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Research Publications for Vickery L (Vic) Arcus

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Author's Publications

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

  • 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

  • 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

  • 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

  • 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

  • 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

  • Summers, E. L., Moon, C. D., Atua, R., & Arcus, V. L. (2016). The structure of a glycoside hydrolase 29 family member from a rumen bacterium reveals unique, dual carbohydrate-binding domains. Acta Crystallographica Section F: Structural Biology Communications, 72(Part 10), 750-761. doi:10.1107/S2053230X16014072

  • 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

  • Nazmi, A. R., Lang, E. J. M., Bai, Y., Allison, T. M., Othman, M. H., Panjikar, S., . . . Parker, E. J. (2016). Interdomain conformational changes provide allosteric regulation en route to chorismate. Journal of Biological Chemistry, 291(42), 21836-21847. doi:10.1074/jbc.M116.741637

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