IgG

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Rheumatoid factors in the pathogenesis of rheumatoid arthritis

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Requirements for the solubilization of immune aggregates by complement. The role of the classical pathway

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Molecular basis of Fc receptor function

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Co-operative interaction of subcomponents of the first component of complement with IgG: a functional defect of dimeric Facb from rabbit IgG

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The plasma protein which inhibits complement-mediated prevention of immune precipitation is an Fc binding protein

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The binding site for C1q on IgG

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Fc-mediated immune precipitation. II. Analysis of precipitating immune complexes by rate-zonal ultracentrifugation

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12 December 2020

Immunohistochemical localization of a plasma protein (glycoprotein 60) which inhibits complement-mediated prevention of immune precipitation.

1 reference

12 December 2020