M.D. Gelenter, K.J. Smith^$, S.Y. Liao^$, V.S. Mandala, A.J. Dregni, M.S. Lamm, Y. Tian, W. Xu, D.J. Pochan, T.J. Tucker, Y. Su, and M. Hong, “The peptide hormone glucagon forms amyloid fibrils with two coexisting β-strand conformations”, Nat. Struct. Mol. Biol., 26, 592-598 (2019).

Featured in MIT News: Chemists discover structure of glucagon fibrils: Study may be a step toward shelf-stable versions of the hormone, which is used to control diabetes.

A.J. Dregni^$, V.S. Mandala^$, H. Wu^$, M.R. Elkins, H.K. Wang, I. Hung, W.F. DeGrado, and M. Hong, “In vitro 0N4R tau fibrils contain a monomorphic β-sheet core enclosed by dynamically heterogeneous fuzzy coat segments”, Proc. Natl. Acad. Sci. USA, 116 (33),  16357-16366 (2019).

Featured in MIT News: Characterizing tau aggregates in neurodegenerative diseases: New research reveals a structural model for amyloid fibrils that could aid in future medicinal interventions for Alzheimer’s, CTE, and more.

M.D. Gelenter, A.J. Dregni, and M. Hong, “Pulsed Third-Spin-Assisted Recoupling NMR for Obtaining Long-Range ¹³C-¹³C and ¹⁵N-¹³C Distance Restraints”, bioRxiv, doi: https://doi.org/10.1101/2020.05.20.105221, (2020).

A.J. Dregni^$, P. Duan^$, and M. Hong, “Hydration and Dynamics of Full-Length Tau Amyloid Fibrils Investigated by Solid-State NMR”, Biochemistry, in press (2020).

^$ denotes equal contribution