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Cited by 184

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Two Human ULBP/RAET1 Molecules with Transmembrane Regions Are Ligands for NKG2D

Bacon, Louise, Eagle, Robert A, Meyer, Martina, Easom, Nicholas, Young, Neil T, Trowsdale, John·2004·The Journal of Immunology

Abstract

We characterized two novel members of the RAET1/ULBP gene cluster, RAET1E and RAET1G. The encoded proteins were similar to the ULBP in their class I-like α1 and α2 domains, but differed in that, instead of being GPI-anchored, their sequences were type 1 membrane-spanning molecules. Both proteins were capable of being expressed at the cell surface. Both proteins bound the activating receptor NKG2D, and RAET1G bound the human CMV protein UL16. The expression of diverse NKG2D-binding molecules in different tissues and with different properties is consistent with multiple modes of infection- or stress-induced activation.

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Crossref · 10.4049/jimmunol.173.2.1078

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Metadata

Authors
Bacon, L., Eagle, R. A., Meyer, M., Easom, N., Young, N. T., & Trowsdale, J.
Venue
The Journal of Immunology
Published
2004-07
Volume
173
Issue
2
Pages
1078-1084
ISSN
  • 0022-1767 (ISSN-L)
  • 1550-6606
OpenAlex
W1658020800
Cited by
184
References
3
FWCI
4.67
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Two Human ULBP/RAET1 Molecules with Transmembrane Regions Are Ligands for NKG2D. https://app.cochat.ai/papers/10.4049/jimmunol.173.2.1078
The paper
Bacon, L., Eagle, R. A., Meyer, M., Easom, N., Young, N. T., & Trowsdale, J. (2004). Two Human ULBP/RAET1 Molecules with Transmembrane Regions Are Ligands for NKG2D. The Journal of Immunology. https://doi.org/10.4049/jimmunol.173.2.1078

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.