The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Structural Heterogeneity and Functional Domains of Murine Immunoglobulin G Fc Receptors
Abstract
Binding of antibodies to effector cells by way of receptors to their constant regions (Fc receptors) is central to the pathway that leads to clearance of antigens by the immune system. The structure and function of this important class of receptors on immune cells is addressed through the molecular characterization of Fc receptors (FcR) specific for the murine immunoglobulin G isotype. Structural diversity is encoded by two genes that by alternative splicing result in expression of molecules with highly conserved extracellular domains and different transmembrane and intracytoplasmic domains. The proteins encoded by these genes are members of the immunoglobulin supergene family, most homologous to the major histocompatibility complex molecule E β . Functional reconstitution of ligand binding by transfection of individual FcR genes demonstrates that the requirements for ligand binding are encoded in a single gene. These studies demonstrate the molecular basis for the functional heterogeneity of FcR's, accounting for the possible transduction of different signals in response to a single ligand.
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Cites
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Cited by
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Metadata
- Authors
- Ravetch, J. V., Luster, A. D., Weinshank, R., Kochan, J., Pavlovec, A., Portnoy, D. A., Hulmes, J., Pan, Y.-C. E., & Unkeless, J. C.
- Venue
- Science
- Published
- 1986-11-07
- Volume
- 234
- Issue
- 4777
- Pages
- 718-725
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1965711974
- Cited by
- 333
- References
- 28
- FWCI
- 42.10
- Type
- journal article
- Language
- en
- Open access
- closed
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- Ravetch, J. V., Luster, A. D., Weinshank, R., Kochan, J., Pavlovec, A., Portnoy, D. A., Hulmes, J., Pan, Y.-C. E., & Unkeless, J. C. (1986). Structural Heterogeneity and Functional Domains of Murine Immunoglobulin G Fc Receptors. Science. https://doi.org/10.1126/science.2946078
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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