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C5A Anaphylatoxin and Its Seven Transmembrane-Segment Receptor

Gerard, C, Gerard, N P·1994·Annual Review of Immunology

Abstract

The molecular cloning of the C5a receptor places this molecule in the superfamily of G-protein coupled receptors. This superfamily is characterized by the presence of signature motifs including seven hydrophobic domains which span the cell membrane and impart a predicted serpentine topology to the receptor proteins. The identification of other members of this family, including receptors for the chemokines IL-8 and Mip-1/Rantes, thrombin, formyl peptide, and platelet activating factor, provide new tools for understanding structure-function relationships relevant to the inflammatory process. This review focuses on the recent biological studies concerning the ligand C5a and its cellular receptor, the structure/activity relationships so far discerned, signal transduction mechanisms, progress toward identification of receptor antagonists, and some likely directions for future studies. Where appropriate, relevant work on related seven transmembrane segment receptors is discussed.

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Metadata

Authors
Gerard, C., & Gerard, N. P.
Venue
Annual Review of Immunology
Published
1994-04
Volume
12
Issue
1
Pages
775-808
ISSN
  • 0732-0582 (ISSN-L)
  • 1545-3278
OpenAlex
W2150842023
Cited by
416
References
0
FWCI
8.33
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: C5A Anaphylatoxin and Its Seven Transmembrane-Segment Receptor. https://app.cochat.ai/papers/10.1146/annurev.iy.12.040194.004015
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Gerard, C., & Gerard, N. P. (1994). C5A Anaphylatoxin and Its Seven Transmembrane-Segment Receptor. Annual Review of Immunology. https://doi.org/10.1146/annurev.iy.12.040194.004015

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