Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Olivia R. Thomas"'
Autor:
Forrest Hoyt, Heidi G. Standke, Efrosini Artikis, Cindi L. Schwartz, Bryan Hansen, Kunpeng Li, Andrew G. Hughson, Matteo Manca, Olivia R. Thomas, Gregory J. Raymond, Brent Race, Gerald S. Baron, Byron Caughey, Allison Kraus
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-7 (2022)
The authors report the near-atomic structure of the ex vivo aRML prion fibril. The comparison between this structure and the previously solved 263K prion fibril shows that both common and divergent features characterize these prion strains and their
Externí odkaz:
https://doaj.org/article/05a74e9b4a094ef891797aa49a2a0b86
Autor:
Patricia Aguilar-Calvo, Adela Malik, Daniel R Sandoval, Christopher Barback, Christina D Orrù, Heidi G Standke, Olivia R Thomas, Chrissa A Dwyer, Donald P Pizzo, Jaidev Bapat, Katrin Soldau, Ryotaro Ogawa, Mckenzie B Riley, K Peter R Nilsson, Allison Kraus, Byron Caughey, Jeffrey J Iliff, David R Vera, Jeffrey D Esko, Christina J Sigurdson
Publikováno v:
PLoS Pathogens, Vol 19, Iss 9, p e1011487 (2023)
Select prion diseases are characterized by widespread cerebral plaque-like deposits of amyloid fibrils enriched in heparan sulfate (HS), a abundant extracellular matrix component. HS facilitates fibril formation in vitro, yet how HS impacts fibrillar
Externí odkaz:
https://doaj.org/article/c83e6fca89c54c42855f3b68597d0988
Autor:
Matteo Manca, Heidi G. Standke, Danielle F. Browne, Mikayla L. Huntley, Olivia R. Thomas, Christina D. Orrú, Andrew G. Hughson, Yongya Kim, Jing Zhang, Curtis Tatsuoka, Xiongwei Zhu, Annie Hiniker, David G. Coughlin, Douglas Galasko, Allison Kraus
Publikováno v:
Acta neuropathologica, vol 146, iss 1
Tau neurofibrillary tangles are a hallmark of Alzheimer’s disease neuropathological change. However, it remains largely unclear how distinctive Alzheimer’s disease tau seeds (i.e. 3R/4R) correlate with histological indicators of tau accumulation.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd1413d0dcae6de0b47ef45aea548355
https://doi.org/10.1007/s00401-023-02574-0
https://doi.org/10.1007/s00401-023-02574-0
Autor:
Forrest Hoyt, Heidi G. Standke, Efrosini Artikis, Cindi L. Schwartz, Bryan Hansen, Kunpeng Li, Andrew G. Hughson, Matteo Manca, Olivia R. Thomas, Gregory J. Raymond, Gerald S. Baron, Byron Caughey, Allison Kraus
Little is known about the structural basis of prion strains. Here we provide a high (3.0 Å) resolution cryo-electron microscopy-based structure of brain-derived fibrils of the mouse anchorless RML scrapie strain which, like the recently determined h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::779805a14887e70f35fd69c774177562
https://doi.org/10.1101/2021.12.22.473909
https://doi.org/10.1101/2021.12.22.473909
