The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
A family of secreted proteins contains homology to the cysteine-rich ligand-binding domain of frizzled receptors
Open accessAbstract
This paper describes the identification of a new family of mammalian genes that encode secreted proteins containing homology to the cysteine-rich ligand-binding domain found in the frizzled family of transmembrane receptors. The secreted frizzled-related proteins (sFRPs) are approximately 30 kDa in size, and each contains a putative signal sequence, a frizzled-like cysteine-rich domain, and a conserved hydrophilic carboxy-terminal domain. The sFRPs are not the products of differential splicing of the known frizzled genes. Glycosylphosphatidylinositol-anchored derivatives of sFRP-2 and sFRP-3 produced in transfected human embryonic kidney cells confer cell-surface binding by the Drosophila Wingless protein. These observations suggest that sFRPs may function in vivo to modulate Wnt signaling, or, alternatively, as novel ligands for as yet unidentified receptors.
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Metadata
- Authors
- Rattner, A., Hsieh, J.-C., Smallwood, P. M., Gilbert, D. J., Copeland, N. G., Jenkins, N. A., & Nathans, J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1997-04
- Volume
- 94
- Issue
- 7
- Pages
- 2859-2863
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1982709013
- Cited by
- 583
- References
- 1
- FWCI
- 7.88
- Type
- journal article
- Language
- en
- Open access
- green
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