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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.
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A.J. Dregni$, V.S. Mandala$, H. Wu$, M.R. Elkins, H.K. Wang, I. Hung, W.F. DeGrado, and M. Hong, “In vitro 0N4R tau fibrils contain a monomorphic β-sheet core enclosed by dynamically heterogeneous fuzzy coat segments”, Proc. Natl. Acad. Sci. USA, 116 (33), 16357-16366 (2019).
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M.D. Gelenter, A.J. Dregni, and M. Hong, “Pulsed Third-Spin-Assisted Recoupling NMR for Obtaining Long-Range 13C-13C and 15N-13C Distance Restraints”, bioRxiv, doi: https://doi.org/10.1101/2020.05.20.105221, (2020).
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A.J. Dregni$, P. Duan$, and M. Hong, “Hydration and Dynamics of Full-Length Tau Amyloid Fibrils Investigated by Solid-State NMR”, Biochemistry, in press (2020).
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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.
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