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Chemical Science|December 22, 2023
The supersaturation perspective on the amyloid hypothesisDiana Portugal Barron, Zhefeng GuoMethods in Enzymology|April 29, 2026
Application of EPR spectroscopy in the structural studies of Aβ oligomers and fibrilsDiana Portugal Barron, Zhefeng GuoThe Analyst|May 2, 2023
A protein aggregation platform that distinguishes oligomers from amyloid fibrilsAmy Zhang, Diana Portugal Barron, Erica W Chen, et al.ACS Chemical Neuroscience|December 18, 2023
EPR Studies of Aβ42 Oligomers Indicate a Parallel In-Register β-Sheet StructureChelsea Jang, Diana Portugal Barron, Lan Duo, et al.Peerj|October 14, 2024
Bivalve microbiomes are shaped by host species, size, parasite infection, and environmentSarah Gignoux-Wolfsohn, Monserrat Garcia Ruiz, Diana Portugal Barron, et al.The Journal of Biological Chemistry|March 16, 2007
The mechanism of the amyloidogenic conversion of T7 endonuclease IZhefeng Guo, David EisenbergBiochemical and Biophysical Research Communications|December 4, 2020
Alzheimer's Aβ42 and Aβ40 form mixed oligomers with direct molecular interactionsLei Gu, Zhefeng GuoBiochemical and Biophysical Research Communications|October 12, 2011
Key residues for the oligomerization of Aβ42 protein in Alzheimer's diseaseSam Ngo, Zhefeng GuoBiochemical and Biophysical Research Communications|April 16, 2021
Lipid membranes induce structural conversion from amyloid oligomers to fibrilsLei Gu, Zhefeng GuoProtein Science : a Publication of the Protein Society|June 17, 2008
The structure of a fibril-forming sequence, NNQQNY, in the context of a globular foldZhefeng Guo, David EisenbergPageof 5