ArticleProceedings of the National Academy of Sciences of the United States of America2003
Identification of a PU.1-IRF4 protein interaction surface predicted by chemical exchange line broadening.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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Who cites it
8 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Fine mapping of the celiac disease-associated LPP locus reveals a potential functional variant.Human molecular genetics · 2014Pooled it
- PU.1-c-Jun interaction is crucial for PU.1 function in myeloid development.Communications biology · 2022Article
- Role of IRF4-Mediated Inflammation: Implication in Neurodegenerative Diseases.Neurology & neurotherapy open access journal · 2017Article
- Probing the electrostatics and pharmacological modulation of sequence-specific binding by the DNA-binding domain of the ETS family transcription factor PU.1: a binding affinity and kinetics investigation.Journal of molecular biology · 2013Article
- IFN regulatory factor 4 regulates the expression of a subset of Th2 cytokines.Journal of immunology (Baltimore, Md. : 1950) · 2009Article
- Molecular Modeling of Geometries, Charge Distributions, and Binding Energies of Small, Drug-Like Molecules Containing Nitrogen Heterocycles and Exocyclic Amino Groups in the Gas Phase and Aqueous Solution.Journal of chemical theory and computation · 2008Article
- Article
- Backbone dynamics of complement control protein (CCP) modules reveals mobility in binding surfaces.Protein science : a publication of the Protein Society · 2004Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Relaxation values reflecting residue-specific line broadening revealed amino acids in the DNA-binding domain of PU.1 on a surface potentially involved in protein-protein interactions. Mutation of these amino acids did not cause protein unfolding but destabilized PU.1-DNA binding. Addition of IFN response factor 4 to form the ternary complex recovered binding stability. Fluorescence quenching experiments proved that this surface of PU.1 interacts with IFN response factor 4 during binding. Our results provide evidence that residues that display increased conformational exchange can be used to predict areas of protein-protein interactions.
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Registered trials
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