Ari Gafni

Biological Chemistry University of Michigan, Ann Arbor, Ann Arbor, MI 
Structural Enzymology, Protein Processing and Folding
"Ari Gafni"

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Chang CC, Edwald E, Veatch S, et al. (2018) Interactions of amyloid-β peptides on lipid bilayer studied by single molecule imaging and tracking. Biochimica Et Biophysica Acta
Johnson RD, Steel DG, Gafni A. (2014) Structural evolution and membrane interactions of Alzheimer's amyloid-beta peptide oligomers: new knowledge from single-molecule fluorescence studies. Protein Science : a Publication of the Protein Society. 23: 869-83
Chang CC, Althaus JC, Carruthers CJ, et al. (2013) Synergistic interactions between Alzheimer's Aβ40 and Aβ42 on the surface of primary neurons revealed by single molecule microscopy. Plos One. 8: e82139
Johnson RD, Schauerte JA, Chang CC, et al. (2013) Single-molecule imaging reveals aβ42:aβ40 ratio-dependent oligomer growth on neuronal processes. Biophysical Journal. 104: 894-903
Chang C, Althaus C, Carruthers C, et al. (2013) Synergistic Interactions of Alzheimer's Aβ40 and Aβ42 on the Surface of Primary Neurons by Single Molecule Microscopy Biophysical Journal. 104: 575a
Ding H, Schauerte JA, Steel DG, et al. (2012) β-Amyloid (1-40) peptide interactions with supported phospholipid membranes: a single-molecule study. Biophysical Journal. 103: 1500-9
Chang C, Gafni A, Steel D. (2012) Single Molecule Study of the Oligomerization of Alzheimer's Aβ40 and Aβ42 on the Surface of Phospholipid Membranes Biophysical Journal. 102: 77a
Johnson R, Schauerte J, Althaus C, et al. (2012) Single Molecule Fluorescence Microscopy Reveals Neurite-Bound Amyloid-Beta Oligomers Biophysical Journal. 102: 723a
Aravamudhan P, Gafni A, Steel D. (2012) Single Molecule Studies of Interaction Between Alzheimer's Amyloid-β Peptides of different Lengths Biophysical Journal. 102: 442a
Johnson RD, Schauerte JA, Wisser KC, et al. (2011) Direct observation of single amyloid-β(1-40) oligomers on live cells: binding and growth at physiological concentrations. Plos One. 6: e23970
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