Samuel A. Kotler
Affiliations: | 2011-2015 | Biophysics | University of Michigan, Ann Arbor, Ann Arbor, MI |
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| Ratha BN, Kar RK, Bednarikova Z, et al. (2020) Molecular Details of A Salt-Bridge and Its Role in Insulin Fibrillation by NMR and Raman Spectroscopic Analysis. The Journal of Physical Chemistry. B |
| Brender JR, Ghosh A, Kotler SA, et al. (2019) Probing transient non-native states in amyloid beta fiber elongation by NMR. Chemical Communications (Cambridge, England) |
| Bhattacharyya D, Mohite GM, Krishnamoorthy J, et al. (2019) Lipopolysaccharide from Gut Microbiota Modulates α-Synuclein Aggregation and Alters its Biological Function. Acs Chemical Neuroscience |
| Kotler SA, Tugarinov V, Schmidt T, et al. (2019) Probing initial transient oligomerization events facilitating Huntingtin fibril nucleation at atomic resolution by relaxation-based NMR. Proceedings of the National Academy of Sciences of the United States of America. 116: 3562-3571 |
| Kotler SA, Ramamoorthy A. (2018) Preparation of Stable Amyloid-β Oligomers Without Perturbative Methods. Methods in Molecular Biology (Clifton, N.J.). 1777: 331-338 |
| Ceccon A, Schmidt T, Tugarinov V, et al. (2018) Interaction of Huntingtin Exon-1 Peptides with Lipid-Based Micellar Nanoparticles Probed by Solution NMR and Q-Band Pulsed EPR. Journal of the American Chemical Society |
| Sciacca MFM, Chillemi R, Sciuto S, et al. (2018) A blend of two resveratrol derivatives abolishes hIAPP amyloid growth and membrane damage. Biochimica Et Biophysica Acta |
| Kotler SA, Brender JR, Vivekanandan S, et al. (2015) High-resolution NMR characterization of low abundance oligomers of amyloid-β without purification. Scientific Reports. 5: 11811 |
| Lee DK, Bhunia A, Kotler SA, et al. (2015) Detergent-type membrane fragmentation by MSI-78, MSI-367, MSI-594, and MSI-843 antimicrobial peptides and inhibition by cholesterol: a solid-state nuclear magnetic resonance study. Biochemistry. 54: 1897-907 |
| Kotler SA, Walsh P, Brender JR, et al. (2014) Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease. Chemical Society Reviews. 43: 6692-700 |