Zobrazeno 1 - 10
of 254
pro vyhledávání: '"Stephen J. DeArmond"'
Autor:
Matteo Paoletti, Eduardo Caverzasi, Maria Luisa Mandelli, Jesse A. Brown, Roland G. Henry, Bruce L. Miller, Howard J. Rosen, Stephen J. DeArmond, Stefano Bastianello, William W. Seeley, Michael D. Geschwind
Publikováno v:
Human Brain Mapping. 43:4158-4173
Grey matter involvement is a well-known feature in sporadic Creutzfeldt-Jakob disease (sCJD), yet precise anatomy-based quantification of reduced diffusivity is still not fully understood. Default Mode Network (DMN) areas have been recently demonstra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1aeb665aca055622f420eeca3d227bf0
https://doi.org/10.1002/hbm.25945
https://doi.org/10.1002/hbm.25945
Autor:
Daehee Hwang, Inyoul Y Lee, Hyuntae Yoo, Nils Gehlenborg, Ji‐Hoon Cho, Brianne Petritis, David Baxter, Rose Pitstick, Rebecca Young, Doug Spicer, Nathan D Price, John G Hohmann, Stephen J DeArmond, George A Carlson, Leroy E Hood
Publikováno v:
Molecular Systems Biology, Vol 5, Iss 1, Pp 1-23 (2009)
Abstract Prions cause transmissible neurodegenerative diseases and replicate by conformational conversion of normal benign forms of prion protein (PrPC) to disease‐causing PrPSc isoforms. A systems approach to disease postulates that disease arises
Externí odkaz:
https://doaj.org/article/42301565d732456eae622d19479c865e
Publikováno v:
PLoS Pathogens, Vol 10, Iss 4, p e1003990 (2014)
Bank voles are uniquely susceptible to a wide range of prion strains isolated from many different species. To determine if this enhanced susceptibility to interspecies prion transmission is encoded within the sequence of the bank vole prion protein (
Externí odkaz:
https://doaj.org/article/156873200a4b4cd5a91bbf5c44f8dddd
Autor:
Misol Ahn, Krystyna Bajsarowicz, Abby Oehler, Azucena Lemus, Krystof Bankiewicz, Stephen J DeArmond
Publikováno v:
PLoS ONE, Vol 9, Iss 5, p e98496 (2014)
Prion disease is caused by a single pathogenic protein (PrPSc), an abnormal conformer of the normal cellular prion protein PrPC. Depletion of PrPC in prion knockout mice makes them resistant to prion disease. Thus, gene silencing of the Prnp gene is
Externí odkaz:
https://doaj.org/article/66afdabe53f04fc4be59002124875636
Autor:
Derek Silvius, Rose Pitstick, Misol Ahn, Delisha Meishery, Abby Oehler, Gregory S Barsh, Stephen J DeArmond, George A Carlson, Teresa M Gunn
Publikováno v:
PLoS ONE, Vol 8, Iss 1, p e55575 (2013)
Prion diseases are rare but invariably fatal neurodegenerative disorders. They are associated with spongiform encephalopathy, a histopathology characterized by the presence of large, membrane-bound vacuolar structures in the neuropil of the brain. Wh
Externí odkaz:
https://doaj.org/article/b2b8b31ef7854c5ab7bc2e32748e7c28
Autor:
Misol Ahn, Sina Ghaemmaghami, Yong Huang, Puay-Wah Phuan, Barnaby C H May, Kurt Giles, Stephen J DeArmond, Stanley B Prusiner
Publikováno v:
PLoS ONE, Vol 7, Iss 7, p e39112 (2012)
The lipophilic cationic compound quinacrine has been used as an antimalarial drug for over 75 years but its pharmacokinetic profile is limited. Here, we report on the pharmacokinetic properties of quinacrine in mice. Following an oral dose of 40 mg/k
Externí odkaz:
https://doaj.org/article/b1378581b9864925bf5d24e3b527f0f3
Autor:
Karah Nazor Friberg, Gene Hung, Ed Wancewicz, Kurt Giles, Chris Black, Sue Freier, Frank Bennett, Stephen J DeArmond, Yevgeniy Freyman, Pierre Lessard, Sina Ghaemmaghami, Stanley B Prusiner
Publikováno v:
Molecular Therapy: Nucleic Acids, Vol 1, Iss C (2012)
Mice deficient for the cellular prion protein (PrPC) do not develop prion disease; accordingly, gene-based strategies to diminish PrPC expression are of interest. We synthesized a series of chemically modified antisense oligonucleotides (ASOs) target
Externí odkaz:
https://doaj.org/article/e903ab1e0ba844ac9d3324d05a35cd78
Autor:
David C. Perry, John Q. Trojanowski, Sang Won Seo, Stephanie E. Gaus, Manu Sidhu, Jose Norberto S. Vargas, Adam L. Boxer, Stephen J. DeArmond, Marie-Pierre Thibodeau, Katherine D. Rankin, Alice Y. Hua, Lea T. Grinberg, Joel H. Kramer, Bruce L. Miller, Isabel J. Sible, Gil D. Rabinovici, Maria Luisa Gorno-Tempini, Howard J. Rosen, Eric J. Huang, William W. Seeley
Publikováno v:
Neurology, vol 90, iss 12
ObjectiveTo examine clinicopathologic correlations in early vs late age at onset frontotemporal dementia (FTD) and frontotemporal lobar degeneration (FTLD).MethodsAll patients were clinically evaluated and prospectively diagnosed at the UCSF Memory a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6a678859b795985b40fda1ff2573390
https://doi.org/10.1212/wnl.0000000000005163
https://doi.org/10.1212/wnl.0000000000005163
Autor:
Joel C Watts, Jan Stöhr, Sumita Bhardwaj, Holger Wille, Abby Oehler, Stephen J Dearmond, Kurt Giles, Stanley B Prusiner
Publikováno v:
PLoS Pathogens, Vol 7, Iss 11, p e1002382 (2011)
The central event in prion diseases is the conformational conversion of the cellular prion protein (PrP(C)) into PrP(Sc), a partially protease-resistant and infectious conformer. However, the mechanism by which PrP(Sc) causes neuronal dysfunction rem
Externí odkaz:
https://doaj.org/article/231bd22d391c4443a3bd25e5e8b0c570
Autor:
David Westaway, Sacha Genovesi, Nathalie Daude, Rebecca Brown, Agnes Lau, Inyoul Lee, Charles E Mays, Janaky Coomaraswamy, Brenda Canine, Rose Pitstick, Allen Herbst, Jing Yang, Kerry W S Ko, Gerold Schmitt-Ulms, Stephen J Dearmond, Debbie McKenzie, Leroy Hood, George A Carlson
Publikováno v:
PLoS Pathogens, Vol 7, Iss 11, p e1002391 (2011)
During prion infections of the central nervous system (CNS) the cellular prion protein, PrP(C), is templated to a conformationally distinct form, PrP(Sc). Recent studies have demonstrated that the Sprn gene encodes a GPI-linked glycoprotein Shadoo (S
Externí odkaz:
https://doaj.org/article/e584a8d43c0742d5a8d9a9a1c72ee629