1
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.
2
A.J. Dregni$, V.S. Mandala$, H. Wu$, M.R. Elkins, H.K. Wang, I. Hung, W.F. DeGrado, and M. Hong, “In vitro 0N4R tau fibrils contain a monomorphic β-sheet core enclosed by dynamically heterogeneous fuzzy coat segments”, Proc. Natl. Acad. Sci. USA, 116 (33), 16357-16366 (2019).
3
M.D. Gelenter, A.J. Dregni, and M. Hong, “Pulsed Third-Spin-Assisted Recoupling NMR for Obtaining Long-Range 13C-13C and 15N-13C Distance Restraints”, J. Phys. Chem., 124, 7138-7151 (2020).
4
A.J. Dregni$, P. Duan$, and M. Hong, “Hydration and Dynamics of Full-Length Tau Amyloid Fibrils Investigated by Solid-State NMR”, Biochemistry, in press (2020).
5
V.S. Mandala, M.J. McKay, A.A. Shcherbakov, A.J. Dregni, A. Kolocouris, and M. Hong, “Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers”, Nat. Struct. Mol. Biol. in press (2020)
Featured in MIT News: Chemists discover the structure of a key coronavirus protein: The protein, which acts as an ion channel, could be a target for new drugs against the SARS-CoV-2 virus.
6
M.D. Gelenter$,V.S. Mandala$, M.J.M. Niesen$, D.A. Sharon$, A. J. Dregni, A. P. Willard, and M. Hong, “Water orientation and dynamics in the closed and open influenza B virus M2 proton channels”, Commun. Biol., 4, 338 (2020).
7
A.J. Dregni, H. K. Wang, H. Wu, P. Duan, W.F. DeGrado and M. Hong, “Inclusion of the C-Terminal Domain in the Tau Amyloid Fibril Core Revealed by Solid-State NMR Spectroscopy”, J. Am. Chem. Soc., online ahead of print (2021).
$ denotes equal contribution
