Shannon E. Hill, Ph.D.
Affiliations: | Physics | University of South Florida, Tampa, FL, United States |
Area:
Optical recording, protein aggregartion, light scatteringGoogle:
"Shannon Hill"Mean distance: 18.4 (cluster 6) | S | N | B | C | P |
Parents
Sign in to add mentorMartin Muschol | grad student | 2011 | University of South Florida | |
(Physical Models of Amyloid Fibril Assembly.) |
BETA: Related publications
See more...
Publications
You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect. |
Saccuzzo EG, Mebrat MD, Scelsi HF, et al. (2024) Competition between inside-out unfolding and pathogenic aggregation in an amyloid-forming β-propeller. Nature Communications. 15: 155 |
Esquivel AR, Hill SE, Blair LJ. (2023) DnaJs are enriched in tau regulators. International Journal of Biological Macromolecules. 253: 127486 |
Hill SE, Beaulieu-Abdelahad D, Lemus A, et al. (2023) . Acs Chemical Biology |
Jiang L, Chakraborty P, Zhang L, et al. (2023) Chaperoning of specific tau structure by immunophilin FKBP12 regulates the neuronal resilience to extracellular stress. Science Advances. 9: eadd9789 |
Hill SE, Esquivel AR, Ospina SR, et al. (2022) Chaperoning activity of the cyclophilin family prevents tau aggregation. Protein Science : a Publication of the Protein Society. 31: e4448 |
Gao Y, Saccuzzo EG, Hill SE, et al. (2021) Structural Arrangement within a Peptide Fibril Derived from the Glaucoma-Associated Myocilin Olfactomedin Domain. The Journal of Physical Chemistry. B |
Webster JM, Darling AL, Sanders TA, et al. (2020) Hsp22 with an N-Terminal Domain Truncation Mediates a Reduction in Tau Protein Levels. International Journal of Molecular Sciences. 21 |
Wang Y, Gao Y, Hill SE, et al. (2018) Simulations and Experiments Delineate Amyloid Fibrilization by Peptides Derived from Glaucoma-Associated Myocilin. The Journal of Physical Chemistry. B |
Hill SE, Donegan RK, Lieberman RL. (2014) The glaucoma-associated olfactomedin domain of myocilin forms polymorphic fibrils that are constrained by partial unfolding and peptide sequence. Journal of Molecular Biology. 426: 921-35 |
Foley J, Hill SE, Miti T, et al. (2013) Structural fingerprints and their evolution during oligomeric vs. oligomer-free amyloid fibril growth. The Journal of Chemical Physics. 139: 121901 |