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Professor Renwick Dobson

Contact

Department: School of Biological Sciences

Email: renwick.dobson@canterbury.ac.nz

Direct Dial: +64 3 3695145

Office: Julius von Haast 620

Language: English

About
Research / Creative works
Supervision
Networks
Projects
Methods & Equipment

Fields of Research

  • Enzymology
  • Enzyme evolution and Enzyme design
  • Structural biology
  • Biophysics

Researcher Summary

Research in our lab focuses on the structure, function and inhibition of key enzymes involved in infection and disease.  We are also interested in the evolution of enzyme function, and conversely its design and manipulation.

We study a variety of enzymes: from those responsible for the biosynthesis of amino acids, in particular lysine, since these are validated drug targets; to glycolytic enzymes, such as pyruvate kinase, since these are tractable model systems to understand enzyme allostery.  The list is ever increasing.

A common theme in the lab is the role protein-protein interactions in a variety of biological systems, mostly derived from bacteria, but more recently including eukaryotic proteins involved in cancer, where we hope to address the twin problems of how and why proteins form complexes and the functional consequences of these associations.

Subject Area: Disciplines

  • Biology: Molecular, Cellular and Whole Organism Biology: Biochemistry; Biomolecular Interactions

Research/Scholarly/Creative Works

Journal Articles
  • Mckerchar HJ., Lento C., Bennie RZ., Crowther JM., Dolamore F., Dyer JM., Clerens S., Mercadante D., Wilson DJ. and Dobson RCJ. (2023) The protein dynamics of bovine and caprine β-lactoglobulin differ as a function of pH. Food Chemistry 408 http://dx.doi.org/10.1016/j.foodchem.2022.135229.
  • Abeysekera GS., Love MJ., Manners SH., Billington C. and Dobson RCJ. (2022) Bacteriophage-encoded lethal membrane disruptors: Advances in understanding and potential applications. Frontiers in Microbiology 13 http://dx.doi.org/10.3389/fmicb.2022.1044143.
  • Board AJ., Crowther JM., Acevedo-Fani A., Meisrimler CN., Jameson GB. and Dobson RCJ. (2022) How plants solubilise seed fats: revisiting oleosin structure and function to inform commercial applications. Biophysical Reviews 14(1): 257-266. http://dx.doi.org/10.1007/s12551-021-00923-5.
  • Bozzola T., Scalise M., Larsson CU., Newton-Vesty MC., Rovegno C., Mitra A., Cramer J., Wahlgren WY., Radhakrishnan Santhakumari P. and Johnsson RE. (2022) Sialic Acid Derivatives Inhibit SiaT Transporters and Delay Bacterial Growth. ACS Chemical Biology 17(7): 1890-1900. http://dx.doi.org/10.1021/acschembio.2c00321.
  • Harper AR., Dobson RCJ., Morris VK. and Moggré GJ. (2022) Fermentation of plant-based dairy alternatives by lactic acid bacteria. Microbial Biotechnology 15(5): 1404-1421. http://dx.doi.org/10.1111/1751-7915.14008.
  • Lassé M., Stampfli AR., Orban T., Bothara RK., Gerrard JA., Fairbanks AJ., Pattinson NR. and Dobson RCJ. (2022) Corrigendum to “Reaction dynamics and residue identification of haemoglobin modification by acrolein, a lipid-peroxidation by-product” [Biochimica et Biophysica Acta (BBA) - General Subjects Volume 1865, Issue 12, December 2021, 130013] (BBA - General Subjects (2021) 1865(12), (S0304416521001720), (10.1016/j.bbagen.2021.130013)). Biochimica et Biophysica Acta - General Subjects 1866(5) http://dx.doi.org/10.1016/j.bbagen.2022.130117.
  • Love MJ., Coombes D., Ismail S., Billington C. and Dobson RCJ. (2022) The structure and function of modular Escherichia coli O157:H7 bacteriophage FTBEc1 endolysin, LysT84: Defining a new endolysin catalytic subfamily. Biochemical Journal 479(2): 207-223. http://dx.doi.org/10.1042/BCJ20210701.
  • Meffan R., Menges J., Dolamore F., Mak D., Fee C., Dobson R. and Nock V. (2022) Capillaric-Field Effect Transistors. Microsystem & Nanoengineering 8 33 http://dx.doi.org/10.1038/s41378-022-00360-8.
  • Turk LS., Currie MJ., Dobson RCJ. and Comoletti D. (2022) Structure of Reelin repeat 8 and the adjacent C-terminal region. Biophysical Journal 121(13): 2526-2537. http://dx.doi.org/10.1016/j.bpj.2022.06.002.
  • Watkin SAJ., Bennie R., Gilkes J., Nock V., Pearce FG. and Dobson R. (2022) On the utility of microfluidic systems to study protein interactions: advantages, challenges, and applications. European Biophysics Journal http://dx.doi.org/10.1007/s00249-022-01626-9.
  • Arif T., Currie MJ., Dobson RCJ., Newson HL., Poonthiyil V., Fairbanks AJ., North RA. and Rendle PM. (2021) Synthesis of N-acetylmannosamine-6-phosphate derivatives to investigate the mechanism of N-acetylmannosamine-6-phosphate 2-epimerase. Carbohydrate Research 510 http://dx.doi.org/10.1016/j.carres.2021.108445.
  • Crowther JM., Gilmour LH., Porebski BT., Heath SG., Pattinson NR., Owen MC., Fredericks R., Buckle AM., Fee CJ. and Göbl C. (2021) Molecular basis of a redox switch: Molecular dynamics simulations and surface plasmon resonance provide insight into reduced and oxidised angiotensinogen. Biochemical Journal 478(17): 3319-3330. http://dx.doi.org/10.1042/BCJ20210476.
  • Currie MJ., Manjunath L., Horne CR., Rendle PM., Subramanian R., Friemann R., Fairbanks AJ., Muscroft-Taylor AC., North RA. and Dobson RCJ. (2021) N-acetylmannosamine-6-phosphate 2-epimerase uses a novel substrate-assisted mechanism to catalyze amino sugar epimerization. Journal of Biological Chemistry 297(4) http://dx.doi.org/10.1016/j.jbc.2021.101113.
  • Davies JS., Currie MJ., Wright JD., Newton-Vesty MC., North RA., Mace PD., Allison JR. and Dobson RCJ. (2021) Selective Nutrient Transport in Bacteria: Multicomponent Transporter Systems Reign Supreme. Frontiers in Molecular Biosciences 8 http://dx.doi.org/10.3389/fmolb.2021.699222.
  • Horne CR., Venugopal H., Panjikar S., Wood DM., Henrickson A., Brookes E., North RA., Murphy JM., Friemann R. and Griffin MDW. (2021) Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism. Nature Communications 12(1) http://dx.doi.org/10.1038/s41467-021-22253-6.
  • Hudson-King TR., Ahuriri-Driscoll A. and Dobson R. (2021) Consulting with Māori during development of a point-of-care device; translational and experiential findings. SOCARXIV papers http://dx.doi.org/10.31235/osf.io/w2tbc.
  • Klionsky DJ., Abdel-Aziz AK., Abdelfatah S., Abdellatif M., Abdoli A., Abel S., Abeliovich H., Abildgaard MH., Abudu YP. and Acevedo-Arozena A. (2021) Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1. Autophagy 17(1): 1-382. http://dx.doi.org/10.1080/15548627.2020.1797280.
  • Lassé M., Stampfli AR., Orban T., Bothara RK., Gerrard JA., Fairbanks AJ., Pattinson NR. and Dobson RCJ. (2021) Reaction dynamics and residue identification of haemoglobin modification by acrolein, a lipid-peroxidation by-product. Biochimica et Biophysica Acta - General Subjects 1865(12) http://dx.doi.org/10.1016/j.bbagen.2021.130013.
  • Love MJ., Coombes D., Manners SH., Abeysekera GS., Billington C. and Dobson RCJ. (2021) The molecular basis for escherichia coli O157:H7 phage FAHEC1 endolysin function and protein engineering to increase thermal stability. Viruses 13(6) http://dx.doi.org/10.3390/v13061101.
  • Manjunath L., Coombes D., Davies J., Dhurandhar M., Tiwari VR., Dobson RCJ., Sowdhamini R., Ramaswamy S. and Bose S. (2021) Quaternary variations in the structural assembly of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella multocida. Proteins: Structure, Function and Bioinformatics 89(1): 81-93. http://dx.doi.org/10.1002/prot.25996.
  • Parthasarathy A., Borrego EJ., Savka MA., Dobson RCJ. and Hudson AO. (2021) Amino acid–derived defense metabolites from plants: A potential source to facilitate novel antimicrobial development. Journal of Biological Chemistry 296 http://dx.doi.org/10.1016/j.jbc.2021.100438.
  • Peskin AV., Meotti FC., Kean KM., Göbl C., Peixoto AS., Pace PE., Horne CR., Heath SG., Crowther JM. and Dobson RCJ. (2021) Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2. Journal of Biological Chemistry 296 http://dx.doi.org/10.1016/j.jbc.2021.100494.
  • Pilapitiya DH., Harris PWR., Hanson-Manful P., McGregor R., Kowalczyk R., Raynes JM., Carlton LH., Dobson RCJ., Baker MG. and Brimble M. (2021) Antibody responses to collagen peptides and streptococcal collagen-like 1 proteins in acute rheumatic fever patients. Pathogens and Disease 79(6) http://dx.doi.org/10.1093/femspd/ftab033.
  • Turk LS., Kuang X., Dal Pozzo V., Patel K., Chen M., Huynh K., Currie MJ., Mitchell D., Dobson RCJ. and D'Arcangelo G. (2021) The structure-function relationship of a signaling-competent, dimeric Reelin fragment. Structure 29(10): 1156-1170.e6. http://dx.doi.org/10.1016/j.str.2021.05.012.
  • Wood DM., Dobson RCJ. and Horne CR. (2021) Using cryo-EM to uncover mechanisms of bacterial transcriptional regulation. Biochemical Society Transactions 49(6): 2711-2726. http://dx.doi.org/10.1042/BST20210674.
  • Adams LE., Rynkiewicz P., Babbitt GA., Mortensen JS., North RA., Dobson RCJ. and Hudson AO. (2020) Comparative Molecular Dynamics Simulations Provide Insight Into Antibiotic Interactions: A Case Study Using the Enzyme L,L-Diaminopimelate Aminotransferase (DapL). Frontiers in Molecular Biosciences 7 http://dx.doi.org/10.3389/fmolb.2020.00046.
  • Coombes D., Davies JS., Newton-Vesty MC., Horne CR., Setty TG., Subramanian R., Moir JWB., Friemann R., Panjikar S. and Griffin MDW. (2020) The basis for non-canonical ROK family function in the N-acetylmannosamine kinase from the pathogen Staphylococcus aureus. Journal of Biological Chemistry 295(10): 3301-3315. http://dx.doi.org/10.1074/jbc.RA119.010526.
  • Cree SL., Chua EW., Crowther J., Dobson RCJ. and Kennedy MA. (2020) G-quadruplex structures bind to EZ-Tn5 transposase. Biochimie 177: 190-197. http://dx.doi.org/10.1016/j.biochi.2020.07.022.
  • Crowther JM., Broadhurst M., Laue TM., Jameson GB., Hodgkinson AJ. and Dobson RCJ. (2020) On the utility of fluorescence-detection analytical ultracentrifugation in probing biomolecular interactions in complex solutions: a case study in milk. European Biophysics Journal 49(8): 677-685. http://dx.doi.org/10.1007/s00249-020-01468-3.
  • Dobson RCJ. and Patel TR. (2020) Analytical ultracentrifugation: still the gold standard that offers multiple solutions. European Biophysics Journal 49(8): 673-676. http://dx.doi.org/10.1007/s00249-020-01483-4.
  • Gangi Setty T., Sarkar A., Coombes D., Dobson RCJ. and Subramanian R. (2020) Structure and Function of N-Acetylmannosamine Kinases from Pathogenic Bacteria. ACS Omega 5(48): 30923-30936. http://dx.doi.org/10.1021/acsomega.0c03699.
  • Horne CR., Henrickson A., Demeler B. and Dobson RCJ. (2020) Multi-wavelength analytical ultracentrifugation as a tool to characterise protein–DNA interactions in solution. European Biophysics Journal 49(8): 819-827. http://dx.doi.org/10.1007/s00249-020-01481-6.
  • Horne CR., Kind L., Davies JS. and Dobson RCJ. (2020) Cover Image, Volume 88, Issue 5. Proteins: Structure, Function, and Bioinformatics 88(5) http://dx.doi.org/10.1002/prot.25721.
  • Horne CR., Kind L., Davies JS. and Dobson RCJ. (2020) On the structure and function of Escherichia coli YjhC: An oxidoreductase involved in bacterial sialic acid metabolism. Proteins: Structure, Function and Bioinformatics 88(5): 654-668. http://dx.doi.org/10.1002/prot.25846.
  • Love MJ., Abeysekera GS., Muscroft-Taylor AC., Billington C. and Dobson RCJ. (2020) On the catalytic mechanism of bacteriophage endolysins: Opportunities for engineering. Biochimica et Biophysica Acta - Proteins and Proteomics 1868(1) http://dx.doi.org/10.1016/j.bbapap.2019.140302.
  • Love MJ., Dobson RCJ. and Billington C. (2020) Stemming the tide of antibiotic resistance by exploiting bacteriophages. Biochemist 42(6): 6-11. http://dx.doi.org/10.1042/BIO20200074.
  • Meng Y., Sheen CR., Magon NJ., Hampton MB. and Dobson RCJ. (2020) Structure-function analyses of alkylhydroperoxidase D from Streptococcus pneumoniae reveal an unusual three-cysteine active site architecture. Journal of Biological Chemistry 295(10): 2984-2999. http://dx.doi.org/10.1074/jbc.RA119.012226.
  • Menges J., Meffan C., Dolamore F., Fee C., Dobson R. and Nock V. (2020) New flow control systems in capillarics: Off valves. Lab on a Chip http://dx.doi.org/10.1039/D0LC00811G.
  • Metcalfe RD., Aizel K., Zlatic CO., Nguyen PM., Morton CJ., Lio DSS., Cheng HC., Dobson RCJ., Parker MW. and Gooley PR. (2020) The structure of the extracellular domains of human interleukin 11α receptor reveals mechanisms of cytokine engagement. Journal of Biological Chemistry 295(24): 8285-8301. http://dx.doi.org/10.1074/JBC.RA119.012351.
  • Nouchikian L., Lento C., Donovan K., Dobson R. and Wilson DJ. (2020) Comparing the Conformational Stability of Pyruvate Kinase in the Gas Phase and in Solution. Journal of the American Society for Mass Spectrometry 31(3): 685-692. http://dx.doi.org/10.1021/jasms.9b00130.
  • Sugrue E., Coombes D., Wood D., Zhu T., Donovan KA. and Dobson RCJ. (2020) The lid domain is important, but not essential, for catalysis of Escherichia coli pyruvate kinase. European Biophysics Journal 49(8): 761-772. http://dx.doi.org/10.1007/s00249-020-01466-5.
  • Suzuki H., Mahapatra D., Board AJ., Steel PJ., Dyer JM., Gerrard JA., Dobson RCJ. and Valéry C. (2020) Sub-Ångstrom structure of collagen model peptide (GPO)10 shows a hydrated triple helix with pitch variation and two proline ring conformations. Food Chemistry 319 http://dx.doi.org/10.1016/j.foodchem.2020.126598.
  • Trevelyan SJ., Brewster JL., Burgess AE., Crowther JM., Cadell AL., Parker BL., Croucher DR., Dobson RCJ., Murphy JM. and Mace PD. (2020) Structure-based mechanism of preferential complex formation by apoptosis signal–regulating kinases. Science Signaling 13(622) http://dx.doi.org/10.1126/scisignal.aay6318.
  • Weatherhead AW., Crowther JM., Horne CR., Meng Y., Coombes D., Currie MJ., Watkin SAJ., Adams LE., Parthasarathy A. and Dobson RCJ. (2020) Structure-Function Studies of the Antibiotic Target l, l-Diaminopimelate Aminotransferase from Verrucomicrobium spinosum Reveal an Unusual Oligomeric Structure. Biochemistry 59(24): 2274-2288. http://dx.doi.org/10.1021/acs.biochem.0c00185.
  • Coombes D., Moir JWB., Poole AM., Cooper TF. and Dobson RCJ. (2019) The fitness challenge of studying molecular adaptation. Biochemical Society Transactions 47(5): 1533-1542. http://dx.doi.org/10.1042/BST20180626.
  • Crowther JM., Cross PJ., Oliver MR., Leeman MM., Bartl AJ., Weatherhead AW., North RA., Donovan KA., Griffin MDW. and Suzuki H. (2019) Structure-function analyses of two plant mesodiaminopimelate decarboxylase isoforms reveal that active-site gating provides stereochemical control. Journal of Biological Chemistry 294(21): 8505-8515. http://dx.doi.org/10.1074/jbc.RA118.006825.
  • Davies JS., Coombes D., Horne CR., Pearce FG., Friemann R., North RA. and Dobson RCJ. (2019) Functional and solution structure studies of amino sugar deacetylase and deaminase enzymes from Staphylococcus aureus. FEBS Letters 593(1): 52-66. http://dx.doi.org/10.1002/1873-3468.13289.
  • Gilkes JM., Sheen CR., Frampton RA., Smith GR. and Dobson RCJ. (2019) The First Purification of Functional Proteins from the Unculturable, Genome-Reduced, Bottlenecked a-Proteobacterium ‘Candidatus Liberibacter solanacearum’. Phytopathology 109(7): 1141-1148. http://dx.doi.org/10.1094/PHYTO-12-18-0486-R.
  • Hoskin TS., Crowther JM., Cheung J., Epton MJ., Sly PD., Elder PA., Dobson RCJ., Kettle AJ. and Dickerhof N. (2019) Oxidative cross-linking of calprotectin occurs in vivo, altering its structure and susceptibility to proteolysis. Redox Biology 24 http://dx.doi.org/10.1016/j.redox.2019.101202.
  • Mantravadi PK., Kalesh KA., Dobson RCJ., Hudson AO. and Parthasarathy A. (2019) The quest for novel antimicrobial compounds: Emerging trends in research, development, and technologies. Antibiotics 8(1) http://dx.doi.org/10.3390/antibiotics8010008.
  • McKerchar HJ., Clerens S., Dobson RCJ., Dyer JM., Maes E. and Gerrard JA. (2019) Protein-protein crosslinking in food: Proteomic characterisation methods, consequences and applications. Trends in Food Science and Technology 86: 217-229. http://dx.doi.org/10.1016/j.tifs.2019.02.005.
  • Atkinson SC., Dogovski C., Wood K., Griffin MDW., Gorman MA., Hor L., Reboul CF., Buckle AM., Wuttke J. and Parker MW. (2018) Substrate Locking Promotes Dimer-Dimer Docking of an Enzyme Antibiotic Target. Structure 26(7): 948-959.e5. http://dx.doi.org/10.1016/j.str.2018.04.014.
  • Crowther JM., Allison JR., Smolenski GA., Hodgkinson AJ., Jameson GB. and Dobson RCJ. (2018) The self-association and thermal denaturation of caprine and bovine β-lactoglobulin. European Biophysics Journal 47(7): 739-750. http://dx.doi.org/10.1007/s00249-018-1300-8.
  • Foglizzo M., Middleton AJ., Burgess AE., Crowther JM., Dobson RCJ., Murphy JM., Day CL. and Mace PD. (2018) A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes. Nature Communications 9 3932: 15. http://dx.doi.org/10.1038/s41467-018-06186-1.
  • Gilkes JM., Frampton RA., Smith GR. and Dobson RCJ. (2018) Potential pathogenicity determinants in the genome of ‘Candidatus Liberibacter solanacearum’, the causal agent of zebra chip disease of potato. Australasian Plant Pathology 47(2): 119-134. http://dx.doi.org/10.1007/s13313-018-0546-z.
  • Gilkes JM., Frampton RA., Smith GR. and Dobson RCJ. (2018) Potential pathogenicity determinants in the genome of ‘Candidatus Liberibacter solanacearum’, the causal agent of zebra chip disease of potato. Australasian Plant Pathology 47(2): 119-134. http://dx.doi.org/10.1007/s13313-018-0546-z.
  • Love MJ., Bhandari D., Dobson RCJ. and Billington C. (2018) Potential for bacteriophage endolysins to supplement or replace antibiotics in food production and clinical care. Antibiotics 7(1): 1-25. http://dx.doi.org/10.3390/antibiotics7010017.
  • Manjunath L., Guntupalli SR., Currie MJ., North RA., Dobson RCJ., Nayak V. and Subramanian R. (2018) Crystal structures and kinetic analyses of N-acetylmannosamine-6-phosphate 2-epimerases from Fusobacterium nucleatum and Vibrio cholerae. Acta Crystallographica Section F: Structural Biology Communications 74(7): 431-440. http://dx.doi.org/10.1107/S2053230X18008543.
  • North RA., Wahlgren WY., Remus DM., Scalise M., Kessans SA., Dunevall E., Claesson E., da Costa TPS., Perugini MA. and Ramaswamy S. (2018) The Sodium Sialic acid symporter from Staphylococcus aureus has altered substrate specificity. Frontiers in Chemistry 6(JUL) http://dx.doi.org/10.3389/fchem.2018.00233.
  • Parthasarathy A., Cross PJ., Dobson RCJ., Adams LE., Savka MA. and Hudson AO. (2018) A Three-Ring circus: Metabolism of the three proteogenic aromatic amino acids and their role in the health of plants and animals. Frontiers in Molecular Biosciences 5(APR) http://dx.doi.org/10.3389/fmolb.2018.00029.
  • Peng F., Widmann S., Wünsche A., Duan K., Donovan KA., Dobson RCJ., Lenski RE. and Cooper TF. (2018) Effects of Beneficial Mutations in pykF Gene Vary over Time and across Replicate Populations in a Long-Term Experiment with Bacteria. Molecular Biology and Evolution 35(1): 202-210. http://dx.doi.org/10.1093/molbev/msx279.
  • Rogov VV., Stolz A., Ravichandran AC., Rios-Szwed DO., Suzuki H., Kniss A., Löhr F., Wakatsuki S., Dötsch V. and Dikic I. (2018) Corrigendum to: Structural and functional analysis of the GABARAP interaction motif (GIM) (EMBO reports, (2017), 18, 8, (1382-1396), 10.15252/embr.201643587). EMBO Reports 19(12) http://dx.doi.org/10.15252/embr.201847268.
  • Schlechter R., Jun H., Bernach M., Oso S., Boyd E., Muñoz-Lintz D., Dobson R., Remus D. and Remus-Emsermann M. (2018) Chromatic bacteria – A broad host-range plasmid and chromosomal insertion toolbox for fluorescent protein expression in bacteria. http://dx.doi.org/10.1101/402172.
  • Schlechter RO., Jun H., Bernach M., Oso S., Boyd E., Muñoz-Lintz DA., Dobson RCJ., Remus DM. and Remus-Emsermann MNP. (2018) Chromatic bacteria – A broad host-range plasmid and chromosomal insertion toolbox for fluorescent protein expression in bacteria. Frontiers in Microbiology 9(DEC) http://dx.doi.org/10.3389/fmicb.2018.03052.
  • Wahlgren WY., Dunevall E., North RA., Paz A., Scalise M., Bisignano P., Bengtsson-Palme J., Goyal P., Claesson E. and Caing-Carlsson R. (2018) Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site. Nature Communications 9(1) http://dx.doi.org/10.1038/s41467-018-04045-7.
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  • Hildebrand JM., Tanzer MC., Lucet IS., Young SN., Spall SK., Sharma P., Pierotti C., Garnier JM., Dobson RCJ. and Webb AI. (2014) Activation of the pseudokinase MLKL unleashes the four-helix bundle domain to induce membrane localization and necroptotic cell death. Proceedings of the National Academy of Sciences of the United States of America 111(42): 15072-15077. http://dx.doi.org/10.1073/pnas.1408987111.
  • McKinnie SMK., Rodriguez-Lopez EM., Vederas JC., Crowther JM., Suzuki H., Dobson RCJ., Leustek T., Triassi AJ., Wheatley MS. and Hudson AO. (2014) Differential response of orthologous L,L-diaminopimelate aminotransferases (DapL) to enzyme inhibitory antibiotic lead compounds. Bioorganic & Medicinal Chemistry 22(1): 523-530.
  • Nazmi AR., Schofield LR., Dobson RCJ., Jameson GB. and Parker EJ. (2014) Destabilization of the Homotetrameric Assembly of 3-Deoxy-d-Arabino-Heptulosonate-7-Phosphate Synthase from the Hyperthermophile Pyrococcus furiosus Enhances Enzymatic Activity. Journal of Molecular Biology 426(3): 656-673. http://dx.doi.org/10.1016/j.jmb.2013.11.008.
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  • Putoczki TL., Dobson RCJ. and Griffin MDW. (2014) The structure of human interleukin-11 reveals receptor-binding site features and structural differences from interleukin-6. Acta Crystallographica Section D: Biological Crystallography D70(9): 2277-2285. http://dx.doi.org/10.1107/S1399004714012267.
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  • Atkinson SC., Dogovski C., Downton MT., Czabotar PE., Dobson RCJ., Gerrard JA., Wagner J. and Perugini MA. (2013) Structural, kinetic and computational investigation of Vitis vinifera DHDPS reveals new insight into the mechanism of lysine-mediated allosteric inhibition. Plant Molecular Biology 81(4-5): 431-446. http://dx.doi.org/10.1007/s11103-013-0014-7.
  • Cross PJ., Allison TM., Dobson RCJ., Jameson GB. and Parker EJ. (2013) Engineering allosteric control to an unregulated enzyme by transfer of a regulatory domain. Proceedings of the National Academy of Sciences of the United States of America 110(6): 2111-2116. http://dx.doi.org/10.1073/pnas.1217923110.
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  • Dayaram A., Opong A., Jäschke A., Hadfield J., Baschiera M., Dobson RCJ., Offei SK., Shepherd DN., Martin DP. and Varsani A. (2012) Molecular characterisation of a novel cassava associated circular ssDNA virus. Virus Research 166(1-2): 130-135. http://dx.doi.org/10.1016/j.virusres.2012.03.009.
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  • Mercadante D., Melton LD., Norris GE., Loo TS., Williams MAK., Dobson RCJ. and Jameson GB. (2012) Bovine ß-Lactoglobulin is dimeric under imitative physiological conditions: Dissociation equilibrium and rate constants over the pH range of 2.5-7.5. Biophysical Journal 103(2): 303-312. http://dx.doi.org/10.1016/j.bpj.2012.05.041.
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  • Griffin MD., Billakanti JM., Gerrard JA., Dobson RCJ. and Pearce FG. (2011) Crystallization and preliminary X-ray diffraction analysis of dihydrodipicolinate synthase 2 from Arabidopsis thaliana. Acta crystallographica Section F: Structural biology and crystallization communications 67(11): 1386-1390. http://dx.doi.org/10.1107/S1744309111033276.
  • Gunn NJ., Gorman MA., Dobson RCJ., Parker MW. and Mulhern TD. (2011) Purification, crystallization, small-angle X-ray scattering and preliminary X-ray diffraction analysis of the SH2 domain of the Csk-homologous kinase. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 67(3): 336-339. http://dx.doi.org/10.1107/S1744309110053728.
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  • Costa SD., P T., Muscroft-Taylor., C A., Dobson., J RC., Devenish., A SR., Jameson. and B G. (2010) How essential is the 'essential' active-site lysine in dihydrodipicolinate synthase? Biochimie 92(7): 837-845.
  • Dommaraju S., Gorman MA., Dogovski C., Pearce FG., Gerrard JA., Dobson RCJ., Parker MW. and Perugini MA. (2010) Cloning, expression and crystallization of dihydrodipicolinate reductase from methicillin-resistant Staphylococcus aureus. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 66(1): 57-60. http://dx.doi.org/10.1107/s1744309109047964.
  • Griffin MDW., Dobson RCJ., Gerrard JA. and Perugini MA. (2010) Exploring the dihydrodipicolinate synthase tetramer: how resilient is the dimer-dimer interface? Archives of Biochemistry and Biophysics 494(1): 58-63. http://dx.doi.org/10.1016/j.abb.2009.11.014.
  • Hor L., Dobson RCJ., Dogovski C., Hutton CA. and Perugini MA. (2010) Crystallization and preliminary X-ray diffraction analysis of diaminopimelate epimerase from Escherichia coli. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 66(1): 37-40. http://dx.doi.org/10.1107/S1744309109047708.
  • Muscroft-Taylor AC., Catchpole RJ., Dobson RCJ., Pearce FG., Perugini MA. and Gerrard JA. (2010) Disruption of quaternary structure in Escherichia coli dihydrodipicolinate synthase (DHDPS) generates a functional monomer that is no longer inhibited by lysine. Archives of Biochemistry and Biophysics 503: 202-206. http://dx.doi.org/10.1016/j.abb.2010.08.009.
  • Voss JE., Scally SW., Taylor NL., Atkinson SC., Griffin MDW., Hutton CA., Parker MW., Alderton MR., Gerrard JA. and Dobson RCJ. (2010) Substrate-mediated stabilization of a tetrameric drug target reveals Achilles heel in anthrax. The Journal of Biological Chemistry 285(8): 5188-5195. http://dx.doi.org/10.1074/jbc.M109.038166.
  • Wubben JM., Dogovski C., Dobson RC., Codd R., Gerrard JA., Parker MW. and Perugini MA. (2010) Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from the psychrophile Shewanella benthica. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 66(11): 1511-1516. http://dx.doi.org/10.1107/S1744309110036791.
  • Zhu T., Bailey MF., Angley LM., Cooper TF. and Dobson RCJ. (2010) The quaternary structure of pyruvate kinase type 1 from Escherichia coli at low nanomolar concentrations. Biochimie 92(1): 116-120. http://dx.doi.org/10.1016/j.biochi.2009.09.016.
  • Atkinson SC., Dobson RCJ., Newman JM., Gorman MA., Dogovski C. and Parker MW. (2009) Crystallization and preliminary X-ray analysis of dihydrodipicolinate synthase from Clostridium botulinum in the presence of its substrate pyruvate. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 65(3): 253-255. http://dx.doi.org/10.1107/S1744309108039018.
  • Dobson RCJ., Perugini MA., Jameson GB. and Gerrard JA. (2009) Specificity versus catalytic potency: the role of threonine 44 in Escherichia coli dihydrodipicolinate synthase mediated catalysis. Biochimie 91(8): 1036-1044. http://dx.doi.org/10.1016/j.biochi.2009.05.013.
  • Domigan LJ., Scally SW., Fogg MJ., Hutton CA., Perugini MA., Dobson RCJ., Muscroft-Taylor AC., Gerrard JA. and Devenish SRA. (2009) Characterisation of dihydrodipicolinate synthase (DHDPS) from Bacillus anthracis. Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics 1794(10): 1510-1516. http://dx.doi.org/10.1016/j.bbapap.2009.06.020.
  • Dommaraju SR., Gorman MA., Dogovski C., Pearce FG., Gerrard JA., Dobson RCJ., Parker MW. and Perugini MA. (2009) Cloning expression and crystallization of Dihydrodipicolinate reductase from Methicillin-resistant Staphylococcus aureus. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 66(1): 57-60.
  • Guo BBB., Devenish SRA., Dobson RCJ., Muscroft-Taylor AC. and Gerrard JA. (2009) The C-terminal domain of Escherichia coli dihydrodipicolinate synthase (DHDPS) is essential for maintenance of quaternary structure and efficient catalysis. Biochemical and Biophysical Research Communications 380(4): 802-806. http://dx.doi.org/10.1016/j.bbrc.2009.01.169.
  • James PF., Dogovski C., Dobson RCJ., Bailey MF., Goldie KN., Karas JA., Scanlon R., O'Hair J. and Perugini A. (2009) Aromatic residues in the C-terminal helix of human apoC-I mediate phospholipid interactions and particle morphology. The Journal of Lipid Research 50(7): 1384-1394. http://dx.doi.org/10.1194/jlr.M800529-JLR200.
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  • Voss JE., Scally SW., Taylor NL., Dogovski C., Alderton MR., Hutton CA., Gerrard JA., Parker MW., Dobson RCJ. and Perugini MA. (2009) Expression, purification, crystallization and preliminary X-ray diffraction analysis of dihydrodipicolinate synthase from Bacillus anthracis in the presence of pyruvate.. Acta Crystallogr Sect F Struct Biol Cryst Commun 65(Pt 2): 188-191. http://dx.doi.org/10.1107/S1744309109000670.
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  • Boughton BA., Dobson RCJ., Gerrard JA. and Hutton CA. (2008) Conformationally constrained diketopimelic acid analogues as inhibitors of dihydrodipicolinate synthase. Bioorganic & Medicinal Chemistry Letters 18: 460-463. http://dx.doi.org/10.1016/j.bmcl.2007.11.108.
  • Boughton BA., Grifftin DW., O'Donnell PA., Dobson RCJ., Perugini MA., Gerrard JA. and Hutton CA. (2008) Irreversible inhibition of dihydrodipicolinate synthase by 4-oxo-heptenedioic acid analogues. Bioorganic & Medicinal Chemistry 16: 9975-9983. http://dx.doi.org/10.1016/j.bmc.2008.10.026.
  • Burgess BR., Dobson RCJ., Bailey MF., Atkinson SC., Griffin MDW., Jameson GB., Parker MW., Gerrard JA. and Perugini MA. (2008) Structure and evolution of a novel dimeric enzyme from a clinically important bacterial pathogen. The Journal of Biological Chemistry 283(41): 27598-27603. http://dx.doi.org/10.1074/jbc.M804231200.
  • Burgess BR., Dobson RCJ., Dogovski C., Jameson GB., Parker MW. and Perugini MA. (2008) Purification, crystallization and preliminary X-ray diffraction studies to near-atomic resolution of dihydrodipicolinate synthase from methicillin-resistant Staphylococcus aureus. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 64(7): 659-661. http://dx.doi.org/10.1107/S1744309108016746.
  • Devenish SR., Gerrard JA., Jameson GB. and Dobson RCJ. (2008) The high-resolution structure of dihydrodipicolinate synthase from Escherichia coli bound to its first substrate, pyruvate. Acta Crystallographica Section F: Structural Biology and Crystallization Communications F64(12): 1092-1095. http://dx.doi.org/10.1107/S1744309108033654.
  • Dobson RCJ., Atkinson SC., Gorman MA., Newman JM., Parker MW. and Perugini MA. (2008) The purification, crystallisation, and preliminary X-ray diffraction analysis of dihydrodipicolinate synthase from Clostridium botulinum. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 64(3): 206-208. http://dx.doi.org/10.1107/S1744309108002819.
  • Dobson RCJ., Griffin MDW., Devenish SRA., Pearce FG., Hutton CA., Gerrard JA., Jameson GB. and Perugini MA. (2008) Conserved main-chain peptide distortions: a proposed role for Ile203 in catalysis by dihydrodipicolinate synthase. Protein Science 17(12): 2080-2090. http://dx.doi.org/10.1110/ps.037440.108.
  • Griffin MDW., Dobson RCJ., Pearce FG., Antonio L., Whitten AE., Liew CK., Mackay JP., Trewhella J., Jameson GB. and Perugini MA. (2008) Evolution of quaternary structure in a homotetrameric enzyme. Journal of Molecular Biology 380(4): 691-703. http://dx.doi.org/10.1016/j.jmb.2008.05.038.
  • Kefala G., Evans GL., Griffin MDW., Devenish SRA., Pearce FG., Perugini MA., Gerrard JA., Weiss MS. and Dobson RCJ. (2008) Crystal structure and kinetic study of dihydrodipicolinate synthase from Mycobacterium tuberculosis. Biochemical Journal 411(2): 351-360. http://dx.doi.org/10.1042/BJ20071360.
  • Mitsakos V., Dobson RCJ., Pearce FG., Devenish SR., Evans GL., Burgess BR., Perugini MA., Gerrard JA. and Hutton CA. (2008) Inhibiting dihydrodipicolinate synthase across species: Towards specificity for pathogens? Bioorganic & Medicinal Chemistry Letters 18(2): 842-844. http://dx.doi.org/10.1016/j.bmcl.2007.11.026.
  • Pearce FG., Dobson RCJ., Weber A., Lane LA., McCammon MG., Squire MA., Perugini MA., Jameson GB., Robinson CV. and Gerrard JA. (2008) Mutating the tight-dimer interface of dihydrodipicolinate synthase disrupts the enzyme quaternary structure: Toward a monomeric enzyme. Biochemistry 47(46): 12108-12117. http://dx.doi.org/10.1021/bi801094t.
  • Dobson RCJ., Devenish SRA., Turner LA., Clifford VR., Pearce FG., Jameson GB. and Gerrard JA. (2005) Role of Arginine 138 in the catalysis and regulation of Escherichia coli dihydrodipicolinate synthase. Biochemistry 44: 13007-13013.
  • Dobson RCJ., Griffin MDW., Jameson GB. and Gerrard JA. (2005) The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance. Acta Crystallographica Section D: Biological Crystallography 61: 1116-1124.
  • Turner JJ., Healy JP., Dobson RCJ., Gerrard JA. and Hutton CA. (2005) Two new irreversible inhibitors of dihydrodipicolinate synthase: diethyl (E,E)-4-oxo-2,5-heptadienedioate and diethyl (E)-4-oxo-2-heptenedioate. Bioorganic and Medicinal Chemistry Letters 15: 995-998.
  • Dobson RCJ., Gerrard JA. and Pearce FG. (2004) Dihydrodipicolinate synthase is not inhibited by its substrate, (S)-aspartate beta-semialdehyde. Biochemical Journal 377: 757-762.
  • Dobson RCJ., Griffin MDW., Roberts SJ. and Gerrard JA. (2004) Dihydrodipicolinate synthase (DHDPS) from Escherichia coli displays partial mixed inhibition with respect to its first substrate, pyruvate. Biochimie 86(4-5): 311-315.
  • Dobson RCJ., Pearce FG. and Gerrard JA. (2004) Dihydrodipicolinate synthase is not inhibited by its substrate, (S)-aspartate semialdehyde. Biochemical Journal 377: 757-762.
  • Dobson RCJ., Valegard K. and Gerrard JA. (2004) The Crystal Structure of Three Site-directed Mutants of Escherichia coli Dihydrodipicolinate Synthase: Further Evidence for a Catalytic Triad. Journal of Molecular Biology 338(2): 329-339.
  • Roberts SJ., Morris JC., Dobson RCJ., Baxter CL. and Gerrard JA. (2004) Two complete syntheses of (S)-aspartate semi-aldehyde and demonstration that Δ2-tetrahydroisophthalic acid is a non-competitive inhibitor of dihydrodipicolinate synthase. Arkivoc 2004(10): 166-177.
  • Roberts SJ., Morris JC., Dobson RCJ. and Gerrard JA. (2003) The preparation of (S)-Aspartate semi-aldehyde appropriate for use in biochemical studies. Bioorganic and Medicinal Chemistry Letters 13(2): 265-267.
Oral Presentations
  • Dobson RCJ. (2017) Bacterial sialic acid import and regulation. Victoria University Wellington: School of Biological Sciences Seminar Series.
  • Dobson RCJ. (2017) Bacterial sialic acid import. University of Auckland: New Zealand Membrane Protein Biology Synposium.
  • Dobson RCJ. (2017) Bacterial sialic acid improt. Bunker Bay, WA, Australia: 31st Biennial Conference of the Society of Crystallographers in Australia and New Zealand, Crystal31, 04 Dec 2017.
  • Dobson RCJ. (2017) The anatomy of an adapted enzyme. Bangalore, India: The National Centre for Biological Sciences (NCBS) Seminar Series, 14 Jul 2017.
  • Dobson RCJ. (2017) The anatomy of an adapted enzyme. Glasgow, UK: AUC2017, 27 Jul 2017.
  • Dobson RCJ. (2017) The anatomy of an adapted enzyme. University of Otago, Dunedin: GSA/NZSBMB 2017.
  • Dobson RCJ. (2016) Bacterial sialic acid import and regulation. Danbury, CT, USA: Advanced AUC Workshop Symposium.
  • Dobson RCJ. (2016) The anatomy of an adapted enzyme. Christchurch: Joint NZMS-NZSBMB conference.
  • Dobson RCJ. (2016) Using hydrogen/deuterium exchange mass spectrometry to untangle allosteric mechanisms. University of Otago, Christchurch: Otago Mass Spectrometry Symposium.
  • Dobson RCJ. (2015) Not different, just better: The adaptive evolution of a glycolytic enzyme. University of Auckand, New Zealand.
  • Dobson RCJ. (2015) Not different, just better: The adaptive evolution of a glycolytic enzyme. University of Houston, TX, USA: Seminar.
  • Dobson RCJ. (2015) Not different, just better: The adaptive evolution of a glycolytic enzyme. University of York, Toronto, Canada.
  • Dobson RCJ. (2013) Enzymes: dynamics, quaternary structure and evolution. Massey University,: Institute of Molecular BioSciences Seminar Series.
  • Dobson RCJ. (2013) Enzymes: dynamics, quaternary structure and evolution. University of Auckland, Medical School: School Seminar Series.
  • Dobson RCJ. (2012) Applied Research at the Biomolecular Interaction Centre. Plant & Food research, Lincoln, NZ.
  • Dobson RCJ. (2012) Seeing is believing: the joys and pitfalls of structural biology. St Marks Church, Avonhead, Christchurch: U3A Godley Seminar Series.
  • Dobson RCJ. (2009) The role of oligomerisation in enzyme function: Structure and evolution of an essential bacterial enzyme. Europen Moleculay Biology Laboratory - Hamburg: EMBL Seminar Series.
  • Dobson RCJ. (2009) The role of oligomerisation in enzyme function: Structure and evolution of an essential bacterial enzyme. Swiss Federal Institute of Technology (ETH) - Zürich: Laboratory of Physical Chemistry Seminar Series.
  • Dobson RCJ. (2009) The role of oligomerisation in enzyme function: Structure and evolution of an essential bacterial enzyme. Department of Biochemistry, University of Bristol: Department of Biochemistry Seminar Series.
  • Dobson RCJ. and Gerrard JA. (2001) Understanding Lysine Biosynthesis: regulation of dihydrodipicolinate synthase. Napier, New Zealand: Molecules for Life, 06 Oct 2004.
Conference Contributions - Other
  • Board AJ., Dobson RCJ., Crowther J. and Jameson G. (2018) The role of protein interactions in complex food. Riddet Conference, 10 Jul 2018.
  • Currie M., North RA. and Dobson R. (2018) Probing the catalytic mechanism of N-acetylmannosamine-6-phosphate 2-epimerase from methicillin-resistant Staphylococcus aureus. Lorne, VIC, Australia: Lorne Protein Structure and Function Conference, 4 Feb 2018.
  • Watkin S., Dobson R. and Nock VM. (2018) Tracking diffusion using fluorescence microscopy. Auckland, New Zealand: Australia and New Zealand Nano and Microfluidics 2018, 26-29 Jun 2018.
  • Crowther J., Hodgkinson A., Jameson G. and Dobson R. (2017) Understanding whey proteins. Melbourne, Australia: Lorne Conference on Protein Structure and Function, 5-8 Feb 2017.
  • North RA. and Dobson RC. (2017) Bacterial sialic acid import. Tällberg, Sweden: The 21st Annual Conference of the Swedish Structural Biology Network.
  • North RA. and Dobson RC. (2017) The structure and function of a bacterial sialic acid transporter. Christchurch, New Zealand: Biomolecular Interaction Centre Biomedical Symposium.
  • North RA. and Dobson RCJ. (2017) The structure and function of a bacterial sialic acid transporter. Queenstown, New Zealand: Queenstown Molecular Biology: Proteins, 8 Sep 2017.
  • Watkin S., Pearce FG., Dobson R. and Nock VM. (2017) Developing New Microfluidic Tools for the Biochemistry Toolbox. Lorne, Australia: 42nd Lorne Conference on Protein Structure and Function, 5-8 Feb 2017.
  • Crowther J., Hodgkinson A., Jameson G. and Dobson R. (2016) Characterisation and comparison of β-lactoglobulin orthologues. Queenstown, New Zealand: Queenstown Molecular Biology, 27-31 Aug 2016.
  • North RA. and Dobson R. (2016) Bacterial sialic acid import. Christchurch, New Zealand: Annual Biomolecular Interaction Centre Symposium.
  • Crowther J., Hodgkinson A., Jameson G. and Dobson R. (2015) Characterisation and comparison of β-lactoglobulin orthologues. Boston, USA: Experimental Biology, 28 Mar-1 Apr 2015.
  • Crowther J., Hodgkinson A., Jameson G. and Dobson R. (2015) Characterisation and comparison of β-lactoglobulin orthologues. Melbourne, Australia: Lorne Conference on Protein Structure and Function, 8-11 Feb 2015.
  • Crowther J., Hodgkinson A., Jameson G. and Dobson R. (2015) Characterisation and comparison of β-lactoglobulin orthologues. New Hampshire, USA: Gordon Research Conference: Proteins, 14-19 Jun 2015.
  • Dobson RCJ. (2014) Not different, just better: The adaptive evolution of a glycolytic enzyme. Canberra, Australia: COMBIO2014, 28 Sep-2 Oct 2014.
  • Donovan KA., Peng F., Kessans SA., Cooper TF. and Dobson RCJ. (2014) The adaptive evolution of a key glycolytic enzyme. Lorne, Australia: 39th Lorne Protein Structure and Function Conference, 6-9 Feb 2014.
  • Lim YC., Catimel B., Tran M., Anasir MI., Wong B., Dobson RCJ., Scholz G., Lio D., Kamarruddin MA. and Griffin MDW. (2014) Identification of the determinant of CSK-homologous kinase (CHK) important for its tumour suppressor effects. Lorne, Australia: 39th Lorne Protein Structure and Function Conference, 9-13 Feb 2014.
  • Mahapatra D., Gerrard JA., Dyer J., Dobson RCJ., Valery C., Steel PJ. and Suzuki H. (2014) Self assembly of collagen model peptides. Lorne, Australia: 39th Lorne Protein Structure and Function Conference, 6-9 Feb 2014.
  • Muscroft-Taylor A., Seizova S., Huisman F. and Dobson RCJ. (2014) Chemo-enzymatic approaches to the biosynthesis of sialylated materials. Lorne, Australia: 39th Lorne Protein Structure and Function Conference, 9-13 Feb 2014.
  • North RA. and Dobson RC. (2014) Probing novel antibiotic targets within sialic acid catabolism. Tällberg, Sweden: The 18th Annual Conference of the Swedish Structural Biology Network, 13 Jun 2014.
  • North RA. and Dobson RCJ. (2014) Probing novel antibiotic targets within sialic acid catabolism. Tällberg, Sweden: The 18th Annual Conference of the Swedish Structural Biology Network, 13 Jun 2014.
  • North RA., Kessans SA., Suzuki H., Watson AJ., Griffin MDW., Fairbanks AJ. and Dobson RCJ. (2014) Novel Antibiotic Targets within Sialic Acid Catabolism. Lorne, Australia: 40th Lorne Protein Structure and Function Conference, 6-9 Feb 2014.
  • Pandey R., Pearce FG., Dyer J., Dobson RCJ., Valéry C. and Gerrard JA. (2014) Self assembly of protein inspired peptides. Lorne, Australia: 39th Lorne Protein Structure and Function Conference, 6-9 Feb 2014.
  • Ravichandran A., Suzuki H., Tabata K., Rogov V., McEwan D., Wild P., Law A., Morita E., Dikic I. and Wakatsuki S. (2014) You are what you eat: Molecular mechanisms for autophagosome formation. Hanmer Springs, New Zealand: New Zealand Structural Biology Conference 2014, 30 Jun-2 Jul 2014.
  • Ravichandran AC., Suzuki H., Law A., Morita E. and Dobson RCJ. (2014) Mode of interaction of LC3A and GABARAP with ATG16L1. Lorne, Australia: 39th Lorne Protein Structure and Function Conference, 9-13 Feb 2014.
  • Crowther J., Hudson A., Atkinson S. and Dobson R. (2013) A structural characterisation of Diaminopimelate Decarboxylase from Arabidopsis thaliana. Melbourne, Australia: Lorne Conference on Protein Structure and Function, 10-13 Feb 2013.
  • Dobson RCJ. (2013) Not different, just better: adaptations in a glycolytic enzyme. Christchurch, New Zealand: BIC Symposium, 23-23 Aug 2013.
  • Dobson RCJ. (2013) Not different, just better: the adaptive evolution of a glycolytic enzyme. Denver, CO, USA: Mechanisms of Protein Evolution, 7-9 Feb 2013.
  • Donovan KA., Kessans SA. and Dobson RCJ. (2013) Regulatory switch of a key glycolytic enzyme. Lorne, Australia: 38th Lorne Protein Structure and Function Conference, 9-13 Feb 2013.
  • Donovan KA., Kessans SA., Peng F., Zhu T., Cooper TF. and Dobson RCJ. (2013) Not different, just better: the adaptive evolution of a glycolytic enzym. Melbourne, Australia: Australian Society for Biophysics Annual Meeting, 24-27 Nov 2013.
  • Gilmour L., Pattinson N., Owen M., Yandle T., Fee C. and Dobson RCJ. (2013) The Redox Switch That Could Make All The Difference! Lorne, Australia: 38th Lorne Protein Structure and Function Conference, 5-9 Feb 2013.
  • Mandani A., Thompson D., Dobson R., Gieseg S. and Badami K. (2013) Electro-Chemical Changes with ABO-Incompatible Red Blood Cell Transfusions. Gold Coast, Australia: HAA 2013, 20-23 Oct 2013.
  • Orban T., Lasse M., Fairbanks AJ. and Dobson RCJ. (2013) Aldehyde-Hemoglobin adducts act as biomarker for diabetic complications. Christchurch, New Zealand: MedTech in Christchurch, 18-18 Dec 2013.
  • Atkinson SC., Dogovski C., Dobson RC. and Perugini MA. (2012) INSIGHTS INTO REGULATION AND INHIBITION OF AN ESSENTIAL ENZYME IN BACTERIA AND PLANTS. Lorne, Australia: 37th Lorne Protein Structure and Function Conference, 5-9 Feb 2012.
  • Cross PJ., Dobson RCJ., Patchett ML. and Parker EJ. (2012) UNRAVELLING THE EVOLUTION OF ALLOSTERIC CONTROL IN A CRUCIAL BIOSYNTHETIC ENZYME. Lorne, Australia: 37th Lorne Protein Structure and Function Conference, 5-9 Feb 2012.
  • Hor L., Dobson RCJ., Hutton CA. and Perugini MA. (2012) BACTERIAL DIAMINOPIMELATE EPIMERASE FORMS AN ACTIVE DIMER. Lorne, Australia: 37th Lorne Protein Structure and Function Conference, 5-9 Feb 2012.
  • Keller S., Billakanti J., Wason A., Griffin MDW., Dobson RCJ., Perugini MA., Gerrard JA. and Pearce FG. (2012) CHARACTERISATION OF DHDPS AND DHDPR FROM ARABIDOPSIS THALIANA. Lorne, Australia: 38th Lorne Protein Structure and Function Conference, 5-9 Feb 2012.
  • Wubben J., Dogovski C., Dobson RCJ., Codd R., Gerrard JA., Parker MW. and Perugini MA. (2012) DYNAMICS OF AN ESSENTIAL ENZYME FROM A “COLD” BACTERIUM; INSIGHTS INTO THE MOLECULAR EVOLUTION OF QUATERNARY STRUCTURE. Lorne, Australia: 37th Lorne Protein Structure and Function Conference, 5-9 Feb 2012.
  • Dobson R. (2011) A new pathway to lysine biosynthesis: L,L-Diaminopimelate aminotransferase. Rotorua, New Zealand: Crystal 27 SCANZ Conference 2011, 27-30 Apr 2011.
  • Giron IO., Dobson RCJ. and Hudson AO. (2011) Characterization of L,L-diaminopimelate aminotransferase from Chlamydomonas reinhardtii. Minneapolis, MN, USA: Plant Biology 2011, 6-10 Aug 2011.
  • Hor L., Dogovski C., Dobson RCJ., Hutton CA. and Perugini MA. (2011) Characterisation and structure of E. coli diaminopimelate epimerase. Lorne, Australia: Lorne Protein Structure and Function Conference, 6-10 Feb 2011.
  • Atkinson SC., Dogovski C., Dobson RCJ. and Perugini MA. (2010) Structure of Dihydrodipicolinate Synthase from Bacteria and Plants: Insights into Regulation and Inhibition of a Valid Drug Target. Erice, Italy: Erice 2010: Structure and Function from Macromolecular Crystallography, 10-10 Jun 2010.
  • Atkinson SC., Dogovski C., Dobson RCJ. and Perugini MA. (2010) Structure, function and inhibition of Agrobacterium tumefaciens DHDPS Sarah C. Atkinson, Con Dogovski, Renwick C. J. Dobson, Matthew A. Perugini. Lorne, Australia: Lorne Protein Structure and Function conference, 7-7 Feb 2010.
  • Dobson RCJ. (2010) Structure and enzymology of diaminopimelate epimerase. Waiheke Island, New Zealand: NZ Structural Biology Meeting, 14-16 Jun 2010.
  • Hor L., Dobson RCJ., Dogovski C., Hutton CA. and Perugini MA. (2010) Characterisation and structure of E. coli diaminopimelate epimerase. Waterville Valley, NH, USA: 2010 Gordon Conference on Enzymes, Coenzymes & Metabolic Pathways, 18-23 Jul 2010.
  • Hor L., Dogovski C., Dobson RCJ., Hutton CA. and Perugini MA. (2010) Bacterial Diamiopimelate Epimerase: A Target for Rational Drug Design. Lorne, Australia: Lorne Protein Structure and Function Conference, 7-11 Feb 2010.
  • Dobson RCJ. (2009) The role of oligomerisation in enzyme function: Structure and evolution of an essential bacterial enzyme. Christchurch, New Zealand: Combio 2009, 6-10 Dec 2009.
  • Hor L., Dogovski C., Dobson RCJ., Hutton CA. and Perugini MA. (2009) Bacterial Lysine Biosynthesis: A Target for Rational Drug Design. Melbourne, Australia: Melbourne Protein Group, 15-15 Jul 2009.
  • Dobson RCJ. (2008) The structural biology of a dimeric dihydrodipicolinate synthase. Cairns, Australia: The Joint 2nd Pacific Rim International Conference on Protein Science and 4th Asian-Oceania Human Proteome Organization, 22-26 Jun 2008.
  • Hodder AN., Gilson PR., Dobson RCJ., Perugini MA., Norton RS. and Crabb BS. (2008) Analysis of the highly conserved C-terminal domain od SERA5 from Plasmodium faciparum. Lorne, Australia: Lorne Protein Structure and Function Conference, 8-12 Feb 2008.
  • Dobson RCJ., Jameson GB. and Gerrard JA. (2006) Investigating catalytic and regulatory mechanisms in dihydrodipicolinate synthase. Auckland, New Zealand: 1st New Zealand Structural Biology Meeting, 18-19 Mar 2006.
  • Evans GL., Devenish SRA., Dobson RCJ., Pearce FG. and Gerrard JA. (2006) Kinetic study of dihydrodipicolinate synthase (DHDPS) from Mycobacterium tuberculosis. Lorne, Australia: 31st Annual Lorne Conference on Protein Structure and Function, 5-9 Feb 2006.
  • Dobson RCJ. and Gerrard JA. (2005) Investigating Catalytic and Regulatory Mechanisms in Dihydrodipicolinate Synthase (DHDPS). Barcelona, Spain: VIth European Symposium of the Protein Society, 1 May 2005.
  • Dobson RCJ. and Gerrard JA. (2005) Investigating Catalytic and Regulatory Mechanisms in Dihydrodipicolinate Synthase (DHDPS). Lorne, Australia: 30th Annual Lorne Conference on Protein Structure and Function, 6 Feb 2005.
  • Dobson RCJ. and Gerrard JA. (2004) Investigating Catalytic and Regulatory Mechanisms in Dihydrodipicolinate Synthase (DHDPS). Lorne, Australia: 29th Lorne Conference on Protein Structure and Function, 8 Feb 2004.
  • Dobson RCJ. and Gerrard JA. (2002) Probing the Catalytic Mechanism of DHDPS. Lorne, Australia: 27th Annual Lorne Conference on Protein Structure and Function, 10 Feb 2002.
  • Gerrard JA., Pearce FG. and Dobson RCJ. (2002) Is dihydrodipicolinate synthase inhibited by its substrate? Lorne, Australia: 27th Annual Lorne Conference on Protein Structure and Function, 9 Feb 2002.
  • Gerrard JA. and Dobson RCJ. (2000) Studying Mechanisms in DHDPS. Wellington, New Zealand: ComBio 2000, 11 Dec 2000.
  • Gerrard JA., Pearce FG. and Dobson RCJ. (2000) Is dihydrodipicolinate synthase inhibited by its substrate? Wellington, New Zealand: ComBio 2000, 11 Dec 2000.
  • Dobson RCD. and Gerrard JA. (1999) Regulation of dihydrodipicolinate synthase in E. coli. Queenstown, New Zealand: Annual Queenstown Molecular Biology Conference, 1 Jan 1999.
Conference Contributions - Published
  • Meffan RC., Mak D., Menges J., Dolamore F., Fee C., Dobson RCJ. and Nock V. (2022) Field Effect Transistor-Like Control of Capillaric Flow Using Off-Valves. In IEEE Symposium on Mass Storage Systems and Technologies 2022-January: 263-266. http://dx.doi.org/10.1109/MEMS51670.2022.9699604.
  • Meffan R., Menges J., Dolamore F., Fee C., Dobson R. and Nock V. (2020) Transistor off-valve based feedback, metering and logic operations in capillary microfluidics. In http://dx.doi.org/10.1109/MEMS51782.2021.9375175.
  • Wahlgren WY., Dunevall E., North RA., Paz A., Scalise M., Bisignano P., Bengtsson-Palme J., Goyal P., Claesson E. and Nilsson U. (2017) Structural Insights into Bacterial Sialic Acid Transport. In GLYCOBIOLOGY 27(12): 1233-1233.
  • Buckle AM., Androulakis S., Schmidberger J., Bate M., DeGori R., Beitz A., McGowan S., Porter C., Harrison A. and Hunter J. (2008) Federated repositories of X-ray diffraction images. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES 64: C153-C154. http://dx.doi.org/10.1107/S0108767308095056.
  • Zhu T., Fei N., Perugini MA., Cooper TF. and Dobson RCJ. (2008) In vivo evolution of Escherichia coli pyruvate kinase type I: how does genotypic evolution affect phenotype? In Journal of Proteomics & Bioinformatics 1: 237-238.
Theses / Dissertations
  • Dobson RCJ. (2004) Investigating the catalytic and regulatory mechanisms of dihydrodipicolinate synthase. Christchurch, New Zealand. University of Canterbury.
Chapters
  • Hudson AO., Savka MA., Pearce FG. and Dobson R. (2017) Lysine biosynthesis in microorganisms.. In D'Mello JPF (Ed.), The handbook of microbial metabolism of amino acids.CABI. http://dx.doi.org/10.1079/9781780647234.0049.
  • Watkin SAJ., Ryan TM., Miller AG., M. Nock V., Pearce FG. and Dobson RCJ. (2017) Microfluidics for Small-Angle X-ray Scattering. X-ray Scattering: 1-17. Rijeka: InTech. http://dx.doi.org/10.5772/65678.
  • Crowther J., Jameson G., Hodgkinson A. and Dobson R. (2016) Structure, Oligomerisation and Interactions of β-Lactoglobulin. In Gigli I (Ed.), Milk Proteins - From Structure to Biological Properties and Health Aspects: 33-50.InTech. http://dx.doi.org/10.5772/62992.
  • Dogovski C., Atkinson SC., Dommaraju SR., Dobson RCJ., Perugini MA., Hor L., Huton CA. and Gerrard JA. (2009) Lysine biosynthesis in bacteria - An unchartered pathway for novel antibiotic design. In Doelle HW; Rokem S (Ed.), Biotechnology Volume XI: 146-166. Oxford: Eolss Publishers.
Additional Publications
  • Heinemann JA., Dobson R. and Walker S. (2012) Serological evaluation of sheep.Confidential. 5pp.

Student Supervision

Displaying all items.
    Completed
  • PhD - Atkinson S: The structure and function of DHDPS from Clostridium botulinum. (2012)
  • PhD - Dayaram A: Characterisation of novel cycloviruses (2015)
  • PhD - Horne C: Regulation of bacterial sialic acid metabolism (2019)
  • PhD - Pandey R: Self assembly of protein inspired peptides (2015)
  • PhD - Peng F: Epistasis and protein evolution (2015)
  • PhD - Sun X: Enhanced Protein Functionalities (2016)
  • PhD - Wason A: LSR proteins and nano-structures (2014)
  • PhD - Weusten M: Structure and function of KDO8PS (2021)
  • PhD - Wheeler N: A profile based method for measuring the impact of genetic variation. (2017)
  • Masters - Mahapatra D: Collagen peptides as nanomaterials (2017)

Affiliations

  • Australian Society for Biochemistry and Molecular Biology (ASBMB) (Professional Organisation): Member
  • Maurice Wilkins Centre for Molecular Biodiscovery (Teaching/Research Organisation): Affiliate Investigator
  • New Zealand Institute of Chemistry (NZIC) (Professional Organisation): Member
  • New Zealand Society for Biochemistry and Molecular Biology (NZSBMB) (Professional Organisation): Member
  • Royal Society of New Zealand (RSNZ) (Professional Organisation): Member
  • Society of Crystallographers in Australia and New Zealand (SCANZ) (Professional Organisation): Member

Research Projects

  • Unravelling molecular details of protein interactions that drive Alzheimers disease.

Key Methodologies

  • Macromolecular crystallography
  • Analytical ultracentrifugation
  • Protein and Enzyme engineering
  • Molecular Biology (PCR, gene sub-cloning and over-expression)
  • Protein expression and purification
  • Small angle X-ray and neutron scattering
  • Multiangle laser light scattering (MALLS)
  • Mass spectrometry
  • Circular dichroism
  • Fluorescence spectroscopy
  • Isothermal titration microcalorimetry
  • Protein dynamics (NMR and MD simulations, via collaborations)

Equipment

  • Analytical ultracentrifuge
  • Centrifuge Mini, minispin plus Eppendorf
  • Centrifuge Mini, minispin plus Eppendorf
  • Crystallography stereo microscope
  • Fluoroesence Spectrophotometer Cary 100 Varian
  • Gel Box, Biorad
  • Ph meter, utrabasic Denver
  • Rocking Platform, Ultra Rocker Biorad
  • Rotor vap, Buchi R-114 Watson Victor
  • Shaker Orbital, KS250basic IKA
  • Spectrophotometer Smart, ss3000 Biorad
  • Stirrer, Colour Squid IKA
  • Stirrer/heating, MST11 Techmatic
  • UV Visable Spectrophotomer, Cary 100 Varian
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