ArticlePloS one2015
Structure-Based Phylogenetic Analysis of the Lipocalin Superfamily.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- A conserved sequence insert of fibrillins is involved in plastoglobule association and lipid binding.Plant & cell physiology · 2026Article
- Structural phylogenetics unravels the evolutionary diversification of communication systems in gram-positive bacteria and their viruses.Nature structural & molecular biology · 2025Article
- Neutrophil Gelatinase-Associated Lipocalin: Biological Aspects and Potential Diagnostic Use in Acute Kidney Injury.Journal of clinical medicine · 2025Review
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- Role of Small Molecule Ligands in IgE-Mediated Allergy.Current allergy and asthma reports · 2023Review
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- Article
- Beta-Lactoglobulin as a Model Food Protein: How to Promote, Prevent, and Exploit Its Unfolding Processes.Molecules (Basel, Switzerland) · 2022Review
- Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?Clinical reviews in allergy & immunology · 2022Review
- Purification and Characterisation of Two Novel Pigment Proteins from the Carapace of Red Swamp Crayfish (Foods (Basel, Switzerland) · 2021Article
- Insights into topology and membrane interaction characteristics of plastoglobule-localized AtFBN1a and AtLOX2.Plant signaling & behavior · 2021Article
- Driving CARs with alternative navigation tools - the potential of engineered binding scaffolds.The FEBS journal · 2021Review
- Catalytic mechanism andNature catalysis · 2021Article
- R-hydroxynitrile lyase from the cyanogenic millipede, Chamberlinius hualienensis-A new entry to the carrier protein family Lipocalines.The FEBS journal · 2021Article
- Tick Saliva and Salivary Glands: What Do We Know So Far on Their Role in Arthropod Blood Feeding and Pathogen Transmission.Frontiers in cellular and infection microbiology · 2021Review
- An Evolutionary Perspective of the Lipocalin Protein Family.Frontiers in physiology · 2021Article
- Article
- A conformation-specific ON-switch for controlling CAR T cells with an orally available drug.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Cell Wall PAC (Proline-Rich, Arabinogalactan Proteins, Conserved Cysteines) Domain-Proteins Are Conserved in the Green Lineage.International journal of molecular sciences · 2020Article
- Retinol-binding protein 2 (RBP2): biology and pathobiology.Critical reviews in biochemistry and molecular biology · 2020Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipocalins constitute a superfamily of extracellular proteins that are found in all three kingdoms of life. Although very divergent in their sequences and functions, they show remarkable similarity in 3-D structures. Lipocalins bind and transport small hydrophobic molecules. Earlier sequence-based phylogenetic studies of lipocalins highlighted that they have a long evolutionary history. However the molecular and structural basis of their functional diversity is not completely understood. The main objective of the present study is to understand functional diversity of the lipocalins using a structure-based phylogenetic approach. The present study with 39 protein domains from the lipocalin superfamily suggests that the clusters of lipocalins obtained by structure-based phylogeny correspond well with the functional diversity. The detailed analysis on each of the clusters and sub-clusters reveals that the 39 lipocalin domains cluster based on their mode of ligand binding though the clustering was performed on the basis of gross domain structure. The outliers in the phylogenetic tree are often from single member families. Also structure-based phylogenetic approach has provided pointers to assign putative function for the domains of unknown function in lipocalin family. The approach employed in the present study can be used in the future for the functional identification of new lipocalin proteins and may be extended to other protein families where members show poor sequence similarity but high structural similarity.
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