23. R. Pandey, T. Olabi, M. Lee, B. Urbanc, "Distinct Aβ40 and Aβ42 co-assembly pathways with free lipids: Experiment-driven MD study". submitted (2026).
22. P. Saha, T. Liyanaarachchige, A. Alim, J. Paek, M. Lee, "Aβ42-Driven α-synuclein Fibril Polymorphism and Distinct Intracellular Aggregation", submitted (2026).
21. A. Alim, S. Lwin, P. Saha, Y. Baek, M. Lee, J. Paek, “Vascularizing neurospheroids to probe vascular contributions to α-synuclein pathology in Parkinson's disease”, Submitted (2026).
20. L. Shahriari, C Biju, L.N. Elam, H.E. Fowler, Y. Baek, M. Lee, S. C. Leguizamon, S. Kim, “Catalyst-free dynamic crosslinking of polydicyclopentadiene via thiol-ene/imine chemistry” ACS Mater. Lett. (2026).
19. K.R. Thurber, M. Lee, R. Tycko, “Brain-seeded 42-residue amyloid-β fibrils that resemble fibrils directly extracted from Alzheimer’s disease brain tissue”, J. Mol. Biol. 438, 169983 (2026).
18. Y. Baek, A. Alim, Y. Dong, T. Olabi, J. Paek, M. Lee, “Lipid Acyl Chain-Driven α-Synuclein Fibril Polymorphisms and Neuronal Pathologies”, ACS chemical neuroscience 17 (7), 1286-1302. (2026).
17. A. Alim, Y. Baek, M. Lee, J. Paek, “Microengineering of the capillary interface of midbrain dopaminergic neurons to study Parkinson’s disease vascular alterations”, Communications engineering (2026).
16. C.B. Wilson, M. Lee, W.M. Yau, R. Tycko, “Conformations of a Low-Complexity Protein in Homogeneous and Phase Separated Frozen Solutions”, Biophys. J. 123 (23), 4097-4114 (2024).
15. Y. Baek, M. Lee, "Exploring the complexity of amyloid beta fibrils: Structural polymorphisms and molecular interactions", Biochem.Soc.Trans. (2024).
14. Y. Baek, M. Lee, "Solid-state NMR spectroscopic analysis for structure determination of a zinc-bound catalytic amyloid fibril", Methods Enzymol. 697, 435-471 (2024)
13. M. Lee, W.M. Yau, J.M. Louis, R. Tycko, “Structures of brain-derived 42-residue amyloid β fibril polymorphs with unusual molecular conformations and intermolecular interactions”, Proc. Natl. Acad. Sci. USA. 120 (11) e2218831120 (2023).
12. S. Kim, M. Lee, M. Hong, N. Holten-Andersen, “Quantitative Correlation between Bound Water and Mechanical Stress-relaxation in Dehydrated Metal-Coordinate Polymer Networks“, Chem. Materials, 34, 10329-10337 (2022).
11. C. A. Roden, Y. Dai, C. Giannetti, I. Seim, M. Lee, R. Sealfon, G. A. McLaughlin, M. A. Boerneke, C. Iserman, S. A. Wey, J. L. Ekena, O. G. Troyanskaya, K. M. Weeks, L. You, A. Chilkoti, A. S. Gladfelter, “Double-stranded RNA drives SARS-CoV-2 Nucleocapsid Protein to Undergo Phase separation at Specific Temperatures”, Nucleic Acids Res. 50 (14), 8168-8192 (2022).
10. M. Lee, U. Ghosh, K.R. Thurber, M. Kato, R. Tycko, “Molecular Structure and Interactions within Amyloid-Like Fibrils Formed by a Low Complexity Protein Sequence from FUS”, Nat. Commun. 11, 5735 (2020).
9. M. Lee, C.M. Morgan, M. Hong, “Fully Hydrophobic HIV gp41 Adopts a Hemifusion-like Conformation in Phospholipid Bilayers”, J. Biol.Chem. 294, 14732-14744 (2019).
8. S. Y. Liao, M. Lee, M. Hong, “Interplay Between Membrane Curvature and Protein Conformational Equilibrium Investigated by Solid-State NMR”, J. Struct. Biol. 206 (1), 20-28 (2019).
7. M. Lee, B. Kwon, A. Waring, M. Hong, “Oligomeric Structure and Three-dimensional Fold of the HIV gp41 MPER and Transmembrane Domain in Phospholipid Bilayers”, J. Am. Chem. Soc. 140 (26), 8246-8259 (2018).
6. M. Lee, H. Yao, B. Kwon, A. Waring, P. Ruchala, C. Singh, M. Hong, “Conformation and Trimer Association of the Transmembrane Domain of the Parainfluenza Fusion Protein in Lipid Bilayers From Solid-State NMR: Insights into the Sequence Determinants of Fusion Activity and Trimer stability”, J. Mol. Biol. 430, 695-709 (2018).
5. M. Lee, T. Wang, O.V. Makhlynets, Y. Wu, N.P. Polizzi, H. Wu, P.M. Gosavi, J. Stöhr, I.V. Korendovych, W.F. DeGrado, M. Hong, “Zinc-Binding Structure of a Catalytic Amyolid from Solid-State NMR”, Proc. Natl. Acad. Sci. USA 114 (24), 6191-6196 (2017).
4. H.W. Yao, M. Lee, S. Y. Liao, and M. Hong, “Solid-State Nuclear Magnetic Resonance Investigation of the Structural Topology and Lipid Interactions of a Viral Fusion Protein Chimera Containing the Fusion Peptide and Transmambrane Domain”, Biochemistry 55, 6787-6800 (2016).
3. J. K. Williams, D. Tietze, M. Lee, J. Wang, and M. Hong, “Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel”, J. Am. Chem. Soc. 138, 8143-8155 (2016).
2. S. Y. Liao, M. Lee, T. Wang, I. Sergeyev, and M. Hong, “Efficient Dynamic Nuclear Polarization NMR of Membrane Proteins: Optimal Sample Preparation Protocols, Sensitivity and Resolution Assessment, and Radical Location”, J. Biomol. NMR 64, 223-237 (2016).
1. M. Lee and M. Hong, “Cryoprotection of Lipid Membranes for High-Resolution Solid-State NMR Studies of Membrane Peptides and Proteins at Low Temperature”, J.Biomol. NMR 59, 263-277 (2014).