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2015
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Hydrogen-atom abstraction from a model amino acid: dependence on the attacking radical.
Amos R.I.J., Chan B., Easton C.J., Radom L.
J. Phys. Chem. B (2015), 119(3), 783-788. DOI: 10.1021/jp505217q
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X-ray structure of the amidase domain of AtzF, the allophanate hydrolase from the cyanuric acid-mineralizing multienzyme complex.
Balotra S., Newman J., Cowieson N.P., French N.G., Campbell P.M., Briggs L.J., Warden A.C., Easton C.J., Peat T.S., Scott C.
Appl. Environ. Microbiol. (2015), 8(2), 470-480. DOI: 10.1128/AEM.02783-14
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Biosynthetic incorporation of fluorinated amino acids into peptides and proteins.
Fraser S.A., Easton C.J.
Aust. J. Chem. (2015), 68(1), 9-12. DOI: 10.1071/CH14356
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Outcome-changing effect of polarity reversal in hydrogen-atom-abstraction reactions.
Chan, B., Radom, L., Easton, C.J.
J. Phys. Chem. A (2015), 119(16), 3843-3847. 10.1021/acs.jpca.5b01890
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2014
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Hydrogen from formic acid through its selective disproportionation over
sodium germinate – a non-transition-metal catalysis system.
Amos R.I.J., Heinroth F., Chan B., Zheng S., Haynes B.S., Easton C.J., Masters A.F., Radom L., Maschmeyer T.
Angew. Chem. Int. Ed. (2014), 53(42), 11275–11279. DOI: 10.1002/anie.201405360
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Formate production through carbon dioxide hydrogenation with recombinant whole cell biocatalysts.
Alissandratos A., Kim H.-K., Easton C.J.
Bioresour. Technol. (2014), 164, 7–11. DOI: 10.1016/j.biortech.2014.04.064
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2013
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Formate production through biocatalysis.
Alissandratos A., Kim H.-K., Easton C.J.
Bioengineered (2013), 4(5), 348–350. DOI: 10.4161/bioe.25360
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Clostridium carboxidivorans strain P7T recombinant formate dehydrogenase catalyzes reduction of CO2 to formate.
Alissandratos A., Kim H.-K., Matthews H., Hennessy J.E., Philbrook A., Easton C.J.
PAppl. Environ. Microbiol. (2013), 79(2), 741–744. DOI: 10.1128/AEM.02886-12
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In situ deprotection and incorporation of unnatural amino acids during cell-free protein synthesis.
Arthur I.N., Hennessy J.E., Padmakshan D., Stigers D.J., Lesturgez S., Fraser S.A., Liutkus M., Otting G., Oakeshott J.G., Easton C.J.
Chem. Eur. J. (2013), 19(21), 6824–6830 DOI: 10.1002/chem.201203923
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Production and regulation of levels of amidated peptide hormones.
Cao F., Easton C.J.
Aust. J. Chem. (2013), 66(3), 297–307. DOI: 10.1071/CH12546
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Beckwith memorial symposium on free radical chemistry.
Easton C.J.
Aust. J. Chem. (2013), 66(3), 284–285. DOI: 10.1071/CH13085
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Complexation of crystal violet, pyronine B, and rhodamine B by linked β-cyclodextrin trimers.
Nguyen H.-T., Pham D.-T., Easton C.J., Lincoln S.F.
Aust. J. Chem. (2013), 66(9), 1057–1064. DOI: 10.1071/CH13172
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Host-guest chemistry of linked β-cyclodextrin trimers and adamantyl substituted poly(acrylate)s in aqueous solution.
Nguyen H.-T., Pham D.-T., Lincoln S.F., Wang J., Guo X., Easton C.J., Prud’homme R.K.
Polym. Chem. (2013), 4(3), 820–829. DOI: 10.1039/c2py20746j
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Biochemical processes for generating fuels and commodity chemicals from lignocellulosic biomass.
Philbrook A., Alissandratos A., Easton C.J.
Environmental Biotechnology – New Approaches and Prospective Applications. Petre M., ed., InTech: Rijeka, Croatia (2013), Chapter 3, pp. 39–64.
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Co-polymerization analysis of thermosetting resins using 1H-15N-13C triple resonance NMR spectroscopy.
Philbrook A., Earnshaw S., Easton C.J., Keniry M.A., Latter M.J.
J. Appl. Polym. Sci. (2013), 128(5), 3375–3381. DOI: 10.1002/app.38516
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2012
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Carbamate kinases from hyperthermophilic bacteria and their use for producing carbamoyl phosphate and urea.
Hennessy J.E., Philbrook A., Bartkus D.M., Easton C.J., Scott C., Oakeshott J.G., Kim H.-K., Latter M.J.
International Patent No. WO2012171070 A1. (2012), 64 pp.
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Reactivities of amino acid derivatives toward hydrogen abstraction by Cl• and OH•.
Chan B., O’Reilly R.J., Easton C.J., Radom L.
J. Org. Chem. (2012), 77(21), 9807–9812. DOI: 10.1021/jo3021538
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Prohormone-substrate peptide sequence recognition by peptidylglycine α-amidating monooxygenase and its reflection in increased glycolate inhibitor potency.
Morris K.M., Cao F., Onagi H., Altamore T.M., Gamble A.B., Easton C.J.
Bioorg. Med. Chem. Lett. (2012), 22(23), 7015–7018. DOI: 10.1016/j.bmcl.2012.10.004
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Cofactor promiscuity among F420-dependent reductases enables them to catalyse both oxidation and reduction of the same substrate.
Lapalikar G.V., Taylor M.C., Warden A.C., Onagi H., Hennessy J.E., Mulder R.J., Scott C., Brown S.E., Russell R.J., Easton C.J., Oakeshott J.G.
Catal. Sci. Technol. (2012), 2(8), 1560–1567. DOI: 10.1039/c2cy20129a
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Incorporation of guanidine and ethylguanidine into thermosetting resins.
Muirhead K., Earnshaw S., Easton C.J., Philbrook A.
J. Appl. Polym. Sci. (2012), 125(S2), E372–E377. DOI: 10.1002/app.36819
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Cross-links between soy protein residues and urea formaldehyde resins.
Philbrook A., Earnshaw S., Easton C.J.
Polym. Prepr. (2012), 53(1), 667–668.
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Specific binding of a β-cyclodextrin dimer to the amyloid β peptide modulates the peptide aggregation process.
Wahlström A., Cukalevski R., Danielsson J., Jarvet J., Onagi H., Rebek J., Linse S., Gräslund A.
Biochemistry (2012), 51(21), 4280–4289. DOI: 10.1021/bi300341j
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Substrate-induced conformational change and isomerase activity of dienelactone hydrolase and its site-specific mutants.
Walker I., Hennessy J.E., Ollis D.L., Easton C.J.
ChemBioChem. (2012), 13(11), 1645–1651. DOI: 10.1002/cbic.201200232
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