Reference Library

  1. Zhang, J., Suflita, M., Fiaschetti, C. M., Li, G., Li, L., Zhang, F., ... & Linhardt, R. J. (2015). High cell density cultivation of a recombinant Escherichia coli strain expressing a 6‐O‐sulfotransferase for the production of bioengineered heparin. Journal of Applied Microbiology, 118(1), 92-98. https://doi.org/10.1111/jam.12684
  2. McDougle, D. R., Baylon, J. L., Meling, D. D., Kambalyal, A., Grinkova, Y. V., Hammernik, J., ... & Das, A. (2015). Incorporation of charged residues in the CYP2J2 FG loop disrupts CYP2J2–lipid bilayer interactions. Biochimica et Biophysica Acta (BBA)-Biomembranes, 1848(10), 2460-2470.https://doi.org/10.1016/j.bbamem.2015.07.015
  3. Smanski, M. J., Bhatia, S., Zhao, D., Park, Y., Woodruff, L. B., Giannoukos, G., ... & Gordon, D. B. (2014). Functional optimization of gene clusters by combinatorial design and assembly. Nature Biotechnology, 32(12), 1241.https://doi.org/10.1038/nbt.3063
  4. Blaszczyk, A. J., Silakov, A., Zhang, B., Maiocco, S. J., Lanz, N. D., Kelly, W. L., ... & Booker, S. J. (2016). Spectroscopic and electrochemical characterization of the iron–sulfur and cobalamin cofactors of TsrM, an unusual radical S-adenosylmethionine methylase. Journal of the American Chemical Society, 138(10), 3416-3426.https://doi.org/10.1021/jacs.5b12592
  5. Lanz, N. D., Lee, K. H., Horstmann, A. K., Pandelia, M. E., Cicchillo, R. M., Krebs, C., & Booker, S. J. (2016). Characterization of lipoyl synthase from Mycobacterium tuberculosis. Biochemistry, 55(9), 1372-1383. https://doi.org/10.1021/acs.biochem.5b01216
  6. Guerra, D., Ballard, K., Truebridge, I., & Vierling, E. (2016). S-nitrosation of conserved cysteines modulates activity and stability of S-nitrosoglutathione reductase (GSNOR). Biochemistry, 55(17), 2452-2464.https://doi.org/10.1021/acs.biochem.5b01373
  7. Sutherland, M. C., Rankin, J. A., & Kranz, R. G. (2016). Heme trafficking and modifications during system I cytochrome c biogenesis: insights from heme redox potentials of Ccm proteins. Biochemistry, 55(22), 3150-3156.https://doi.org/10.1021/acs.biochem.6b00427
  8. Robbins, T., Kapilivsky, J., Cane, D. E., & Khosla, C. (2016). Roles of conserved active site residues in the ketosynthase domain of an assembly line polyketide synthase. Biochemistry, 55(32), 4476-4484. https://doi.org/10.1021/acs.biochem.6b00639
  9. Inan, K., Sal, F. A., Rahman, A., Putman, R. J., Agblevor, F. A., & Miller, C. D. (2016). Microbubble assisted polyhydroxybutyrate production in Escherichia coli. BMC Research Notes, 9(1), 338. https://doi.org/10.1186/s13104-016-2145-9
  10. Wei, Y., Kuzmič, P., Yu, R., Modi, G., & Hedstrom, L. (2016). Inhibition of inosine-5′-monophosphate dehydrogenase from Bacillus anthracis: mechanism revealed by pre-steady-state kinetics. Biochemistry, 55(37), 5279-5288.https://doi.org/10.1021/acs.biochem.6b00265
  11. Tanner, J. J., Frey, B. B., Pemberton, T., & Henzl, M. T. (2016). EF5 is the high-affinity Mg2+ site in ALG-2. Biochemistry, 55(36), 5128-5141. https://doi.org/10.1021/acs.biochem.6b00596
  12. Kennedy, E. N., Menon, S. K., & West, A. H. (2016). Extended N-terminal region of the essential phosphorelay signaling protein Ypd1 from Cryptococcus neoformans contributes to structural stability, phosphostability and binding of calcium ions. FEMS Yeast Research, 16(6) fow068. https://doi.org/10.1093/femsyr/fow068
  13. Roy, J., Adili, R., Kulmacz, R., Holinstat, M., & Das, A. (2016). Development of poly unsaturated fatty acid derivatives of aspirin for inhibition of platelet function. Journal of Pharmacology and Experimental Therapeutics, 359(1), 134-141. https://doi.org/10.1124/jpet.116.234781
  14. Sigala, P. A., Morante, K., Tsumoto, K., Caaveiro, J. M., & Goldberg, D. E. (2016). In-Cell Enzymology To Probe His–Heme Ligation in Heme Oxygenase Catalysis. Biochemistry, 55(34), 4836-4849. https://doi.org/10.1021/acs.biochem.6b00562
  15. Fancher, A. T., Hua, Y., Camarco, D. P., Close, D. A., Strock, C. J., & Johnston, P. A. (2016). Reconfiguring the AR-TIF2 protein–protein interaction HCS assay in prostate cancer cells and characterizing the hits from a LOPAC screen. Assay and Drug Development Technologies, 14(8), 453-477. https://doi.org/10.1089/adt.2016.741
  16. Wang, X., Zhang, Z. T., Wang, Y., & Wang, Y. (2016). Production of polyhydroxybuyrate (PHB) from switchgrass pretreated with a radio frequency-assisted heating process. Biomass and Bioenergy, 94, 220-227. https://doi.org/10.1016/j.biombioe.2016.09.006
  17. Devendran, S., Abdel-Hamid, A. M., Evans, A. F., Iakiviak, M., Kwon, I. H., Mackie, R. I., & Cann, I. (2016). Multiple cellobiohydrolases and cellobiose phosphorylases cooperate in the ruminal bacterium Ruminococcus albus 8 to degrade cellooligosaccharides. Scientific Reports, 6, 35342. https://doi.org/10.1038/srep35342
  18. Parvez, S., Long, M. J., Lin, H. Y., Zhao, Y., Haegele, J. A., Pham, V. N., ... & Aye, Y. (2016). T-REX on-demand redox targeting in live cells. Nature Protocols, 11(12), 2328. https://doi.org/10.1038/nprot.2016.114
  19. Arnold, W. R., Baylon, J. L., Tajkhorshid, E., & Das, A. (2016). Asymmetric binding and metabolism of polyunsaturated fatty acids (PUFAs) by CYP2J2 epoxygenase. Biochemistry, 55(50), 6969-6980. https://doi.org/10.1021/acs.biochem.6b01037
  20. Fiers, W. D., Dodge, G. J., Sherman, D. H., Smith, J. L., & Aldrich, C. C. (2016). Vinylogous dehydration by a polyketide dehydratase domain in curacin biosynthesis. Journal of the American Chemical Society, 138(49), 16024-16036. https://doi.org/10.1021/jacs.6b09748
  21. Le, C. Q., Oyugi, M., Joseph, E., Nguyen, T., Ullah, M. H., Aubert, J., ... & Johnson-Winters, K. (2017). Effects of isoleucine 135 side chain length on the cofactor donor-acceptor distance within F420H2: NADP+ oxidoreductase: a kinetic analysis. Biochemistry and Biophysics Reports, 9, 114-120. https://doi.org/10.1016/j.bbrep.2016.11.012
  22. Plumley, B. A., Martin, K. H., Borlee, G. I., Marlenee, N. L., Burtnick, M. N., Brett, P. J., ... & Borlee, B. R. (2017). Thermoregulation of biofilm formation in Burkholderia pseudomallei is disrupted by mutation of a putative diguanylate cyclase. Journal of Bacteriology, 199(5), e00780-16.https://doi.org/10.1128/JB.00780-16
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