Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Silvia Panico"'
Autor:
Cassandra Terry, Adam Wenborn, Nathalie Gros, Jessica Sells, Susan Joiner, Laszlo L. P. Hosszu, M. Howard Tattum, Silvia Panico, Daniel K. Clare, John Collinge, Helen R. Saibil, Jonathan D. F. Wadsworth
Publikováno v:
Open Biology, Vol 6, Iss 5 (2016)
Mammalian prions are hypothesized to be fibrillar or amyloid forms of prion protein (PrP), but structures observed to date have not been definitively correlated with infectivity and the three-dimensional structure of infectious prions has remained ob
Externí odkaz:
https://doaj.org/article/66baab80ced54423ba33dae7af2b24e3
Autor:
Yukina Goto, Kyohei Shimoda, Hisao Kondo, Yayoi Kaneko, Xiaodong Zhang, Silvia Panico, Rafael Ayala
Publikováno v:
EMBO J
p97ATPase-mediated membrane fusion is required for the biogenesis of the Golgi complex. p97 and its cofactor p47 function in soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE) priming, but the tethering complex for p9
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::999e646d0d7488b75725562312e00d47
https://doi.org/10.15252/embj.2020105853
https://doi.org/10.15252/embj.2020105853
Autor:
Ima-Obong Ebong, Paul S. Freemont, Patrik Kloppsteck, Caroline A. Ewens, Ciaran Mckeown, Carol V. Robinson, Silvia Panico, Xiaodong Zhang
Publikováno v:
The Journal of Biological Chemistry
Background: p97 function is facilitated by a huge array of varied adaptor proteins, including FAF1. Results: FAF1 binds over the AAA rings of p97 alone and in a trimer-hexamer arrangement. Conclusion: p97 and FAF1 bind with a similar affinity and in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00e5a1d9ade7fb653d61a5712bca54ce
http://hdl.handle.net/11588/584902
http://hdl.handle.net/11588/584902
Autor:
Andrew J, Nicoll, Silvia, Panico, Darragh B, Freir, Daniel, Wright, Cassandra, Terry, Emmanuel, Risse, Caroline E, Herron, Tiernan, O'Malley, Jonathan D F, Wadsworth, Mark A, Farrow, Dominic M, Walsh, Helen R, Saibil, John, Collinge
Publikováno v:
Nature Communications
Growing evidence suggests water-soluble, non-fibrillar forms of amyloid-β protein (Aβ) have important roles in Alzheimer’s disease with toxicities mimicked by synthetic Aβ1–42. However, no defined toxic structures acting via specific receptors
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ece46926796dbd48174d0542e8315a97
https://pubmed.ncbi.nlm.nih.gov/24022506
https://pubmed.ncbi.nlm.nih.gov/24022506
Autor:
Jessica M. Mc Donald, Darragh B. Freir, Dominic M. Walsh, Igor Klyubin, Emmanuel A. Asante, John Collinge, Silvia Panico, Andrew J. Nicoll, Richard B. Sessions, Helen R. Saibil, M Farrow, Michael J. Rowan, Anthony R. Clarke, Emmanuel Risse
Publikováno v:
Nature Communications
A role for PrP in the toxic effect of oligomeric forms of Aβ, implicated in Alzheimer's disease (AD), has been suggested but remains controversial. Here we show that PrP is required for the plasticity-impairing effects of ex vivo material from human
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::438a4a79832c9dd0afde4859dcde9154
https://doi.org/10.1038/ncomms1341
https://doi.org/10.1038/ncomms1341