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Maureen K. Bunger

Researcher at Research Triangle Park

Publications -  23
Citations -  3995

Maureen K. Bunger is an academic researcher from Research Triangle Park. The author has contributed to research in topics: Aryl hydrocarbon receptor nuclear translocator & Aryl hydrocarbon receptor. The author has an hindex of 14, co-authored 23 publications receiving 3485 citations. Previous affiliations of Maureen K. Bunger include National Institutes of Health & RTI International.

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Mop3 Is an Essential Component of the Master Circadian Pacemaker in Mammals

TL;DR: Analysis of Period gene expression in the suprachiasmatic nucleus (SCN) indicates that these behavioral phenotypes arise from loss of circadian function at the molecular level, and provides genetic evidence that MOP3 is the bona fide heterodimeric partner of mCLOCK.
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The microbiome and butyrate regulate energy metabolism and autophagy in the mammalian colon

TL;DR: It is demonstrated that microbiota have a strong effect on energy homeostasis in the colon compared to other tissues and this tissue specificity is due to colonocytes utilizing bacterially produced butyrate as their primary energy source.
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Resistance to 2,3,7,8-tetrachlorodibenzo-p-dioxin toxicity and abnormal liver development in mice carrying a mutation in the nuclear localization sequence of the aryl hydrocarbon receptor

TL;DR: Data support a model where most, if not all, of AHR-regulated biology requires nuclear localization, and homologous recombination to generate mice with a mutation in the AHR nuclear localization/DRE binding domain support this model.
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Progressive arthropathy in mice with a targeted disruption of the Mop3/Bmal-1 locus.

TL;DR: It is observed that Mop3 null mice display an increased mortality after 26 weeks of age and a phenotype best described as a progressive noninflammatory arthropathy, and it is suggested that MOP3 is an inhibitor of ligament and tendon ossification.
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Abnormal Liver Development and Resistance to 2,3,7,8-Tetrachlorodibenzo-p-Dioxin Toxicity in Mice Carrying a Mutation in the DNA-Binding Domain of the Aryl Hydrocarbon Receptor

TL;DR: The generation of a mouse model that expresses an AHR protein capable of ligand binding, interactions with chaperone proteins, functional heterodimerization with ARNT, and nuclear translocation, but is unable to bind DREs suggests that DNA binding is necessary for AHR-mediated developmental and toxic signaling.