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Lipocalins - a family portrait
Open accessAbstract
Lipocalins are a widely distributed group of proteins whose common feature is the presence of six-or eight-stranded beta-barrel in their tertiary structure and highly conservative motifs short conserved region, (SCR) in their amino acid sequences. The presence of three SCRs is typical for kernel lipocalins, while outlier lipocalins have only one or two such regions. Owing to their ability to bind and transport small, hydrophobic molecules, lipocalins participate in the distribution of such substances. However, the physiological significance of lipocalins is not limited to transfer processes. They play an important role in the regulation of immunological and developmental processes, and are also involved in the reactions of organisms to various stress factors and in the pathways of signal transduction. Of special interest is the enzymatic activity found in a few members of the lipocalin family, as well as the interaction with natural membranes, both directly with lipids and through membrane-localized protein receptors.
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“Lipocalin (LCN) proteins are secreted proteins that bind small hydrophobic ligands through their conical β barrels [252,253].”
From Hepatokines and metabolism: Deciphering communication from the liver (2021) · cites this paper as [252]
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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
The lipocalin protein family: structural and sequence overview
Flower, D. R., North, A. C. T., & Sansom, C. E. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00148-5 · Cited by 868
An 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
Marín, E., Nussaume, L., Quesada, A., Gonneau, M., Sotta, B., Hugueney, P., Frey, A., & Marion‐Poll, A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00589.x · Cited by 550
The three‐dimensional structure of retinol‐binding protein.
Newcomer, M. E., Jones, T. A., Aqvist, J., Sundelin, J., Eriksson, U., Rask, L., & Peterson, P. A. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb01995.x · Cited by 405
The core lipocalin, bovine β-lactoglobulin
Sawyer, L., & Kontopidis, G. A. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00160-6 · Cited by 380
A Model for the Denaturation and Aggregation of β‐Lactoglobulin
Roefs, S. P. F. M., & de Kruif, C. G. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.00883.x · Cited by 378
Biochemistry of the violaxanthin cycle in higher plants
Yamamoto, H. Y. (1979) · Pure and Applied Chemistry · doi:10.1351/pac197951030639 · Cited by 372
Structure 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
A Novel Human Apolipoprotein (apoM)
Xu, N., & Dahlbäck, B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.44.31286 · Cited by 336
Research works printed but not linked: 4
- Hager, 1969, Lichtebedingte pH-Erniedrigung in einem Chloroplasten-Kompartiment als Ursache der enzymatischen Violaxanthin-Zeaxanthin-Umwandlungen; Benziehungen und Photophosphorylierung. Planta, 89, 224
- Hager A. Die reversiblen lichtabhängigen Xanthophyllumwandlungen in Chloroplasten. In: F.-C. Czygen Ed., Pigments in Plants, Fischer, Stuttgart 1985, pp. 57–79.
- Quarnby, 1977, Comp Biochem Physiol, 56, 55
- Suzuki, 2004, Molecular evolution of epididymal lipocalin genes localized on mouse chromosome 2 ene, 339, 49
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Martínez‐Martínez, E., Buonafine, M., Boukhalfa, I., Ibarrola, J., Fernández‐Celis, A., Kolkhof, P., Rossignol, P., Girerd, N., Mulder, P. G. H., López‐Andrés, N., et al. (2017) · Hypertension · doi:10.1161/hypertensionaha.117.09791 · Cited by 92
Levesque‐Tremblay, G., Havaux, M., & Ouellet, F. (2009) · The Plant Journal · doi:10.1111/j.1365-313x.2009.03991.x · Cited by 89
Hilger, C., Kuehn, A., & Hentges, F. (2012) · Current Allergy and Asthma Reports · doi:10.1007/s11882-012-0283-2 · Cited by 86
Boca, S., KOESTLER, F., Ksas, B., Chevalier, A., Leymarie, J., Fekete, Á., Mueller, M. J., & Havaux, M. (2013) · Plant Cell & Environment · doi:10.1111/pce.12159 · Cited by 82
Garab, G., Ughy, B., & Goss, R. (2016) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-25979-6_6 · Cited by 81
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Garab, G., Yaguzhinsky, L. S., Dlouhý, O., Nesterov, S. V., Špunda, V., & Gasanoff, E. S. (2022) · Progress in Lipid Research · doi:10.1016/j.plipres.2022.101163 · Cited by 71
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Zhang, Y., Zhao, Y., & Huang, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036772 · Cited by 46
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Kronfel, C. M., Kuzin, A. P., Forouhar, F., Biswas, A., Su, M., Lew, S., Seetharaman, J., Xiao, R., Everett, J. K., Ma, L.-C., et al. (2013) · Biochemistry · doi:10.1021/bi401192z · Cited by 33
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Portman, K. L., Long, J., Carr, S. B., Briand, L. V., Winzor, D. J., Searle, M. S., & Scott, D. J. (2014) · Biochemistry · doi:10.1021/bi5002344 · Cited by 32
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Schreck, K., & Melzig, M. F. (2018) · Molecules · doi:10.3390/molecules23102544 · Cited by 33
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Miyamoto, T., Kashima, H., 鈴木, 昭., Kikuchi, N., Konishi, I., Seki, N., & Shiozawa, T. (2011) · Human Pathology · doi:10.1016/j.humpath.2010.07.027 · Cited by 32
Kristiansson, A., Gram, M., Flygare, J., Hansson, S. R., Åkerström, B., & Storry, J. R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197234 · Cited by 33
Hilger, C., Swiontek, K., Kler, S., Diederich, C., Lehners, C., Vogel, L., Vieths, S., & Hentges, F. (2011) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2011.03726.x · Cited by 30
Sade, D., Eybishtz, A., Gorovits, R., Sobol, I., & Czosnek, H. H. (2012) · Plant Molecular Biology · doi:10.1007/s11103-012-9946-6 · Cited by 30
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Alvarez, S., Choudhury, S. R., Sivagnanam, K., Hicks, L. M., & Pandey, S. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00150 · Cited by 26
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Siddappa, P. K., Kochhar, R. K., Sarotra, P., Medhi, B., Jha, V., & Gupta, V. (2018) · JGH Open · doi:10.1002/jgh3.12112 · Cited by 26
Yang, F., Wang, M., Ma, Y., Ma, W., & Yang, W. (2011) · Journal of Experimental Zoology Part A Ecological Genetics and Physiology · doi:10.1002/jez.706 · Cited by 25
Kopeć, K., Pędziwiatr, M., Gront, D., Sztatelman, O., Sławski, J., Łazicka, M., Worch, R., Zawada, K. D., Makarova, K., Nyk, M., et al. (2019) · ACS Omega · doi:10.1021/acsomega.9b00505 · Cited by 24
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Perez‐Miller, S., Zou, Q., Novotný, M. V., & Hurley, T. D. (2010) · Protein Science · doi:10.1002/pro.426 · Cited by 24
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Gonzalez-Fernandez, F., Baer, C. A., & Ghosh, D. (2007) · BMC Biochemistry · doi:10.1186/1471-2091-8-15 · Cited by 23
Jobichen, C., Fernandis, A. Z., Velázquez‐Campoy, A., Leung, K. Y., Mok, Y., Wenk, M. R., & Sivaraman, J. (2009) · Biochemical Journal · doi:10.1042/bj20081588 · Cited by 23
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Malinina, L. V., Patel, D. J., & Brown, R. E. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044445 · Cited by 22
Kielkopf, C. S., Ghosh, M., Anand, G. S., & Brown, S. H. J. (2018) · Protein Science · doi:10.1002/pro.3534 · Cited by 20
Nuylert, A., Nakabayashi, M., Yamaguchi, T., & Asano, Y. (2020) · ACS Omega · doi:10.1021/acsomega.0c03070 · Cited by 20
Chiu, H., Bakolitsa, C., Skerra, A., Lomize, A. L., Carlton, D. D., Miller, M. D., Krishna, S., Abdubek, P., Astakhova, T., Axelrod, H. L., et al. (2009) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309109037749 · Cited by 20
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Metadata
- Authors
- Grzyb, J., Latowski, D., & Strzałka, K.
- Affiliations
- Jagiellonian University (PL)
- Corresponding author
- Strzałka, Kazimierz
- Venue
- Journal of Plant Physiology
- Publisher
- Elsevier BV
- Published
- 2006-09
- Volume
- 163
- Issue
- 9
- Pages
- 895-915
- ISSN
- 0176-1617 (ISSN-L)
- OpenAlex
- W2015717581
- Cited by
- 205
- References
- 155
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 4 · 2023: 11 · 2022: 8 · 2021: 10 · 2020: 16 · 2019: 7 · 2018: 5 · 2017: 15 · 2016: 9 · 2015: 10 · 2014: 10 · 2013: 9 · 2012: 25
- FWCI
- 0.88
- Type
- journal article
- Language
- en
- Open access
- green
- ruj.uj.edu.pl
- Licence
- Locations
- Journal of Plant Physiology (publishedVersion)
- PubMed (publishedVersion)
- Homo Politicus (Academy of Humanities and Economics in Lodz) (submittedVersion, cc-by-nc-nd)
- 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 › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- lipocalin, beta-barrel proteins, lipid binding, cell surface receptors, enzyme activity, stress response, signal transduction, plant proteins
- MeSH terms
- Amino Acid Sequence, Animals, Carrier Proteins, Membrane Proteins, Models, Molecular, Plants, Conserved Sequence, Protein Structure, Tertiary
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