The lipocalin protein family: structural and sequence overview.
By Darren R. Flower, A. North, C. Sansom. 2000
840 citations recorded by the source corpus.
Subfields: Hematology, Immunology and Allergy, Nutrition and Dietetics
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In Nutrition and Dietetics
Citations in the corpus
- Accurate prediction of protein structures and interactions using a 3-track neural network (2021, neutral): “3C) belonging to an extended superfamily that includes metalloprotease inhibitors (MPIs) (25).”
- Structure and biotechnological applications of odorant-binding proteins (2013, background): “1998) belong to the superfamily of lipocalins (Flower 1996; Flower et al. 2000) that include carrier proteins, such as retinol-binding protein, βlactoglobulin and other proteins of different functions.”
- Odorant binding and conformational changes of a rat odorant-binding protein. (2004, background): “…be localized in the hydrophobic cavity shaped by the β-barrel structure, called the calyx (Vincent et al., 2000; Ramoni et al., 2001), as reported for other lipocalins (Flower et al., 2000), even in dimeric β-lactoglobulin in which only one of the two calyces is occupied (Ragona et al., 2000).”
- Mechanisms of cell protection by heme oxygenase-1. (2010, background): “Other proteins can bind free heme in plasma, including α1-microglobulin (molecular weight: ∼26 kDa; human; P02760), a member of the lipocalin protein superfamily with which it shares the ability to carry small lipophilic ligands in hydrophobic pockets (213) (Figure 6).”
- An iron delivery pathway mediated by a lipocalin. (2002, background): “Discussion Lipocalins are structurally related proteins that transport a variety of ligands (Flower et al., 2000).”
- High resolution X‐ray structures of mouse major urinary protein nasal isoform in complex with pheromones (2010, background): “conservation of cavity residues simply reflects the diverse nature of ligands accomodated by a common architecture.(22,32,42,43,48)”
- Invited Review: β-Lactoglobulin: Binding Properties, Structure, and Function (2004, background): “A signaling or activity-modulator role appears to be less likely, not just because of the paucity of similar roles reported for other lipocalins (Flower et al., 2000), but also because the data supporting these various activities appear rather circumstantial.”
- The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes. (2009, background): “Their sequences are quite diverse but all the proteins adopt an eight-stranded b-barrel structure [1,2].”
- Role of Receptors in Bacillus thuringiensis Crystal Toxin Activity (2007, background): “family (41, 42) and contained 15 prototypic lipocalin domains.”