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Marilyn G. Pray-Grant

Researcher at Pennsylvania State University

Publications -  5
Citations -  1612

Marilyn G. Pray-Grant is an academic researcher from Pennsylvania State University. The author has contributed to research in topics: SAGA complex & Aryl hydrocarbon receptor. The author has an hindex of 5, co-authored 5 publications receiving 1569 citations. Previous affiliations of Marilyn G. Pray-Grant include Howard Hughes Medical Institute.

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Characterization of a Subset of the Basic-Helix-Loop-Helix-PAS Superfamily That Interacts with Components of the Dioxin Signaling Pathway

TL;DR: The expression profiles of the AHR, MOP1, and MOP2 mRNAs, coupled with the observation that they all share ARNT as a common dimeric partner, suggests that the cellular pathways mediated by Mop1 and Mop2 may influence or respond to the dioxin signaling pathway.
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Hepatitis B Virus X-Associated Protein 2 Is a Subunit of the Unliganded Aryl Hydrocarbon Receptor Core Complex and Exhibits Transcriptional Enhancer Activity

TL;DR: XAP2 enhanced the ability of endogenous murine and human AhR complexes to activate a dioxin-responsive element–luciferase reporter twofold, following transient expression of XAP2 in Hepa 1c1c7 and HeLa cells.
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Protein kinase C activity is required for aryl hydrocarbon receptor pathway-mediated signal transduction.

TL;DR: A PKC-mediated event is required for the hAhR to form a functional transcriptional complex that leads to trans-activation and that the DRE is the minimal DNA element required for PMA to enhance AhR-mediated trans- activation.
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A Conserved Motif Present in a Class of Helix-Loop-Helix Proteins Activates Transcription by Direct Recruitment of the SAGA Complex

TL;DR: This work identifies a novel motif, LDFS, present in the vertebrate class I HLH proteins as well as in a yeast HLH protein that is essential for transactivation and provides both genetic and biochemical evidence that the highly conserved LDFs motif stimulates transcription by direct recruitment of the SAGA histone acetyltransferase complex.