The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
The endocytic receptor megalin binds the iron transporting neutrophil‐gelatinase‐associated lipocalin with high affinity and mediates its cellular uptake
Abstract
We show here that megalin, a member of the low‐density lipoprotein receptor family expressed in polarized epithelia, binds NGAL with high affinity, as shown by surface plasmon resonance analysis. Furthermore, a rat yolk sac cell line known to express high levels of megalin, endocytosed NGAL by a mechanism completely blocked by an antibody against megalin.
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Cites
The lipocalin protein family: structure and function
FLOWER, D. R. (1996) · Biochemical Journal · doi:10.1042/bj3180001 · Cited by 1,679 · cited 1×
“Lipocalins constitute a family of more than 30 proteins, found in species as separate as insects and man [1,2].”
BackgroundGoetz, D. H., Holmes, M. A., Borregaard, N., Bluhm, M. E., Raymond, K. N., & Strong, R. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00708-6 · Cited by 1,355
Self-citationAn Iron Delivery Pathway Mediated by a Lipocalin
Yang, J., Goetz, D., Li, J.-Y., Wang, W., Mori, K., Setlik, D., Du, T., Erdjument-Bromage, H., Tempst, P., Strong, R., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00710-4 · Cited by 651
Self-citationCowland, J. B., Sørensen, O. E., Sehested, M., & Borregaard, N. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.12.6630 · Cited by 354
Self-citation
Cited by
Siderophore-Based Iron Acquisition and Pathogen Control
Miethke, M., & Marahiel, M. A. (2007) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00012-07 · Cited by 1,774
Regulation of cellular iron metabolism
Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986
Dual Action of Neutrophil Gelatinase–Associated Lipocalin
Schmidt-Ott, K. M., Mori, K., Li, J. Y., Kalandadze, A., Cohen, D. J., Devarajan, P., & Barasch, J. (2007) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006080882 · Cited by 772
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554
Regulation of iron transport and the role of transferrin
Gkouvatsos, K., Papanikolaou, G., & Pantopoulos, K. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.10.013 · Cited by 518
Metadata
- Authors
- Hvidberg, V., Jacobsen, C., Strong, R. K., Cowland, J. B., Moestrup, S. K., & Borregaard, N.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2004-12-24
- Volume
- 579
- Issue
- 3
- Pages
- 773-777
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2053023199
- Cited by
- 350
- References
- 4
- FWCI
- 5.85
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: The endocytic receptor megalin binds the iron transporting neutrophil‐gelatinase‐associated lipocalin with high affinity and mediates its cellular uptake. https://app.cochat.ai/papers/10.1016/j.febslet.2004.12.031
- The paper
- Hvidberg, V., Jacobsen, C., Strong, R. K., Cowland, J. B., Moestrup, S. K., & Borregaard, N. (2005). The endocytic receptor megalin binds the iron transporting neutrophil‐gelatinase‐associated lipocalin with high affinity and mediates its cellular uptake. FEBS Letters. https://doi.org/10.1016/j.febslet.2004.12.031
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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.
