ArticleThe Journal of biological chemistry2010
The v-myc-induced Q83 lipocalin is a siderocalin.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- TargetingRSC medicinal chemistry · 2023Review
- Site-Specific Siderocalin Binding to Ferric and Ferric-Free Enterobactin As Revealed by Mass Spectrometry.ACS chemical biology · 2020Article
- The anti-bacterial iron-restriction defence mechanisms of egg white; the potential role of three lipocalin-like proteins in resistance against Salmonella.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2019Article
- Lipocalin 2 alleviates iron toxicity by facilitating hypoferremia of inflammation and limiting catalytic iron generation.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2016Article
- Article
- Biochemical and Structural Characterization of the Interaction between the Siderocalin NGAL/LCN2 (Neutrophil Gelatinase-associated Lipocalin/Lipocalin 2) and the N-terminal Domain of Its Endocytic Receptor SLC22A17.The Journal of biological chemistry · 2016Article
- The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepB.The Journal of biological chemistry · 2014Article
- Siderocalins: Siderophore binding proteins evolved for primary pathogen host defense.Current opinion in chemical biology · 2013Review
- Toward rational fragment-based lead design without 3D structures.Journal of medicinal chemistry · 2012Article
- Cellular and mitochondrial iron homeostasis in vertebrates.Biochimica et biophysica acta · 2012Review
- Mammalian siderophores, siderophore-binding lipocalins, and the labile iron pool.The Journal of biological chemistry · 2012Review
- Characterization of chicken spleen transcriptome after infection with Salmonella enterica serovar Enteritidis.PloS one · 2012Article
- Galline Ex-FABP is an antibacterial siderocalin and a lysophosphatidic acid sensor functioning through dual ligand specificities.Structure (London, England : 1993) · 2011Article
- Siderocalin Q83 exhibits differential slow dynamics upon ligand binding.Journal of biomolecular NMR · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Siderocalins are atypical lipocalins able to capture siderophores with high affinity. They contribute to the innate immune response by interfering with bacterial siderophore-mediated iron uptake but are also involved in numerous physiological processes such as inflammation, iron delivery, tissue differentiation, and cancer progression. The Q83 lipocalin was originally identified based on its overexpression in quail embryo fibroblasts transformed by the v-myc oncogene. We show here that Q83 is a siderocalin, binding the siderophore enterobactin with an affinity and mode of binding nearly identical to that of neutrophil gelatinase-associated lipocalin (NGAL), the prototypical siderocalin. This strengthens the role of siderocalins in cancer progression and inflammation. In addition, we also present the solution structure of Q83 in complex with intact enterobactin and a detailed analysis of the Q83 binding mode, including mutagenesis of the critical residues involved in enterobactin binding. These data provide a first insight into the molecular details of siderophore binding and delineate the common molecular properties defining the siderocalin protein family.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.