C. Denise Okafor - Publications

Affiliations: 
Georgia Institute of Technology and Emory University, Atlanta, GA, United States 
Area:
Biochemistry, computational modeling

13 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2020 Tillman MC, Imai N, Li Y, Khadka M, Okafor CD, Juneja P, Adhiyaman A, Hagen SJ, Cohen DE, Ortlund EA. Allosteric regulation of thioesterase superfamily member 1 by lipid sensor domain binding fatty acids and lysophosphatidylcholine. Proceedings of the National Academy of Sciences of the United States of America. PMID 32820071 DOI: 10.1073/Pnas.2003877117  0.4
2020 Guth-Metzler R, Bray MS, Frenkel-Pinter M, Suttapitugsakul S, Montllor-Albalate C, Bowman JC, Wu R, Reddi AR, Okafor CD, Glass JB, Williams LD. Cutting in-line with iron: ribosomal function and non-oxidative RNA cleavage. Nucleic Acids Research. PMID 32663277 DOI: 10.1093/Nar/Gkaa586  0.68
2019 Okafor CD, Hercules D, Kell SA, Ortlund EA. Rewiring Ancient Residue Interaction Networks Drove the Evolution of Specificity in Steroid Receptors. Structure (London, England : 1993). PMID 31831214 DOI: 10.1016/J.Str.2019.11.012  0.4
2018 Frank F, Okafor CD, Ortlund EA. The first crystal structure of a DNA-free nuclear receptor DNA binding domain sheds light on DNA-driven allostery in the glucocorticoid receptor. Scientific Reports. 8: 13497. PMID 30201977 DOI: 10.1038/S41598-018-31812-9  0.4
2018 Okafor CD, Pathak MC, Fagan CE, Bauer NC, Cole MF, Gaucher EA, Ortlund EA. Structural and Dynamics Comparison of Thermostability in Ancient, Modern, and Consensus Elongation Factor Tus. Structure (London, England : 1993). 26: 118-129.e3. PMID 29276038 DOI: 10.1016/J.Str.2017.11.018  0.4
2017 Weikum ER, Okafor DC, D'Agostino EH, Colucci JK, Ortlund EA. Structural analysis of the glucocorticoid receptor ligand-binding domain in complex with triamcinolone acetonide and a fragment of the atypical coregulator, SHP. Molecular Pharmacology. PMID 28396564 DOI: 10.1124/Mol.117.108506  0.72
2017 Mays SG, Okafor CD, Tuntland ML, Whitby RJ, Dharmarajan V, Stec J, Griffin PR, Ortlund EA. Structure and Dynamics of the Liver Receptor Homolog 1-PGC1α Complex. Molecular Pharmacology. PMID 28363985 DOI: 10.1124/Mol.117.108514  0.4
2017 Okafor CD, Lanier KA, Petrov AS, Athavale SS, Bowman JC, Hud NV, Williams LD. Iron mediates catalysis of nucleic acid processing enzymes: support for Fe(II) as a cofactor before the great oxidation event. Nucleic Acids Research. PMID 28334877 DOI: 10.1093/Nar/Gkx171  0.68
2016 Mays SG, Okafor CD, Whitby RJ, Goswami D, Stec JO, Flynn AR, Dugan MC, Jui NT, Griffin PR, Ortlund EA. Crystal Structures of the Nuclear Receptor, Liver Receptor Homolog 1, Bound to Synthetic Agonists Reveal a Novel Mechanism of Activation. The Journal of Biological Chemistry. PMID 27694446 DOI: 10.1074/Jbc.M116.753541  0.4
2016 Gulen B, Petrov AS, Okafor CD, Vander Wood D, O'Neill EB, Hud NV, Williams LD. Ribosomal small subunit domains radiate from a central core. Scientific Reports. 6: 20885. PMID 26876483 DOI: 10.1038/Srep20885  0.64
2013 Hsiao C, Chou IC, Okafor CD, Bowman JC, O'Neill EB, Athavale SS, Petrov AS, Hud NV, Wartell RM, Harvey SC, Williams LD. RNA with iron(II) as a cofactor catalyses electron transfer. Nature Chemistry. 5: 525-8. PMID 23695635 DOI: 10.1038/Nchem.1649  0.64
2012 Petrov AS, Bernier CR, Hsiao C, Okafor CD, Tannenbaum E, Stern J, Gaucher E, Schneider D, Hud NV, Harvey SC, Williams LD. RNA-magnesium-protein interactions in large ribosomal subunit. The Journal of Physical Chemistry. B. 116: 8113-20. PMID 22712611 DOI: 10.1021/Jp304723W  0.64
2012 Engelhart AE, Cafferty BJ, Okafor CD, Chen MC, Williams LD, Lynn DG, Hud NV. Nonenzymatic ligation of DNA with a reversible step and a final linkage that can be used in PCR. Chembiochem : a European Journal of Chemical Biology. 13: 1121-4. PMID 22556064 DOI: 10.1002/Cbic.201200167  0.64
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