Mark P Foster

Affiliations: 
Ohio State University, Columbus, Columbus, OH 
Area:
NMR, Structural Biology, Biochemistry, Protein Dynamics, RNA-Protein Interactions, DNA Recombinases, Molecular Recognition, RNA Dynamics
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"Mark Foster"
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Publications

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McElroy C, Ihms E, Yadav DK, et al. (2023) Solution structure, dynamics and tetrahedral assembly of Anti-TRAP, a homo-trimeric triskelion-shaped regulator of tryptophan biosynthesis in . Biorxiv : the Preprint Server For Biology
Ma X, Bakhtina M, Shulgina I, et al. (2023) Structural basis of tRNAPro acceptor stem recognition by a bacterial trans-editing domain. Nucleic Acids Research
Li W, Norris AS, Lichtenthal K, et al. (2022) Thermodynamic coupling between neighboring binding sites in homo-oligomeric ligand sensing proteins from mass resolved ligand-dependent population distributions. Protein Science : a Publication of the Protein Society. 31: e4424
Stachowski K, Norris AS, Potter D, et al. (2022) Mechanisms of Cre recombinase synaptic complex assembly and activation illuminated by Cryo-EM. Nucleic Acids Research
Wagner N, Foster MP. (2022) Nearest-Neighbor Effects Modulate Spacer DNA Chemical Shifts and Guide Oligonucleotide Design for Nuclear Magnetic Resonance Studies. Biochemistry
Wen J, Liao H, Stachowski K, et al. (2020) Rational design of cell-permeable cyclic peptides containing a d-Pro-l-Pro motif. Bioorganic & Medicinal Chemistry. 28: 115711
Unnikrishnan A, Amero C, Yadav DK, et al. (2020) DNA binding induces a -to- switch in Cre recombinase to enable intasome assembly. Proceedings of the National Academy of Sciences of the United States of America
Holmquist M, Ihms EC, Gollnick P, et al. (2020) Population distributions from native mass spectrometry titrations reveal nearest-neighbor cooperativity in the ring-shaped oligomeric protein TRAP. Biochemistry
Unnikrishnan A, Amero C, Foster M. (2018) Protein Dynamics Underlie Cre-loxp DNA Recombination Biophysical Journal. 114
Danhart EM, Bakhtina M, Cantara WA, et al. (2017) Conformational and chemical selection by a trans-acting editing domain. Proceedings of the National Academy of Sciences of the United States of America
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