The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
The lipocalin protein family: structural and sequence overview
Abstract
Lipocalins are remarkably diverse at the sequence level yet have highly conserved structures. Most lipocalins share three characteristic conserved sequence motifs - the kernel lipocalins - while others are more divergent family members - the outlier lipocalins - typically sharing only one or two. This classification is a useful tool for analysing the family, and within these large sets are smaller groups sharing much higher levels of sequence similarity. The lipocalins are also part of a larger protein superfamily: the calycins, which includes the fatty acid binding proteins, avidins, a group of metalloproteinase inhibitors, and triabin. The superfamily is characterised by a similar structure (a repeated +1 topology beta-barrel) and by the conservation of a remarkable structural signature.
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“The ADAM (A Disintegrin And Metalloprotease) and ADAMTS families of metalloproteases are encoded by over 40 human genes, mediate cell-cell and cell-matrix interactions (20, 21) and are involved in a range of human diseases, including cancer metastasis, inflammatory disorders, neurological diseases and asthma (21, 22).”
From Accurate prediction of protein structures and interactions using a 3-track network (2021) · cites this paper as [20]
Citations
Cites
Murzin, A. G., Brenner, S. E., Hubbard, T., & Chothia, C. (1995) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80134-2 · Cited by 6,445
The lipocalin protein family: structure and function
FLOWER, D. R. (1996) · Biochemical Journal · doi:10.1042/bj3180001 · Cited by 1,679
Self-citationThe PROSITE database, its status in 1999
Hofmann, K., Bücher, P., Falquet, L., & Bairoch, A. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.1.215 · Cited by 1,092
Green, N. M. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)84259-j · Cited by 1,020
Bovine β-lactoglobulin at 1.8 Å resolution — still an enigmatic lipocalin
Brownlow, S., Morais-Cabral, J. H., Cooper, R. A., Flower, D. R., Yewdall, S. J., Polikarpov, I., North, A. C. T., & Sawyer, L. (1997) · Structure · doi:10.1016/s0969-2126(97)00205-0 · Cited by 714
Self-citationLipid-Binding Proteins: A Family of Fatty Acid and Retinoid Transport Proteins
Banaszak, L. J., Winter, N. S., Xu, Z., Bernlohr, D., Cowan, S. W., & Jones, A. T. (1994) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60639-7 · Cited by 483
Borgstahl, G. E. O., Williams, D. R., & Getzoff, E. D. (1995) · Biochemistry · doi:10.1021/bi00019a004 · Cited by 438
Harpaz, Y., & Chothia, C. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1312 · Cited by 435
Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography
Böcskei, Z., Groom, C. R., Flower, D. R., Wright, C. E., Phillips, S. E. V., Cavaggioni, A., Findlay, J. B. C., & North, A. C. T. (1992) · Nature · doi:10.1038/360186a0 · Cited by 361
Self-citationStructure and sequence relationships in the lipocalins and related proteins
Flower, D. R., North, A. C. T., & Attwood, T. K. (1993) · Protein Science · doi:10.1002/pro.5560020507 · Cited by 342
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Zhang, Y., Yu, L., Xue, L., Liu, F., Jing, R., & Luo, J. (2025) · PLoS ONE · doi:10.1371/journal.pone.0319329 · Cited by 2
Ramadan, S. S., El-latif, S. E. A., Mahmoud, A. H., Awad, A. G., El‐Khadragy, M. F., Elshopakey, G. E., & Moneim, A. E. A. (2025) · Journal of Agriculture and Food Research · doi:10.1016/j.jafr.2025.102199 · Cited by 2
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Dubey, V. P., Pal, B., Srikantan, S., Pottabathini, S., De, P. K., & Sankaranarayanan, R. (2010) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309110008237 · Cited by 2
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Ascenzi, P., di Masi, A., Leboffe, L., Fanali, G., & Fasano, M. (2016) · RENDICONTI LINCEI · doi:10.1007/s12210-016-0562-2 · Cited by 2
Amin, E., saad, E., Allam, H. M., & Zidan, A. A. (2014) · Zagazig University Medical Journal · doi:10.21608/zumj.2014.4348 · Cited by 2
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Demchenko, A. P. (2015) · Springer eBooks · doi:10.1007/978-3-319-20780-3_7 · Cited by 2
Gasymov, O. K., Abduragimov, A. R., & Glasgow, B. J. (2015) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2015.06.043 · Cited by 2
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Ahnström, J. (2009) · Lund University Publications (Lund University) · Cited by 2
Espinel, M. D. C. (2014) · UVaDOC UVaDOC University of Valladolid Documentary Repository (University of Valladolid) · doi:10.35376/10324/7752 · Cited by 2
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Zhang, Y., Fan, H., Gao, K., Zhang, S., Lu, R., Cao, X., Xu, X., & Liu, J. (2024) · Aquaculture Reports · doi:10.1016/j.aqrep.2024.102386 · Cited by 1
McLean, Z., Thomas, M. E., & Belcher, S. M. (2025) · Toxicological Sciences · doi:10.1093/toxsci/kfaf178 · Cited by 2
Hu, X., Zhou, T., Cui, T., Du, Y., Song, C., Chang, W., Xiong, J., Qin, J., Deng, L., & Ji, W.-K. (2025) · Nature Communications · doi:10.1038/s41467-025-68157-7 · Cited by 1
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Wang, S., Ma, J., Wang, Q., Guan, Y., Hu, X., & Huang, J. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117089 · Cited by 1
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Catherine, L., Lown, C., & Etsuko, N. (2011) · InTech eBooks · doi:10.5772/22831 · Cited by 1
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Wu, X., Wang, W. P., Li, X., Xu, H. Y., Wu, H., & Liu, Z. G. (2012) · PubMed · doi:10.3967/0895-3988.2012.03.012 · Cited by 1
Fortin, R., Ceciliani, F., Sartorelli, P., Miranda-Ribera, A., Musante, L., Candiano, G., Greppi, G. F., & Roncada, P. (2007) · Italian Journal of Animal Science · doi:10.4081/ijas.2007.1s.430 · Cited by 1
Armanmehr, S., Kalhor, H. R., & Tabarraei, A. (2016) · Protein Expression and Purification · doi:10.1016/j.pep.2016.01.016 · Cited by 1
Schott, M. (2009) · Yearbook of Endocrinology · doi:10.1016/s0084-3741(09)79322-9 · Cited by 1
Lindeberg, H., Burchmore, R., & Kennedy, M. W. (2017) · Royal Society Open Science · doi:10.1098/rsos.161085 · Cited by 1
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Devapatla, P., Jeng, W. Y., Chiu, W., & Hsieh‐Li, H. M. (2025) · Kidney Research and Clinical Practice · doi:10.23876/j.krcp.23.339 · Cited by 1
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Persaud, K. C. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-809324-5.23878-9 · Cited by 1
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Xu, N., & Nilsson‐Ehle, P. (2007) · doi:10.1002/9783527625178.ch4 · Cited by 1
Micas, A. F. D. (2012) · doi:10.11606/t.17.2012.tde-22042013-091502 · Cited by 1
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Maestro, R. P. (2018) · UVaDOC UVaDOC University of Valladolid Documentary Repository (University of Valladolid) · doi:10.35376/10324/33119 · Cited by 1
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Crowther, J. M., Broadhurst, M., Laue, T. M., Jameson, G. B., Hodgkinson, A. J., & Dobson, R. C. J. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/675587 · Cited by 1
Zhang, S., Li, X., Zhao, S., Drobizhev, M. A., & Ai, H. (2021) · Nature Methods · doi:10.1038/s41592-021-01148-w · Cited by 1
RetractedPevsner, J. (2009) · doi:10.1002/9780470451496.ch11 · Cited by 1
Lowe, N. E., & Chang, R. L. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.29.478329 · Cited by 1
Hussein, M. M., Althagafi, H. A. E., Alharthi, F. R., Albrakati, A., Alsharif, K. F., Theyab, A., Kassab, R. B., Mufti, A. H., Algahtani, M., Oyouni, A. A. A., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1255144/v1 · Cited by 1
Sodetz, J. M., & Plumb, M. E. (2005) · Encyclopedia of Life Sciences · doi:10.1038/npg.els.0003977 · Cited by 1
Zhang, Y., Fan, H., Gao, K., Zhang, S., Lu, R., Cao, X., Xu, X., & Liu, J. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4877642 · Cited by 1
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Metadata
- Authors
- Flower, D. R., North, A. C. T., & Sansom, C. E.
- Affiliations
- Jenner Institute (GB)
- University of Leeds (GB)
- University of London (GB)
- Corresponding author
- Flower, Darren R.
- ORCID
- Flower, Darren R.
- Venue
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Publisher
- Elsevier BV
- Published
- 2000-10
- Volume
- 1482
- Issue
- 1-2
- Pages
- 9-24
- ISSN
- 0167-4838 (ISSN-L)
- OpenAlex
- W2038438679
- Cited by
- 868
- References
- 59
- Citations by year
- 2026: 18 · 2025: 26 · 2024: 25 · 2023: 27 · 2022: 29 · 2021: 33 · 2020: 37 · 2019: 27 · 2018: 29 · 2017: 35 · 2016: 46 · 2015: 39 · 2014: 51 · 2013: 37 · 2012: 60
- FWCI
- 1.34
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- lipocalin, protein superfamilies, conserved motifs, fatty acid binding protein, avidin, metalloproteinase inhibitors, protein structure conservation
- MeSH terms
- Fatty Acid-Binding Protein 7, Amino Acid Sequence, Animals, Carrier Proteins, Humans, Lactoglobulins, Models, Molecular, Molecular Sequence Data, Neoplasm Proteins, Protein Conformation, Sequence Homology, Amino Acid, Insect Proteins, Tumor Suppressor Proteins, Fatty Acid-Binding Proteins
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