Research Publications for Vickery L (Vic) Arcus

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Publications ByARCUS, Vickery L (Vic)

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  • Robinson, J. M., O Neill, T. A., Ryburn, J., Liang, L. L., Arcus, V. L., & Schipper, L. A. (2017). Rapid laboratory measurement of the temperature dependence of soil respiration and application to changes in three diverse soils through the year. Biogeochemistry, 133(1), 101-112. doi:10.1007/s10533-017-0314-0

  • Hobbs, J. K., Jiao, W., Easter, A. D., Parker, E. J., Schipper, L. A., & Arcus, V. L. (2017). Change in Heat Capacity for Enzyme Catalysis Determines Temperature Dependence of Enzyme Catalyzed Rates. ACS Chemical Biology, 12(3), 868. doi:10.1021/acschembio.7b00065

  • Jones, H. B. L., Wells, S. A., Prentice, E. J., Kwok, A., Liang, L. L., Arcus, V. L., & Pudney, C. R. (2017). A complete thermodynamic analysis of enzyme turnover links the free energy landscape to enzyme catalysis. The FEBS Journal, 14 pages. doi:10.1111/febs.14152

  • Prentice, E. J., & Arcus, V. (2017). Understanding biological rates and their temperature dependence, from enzymes to ecosystems. Poster session presented at the meeting of AGU (American Geophysical Union) Fall Meeting. New Orleans Ernest N. Morial Convention Center, New Orleans, Louisiana, USA.

  • Liang, L. L., Arcus, V. L., Heskel, M. A., O'Sullivan, O. S., Weerasinghe, L. K., Creek, D., . . . Schipper, L. A. (2017). Macromolecular Rate Theory (MMRT) provides a thermodynamics rationale to underpin the convergent temperature response in plant leaf respiration. Global Change Biology. doi:10.1111/gcb.13936

  • Mulholland, C. V., Ruthe, A., Cursons, R. T., Durrant, R., Karalus, N., Coley, K., . . . Aung, H. L. (2017). Rapid molecular diagnosis of the Mycobacterium tuberculosis Rangipo strain responsible for the largest recurring TB cluster in New Zealand. Diagnostic Microbiology and Infectious Disease, 3 pages. doi:10.1016/j.diagmicrobio.2017.03.012

  • Firestone, R. S., Cameron, S. A., Karp, J. M., Arcus, V. L., & Schramm, V. L. (2017). Heat capacity changes for transition-state analogue binding and catalysis with Human 5 '-methylthioadenosine phosphorylase. ACS Chemical Biology, 12(2), 464-473. doi:10.1021/acschembio.6b00885

  • Summers, E. L., Cumming, M. H., Oulavallickal, T., Roberts, N. J., & Arcus, V. L. (2017). Structures and kinetics for plant nucleoside triphosphate diphosphohydrolases support a domain motion catalytic mechanism. Protein Science. doi:10.1002/pro.3199

  • van der Kamp, M. W., Prentice, E. J., Kraakman, K. L., Connolly, M., Mulholland, A. J., & Arcus, V. L. (2017). Dynamical origins of heat capacity changes in enzyme catalysed reactions. bioRxiv. doi:10.1101/165324

  • Arcus, V. L., Prentice, E. J., Hobbs, J. K., Mulholland, A. J., Van der Kamp, M. W., Pudney, C. R., . . . Schipper, L. A. (2016). On the Temperature Dependence of Enzyme-Catalyzed Rates. Biochemistry, 55(12), 1681-1688. doi:10.1021/acs.biochem.5b01094

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