The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Occurrence, structure, biochemical properties and technological characteristics of lactoferrin
Open accessAbstract
The structure of the iron-binding glycoprotein lactoferrin, present in milk and other exocrine secretions, has been elucidated in great detail, both the three-dimensional protein structure and the attached N-glycans. Structure–function relationships are being established. From these studies a function for lactoferrin in host defence and modulation of iron metabolism emerges. This paper describes in some detail how iron and other cations may be bound by lactoferrins from human or bovine sources and elucidates parts of the molecule that are critical for interactions with cells and biomolecules. Furthermore, the technological aspects, more specifically the heat-sensitivity, of bovine lactoferrin in different matrices are described.
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Citations
Cites
Identification of the bactericidal domain of lactoferrin
Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., Kawase, K., & Tomita, M. (1992) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(92)90346-f · Cited by 892
Lactoferrin: molecular structure and biological function
Lönnerdal, B., & Iyer, S. (1995) · Annual Review of Nutrition · doi:10.1146/annurev.nu.15.070195.000521 · Cited by 781
Lactoferrin: a general review.
Levay, P., & Viljoen, M. (1995) · PubMed · Cited by 648
Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution
Moore, S. A., Anderson, B. F., Groom, C. R., Haridas, M., & Baker, E. N. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1386 · Cited by 419
Harmsen, M. C., Swart, P. J., Bethune, M.-P. D., Pauwels, R., Clercq, E. D., The, T. B., & Meijer, D. K. F. (1995) · Journal of Infectious Diseases · doi:10.1093/infdis/172.2.380 · Cited by 379
Biological role of lactoferrin
Sanchez, L., Calvo, M., & Brock, J. H. (1992) · Archives of Disease in Childhood · doi:10.1136/adc.67.5.657 · Cited by 378
Molecular cloning and sequence analysis of bovine lactotransferrin
PIERCE, A., COLAVIZZA, D., BENAISSA, M., MAES, P., TARTAR, A., MONTREUIL, J., & SPIK, G. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb15801.x · Cited by 253
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Cited by
Lactoferrin: Balancing Ups and Downs of Inflammation Due to Microbial Infections
Drago-Serrano, M., Campos-Rodríguez, R., Carrero, J., & De la Garza, M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18030501 · Cited by 151
Heat-induced denaturation and bioactivity changes of whey proteins
Zhang, L., Zhou, R., Zhang, J., & Zhou, P. (2021) · International Dairy Journal · doi:10.1016/j.idairyj.2021.105175 · Cited by 114
Stratakos, A. C., & Grant, I. R. (2018) · Food Microbiology · doi:10.1016/j.fm.2018.05.011 · Cited by 67
Santos-Pereira, C., Andrés, M. T., Chaves, S. R., Fierro, J. F., Gerós, H., Manon, S., Rodrigues, L. R., & Côrte-Real, M. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.12.224 · Cited by 21
Metadata
- Authors
- Steijns, J. M., & van Hooijdonk, A. C. M.
- Venue
- British Journal of Nutrition
- Publisher
- Cambridge University Press (CUP)
- Published
- 2000-11
- Volume
- 84
- Issue
- S1
- Pages
- 11-17
- ISSN
- 0007-1145 (ISSN-L)
- 1475-2662
- OpenAlex
- W1999193936
- Cited by
- 310
- References
- 45
- FWCI
- 5.08
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Steijns, J. M., & van Hooijdonk, A. C. M. (2000). Occurrence, structure, biochemical properties and technological characteristics of lactoferrin. British Journal of Nutrition. https://doi.org/10.1017/s0007114500002191
Data sources
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.