Michael G. Poirier
Affiliations: | Physics | Ohio State University, Columbus, Columbus, OH |
Area:
General Biophysics, BiochemistryGoogle:
"Michael Poirier"Mean distance: (not calculated yet)
Parents
Sign in to add mentorJohn F. Marko | grad student | 1996-2001 | University of Illinois, Chicago | |
(Micromechanical-biochemical studies of mitotic chromosome elasticity and structure.) |
Children
Sign in to add traineeAlex M. Mooney | grad student | 2012 | Ohio State |
Justin A. North | grad student | 2012 | Ohio State |
Marek Simon | grad student | 2012 | Ohio State |
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Publications
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Becht DC, Kanai A, Biswas S, et al. (2024) The winged helix domain of MORF binds CpG islands and the TAZ2 domain of p300. Iscience. 27: 109367 |
Gaurav N, Kanai A, Lachance C, et al. (2024) Guiding the HBO1 complex function through the JADE subunit. Nature Structural & Molecular Biology |
Sun W, Lebedenko OO, Salguero NG, et al. (2023) Conformational and Interaction Landscape of Histone H4 Tails in Nucleosomes Probed by Paramagnetic NMR Spectroscopy. Journal of the American Chemical Society |
Jergens E, de Araujo Fernandes-Junior S, Cui Y, et al. (2023) DNA-caged nanoparticles electrostatic self-assembly. Nanoscale |
Donovan BT, Chen H, Eek P, et al. (2023) Basic helix-loop-helix pioneer factors interact with the histone octamer to invade nucleosomes and generate nucleosome-depleted regions. Molecular Cell |
Becht DC, Klein BJ, Kanai A, et al. (2023) MORF and MOZ acetyltransferases target unmethylated CpG islands through the winged helix domain. Nature Communications. 14: 697 |
Donovan BT, Luo Y, Meng Z, et al. (2023) The nucleosome unwrapping free energy landscape defines distinct regions of transcription factor accessibility and kinetics. Nucleic Acids Research |
Smrt ST, Gonzalez Salguero N, Thomas JK, et al. (2023) Histone H3 core domain in chromatin with different DNA linker lengths studied by H-Detected solid-state NMR spectroscopy. Frontiers in Molecular Biosciences. 9: 1106588 |
Sapp N, Burge N, Cox K, et al. (2022) HIV-1 Preintegration Complex Preferentially Integrates the Viral DNA into Nucleosomes Containing Trimethylated Histone 3-Lysine 36 Modification and Flanking Linker DNA. Journal of Virology. e0101122 |
Burge NL, Thuma JL, Hong ZZ, et al. (2022) H1.0 C Terminal Domain Is Integral for Altering Transcription Factor Binding within Nucleosomes. Biochemistry. 61: 625-638 |