Articles

1. Williams, T. L. et al. 2024. Secondary amine catalysis in enzyme design: broadening protein template diversity through genetic code expansion. Angewandte Chemie International Edition (10.1002/anie.202403098)
2. Tang, T. M. S. and Luk, L. Y. P. 2024. Towards controlling activity of a peptide asparaginyl ligase (PAL) by lumazine synthetase compartmentalization. Faraday Discussions (10.1039/D4FD00002A)
3. Lander, A. J., Kong, Y., Jin, Y., Wu, C. and Luk, L. Y. P. 2023. Deciphering the synthetic and refolding strategy of a cysteine-rich domain in the tumor necrosis factor receptor (TNF-R) for racemic crystallography analysis and d-peptide ligand discovery. ACS Bio & Med Chem Au (10.1021/acsbiomedchemau.3c00060)
4. Ma, M., Tang, S. T., Dickerson, M. T. and Luk, L. Y. 2023. Preparing recombinant “Split AEP” for protein labeling. In: Methods in Enzymology., Vol. 690. Methods in Enzymology Elsevier, pp. 501-540., (10.1016/bs.mie.2023.07.004)
5. Lander, A. J., Mercado, L. D., Li, X., Taily, I. M., Findlay, B. L., Jin, Y. and Luk, L. Y. P. 2023. Roles of inter- and intramolecular tryptophan interactions in membrane-active proteins revealed by racemic protein crystallography. Communications Chemistry 6(1), article number: 154. (10.1038/s42004-023-00953-y)
6. Cardella, D., Tsai, Y. and Luk, L. Y. P. 2023. Towards the use of an amino acid cleavable linker for solid-phase chemical synthesis of peptides and proteins. Organic and Biomolecular Chemistry 21, pp. 966-969. (10.1039/d2ob02198f)
7. Hayes, H. C. and Luk, L. Y. P. 2023. Investigating the effects of cyclic topology on the performance of a plastic degrading enzyme for polyethylene terephthalate degradation. Scientific Reports 13, article number: 1267. (10.1038/s41598-023-27780-4)
8. Lander, A. J., Jin, Y. and Luk, L. Y. P. 2022. D‐peptide and d‐protein technology: recent advances, challenges, and opportunities. ChemBioChem, article number: e202200537. (10.1002/cbic.202200537)
9. Allemann, R. K., Samperio, R., Mart, R., Luk, L., Tsai, Y., Jones, A. and Cruz Samperio, R. 2022. Spatio-temporal control of cell death by selective delivery of photo-activatable proteins. ChemBioChem 23(12), article number: e202200115. (10.1002/cbic.202200115)
10. Cardella, D., Deng, W., Luk, L. Y. P. and Tsai, Y. 2022. Effect of trimethine cyanine dye- and folate-conjugation on the in vitro biological activity of proapoptotic peptides. Biomolecules 12(5), article number: 725. (10.3390/biom12050725)
11. Galmés, M. ?., Nodling, A. R., He, K., Luk, L. Y. P., Swiderek, K. and Moliner, V. 2022. Computational design of an amidase by combining the best electrostatic features of two promiscuous hydrolases. Chemical Science 13(17), pp. 4779-4787. (10.1039/D2SC00778A)
12. Galmés, M. ?.et al. 2021. Combined theoretical and experimental study to unravel the differences in promiscuous amidase activity of two nonhomologous enzymes. ACS Catalysis 11(14), pp. 8635-8644. (10.1021/acscatal.1c02150)
13. Williams, T. L.et al. 2021. Transferability of N-terminal mutations of pyrrolysyl-tRNA synthetase in one species to that in another species on unnatural amino acid incorporation efficiency. Amino Acids 53, pp. 89-96. (10.1007/s00726-020-02927-z)
14. Tang, T. M. S. L. and Luk, L. Y. P. 2021. Asparaginyl endopeptidases: enzymology, applications and limitations. Organic and Biomolecular Chemistry (10.1039/D1OB00608H)
15. Adesina, A. S., Luk, L. Y. P. and Allemann, R. K. 2021. Cryo‐kinetics reveal dynamic effects on the chemistry of human dihydrofolate reductase. ChemBioChem (10.1002/cbic.202100017)
16. Hayes, H. C., Luk, L. Y. P. and Tsai, Y. 2021. Approaches for peptide and protein cyclisation. Organic and Biomolecular Chemistry (10.1039/D1OB00411E)
17. Santi, N.et al. 2021. Transfer hydrogenations catalyzed by streptavidin-hosted secondary amine organocatalyst. Chemical Communications 57(15), pp. 1919-1922. (10.1039/D0CC08142F)
18. Sophie R Thomas, Riccardo Bonisignore, Jorge S Escudero, Samual M Meier-Menches, Christopher Brown, Mike Wolf, Giampaolo Barone, Louis YP Luk*, Angela Casini*. Exploring the chemoselectivity towards cysteine arylation by cyclometalated Au(III) compounds: new mechanistic insights. ChemBioChem 2020 (10.1002/cbic.202000262)
19. Nicolò Santi, Louis C Morrill, Louis YP Luk*. Streptavidin-hosted Organocatalytic Aldol Addition. Molecules, 2020, 25, 2457. (10.3390/molecules25102457)
20. Simon TM Tang, Davide Cardella, Alexander J Lander, Xuefei Li, Jorge S Escudero, Yu-Hsuan Tsai, Louis YP Luk*. Use of an asparaginyl endopeptidase for chemo-enzymatic peptide and protein labeling. Chem. Sci., 2020, 11, 5881. (10.1039/D0SC02023K)
21. Nödling, A. R.et al. 2020. Enabling protein-hosted organocatalytic transformations. RSC Advances 10(27), pp. 16147-16161. (10.1039/D0RA01526A)
22. Nödling, A.et al. 2020. Cyanine dye mediated mitochondrial targeting enhances the anti-cancer activity of small-molecule cargoes. Chemical Communications (10.1039/C9CC07931A)
23. Zheng, X.et al. 2020. Condensation of 2-((Alkylthio)(aryl)methylene)malononitrile with 1,2-Aminothiol as a novel bioorthogonal reaction for site-specific protein modification and peptide cyclization. Journal of the American Chemical Society 142(11), pp. 5097-5103. (10.1021/jacs.9b11875)
24. Mills, E. M.et al. 2020. Applying switchable Cas9 variants to in vivo gene editing for therapeutic applications. Cell Biology and Toxicology 36, pp. 17-29. (10.1007/s10565-019-09488-2)
25. Meier-Menches, S. M.et al. 2020. Comparative biological evaluation and G-quadruplex interaction studies of two new families of organometallic gold(I) complexes featuring N-heterocyclic carbene and alkynyl ligands. Journal of Inorganic Biochemistry 202, article number: 110844. (10.1016/j.jinorgbio.2019.110844)
26. Allemann, R. K.et al. 2019. Heavy enzymes and the rational redesign of protein catalysts. ChemBioChem 20(22), pp. 2807-2812. (10.1002/cbic.201900134)
27. Angelastro, A.et al. 2019. Loss of hyperconjugative effects drives hydride transfer during dihydrofolate reductase catalysis. ACS Catalysis 9(11), pp. 10343-10349. (10.1021/acscatal.9b02839)
28. Mills, E. M.et al. 2019. Applying switchable Cas9 variants to in vivo gene editing for therapeutic applications. Cell Biology and Toxicology (10.1007/s10565-019-09488-2)
29. Nodling, A. R.et al. 2019. Using genetically incorporated unnatural amino acids to control protein functions in mammalian cells. Essays in Biochemistry 63(2), pp. 237-266. (10.1042/EBC20180042)
30. Scott, A. F.et al. 2019. Crystal structure and biophysical analysis of furfural detoxifying aldehyde reductase from clostridium beijerinkii. Applied and Environmental Microbiology, pp. -. (10.1128/AEM.00978-19)
31. Patel, S. G.et al. 2019. Cell-penetrating peptide sequence and modification dependent uptake and subcellular distribution of green florescent protein in different cell lines. Scientific Reports 9(1), 6298. (10.1038/s41598-019-42456-8)
32. Williams TL, et al. 2018. Carbapenems as water soluble organocatalysts. Wellcome Open Res. 3, 107 (doi: 10.12688/wellcomeopenres.14721.1)
33. Nodling, A. R.et al. 2018. Reactivity and selectivity of iminium organocatalysis improved by a protein host. Angewandte Chemie International Edition 57(38), pp. 12478-12482. (10.1002/anie.201806850) 
34. Suzuki, T.et al. 2018. Switchable genome editing via genetic code expansion. Scientific Reports 8(1), 10051. (10.1038/s41598-018-28178-3) 
35. Allemann, R.et al. 2018. Isotope substitution of promiscuous alcohol dehydrogenase reveals origin of substrate preference in transition state. Angewandte Chemie International Edition 57(12), pp. 3128-3131. (10.1002/anie.201712826) 
36. Świderek, K.et al. 2018. Reaction mechanism of organocatalytic Michael addition of nitromethane to cinnamaldehyde: a case study on catalyst regeneration and solvent effects. Journal of Physical Chemistry A 122(1), pp. 451-459. (10.1021/acs.jpca.7b11803) 
37. Liao, J.et al. 2017. Acetylome of acinetobacter baumannii SK17 reveals a highly-conserved modification of histone-like protein HU. Frontiers in Molecular Biosciences 4, article number: 77. (10.3389/fmolb.2017.00077) 
38. Wilkins, L.et al. 2017. Reactions of biologically inspired hydride sources with B(C6F5)3. Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 375(2101), article number: 20170009. (10.1098/rsta.2017.0009) 
39. Angelastro, A.et al. 2017. Chemoenzymatic assembly of isotopically labeled folates. Journal of the American Chemical Society 139(37), pp. 13047-13054. (10.1021/jacs.7b06358) 
40. Lai, S.et al. 2017. Site-specific His/Asp phosphoproteomic analysis of prokaryotes reveals putative targets for drug resistance. BMC Microbiology 17(1), article number: 123. (10.1186/s12866-017-1034-2) 
41. Loveridge, E.et al. 2017. Reduction of folate by dihydrofolate reductase from thermotoga maritima. Biochemistry 56(13), pp. 1879-1886. (10.1021/acs.biochem.6b01268) 
42. Angelastro, A.et al. 2016. A versatile disulfide-driven recycling system for NADP+ with high cofactor turnover number. ACS Catalysis 7, pp. 1025-1029. (10.1021/acscatal.6b03061) 
43. Castillo, J.et al. 2016. β1 subunit-induced structural rearrangements of the Ca2+- and voltage-activated (BK) channel. Proceedings of the National Academy of Sciences of the United States of America 113(23), pp. E3231-E3239. (10.1073/pnas.1606381113) 
44. Ruiz-Pernía, J.et al. 2016. Minimization of dynamic effects in the evolution of dihydrofolate reductase. Chemical Science 7(5), pp. 3248-3255. (10.1039/C5SC04209G) 
45. Luk, L.et al. 2015. Chemical ligation and isotope labeling to locate dynamic effects during catalysis by dihydrofolate reductase. Angewandte Chemie – International Edition 54(31), pp. 9016-9020. (10.1002/anie.201503968) 
46. Luk, L. Y. P., Loveridge, E. J. and Allemann, R. K. 2015. Protein motions and dynamic effects in enzyme catalysis. Physical Chemistry Chemical Physics 17, pp. 30817-30827. (10.1039/C5CP00794A) 
47. Luk, L.et al. 2014. Protein isotope effects in dihydrofolate reductase from Geo-bacillus stearothermophilus show entropic-enthalpic com-pensatory effects on the rate constant. Journal of the American Chemical Society 136(49), pp. 17317-17323., article number: 141114165738006. (10.1021/ja5102536) 
48. Luk, L. Y. P., Loveridge, E. J. and Allemann, R. K. 2014. Different dynamical effects in mesophilic and hyperthermophilic dihydrofolate reductases. Journal of the American Chemical Society 136(19), pp. 6862-6865. (10.1021/ja502673h)
49. Guo, J.et al. 2014. Thermal adaptation of dihydrofolate reductase from the moderate thermophile geobacillus stearothermophilus. Biochemistry 53(17), pp. 2855-2863. (10.1021/bi500238q) 
50. Behiry, E.et al. 2014. Role of the occluded conformation in bacterial dihydrofolate reductases. Biochemistry 53(29), pp. 4761-4768. (10.1021/bi500507v) 
51. Ruiz-Pernia, J.et al. 2013. Increased dynamic effects in a catalytically compromised variant of Escherichia coli dihydrofolate reductase. Journal of the American Chemical Society 135(49), pp. 18689-18696. (10.1021/ja410519h)
52. Luk, L.et al. 2013. Unraveling the role of protein dynamics in dihydrofolate reductase catalysis. Proceedings of the National Academy of Sciences of the United States of America 110(41), pp. 16344-16349. (10.1073/pnas.1312437110)
53. Guo, J.et al. 2013. Effect of dimerization on dihydrofolate reductase catalysis. Biochemistry 52(22), pp. 3881-3887. (10.1021/bi4005073)
54. 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
55. Luk, L. Y. P., Qian, Q. and Tanner, M. E. 2011. A cope rearrangement in the reaction catalyzed by dimethylallyltryptophan synthase?. Journal of the American Chemical Society 133(32), pp. 12342-12345. (10.1021/ja2034969)
56. Luk, L. Y. P. and Tanner, M. E. 2009. Mechanism of dimethylallyltryptophan synthase: Evidence for a dimethylallyl cation intermediate in an aromatic prenyltransferase reaction. Journal of the American Chemical Society 131(39), pp. 13932-13933. (10.1021/ja906485u)
57. Luk, L.et al. 2007. Mechanistic studies on norcoclaurine synthase of benzylisoquinoline alkaloid biosynthesis:  An enzymatic Pictet-Spengler reaction. Biochemistry 46(35), pp. 10153-10161. (10.1021/bi700752n)