Publications


For an up-to-date list of Jackson Lab publications – click here to view Colin Jackson’s Google Scholar Publication Page. 

Google_Scholar_logo_2015


2019

Bashiri, G., Antoney, J., Jirgis, E. N. M., Shah, M. V., Ney, B., Copp, J., … Jackson, C. J. (2019). A revised biosynthetic pathway for the cofactor F420 in prokaryotes. Nature Communications, 10(1), 1558. https://doi.org/10.1038/s41467-019-09534-x

JA Kaczmarski, JA Mitchell, MA Spence, V Vongsouthi, CJ Jackson. (2019) Structural and evolutionary approaches to the design and optimization of fluorescence-based small molecule biosensors. Current opinion in structural biology 57, 31-38

Florian Baier, Nansook Hong, Gloria Yang, Anna Pabis, Charlotte M Miton, Alexandre Barrozo, Paul D Carr, Shina CL Kamerlin, Colin J Jackson, Nobuhiko Tokuriki (2019) Cryptic genetic variation shapes the adaptive evolutionary potential of enzymes. eLife 8, e40789

David C Thorn, Aidan B Grosas, Peter D Mabbitt, Nicholas J Ray, Colin J Jackson, John A Carver (2019) The Structure and Stability of the Disulfide-Linked γS-Crystallin Dimer Provide Insight into Oxidation Products Associated with Lens Cataract Formation. Journal of molecular biology 431 (3), 483-497

T Izoré, J Tailhades, MH Hansen, JA Kaczmarski, CJ Jackson, MJ Cryle (2019). Drosophila melanogaster nonribosomal peptide synthetase Ebony encodes an atypical condensation domain. Proceedings of the National Academy of Sciences, 201811194

Hopkins, D. H., Rane, R. V., Younus, F., Coppin, C. W., Pandey, G., Jackson, C. J., & Oakeshott, J. G. (2019). The molecular basis for the neofunctionalization of the juvenile hormone esterase duplication in Drosophila. Insect Biochemistry and Molecular Biology. https://doi.org/10.1016/j.ibmb.2019.01.001

2018

Harold, L. K., Antoney, J., Ahmed, F. H., Hards, K., Carr, P. D., Rapson, T., … Cook, G. M. (2018). FAD-sequestering proteins protect mycobacteria against hypoxic and oxidative stress. The Journal of Biological Chemistry. https://doi.org/10.1074/jbc.RA118.006237

Hong, N.-S., Petrović, D., Lee, R., Gryn’ova, G., Purg, M., Saunders, J., Bauer, P., Carr, P. D., Lin, C.-Y., Mabbitt, P. D., Zhang, W., Altamore, T., Easton, C., Coote, M. L., Kamerlin, S. C. L. and Jackson, C. J. (2018) ‘The evolution of multiple active site configurations in a designed enzyme’, Nature Communications, 9(1), p. 3900. doi: 10.1038/s41467-018-06305-y.

94. Zhang, W. H., Herde, M. K., Mitchell, J. A., Whitfield, J. H., Wulff, A. B., Vongsouthi, V., Sanchez-Romero, I., Gulakova, P. E., Minge, D., Breithausen, B., Schoch, S., Janovjak, H., Jackson, C. J. and Henneberger, C. (2018) ‘Monitoring hippocampal glycine with the computationally designed optical sensor GlyFS’, Nature Chemical Biology. doi: 10.1038/s41589-018-0108-2.

93. Kirk, J., Huber, T., & Jackson, C. J. (2018). Chapter 6: Modulating Enzyme Activity via Incorporation of Non-canonical Amino Acids. In G. Williams & M. Hall (Eds.), Modern Biocatalysis: Advances Towards Synthetic Biological Systems (pp. 153–177). The Royal Society of Chemistry. https://doi.org/10.1039/9781788010450-00153

92. Campbell, E. C., Grant, J., Wang, Y., Sandhu, M., Williams, R. J., Nisbet, D. R., Perriman, A. W., Lupton, D. W. and Jackson, C. J. (2018) ‘Hydrogel-Immobilized Supercharged Proteins’, Advanced Biosystems. Wiley-Blackwell, p. 1700240. doi: 10.1002/adbi.201700240.

91. BE Clifton, JA Kaczmarski, PD Carr, ML Gerth, N Tokuriki, CJ Jackson. (2018). Evolution of cyclohexadienyl dehydratase from an ancestral solute-binding protein.Nature Chemical Biology. 

90. Campbell, E., Correy, G., Mabbitt, P., Buckle, A., Tokuriki, N., Jackson, C. (2018). Laboratory evolution of protein conformational dynamics. Current Opinion in Structural Biology, 50, 49–57. DOI: 10.1016/j.sbi.2017.09.005


2017

89. Ney, B., Carere, C., Sparling, R., Jirapanjawat, T., Stott, M., Jackson, C., … Greening, C. (2017). Cofactor tail length modulates catalysis of bacterial F420-dependent oxidoreductases. Frontiers in Microbiology, 8, 1902. https://doi.org/10.3389/FMICB.2017.01902

88.  Hopkins, D. H., Fraser, N. J., Mabbitt, P. D., Carr, P. D., Oakeshott, J. G., & Jackson, C. J. (2017). Structure of an insecticide sequestering carboxylesterase from the disease vector Culex quinquefasciatus: what makes an enzyme a good insecticide sponge? Biochemistry, acs.biochem.7b00774. https://doi.org/10.1021/acs.biochem.7b00774

87. Correy, G., Zaidman, D., Carvalho, S., Mabbitt, P. D., James, P. J., Kotze, A. C., … Jackson, C. J. (2017). Overcoming insecticide resistance through computational inhibitor design. bioRxiv (Pre-print). Retrieved from http://biorxiv.org/content/early/2017/07/10/161430.abstract

86. Buckler, J. N., Taher, E. S., Fraser, N. J., Willis, C., Carr, P. D., Jackson, C. J., … Banwell, M. G. (2017). The Synthesis of Certain Derivatives and Analogues of (–) – and ( + ) -Galanthamine and an Assessment of their Capacities to Inhibit Acetylcholine Esterase an Assessment of their Capacities to Inhibit Acetylcholine Esterase. https://doi.org/10.1021/acs.joc.7b01062

85. Banwell, M., Xu, X., Kim, H.-S., Chen, W.-M., Ma, X., Correy, G. J., … Carr, P. D. (2017). Total Syntheses of the Amaryllidaceae Alkaloids Zephycandidine III and Lycosinine A and Their Evaluation as Inhibitors of Acetylcholinesterase. European Journal of Organic Chemistry. https://doi.org/10.1002/ejoc.201700705

84. Clifton, B. E., Kaczmarski, J. A., Carr, P. D., Gerth, M. L., Tokuriki, N., Jackson, C. J. (2017) Evolution of an enzyme from a solute-binding protein. Preprint available on bioRxiv: https://doi.org/10.1101/157495.

83. Greening, C., Jirapanjawat, T., Afroze, S., Ney, B., Scott, C., Pandey, G., Lee, B. M., Russell, R. J., Jackson, C. J., Oakeshott, J. G., Taylor, M. C., Warden, A. C. (2017) Mycobacterial F420H2-dependent reductases promiscuously reduce diverse compounds through a common mechanism. Frontiers in Microbiology. doi: 10.3389/fmicb.2017.01000

82. Rouet, R., Langley, D. B., Schofield, P., Christie, M., Roome, B., Porebski, B. T., … Christ, D. (2017). Structural reconstruction of protein ancestry. Proceedings of the National Academy of Sciences, 114(15), 3897–3902. https://doi.org/10.1073/PNAS.1613477114

81. Sugrue, E., Hartley, C. J., Scott, C., & Jackson, C. J. (2016). The evolution of new catalytic mechanisms for xenobiotic hydrolysis in bacterial metalloenzymes. Australian Journal of Chemistry, 69(12), 1383–1395. https://doi.org/10.1071/CH16426

80. Faisal Younus, Nicholas J. Fraser, Chris W. Coppin, Jian-Wei Liu, Galen J. Correy, Thomas Chertemps, Gunjan Pandey, Martine Maïbèche, Colin J. Jackson, J. G. O. (2017). Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in. Scientific Reports, (April), 1–12. https://doi.org/10.1038/srep46188

79. Fisher, C. R., Kaczmarski, J. A., Sutton, H. J., Clifton, B., Cai, Y., Dups, J. N., … Cockburn, I. A. (2017). Multivalency drives the neutralizing activity of antibodies against the Plasmodium falciparum circumsporozoite protein. bioRxiv (Pre-Print). https://doi.org/https://doi.org/10.1101/108746

78. Clifton, B. E., Whitfield, J. H., Sanchez-Romero, I., Herde, M. K., Henneberger, C., Janovjak, H., & Jackson, C. J. (2017). Ancestral Protein Reconstruction and Circular Permutation for Improving the Stability and Dynamic Range of FRET Sensors. In V. Stein (Ed.), Synthetic Protein Switches: Methods and Protocols (pp. 71–87). New York, NY: Springer New York. https://doi.org/10.1007/978-1-4939-6940-1_5

77. Mitchell, J. A., Zhang, W. H., Herde, M. K., Henneberger, C., Janovjak, H., O’Mara, M. L., & Jackson, C. J. (2017). Method for Developing Optical Sensors Using a Synthetic Dye-Fluorescent Protein FRET Pair and Computational Modeling and Assessment. In V. Stein (Ed.), Synthetic Protein Switches: Methods and Protocols (pp. 89–99). New York, NY: Springer New York. https://doi.org/10.1007/978-1-4939-6940-1_6

76. Sugrue, E., Scott, C., & Jackson, C. J. (2017). Constrained evolution of a bispecific enzyme: lessons for biocatalyst design. Org. Biomol. Chem., 15, 937–946. https://doi.org/10.1039/C6OB02355J


2016

75. Mohamed, A.E., Condic-Jurkic, K., Ahmed, F.H., Yuan, P., O’Mara, M.L., Jackson, C.J., Coote, M.L. (2016) Hydrophobic shielding drives catalysis of hydride transfer in a family of F420H2-dependent enzymes. Biochemistry. doi: 10.1021/acs.biochem.6b00683.

74. Mitchell, J.A.*, Whitfield, J.H.*, Zhang, W.H.*, Henneberger, C., Janovjak, H., O’Mara, M.L., Jackson, C.J. (2016) Rangefinder: a semisynthetic FRET sensor design algorithm. ACS Sens. doi: 10.1021/acssensors.6b00576. *contributed equally.

73. Sugrue, E.S, Carr, P.D., Scott, C., Jackson, C.J. (2016) Active site desolvation and thermostability tradeoffs in the evolution of catalytically diverse triazine hydrolases. Biochemistry. doi: 10.1021/acs.biochem.6b00731.

72. Li, D., Moorman, R., Vanhercke, T., Petrie, J., Singh, S., Jackson, C.J. (2016) Classification and substrate head-group specificity of membrane fatty acid desaturases. Comput. Struct. Biotechnol. J. 14, 341-349. doi: 10.1016/j.csbj.2016.08.003.

71. Jirapanjawat, T., Ney, B., Taylor, M.C., Warden, A.C., Afroze, S., Russell, R.J., Lee, B.M., Jackson, C.J., Oakeshott, J.G., Pandey, G., Greening, C. (2016) The redox cofactor F420 protects mycobacteria from diverse antimicrobial compounds and mediates a reductive detoxification system. Appl. Environ. Microbiol.  doi: 10.1128/AEM.02500-16.

70. Campbell, E.C., Kaltenbach, M., Correy, G.J., Carr, P.D., Porebski, B.T., Livingstone, E.K., Afriat-Jurnou, L., Buckle, A.M., Weik, M., Hollfelder, F., Tokuriki, N., Jackson, C.J. (2016) The role of protein dynamics in the evolution of new enzyme function. Nat. Chem. Biol. 12, 944-950. doi: 10.1038/nchembio.2175.

69. Sugure, E.S., Hartley, C.J., Scott, C., Jackson, C.J. (2016) The evolution of new catalytic mechanisms for xenobiotic hydrolysis in bacterial metalloenzymes. Aust. J. Chem. . doi: 10.1071/CH16426.

68. Ney, B.*, Ahmed, F.H.*, Carere, C.R., Biswas, A., Warden, A.C., Morales, S.E., Pandey, G., Watt, S.J., Oakeshott, J.G., Taylor, M.C., Stott, M.B., Jackson, C.J., Greening, C. (2016) The methanogenic redox cofactor F420 is widely synthesized by aerobic soil bacteria. ISME J. doi: 10.1038/ismej.2016.100. *contributed equally.

67. Yang, G.*, Hong, N.*, Baier, F., Jackson, C.J., Tokuriki, N. (2016) Conformational tinkering drives evolution of a promiscuous activity through indirect mutational effects. Biochemistry. doi: 10.1021/acs.biochem.6b00561.*contributed equally.

66. Chan, K.X., Mabbitt, P.D., Phua, S.Y., Mueller, J.W., Nisar, N., Gigolashvili, T., Stroeher, E., Grassl, J., Arlt, W., Estavillo, G.M., Jackson, C.J., Pogson, B.J. (2016) Sensing and signaling of oxidative stress in chloroplasts by inactivation of the SAL1 phosphoadenosine phosphatase. Proc. Natl. Acad. Sci. doi: 10.1073/pnas.1604936113.

65. Ahmed, F.H., Mohamed, A.E., Carr, P.D., Lee, B.M., Condic-Jurkic, K., O’Mara, M.L., Jackson, C.J. (2016) Rv2074 is a novel F420H2-dependent biliverdin reductase in Mycobacterium tuberculosis. Protein Sci. 25(9), 1692-709. doi: 10.1002/pro.2975.

64. Correy, G.J., Carr, P.D., Meirelles, T., Mabbitt, P.D., Fraser, N.J., Weik, M., Jackson, C.J. (2016) Mapping the accessible conformational landscape of an insect carboxylesterase using kinetic crystallography and conformational ensemble analysis. Structure 24, 977-987. doi: 10.1016/j.str.2016.04.009.

63. Horgan, C.C., Han, Y.-S., Trueman, H., Jackson, C.J., Sutherland, T.D., Rapson, T.D. (2016) Phosphorescent oxygen-sensing and singlet oxygen production by a biosynthetic silk. RSC Adv. 6, 39530-39533. doi: 10.1039/C6RA03731C. (open access)

62. Greening, C.*, Ahmed, F.H.*, Mohamed, A.E., Lee, B., Pandey, G., Warden, A., Scott, C., Oakeshott, J.G., Taylor, M., Jackson, C.J. (2016) F420- and Fo-dependent redox reactions: physiology, biochemistry, and applications. Microbiol. Mol. Biol. Rev. 80, 429-450. doi: 10.1128/MMBR.00070-15. *contributed equally.

61. Fraser, N.J., Liu, J.W., Mabbitt, P.D., Correy, G.J., Coppin, C.W., Lethier, M., Perugini, M.A., Murphy, J.M., Oakeshott, J.G., Weik, M., Jackson, C.J. (2016) Evolution of protein quaternary structure in response to selective pressure for increased thermostability. J. Mol. Biol. 428, 2359-2371. doi: 10.1016/j.jmb.2016.03.014

60. Mabbitt, P.D.*, Correy, G.J.*, Meirelles, T., Fraser, N.J., Coote, M.L., Jackson, C.J. (2016) Conformational disorganization within the active site of a recently evolved organophosphate hydrolase limits its catalytic efficiency. Biochemistry 55, 1408-1417. doi: 10.1021/acs.biochem.5b01322. *contributed equally.

59. Mohamed, A.E., Ahmed, F.H., Arulmozhiraja, S., Lin, C.Y., Taylor, M.C., Krausz, E.R., Jackson, C.J., Coote, M.L. (2016) Protonation state of F420H2 in the prodrug-activating deazaflavin dependent nitroreductase (Ddn) from Mycobacterium tuberculosis. Mol. BioSyst. 12, 1110-1113. doi: 10.1039/C6MB00033A.

58. Clifton, B.E., Jackson, C.J. (2016) Ancestral protein reconstruction yields insights into adaptive evolution of binding specificity in solute-binding proteins, Cell Chem. Biol. 23, 236-245. doi: 10.1016/j.chembiol.2015.12.010.


2015

57. Ahmed, F.H., Carr, P.D., Lee, B.M., Afriat-Jurnou, L., Mohamed, A.E., Hong, N.-S., Flanagan, J., Taylor, M.C., Greening, C., Jackson, C.J. (2015) Sequence-structure-function classification of a catalytically diverse oxidoreductase superfamily in mycobacteria. J. Mol. Biol. 427, 3554-3571. doi: 10.1016/j.jmb.2015.09.021.

56. Riley, B.T., Broendum, S.S., Reboul, C.F., Cowieson, N.P., Costa, M.G.S., Kass, I., Jackson, C.J., Perahia, D., Buckle, A.M., McGowan, S. (2015) Dynamic motion and communication in the streptococcal C1 phage lysin, PlyC. PLoS One 10, e0140219. doi: 10.1371/journal.pone.0140219. (open access)

55. Greening, C., Biswas, A., Carere, C.R., Jackson, C.J., Taylor, M.C., Stott, M.B., Cook, G.M., Morales, S.E. (2015) Genomic and metagenomic surveys of hydrogenase distribution indicate H2 is a widely utilised energy source for microbial growth and survival. ISME J. doi: 10.1038/ismej.2015.153.

54. Kaltenbach, M., Jackson, C.J. Campbell, E.C., Hollfelder, F., Tokuriki, N. (2015) Reverse evolution leads to genotypic incompatibility despite functional and active-site convergence. eLife 4, e06492. doi: 10.7554/eLife.06492. (open access)

53. Whitfield, J.H., Zhang, W.H., Herde, M.K., Clifton, B.E., Radziejewski, J., Janovjak, H., Henneberger, C., Jackson, C.J. (2015) Construction of a robust and sensitive arginine biosensor through ancestral protein reconstruction. Protein Sci. 24, 1412-1422. doi: 10.1002/pro.2721.

52. Van Benschoten, A.H., Afonine, P.V., Terwilliger, T.C., Wall, M.E., Jackson, C.J., Sauter, N.K., Adams, P.D., Urzhumtsev, A., Fraser, J.S. (2015) Predicting X-ray diffuse scattering from translation-libration-screw structural ensembles. Acta Crystallogr. D Biol. Crystallogr. 71, 1657-1667. doi: 10.1107/S1399004715007415

51. Sugrue, E., Fraser, N.J., Hopkins, D.H., Carr, P.D., Khurana, J.L., Oakeshott, J.G., Scott, C., Jackson, C.J. (2015) Evolutionary expansion of the amidohydrolase superfamily in bacteria in response to synthetic compounds: the molinate and diuron hydrolases. Appl. Environ. Microbiol. 71, 2612-2624. doi: 10.1128/AEM.04016-14.


2014

50. Carruthers, T.J., Carr, P.D., Loh, C.T., Jackson, C.J., Otting, G. (2014) Iron(III) located in the dinuclear metallo-β-lactamase IMP-1 by pseudocontact shifts. Angew. Chem. Int. Ed. 53, 14269-14272. doi: 10.1002/anie.201408693.

49. Tokuriki N., Jackson C.J. (2014) Enzyme dynamics and engineering: one step at a time. Chem. Biol.21, 1259-1260. doi: 10.1016/j.chembiol.2014.10.003.

48. Lan P., Jackson C.J., Banwell M.G., Willis A.C. (2014) Synthesis of a D-ring isomer of galanthamine via a radical-based Smiles rearrangement reaction. J. Org. Chem.  79, 6759-64. doi: 10.1021/jo501255c.

47. Carr P.D., Ewens C.L., Dai J., Ollis D.L., Murphy J.M., Jackson C.J., Young I.G. (2014) Crystal structure of the mouse interleukin-3 β-receptor: insights into interleukin‑3 binding and receptor activation.  Biochem J. doi:

46. Jackson C.J., Coppin C.W., Carr P.D., Aleksandrov A., Wilding M., Sugrue E., Ubels J., Paks M., Newman J., Peat T.S., Russell R.J., Field M., Weik M., Oakeshott J.G., Scott C.. (2014) 300-fold increase in production of the Zn2+-dependent dechlorinase TrzN in soluble form via apoenzyme stabilization. Appl. Environ. Microbiol. 80, 4003-11. doi: 10.1128/AEM.00916-14.

45. Naqvi T., Warden A.C., French N., Sugrue E., Carr P.D., Jackson C.J., Scott C. (2014)  A 5000-fold increase in the specificity of a bacterial phosphotriesterase for malathion through combinatorial active site mutagenesis. PLoS One. 9, e94177. doi: 10.1371/journal.pone.0094177.

44. Jackson C.J., Carville A., Ward J., Mansfield K., Ollis D.L., Khurana T., Bird S.B. (2014) Use of OpdA, an organophosphorus (OP) hydrolase, prevents lethality in an African green monkey model of acute OP poisoning. Toxicology 317, 1-5. doi: 10.1016/j.tox.2014.01.003


2013

43. Jackson C.J., Liu J.-W., Carr P.D., Younus F., Coppin C., Meirelles T., Lethier M., Pandey G., Ollis D.L., Russell R.J., Weik M., Oakeshott J.G. Structure and function of an insect α-carboxylesterase (αEsterase7) associated with insecticide resistance. Proc. Nat. Acad. Sci. USA (2013), 110(25), 10177-10182. http://dx.doi.org/10.1073/pnas.1304097110

42. Zhang W.H., Otting G., Jackson C.J. Protein engineering with unnatural amino acids. Curr. Opin. Struct. Biol. (2013), 23(4), 581-587. http://dx.doi.org/10.1016/j.sbi.2013.06.009


2012

41. Afriat-Jurnou L., Jackson C.J., Tawfik D.S. Reconstructing a missing link in the evolution of a recently diverged phosphotriesterase by active-site loop remodeling. Biochemistry (2012), 51(31), 6047-6055. http://dx.doi.org/10.1021/bi300694t

40. Coppin C.W., Jackson C.J., Sutherland T., Hart P.J., Devonshire A.L., Russell R.J., Oakeshott J.G. Testing the evolvability of an insect carboxylesterase for the detoxification of synthetic pyrethroid insecticides. Insect Biochem. Mol. Biol. (2012), 42(5), 343-352. http://dx.doi.org/10.1016/j.ibmb.2012.01.004

39. Gallat F.-X., Brogan A.P.S., Fichou Y., McGrath N., Moulin M., Hartlein M., Combet J., Wuttke J., Mann S., Zaccai G., Jackson C.J., Perriman A.W., Weik M. A polymer surfactant corona dynamically replaces water in solvent-free protein liquids and ensures macromolecular flexibility and activity. J. Am. Chem. Soc. (2012), 134(32), 13168-13171. http://dx.doi.org/10.1021/ja303894g

38. Noor S., Taylor M.C., Russell R.J., Jermiin L.S., Jackson C.J., Oakeshott J.G., Scott C. Intramolecular epistasis and the evolution of a new enzymatic function. PLoS One (2012), 7(6), e39822/1-11. http://dx.doi.org/10.1371/journal.pone.0039822

37. Sharma P., Pandey R., Kumari K., Pandey G., Jackson C.J., Russell R.J., Oakeshott J.G., Lal R. Kinetic and sequence-structure-function analysis of known LinA variants with different hexachlorocyclohexane isomers. PLoS One (2011), 6(9), e25128. http://dx.doi.org/10.1371/journal.pone.0025128

36. Tokuriki N., Jackson C.J., Afriat-Jurnou L., Wyganowski K.T., Tang R., Tawfik D.S. Diminishing returns and tradeoffs constrain the laboratory optimization of an enzyme. Nat. Commun. (2012), 3(12), 1257/1-9. http://dx.doi.org/10.1038/ncomms2246


2011

35. Brittain D.R.B., Pandey R., Kumari K., Sharma P., Pandey G., Lal R., Coote M.L., Oakeshott J.G., Jackson C.J. Competing SN2 and E2 reaction pathways for hexachlorocyclohexane degradation in the gas phase, solution and enzymes. Chem. Commun. (2011), 47(3), 976-978.http://dx.doi.org/10.1039/C0CC02925D

34. Fraser J.S., Jackson C.J. Mining electron density for functionally relevant protein polysterism in crystal structures. Cell. Mol. Life Sci. (2011), 68(11), 1829-1841. http://dx.doi.org/10.1007/s00018-010-0611-4

33. Russell R.J., Scott C., Jackson C.J., Pandey R., Pandey G., Taylor M.C., Coppin C.W., Liu J.-W., Oakeshott J.G. The evolution of new enzyme function: lessons from xenobiotic metabolizing bacteria versus insecticide-resistant insects. Evol. Appl. (2011), 4(2), 225-248. http://dx.doi.org/10.1111/j.1752-4571.2010.00175.x

32. Sharma P., Pandey R., Kumari K., Pandey G., Jackson C.J., Russell R.J., Oakeshott J.G., Lal R Kinetic and sequence-structure-function analysis of known LinA variants with different hexachlorocyclohexane isomers. PLoS One (2011), 6(9), e25128/1-4. http://dx.doi.org/10.1371/journal.pone.0025128

31. Ugwumba I.N., Ozawa K., Xu Z.-Q., Ely F., Foo J.-L., Herlt A.J., Coppin C., Brown S., Taylor M.C., Ollis D.L., Mander L.N., Schenk G., Dixon N.E., Otting G., Oakeshott J.G., Jackson C.J. Improving a natural enzyme activity through incorporation of unnatural amino acids. J. Am. Chem. Soc. (2011), 133(2), 326-333. http://dx.doi.org/10.1021/ja106416g


2010

30. Foo, J.-L., Jackson C.J., Carr P.D., Kim H.-K., Schenk G., Gahan L.R., Ollis D.L. Mutation of outer-shell residues modulates metal ion co-ordination strength in a metalloenzyme. Biochem. J. (2010), 429(2), 313-321. http://dx.doi.org/10.1042/BJ20100233

29. Gresham C., Rosenbaum C., Gaspari R.J., Jackson C.J., Bird S.B. Kinetics and efficacy of an organophosphorus hydrolase in a rodent model of methyl-parathion poisoning. Acad. Emerg. Med. (2010), 17(7), 736-740. http://dx.doi.org/10.1111/j.1553-2712.2010.00798.x

28. Jackson C.J., Gillam E.M.J., Ollis D.L. Directed evolution of enzymes. In Modern Methods in Natural Products Chemistry, Mander L.N., ed. Comprehensive Natural Products Chemistry II: Chemistry and Biology, Vol. 9, Elsevier Science: Oxford, UK (2010), pp. 723-749. http://dx.doi.org/10.1016/B978-008045382-8.00675-4

27. Jackson C.J., Oakeshott J.G., Sanchez-Hernandez J.C., Wheelock, C.E. Caboxylesterases in the metabolism and toxicity of pesticides. In Anticholinesterase Pesticides: Metabolism, Neurotoxicity, and Epidemiology, Satoh T., Gupta R.C., eds. John Wiley and Sons, Hoboken, NJ, USA (2010), pp. 57-75.http://dx.doi.org/10.1002/9780470640500.ch5

26. Jackson C.J., Scott C., Carville A., Mansfield K., Ollis D.L., Bird S.B. Pharmacokinetics of OpdA, an organophosphorus hydrolase, in the African green monkey. Biochem. Pharmacol. (2010), 80(7), 1075-1079. http://dx.doi.org/10.1016/j.bcp.2010.06.008

25. Lal R., Pandey G., Sharma P., Kumari K., Malhotra S., Pandey R., Raina V., Kohler H.-P.E., Holliger C., Jackson C.J., Oakeshott J.G. Biochemistry of microbial degradation of hexachlorocyclohexane and prospects for bioremediation. Microbiol. Mol. Biol. Rev. (2010) 74(1), 58-80.http://dx.doi.org/10.1128/MMBR.00029-09

24. Taylor M.C., Jackson C.J., Tattersall D.B., French N., Peat T.S., Newman J., Briggs L.J., Lapalikar G.V., Campbell P.M., Scott C., Russell R.J., Oakeshott J.G. Identification and characterization of two families of F420H2-dependent reductases from Mycobacteria that catalyze aflatoxin degradation. Mol. Microbiol. (2010), 78(3), 561-575. http://dx.doi.org/10.1111/j.1365-2958.2010.07356.x

Patents:

23. Khurana J.L., Jackson C.J., Scott C., Pandey G., Russell R.J., Oakeshott J.G. Enzymes and methods for hydrolysing a phenylureas, carbamates and organophosphates. International Patent No. WO2010/003184 A1 (2010), 91 pp.

22. Scott C., Russell R.J., Coppin C.W., Oakeshott J.G. Jackson, C.J. Enzymes and methods for degrading S-triazines and diazines. International Patent No. WO2010/025499 A1 (2010), 91 pp.


2009

21. Jackson C.J., Foo J.-L., Tokuriki N., Afriat L., Carr P.D., Kim H.-K., Schenk G., Tawfik D.S., Ollis D.L. Conformational sampling, catalysis, and evolution of the bacterial phosphotriesterase. Proc. Natl. Acad. Sci. USA (2009), 106(51), 21631-21636. http://dx.doi.org/10.1073/pnas.0907548106

20. Jackson C.J., Weir K., Herlt A., Khurana J., Sutherland T.D., Horne I., Easton C., Scott C., Russell R.J., Scott C., Oakeshott J.G. Structure-based rational design of a phosphotriesterase. Appl. Environ. Microbiol. (2009), 75(15), 5153-5156. http://dx.doi.org/10.1128/AEM.00629-09

19. Khersonsky O., Röthlisberger D., Dym O., Albeck S., Jackson C.J., Baker D., Tawfik, D.S. Evolutionary optimization of computationally designed enzymes: Kemp eliminases of the KE07 series. J. Mol. Biol. (2009), 396(4), 1025-1042. http://dx.doi.org/10.1016/j.jmb.2009.12.031

18. Khurana J.L., Jackson C.J., Scott C., Pandey G., Horne I., Russell R.J., Herlt A.J., Easton C.J., Oakeshott J.G. Characterization of the phenylurea hydrolases A and B: founding members of a novel amidohydrolase subgroup. Biochem. J. (2009), 418(2), 431-441. http://dx.doi.org/10.1042/BJ20081488

17. Scott C., Jackson C.J., Coppin C.W., Mourant R.G., Hilton M.E., Sutherland T.D., Russell R.J., Oakeshott J.G. Catalytic improvement and evolution of atrazine chlorohydrolase. Appl. Environ. Microbiol. (2009), 75(7), 2184-2191. http://dx.doi.org/10.1128/AEM.02634-08

16. Weston D.P., Jackson C.J. Use of engineered enzymes to identify organophosphate and pyrethroid-related toxicity in toxicity identification evaluations. Environ. Sci. Technol. (2009), 43(14), 5514-5520. http://dx.doi.org/10.1021/es900434z

Patent:

15. Scott C., Jackson, C.J., Russell R.J., Oakeshott J.G., Coppin C.W. Enzymes and methods for degrading chlorinated S-triazines. International Patent No. WO2009/076711 A1 (2009), 68 pp.


2008

14. Biswas S., Russell R.J., Jackson C.J., Vidovic M., Ganeshina O., Oakeshott J.G., Claudianos C. Bridging the synaptic gap: neuroligins and neurexin I in Apis mellifera. PLoS One (2008), 3(10), e3452/1-19. http://dx.doi.org/10.1371/journal.pone.0003542

13. Hadler K.S., Tanifum E.A., Yip S.H.-C., Mitic N., Guddat L.W., Jackson C.J., Gahan L.R., Nguyen K., Carr P.D., Ollis D.L., Hengge A.C., Larrabee J.A., Schenk G. Substrate-promoted formation of a catalytically competent binuclear center and regulation of reactivity in a glycerophosphodiesterase fromEnterobacter aerogenes. J. Am. Chem. Soc. (2008), 130(43), 14129-14138. http://dx.doi.org/10.1021/ja803346w

12. Jackson C.J., Foo J.-L., Kim H.-K., Carr P.D., Liu J.-W., Salem G., Ollis D.L. In crystallo capture of a Michaelis complex and product-binding modes of a bacterial phosphotriesterase. J. Mol. Biol. (2008), 375(5), 1189-1196. http://dx.doi.org/10.1016/j.jmb.2007.10.061

11. Jackson C.J., Hadler K.S., Carr P.D., Oakley A.J., Yip S., Schenk G., Ollis D.L. Malonate-bound structure of the glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) and characterization of the native Fe2+ metal-ion preference. Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. (2008), 64(8), 681-685. http://dx.doi.org/10.1107/S1744309108017600

10. Jackson C.J., Taylor M.C., Tattersall D.B., French N.G., Carr P.D., Ollis D.L., Russell R.J., Oakeshott J.G. Cloning, expression, purification, crystallization and preliminary X-ray studies of a pyridoxine 5′-phosphate oxidase from Mycobacterium smegmatis. Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. (2008), 64(5), 435-437. http://dx.doi.org/10.1107/S1744309108011512

9. Scott C., Pandey G., Hartley C.J., Jackson, C.J., Cheesman M.J., Taylor M.C., Pandey R., Khurana J.L., Teese M., Coppin C.W., Weir K.M., Jain R.K., Lal R., Russell R.J., Oakeshott J.G. The enzymatic basis for pesticide bioremediation. Indian J. Microbiol. (2008), 48(1), 65-79.http://dx.doi.org/10.1007/s12088-008-0007-4


2007

8. Ely F., Foo J.-L., Jackson C.J., Gahan L.R., Ollis D., Schenk G. Enzymatic bioremediation: organophosphate degradation by binuclear metallo-hydrolases. Curr. Top. Biochem. Res. (2007), 9(2), 63-78.

7. Jackson C.J., Carr P.D., Liu J.-W., Watt S.J., Beck J.L., Ollis D.L. The structure and function of a novel glycerophosphodiesterase from Enterobacter aerogenes. J. Mol. Biol. (2007), 367(4), 1047-1062. http://dx.doi.org/10.1016/j.jmb.2007.01.032


2006

6. Jackson C.J., Carr P.D., Kim H.-K., Liu J.-W., Herrald P., Mitic N., Schenk G., Smith C.A., Ollis D.L. Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: the prominent role of iron in the heterobinuclear active site. Biochem. J. (2006), 397(3), 501-508.http://www.biochemj.org/bj/397/bj3970501.htm

5. Jackson C.J., Carr P.D., Kim H.-K., Liu J.-W., Ollis D.L. The purification, crystallization and preliminary diffraction of a glycerophosphodiesterase from Enterobacter aerogenes. Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. (2006), 62(7), 659-661. http://dx.doi.org/10.1107/S1744309106020021


2005

4. Jackson C.J, Kim H.-K., Carr P.D., Liu J.-W., Ollis D.L. The structure of an enzyme-product complex reveals the critical role of a terminal hydroxide nucleophile in the bacterial phosphotriesterase mechanism. Biochim. Biophys. Acta (2005), 1752(1), 56-64. http://dx.doi.org/10.1016/j.bbapap.2005.06.008

3. Jackson C.J., Liu J.-W., Coote M.L., Ollis D.L. The effects of substrate orientation on the mechanism of a phosphotriesterase. Org. Biomol. Chem. (2005), 3(24), 4343-4350. http://dx.doi.org/10.1039/b512399b

2. Yu McLoughlin S., Jackson C.J, Liu J.-W., Ollis D. Increased expression of a bacterial phosphotriesterase in Escherichia coli through directed evolution. Protein Expr. Purif. (2005), 41(2), 433-440. http://dx.doi.org/10.1016/j.pep.2005.01.012


2004

Yu McLoughlin, S., Jackson, C.J, Liu, J.-W., Ollis, D.L. Growth of Escherichia coli co-expressing phosphotriesterase and glycerophosphodiester phosphodiesterase, using paraoxon as the sole phosphorus source. Appl. Environ. Microbiol. (2004), 70(1), 404-412.

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