Eric J. Toone - Related publications

Affiliations: 
Chemistry Duke University, Durham, NC 
Area:
biocatalysis/applied enzymology, ligand binding and the activity of water, and the synthesis of novel donors of nitric oxide
Website:
http://fds.duke.edu/db/aas/Chemistry/faculty/eric.toone
NOTE: We are testing a new system for identifying relevant work based on semantic analysis that identifies similarities between recently published papers and the current author's publications. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches.
18 most relevant papers in past 60 days:
Year Citation  Score
2022 Oluyemi WM, Samuel BB, Adewumi AT, Adekunle YA, Soliman MES, Krenn L. An Allosteric Inhibitory Potential of Triterpenes from Combretum racemosum on the Structural and Functional Dynamics of Plasmodium falciparum Lactate Dehydrogenase Binding Landscape. Chemistry & Biodiversity. e202100646. PMID 34982514 DOI: 10.1002/cbdv.202100646   
2022 Qu G, Sun Z. In Silico Prediction Methods for Site-Saturation Mutagenesis. Methods in Molecular Biology (Clifton, N.J.). 2397: 49-69. PMID 34813059 DOI: 10.1007/978-1-0716-1826-4_4   
2022 Mouchlis VD, Hayashi D, Vasquez AM, Cao J, McCammon JA, Dennis EA. Lipoprotein-associated phospholipase A: A paradigm for allosteric regulation by membranes. Proceedings of the National Academy of Sciences of the United States of America. 119. PMID 34996868 DOI: 10.1073/pnas.2102953118   
2022 Mohamed Abdelahi MM, El Bakri Y, Lai CH, Subramani K, Anouar EH, Ahmad S, Benchidmi M, Mague JT, Popović-Djordjević J, Goumri-Said S. Novel 3-chloro-6-nitro-1-indazole derivatives as promising antileishmanial candidates: synthesis, biological activity, and molecular modelling studies. Journal of Enzyme Inhibition and Medicinal Chemistry. 37: 151-167. PMID 34894940 DOI: 10.1080/14756366.2021.1995380   
2022 Vishnu Priya B, Sreenivasa Rao DH, Gilani R, Lata S, Rai N, Akif M, Kumar Padhi S. Enzyme engineering improves catalytic efficiency and enantioselectivity of hydroxynitrile lyase for promiscuous retro-nitroaldolase activity. Bioorganic Chemistry. 120: 105594. PMID 35007952 DOI: 10.1016/j.bioorg.2021.105594   
2022 Nagar M, Hayden JA, Sagey E, Worthen G, Park M, Sharma AN, Fetter CM, Kuehm OP, Bearne SL. Altering the binding determinant on the interdigitating loop of mandelate racemase shifts specificity towards that of d-tartrate dehydratase. Archives of Biochemistry and Biophysics. 109119. PMID 35016855 DOI: 10.1016/j.abb.2022.109119   
2022 Kumar M, Tripathi MK, Gupta D, Kumar S, Biswas NR, Ethayathulla AS, Kaur P. N-acetylglucosamine-phosphatidylinositol de-N-acetylase as a novel target for probing potential inhibitor against . Journal of Biomolecular Structure & Dynamics. 1-15. PMID 35014594 DOI: 10.1080/07391102.2021.2025429   
2022 Ma Y, Zhang M, Deng Z, Wang X, Huang H, Yang K, Yuan B, Liu Y, Kang Z. Chiral carbon dots - a functional domain for tyrosinase Cu active site modulation remote target interaction. Nanoscale. PMID 34989754 DOI: 10.1039/d1nr07236f   
2022 Aknin K, Bontemps A, Farce A, Merlet E, Belmont P, Helissey P, Chavatte P, Sari MA, Giorgi-Renault S, Desbène-Finck S. Polycyclic nitrogen heterocycles as potential thymidine phosphorylase inhibitors: synthesis, biological evaluation, and molecular docking study. Journal of Enzyme Inhibition and Medicinal Chemistry. 37: 252-268. PMID 34933639 DOI: 10.1080/14756366.2021.2001806   
2022 Lee JH, Kim S, Jin MS, Kim YC. Discovery of substituted indole derivatives as allosteric inhibitors of m A-RNA methyltransferase, METTL3-14 complex. Drug Development Research. PMID 35040501 DOI: 10.1002/ddr.21910   
2022 Mukhametgalieva AR, Lushchekina SV, Aglyamova AR, Masson P. Steady-state kinetic analysis of human cholinesterases over wide concentration ranges of competing substrates. Biochimica Et Biophysica Acta. Proteins and Proteomics. 1870: 140733. PMID 34662731 DOI: 10.1016/j.bbapap.2021.140733   
2022 Ye C, Zhang R, Dong L, Chi J, Huang F, Dong L, Zhang M, Jia X. α-Glucosidase inhibitors from brown rice bound phenolics extracts (BRBPE): Identification and mechanism. Food Chemistry. 372: 131306. PMID 34638069 DOI: 10.1016/j.foodchem.2021.131306   
2022 Song C, Wu M, Zhang Y, Li J, Yang J, Wei D, Li H, Guo L, Qin J. Bioactive Monomer and Polymer Polyketides from Edible Mushroom as Glutamate Dehydrogenase Inhibitors and Antioxidants. Journal of Agricultural and Food Chemistry. PMID 35029386 DOI: 10.1021/acs.jafc.1c07119   
2022 Holmes JB, Liu V, Caulkins BG, Hilario E, Ghosh RK, Drago VN, Young RP, Romero JA, Gill AD, Bogie PM, Paulino J, Wang X, Riviere G, Bosken YK, Struppe J, et al. Imaging active site chemistry and protonation states: NMR crystallography of the tryptophan synthase α-aminoacrylate intermediate. Proceedings of the National Academy of Sciences of the United States of America. 119. PMID 34996869 DOI: 10.1073/pnas.2109235119   
2022 Zhuge XL, Xie T, Du X, Zhang XX, Hu JP, Yang HL. Non-synonymous substitution of evolutionarily conserved residue in Tau class glutathione transferases alters structural and catalytic features. International Journal of Biological Macromolecules. 197: 39-48. PMID 34896469 DOI: 10.1016/j.ijbiomac.2021.12.040   
2022 Tariq M, Ozbek P, Moin ST. Hydration modulates oxygen channel residues for oxygenation of cysteine dioxygenase: Perspectives from molecular dynamics simulations. Journal of Molecular Graphics & Modelling. 110: 108060. PMID 34768230 DOI: 10.1016/j.jmgm.2021.108060   
2022 Li Y, Song S, Li Y, Du F, Li S, Li J. Novel insights into the inhibitory mechanism of (+)-catechin against trimethylamine-N-oxide demethylase. Food Chemistry. 373: 131559. PMID 34815113 DOI: 10.1016/j.foodchem.2021.131559   
2022 García-García A, Rojas S, Rivas-García L, Navarro-Hortal MD, Romero-Márquez JM, Fernández-Bolaños JG, Choquesillo-Lazarte D, Salinas-Castillo A, López Ó, Quiles JL, Rodríguez-Diéguez A. A gliclazide complex based on palladium towards Alzheimer's disease: promising protective activity against Aβ-induced toxicity in . Chemical Communications (Cambridge, England). PMID 34994366 DOI: 10.1039/d1cc04404d