The DOI matches its Crossref record; 155 of the 155 references it cites were found in a registry or an index.
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]
Citations
Cites
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Items 201–205 of 205
A conserved sequence insert of fibrillins is involved in plastoglobule association and lipid binding
Shivaiah, K., Kithan-Lundquist, R., Kaneshiro, A. K., Boren, D. M., Susanto, F. A., Herrera-Tequia, A., Vermaas, J. V., & Lundquist, P. K. (2026) · Plant and Cell Physiology · doi:10.1093/pcp/pcag047 · Cited by 4
Santin, A., Mezzadrelli, E., Perin, G., & Morosinotto, T. (2026) · Plant Physiology · doi:10.1093/plphys/kiag224
Saliva and Its Roles in the Oral Processing of Food
Carpenter, G. (2026) · doi:10.1002/9781394293346.ch4
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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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