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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
  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
  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
  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


  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
  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


  Formate production through biocatalysis.

Alissandratos A., Kim H.-K., Easton C.J.

Bioengineered (2013), 4(5), 348–350.   DOI: 10.4161/bioe.25360
  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
  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
  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
  Beckwith memorial symposium on free radical chemistry.

Easton C.J.

Aust. J. Chem. (2013), 66(3), 284–285.   DOI: 10.1071/CH13085
  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
  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
  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.   
  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


  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.   
  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
  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
  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
  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
  Cross-links between soy protein residues and urea formaldehyde resins.

Philbrook A., Earnshaw S., Easton C.J.

Polym. Prepr. (2012), 53(1), 667–668.   
  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
  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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