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ACS Chemical Neuroscience|June 13, 2018
Role of Hydrophobicity and Charge of Amyloid-Beta Oligomer Eliminating d-Peptides in the Interaction with Amyloid-Beta MonomersTamar Ziehm, Alexander K Buell, Dieter Willbold
Journal of Oncology Practice|January 3, 2012
Economic assessment of the association of northern california oncologists member practicesRoberta Buell, Patricia Falconer, José Luis González
Journal of Clinical Pharmacology|August 14, 1998
AmBisome (liposomal amphotericin B): a comparative reviewG W Boswell, D Buell, I Bekersky
Chemical Communications (Cambridge, England)|January 5, 2021
Compact fibril-like structure of amyloid β-peptide (1-42) monomersBogdan Barz, Alexander K Buell, Soumav Nath
ACS Chemical Neuroscience|February 19, 2020
The Properties of α-Synuclein Secondary Nuclei Are Dominated by the Solution Conditions Rather than the Seed Fibril StrainAlessia Peduzzo, Sara Linse, Alexander K Buell
Trends in Neurosciences|May 1, 1995
P2X receptors bring new structure to ligand-gated ion channelsA Surprenant, G Buell, R A North
Plant Physiology|September 1, 2025
Plant metabolism: zoom in to the single-cell levelNikolaos Ntelkis, C Robin Buell, Alain Goossens
Physical Chemistry Chemical Physics : PCCP|June 12, 2023
Pyroglutamate-modified amyloid β(3-42) monomer has more β-sheet content than the amyloid β(1-42) monomerSoumav Nath, Alexander K Buell, Bogdan Barz
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