@UMD (*denotes undergraduate students)
Collins. S.C., Keating, P.M., Rich. J., Lee. J. “Effects of the pH-sensing K33 Mutation in the Function of the Lassa Virus Stable Signal Peptide.” Manuscript in preparation.
Collins. S.C., Lee. J. “Influence of cholesterol to the stable signaling peptide of Lassa Virus” Manuscript in preparation.
Schifano. N., Lee J. ” Chemical ligation to investigate the membrane interacting domains.” Manuscript in preparation.
Birtles. D., Pennington. H. N., Keating. P.M., Lee. J. “19F NMR to probe protein-lipid interactions.” Manuscript in preparation.
Pennington. H.N., Arulmony K. Mulvihill Q.M.*, Shin S.*, Im W., Lee J. “Structural Aspects of the Lassa Virus Fusion Peptide and Fusion Loop in Membrane Fusion.” Submitted
Pennington H.N., Lee J. ” Acidic bicelles are a suitable membrane mimic for the Lassa virus fusion domain structural studies.” Biochim. Biophys. Acta – Biomembranes, 2025; 1867, 184428. https://doi.org/10.1016/j.bbamem.2025.184428
Collins S.C., Lee J. ” The Lassa virus stable signaling peptide undergoes a conformational change to aid viral fusion.” Chem. Eur. J. 2025 e202403608 https://doi.org/10.1002/chem.202403608
Birtles D., Lee J. “Exploring the influence of anionic lipids on the initiation of viral fusion” Biochemical Society Transactions (2024) 52 2593–2602 https://doi.org/10.1042/BST20240833
Britles D., Guiyab L.*, Abbas W.*, Lee J. “Positive residues of the SARS-CoV-2 fusion domain are key contributors to the initiation of membrane fusion.” J Biol Chem. 2024 Jul 11:107564. https://doi.org/10.1016/j.jbc.2024.107564
Keating, P.M., Lee, J. Assignment of the Lassa virus transmembrane domain in the prefusion and postfusion states in detergent micelles. Biomol NMR Assign (2024). https://doi.org/10.1007/s12104-024-10184-4
Birtles D., Abbas W.*, Lee J. “Bis(monoacylglycero)phosphate Promotes Membrane Fusion Facilitated by the SARS-CoV-2 Fusion Domain.” J. Phys. Chem. B 2024, 128, 11, 2675–2683 https://doi.org/10.1021/acs.jpcb.3c07863
Pennington. H.N., Birtles, D., Shi. Z.W.*, Lee. J. “A Salt Bridge and Disulfide Bond within the Lassa Virus Fusion Domain Are Required for the Initiation of Membrane Fusion.” ACS Omega 2024 https://doi.org/10.1021/acsomega.3c08632
Birtles D., Lee J. “The SARS-CoV-2 Fusion Domain Provides Clues Towards the Molecular Mechanism for Membrane Fusion” Biochemistry 2023, 62, 21, 3033–3035 https://doi.org/10.1021/acs.biochem.3c00501
Keating P.M., Schifano N. P., Wei X.*, Kong M*. Y., Lee. J. “pH-dependent conformational change within the Lassa virus transmembrane domain elicits efficient membrane fusion.” BBA-Biomembranes https://doi.org/10.1016/j.bbamem.2023.184233
Keating P. M., Pennington H.N., Collins S.C., Lee J. “Purification and Characterization of the Lassa Virus Transmembrane Domain” Biochemistry and Biophysics Reports. 2023;33:101409. https://doi.org/10.1016/j.bbrep.2022.101409
Birtles D, Oh A.E.*, Lee J.”Exploring the pH dependence of the SARS-CoV-2 complete fusion domain and the role of its unique structural features.” Protein Science. 2022;31(9):e4390.https://doi.org/10.1002/pro.4390
Pennington H.N., Lee J. Lassa virus glycoprotein complex review: insights into its unique fusion machinery. Biosci Rep. 2022 Jan 28:BSR20211930. https://doi.org/10.1042/BSR20211930.
Birtles D., & Lee J. Identifying Distinct Structural Features of the SARS-CoV-2 Spike Protein Fusion Domain Essential for Membrane Interaction. Biochemistry, 60(40), 2978–2986. https://doi.org/10.1021/acs.biochem.1c00543
Lee, J., Kreutzberger, A.J.B., Odongo, L., et al. Ebola virus glycoprotein interacts with cholesterol to enhance membrane fusion and cell entry. Nat Struct Mol Biol 28, 181–189 (2021). https://doi.org/10.1038/s41594-020-00548-4
- highlighted in Science: https://www.science.org/doi/10.1126/science.2021.371.6531.twil
Before UMD
Lee J., Nyenhuis D.A., Nelson E.A., Cafiso D.S., White J.M., Tamm L.K. “Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity” Proc. Natl. Acad. Sci. USA. 2017 Sep 19; 114(38): E7987-E7996. https://doi.org/10.1073/pnas.1708052114
Yang S.T., Kreutzberger A.J., Lee J., Kiessling V., Tamm L.K., “The role of cholesterol in membrane fusion.” Chem. Phys. Lipids. 2016, 199: 136-143. https://doi.org/10.1016/j.chemphyslip.2016.05.003
Lee J., Gregory S.M., Nelson E.A., White J.M., Tamm L.K., “The Roles of Histidines and Charged Residues as Potential Triggers of a Conformational Change in the Fusion Loop of Ebola Virus Glycoprotein.” PLoS One. 2016, 11(3):e0152527. https://doi.org/10.1371/journal.pone.0152527
Tamm L.K., Lee J., Liang B., “Capturing glimpses of an elusive HIV gp41 preharipin fusion intermediate.” Structure. 2014, 22 (9), 1225-1226. https://doi.org/10.1016/j.str.2014.08.010
Rui H., Root K.T., Lee J., Glover K.J., Im W., “Probing the u-shaped conformation of caveolin-1 in a bilayer.” Biophys. J. 2014, 106 (6), 1371-1380. https://doi.org/10.1016/j.bpj.2014.02.005
Rieth, M.D.*; Lee, J.*; Glover, K.J., “Probing the caveolin-1 P132L mutant: Critical insights into its oligomeric behavior and structure.” Biochemistry 2012, 51 (18), 3911-3918. (* denotes equal contribution) https://doi.org/10.1021/bi3001853
Lee, J.; Glover, K.J., “The transmembrane domain of caveolin-1 exhibits a helix-break-helix structure.” Biochim. Biophys. Acta 2012, 1818, 1158-1164. https://doi.org/10.1016/j.bbamem.2011.12.033
Mohanty, P.; Lee, J.; Glover, K.J.; Landskron, K., “Discoid bicelles as efficient templates for pillared lamellar periodic mesoporous silicas at pH 7 and ultrafast reaction times.” Nanoscale Res. Lett. 2011, 6, 61-65. https://doi.org/10.1007/s11671-010-9813-9
Diefenderfer, C.; Lee, J.; Mlyanarski, S.; Guo, Y.; Glover, K.J., “Reliable expression and purification of highly insoluble transmembrane domains.” Anal. Biochem. 2009, 384, 274-278. https://doi.org/10.1016/j.ab.2008.09.038
Kang J.E.; Kim H.B.; Lee J.W.; Shin S., “Gold(I)-Catalyzed Intramolecular Hydroamination of Alkyne with Trichloroacetimidates” Org. Lett. 2006, 8, 3537–3540. https://doi.org/10.1021/ol061307r