Zobrazeno 1 - 10
of 195
pro vyhledávání: '"Fred E. Cohen"'
Autor:
Fruma Yehiely, Paul Bamborough, Maria Da Costa, Billie J. Perry, Gopal Thinakaran, Fred E. Cohen, George A. Carlson, Stanley B. Prusiner
Publikováno v:
Neurobiology of Disease, Vol 3, Iss 4, Pp 339-355 (1997)
Prion diseases are disorders of protein conformation that produce neurodegeneration in humans and animals. Studies of transgenic (Tg) mice indicate that a factor designated protein X is involved in the conversion of the normal cellular prion protein
Externí odkaz:
https://doaj.org/article/88c5f85e9c5644c783be20cde95711f4
Autor:
Fruma Yehiely, Paul Bamborough, Maria Da Costa, Billie J. Perry, Gopal Thinakaran, Fred E. Cohen, George A. Carlson, Stanley B. Prusiner
Publikováno v:
Neurobiology of Disease, Vol 10, Iss 1, Pp 67-68 (2002)
Externí odkaz:
https://doaj.org/article/a53344cae47d4386b6978aed2bdc6b86
Autor:
David W Colby, Rachel Wain, Ilia V Baskakov, Giuseppe Legname, Christina G Palmer, Hoang-Oanh B Nguyen, Azucena Lemus, Fred E Cohen, Stephen J DeArmond, Stanley B Prusiner
Publikováno v:
PLoS Pathogens, Vol 6, Iss 1, p e1000736 (2010)
Prions arise when the cellular prion protein (PrP(C)) undergoes a self-propagating conformational change; the resulting infectious conformer is designated PrP(Sc). Frequently, PrP(Sc) is protease-resistant but protease-sensitive (s) prions have been
Externí odkaz:
https://doaj.org/article/05d2fdbcce8f465787a434786e853dd7
Publikováno v:
PLoS Computational Biology, Vol 3, Iss 2, p e16 (2007)
Protein point mutations are an essential component of the evolutionary and experimental analysis of protein structure and function. While many manually curated databases attempt to index point mutations, most experimentally generated point mutations
Externí odkaz:
https://doaj.org/article/73e84d7ff9be4287848c5567d2d704e2
Publikováno v:
Structure. 17:1014-1023
The left-handed parallel beta helix (LbetaH) fold has recently received attention as a possible structure for the prion protein (PrP) in its misfolded state. In light of this interest, we have developed an experimental system to examine the structura
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5397c3a31b657252f78e0a2d04af660
https://doi.org/10.1016/j.str.2009.05.013
https://doi.org/10.1016/j.str.2009.05.013
Autor:
Randy M. Whittal, Stanley B. Prusiner, Michael A. Baldwin, Alma L. Burlingame, Fred E. Cohen, Haydn L. Ball
Publikováno v:
Protein Science. 9:332-343
Electrospray ionization mass spectrometry (ESI-MS) was used to measure the binding of Cu2+ ions to synthetic peptides corresponding to sections of the sequence of the mature prion protein (PrP). ESI-MS demonstrates that Cu2+ is unique among divalent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ffff2fc2c8bf7df0b401cf68747734f
https://doi.org/10.1110/ps.9.2.332
https://doi.org/10.1110/ps.9.2.332
Autor:
Robert W. Mahley, Carsten Korth, Charles J. Epstein, Patrick Tremblay, Fred E. Cohen, Darlene Groth, Gültekin Tamgüney, Lennart Mucke, Pauline M. Rudd, Karen H. Ashe, Karl H. Weisgraber, Jan Sap, George A. Carlson, Eric Rubinstein, Kurt Giles, Ina Tesseur, Pamela Stanley, Xiaoping Yang, Richard C. Moore, William A. Kuziel, Raymond A. Dwek, Michael P. Lisanti, Fruma Yehiely, Tony Wyss-Coray, Tracey Dawson Cruz, Claude Boucheix, David V. Glidden, Jörg Tatzelt, Jackob Moskovitz, Holger Wille, Stanley B. Prusiner, Pierre Lessard, Nobuyo Maeda
Publikováno v:
Journal of General Virology. 89:1777-1788
Prion diseases are caused by conversion of a normally folded, non-pathogenic isoform of the prion protein (PrPC) to a misfolded, pathogenic isoform (PrPSc). Prion inoculation experiments in mice expressing homologous PrPCmolecules on different geneti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6a0b838506a2fe386f9a4239bb2b459
https://doi.org/10.1099/vir.0.2008/001255-0
https://doi.org/10.1099/vir.0.2008/001255-0
Autor:
Holger Wille, Stanley B. Prusiner, Kenneth H. Downing, Cédric Govaerts, Fred E. Cohen, Alexander L. Borovinskiy, Diane Latawiec
Publikováno v:
Archives of Biochemistry and Biophysics. 467:239-248
The insolubility of the disease-causing isoform of the prion protein (PrP(Sc)) has prevented studies of its three-dimensional structure at atomic resolution. Electron crystallography of two-dimensional crystals of N-terminally truncated PrP(Sc) (PrP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70291fe4c821e67ec966c570225f9547
https://doi.org/10.1016/j.abb.2007.08.010
https://doi.org/10.1016/j.abb.2007.08.010
Autor:
Juanita Witkop, Fred E. Cohen, Barnaby C. H. May, Stanley B. Prusiner, R. Kiplin Guy, Julie A. Zorn, Peter B. Madrid, Marc O. Anderson, John Sherrill
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 16:4913-4916
A focused library of variously substituted 9-aminoacridine compounds was screened for bioactivity against accumulation of the infectious prion protein isoform, denoted PrP(Sc), in a cell model of prion replication. The efficacy of compounds against P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6defee09fa8308b76197784ed2b4efb
https://doi.org/10.1016/j.bmcl.2006.06.050
https://doi.org/10.1016/j.bmcl.2006.06.050
Autor:
Gerold Schmitt-Ulms, Kirk C. Hansen, Michael A. Baldwin, Jialing Liu, Jian Yang, Stephen J. DeArmond, Stanley B. Prusiner, Fred E. Cohen, Cynthia Cowdrey
Publikováno v:
Nature Biotechnology. 22:724-731
Because of their sensitivity to solubilizing detergents, membrane protein assemblies are difficult to study. We describe a protocol that covalently conserves protein interactions through time-controlled transcardiac perfusion cross-linking (tcTPC) be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b7157b7fb3c56a7d778d3a7504fc306
https://doi.org/10.1038/nbt969
https://doi.org/10.1038/nbt969