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Journal of Molecular Biology|April 16, 2013
The Alzheimer's amyloid-β(1-42) peptide forms off-pathway oligomers and fibrils that are distinguished structurally by intermolecular organizationWilliam M Tay, Danting Huang, Terrone L Rosenberry, et al.ACS Applied Materials & Interfaces|March 10, 2015
Asymmetric biodegradable microdevices for cell-borne drug deliveryJunfei Xia, Zhibin Wang, Danting Huang, et al.Methods in Molecular Biology (Clifton, N.J.)|May 11, 2018
Solid-State NMR Structural Characterization of Self-Assembled Peptides with Selective 13C and 15N Isotopic LabelsDanting Huang, Benjamin C Hudson, Yuan Gao, et al.Journal of Molecular Biology|April 19, 2015
Antiparallel β-Sheet Structure within the C-Terminal Region of 42-Residue Alzheimer's Amyloid-β Peptides When They Form 150-kDa OligomersDanting Huang, Maxwell I Zimmerman, Patricia K Martin, et al.Journal of Molecular Biology|May 30, 2020
Out-of-Register Parallel β-Sheets and Antiparallel β-Sheets Coexist in 150-kDa Oligomers Formed by Amyloid-β(1-42)Yuan Gao, Cong Guo, Jens O Watzlawik, et al.Pageof 1