1. Behiry, E.M.; Ruiz-Pernia, J.J.; Luk, L.Y.P.; Tuñón, I.; Moliner, V.; Allemann, R.K. Isotope Substitution of Promiscuous Alcohol Dehydrogenase Reveals the Origin of Substrate Preference in the Transition State. Angew. Chem. Int. Ed.57, 3128–3131 (2018). DOI:10.1002/anie.201712826
  2. Świderek, K.; Nödling, A.; Tsai, Y-H.; Luk, L.Y.P.*; Moliner, V.* The Reaction Mechanism of Organocatalytic Michael Addition of Nitromethane to Cinnamaldehyde: A Case Study on Catalyst Regeneration and Solvent Effect. J. Phys. Chem. A. 122, 451-459 (2017). DOI: 10.1021/acs.jpca.7b118039
  3. Liao, J.H.; Tsai, C-H.; Patel, S.G.; Yang, J.T.; Tu, I-F.; Cicero, M.L.; Lipka-Lloyd M.; Wu, W-L.; Shen, W-J.; Ho, M-R.; Chou, C-C.; Sharma, G.R. Okanishi, H.; Luk, L.Y.P.; Tsai, Y-H.; Wu, S-H. Acetylome of Acinetobacter baumannii SK17 a highly conversed modification of histone-like protein HU. Front. Mol. Biosci. 4, 1-12 (2017). DOI: 10.3389/fmolb.201700077
  4. Angelastro, A.; Dawson, W.D.; Luk, L.Y.P.; Loveridge, E.J.; Allemann, R.K. Chemoenzymatic Assembly of Isotopically Labeled Folates. J. Am. Chem. Soc.139, 13047–13054 (2017). DOI: 10.1021/jacs.7b06358
  5. S.-J. Lai, I-F. Tu, W.-L. Wu, J.-T. Yang, L. Y. P. Luk, M.-C. Lai, Y.-H. Tsai, S.-H. Wu, Site-specific His/Asp phosphoproteomic analysis of prokaryotes reveals putative targets for drug resistance. BMC Microbiol. 
  6. Scott, A.F.; Luk, L.Y.P.; Allemann, R.K. Chemical ligation and isotope labeling to locate dynamic effects. Methods in Enzymology. 596, 23-41 (2017). DOI: 10.1016/bs.mie.2017.06.040
  7. , R. L,; , R.L.; , A.;  , G.;  
  8. Angelastro, A.; 
  9. Castillo, J.P.; Sánchez-Rodríguez, J.E.; Hyde, H.C.; Zaelzer, C.A.; Aguayo, D.; Sepúlveda, R.V.; Luk, L.Y.P.; Kent, S.B.H.; Gonzalez-Nilo, F.D.; Bezanilla, F.; Latorre, R.β1-subunit–induced structural rearrangements of the Ca2+– and voltage-activated K+ (BK) channelProc. Natl. Acad. Sci. 113, E3231–E3239, (2016) DOI: 10.1073/pnas.1606381113
  10. Ruiz-Perniaa, J.J.; Behiry, E.; Luk, L.Y.P.; Loveridge, E.J., Tuñónc, I., Moliner, V.; Allemann, R.K.; Minimization of Dynamic Effects in the Evolution of Dihydrofolate Reductase, Chem. Sci. 7, 3248-3255 (2015) DOI: 10.1039/C5SC04209G
  11. Luk, L.Y.P.; Ruiz-Pernia, J.J.; Adesina, A.S.; Loveridge, E.J.; Tuñón, I.; Moliner, V.; Allemann, R.K.; Chemical ligation and isotope labeling to locate dynamic effects during catalysis by dihydrofolate reductase, Angew. Chem. Int. Ed., 54, 9016-9020 (2015) DOI: 10.1002/anie.201503968
  12. Luk, L.Y.P.; Loveridge, E.J.; Allemann, R.K.; Protein motions, dynamic effects and thermal stability in dihydrofolate reductase from the hyperthermophile Thermotoga maritima, book chapter, pp 99-113, Springer.
  13. Luk, L.Y.P.; Loveridge, E.J.; Allemann, R.K.; Protein motions and dynamic effects in enzyme catalysis, Phys. Chem. Chem. Phys., 17, 30817-30827 (2015) DOI: 10.1039/c5cp00794a.
  14. Luk, L.Y.P.; Ruiz-Pernía, J.J.; Dawson, W.M.; Loveridge, E.J.; Tuñón, I.; Moliner, V.; Allemann, R.K.; Protein isotope effects in dihydrofolate reductase from Geobacillus stearothermophilus show entropic-enthalpic compensatory effects on the rate constant, J. Am. Chem. Soc. 136, 17317-17323 (2014) DOI: 10.1021/ja5102536
  15. Guo, J.; Loveridge, E.J.; Luk, L.Y.P.; Allemann, R.K.; Thermal adaptation of dihydrofolate reductase from the moderate thermophile Geobacillus stearothermophilus, Biochemistry, 53, 2855-2863 (2014) DOI: 1021/bi500238q
  16. Behiry, E.M.; Luk, L.Y.P.; Matthews, S.M.; Loveridge, E.J.; Allemann, R.K.; Role of the occluded conformation in bacterial dihydrofolate reductases, Biochemistry, 53, 4761-4768 (2014) DOI: 1021/bi508507v
  17. Luk, L.Y.P.; Loveridge, E.J.; Allemann, R.K.; Different dynamical effects in mesophilic and hyperthermophilic dihydrofolate reductases, J. Am. Chem. Soc., 136, 6862-6865 (2014) DOI: 10.1021/ja502673h
  18. Luk, L.Y.P.; Ruiz-Pernia, J.J.; García-Meseguer, R.; Marti, S.; Loveridge, E.J.; Tuñón, I.; Moliner, V.; Allemann, R.K.; Increased dynamic effects in a ‘dynamic knockout’ of dihydrofolate reductase from Escherichia coli, J. Am. Chem. Soc., 135, 18689-18696 (2013) DOI: 10.1021/ja410519h
  19. Luk, L.Y.P.; Ruiz-Pernia, J.J.; Dawson, W.M.; Roca, M.; Loveridge, E.J.; Glowacki, D.R.; Harvey, J.N.; Mulholland, A.J.; Tuñón, I.; Moliner, V.; Allemann, R.K.; Unravelling the role of protein dynamics in dihydrofolate reductase catalysis, Proc. Natl. Acad. Sci., 110, 16344-16349 (2013) DOI: 10.1073/PNAS.1312437110
  20. Guo, J.; Loveridge, E.J.; Luk, L.Y.P.; Allemann, R.K.; Effect of dimerization on catalysis by dihydrofolate reductase, Biochemistry, 52, 3881-3887 (2013) DOI: 10.1021/bi4005073
  21. Mahmoodi, N.; Qi, Q.; Luk, L.Y.P.; Tanner, M.E.; Rearrangements in the mechanisms of the indole alkaloid prenyltransferases, Pure Appl. Chem., 85, 1935-1948 (2013). DOI: 10.1351/PAC-CON-13-02-02
  22. Luk, L.Y.P.; Qian, Q.; Tanner, M.E.; A Cope rearrangement in the reaction catalyzed by dimethylallyltryptophan synthase? J. Am. Chem. Soc. 133, 12342-12345 (2011); DOI: 10.1021/ja2034969
  23. Luk, L.Y.P.; Tanner, M.E.; Mechanism of dimethylallyltryptophan synthase: evidence for a dimethylallyl cation intermediate in an aromatic prenyltransferase reaction, J. Am. Chem. Soc. 131, 13932-13933 (2009); DOI: 10.1021/ja906485u
  24. Luk, L.Y.P.; Bunn, S.; Liscombe, D.K.; Facchini, P.J.; Tanner, M.E.; Mechanistic studies on norcoclaurine synthase of benzylisoquinoline alkaloid biosynthesis: an enzymatic Pictet-Spengler reaction, Biochemistry, 46, 10153-10161 (2007); DOI: 10.1021/bi700752n