Gerald S. Baron, Ph.D.Rocky Mountain LaboratoriesBuilding 2, Room 2102903 South 4th Street Hamilton, MT 59840-2932Phone: 406-363-9485Fax: firstname.lastname@example.org
Chief, TSE/Prion Cell Biology Section, LPVD
TSEs or prion diseases are under investigation. TSEs are transmissible neurodegenerative disorders associated with the conversion of the normal prion protein PrPC to aggregates of misfolded protein called PrP-res. Our work encompasses several areas, including determining mechanisms of infection, intra- and intercellular transport of TSE agents, and neurodegeneration, in addition to defining the nature of the TSE agent. Biochemical and cell biological approaches in both cell culture and in vivo models of infection are being employed to address these questions.
Dr. Baron received his Ph.D. in biochemistry from the University of Victoria in 1998, studying genes required for intramacrophage growth of the facultative intracellular bacterium Francisella tularensis. He conducted his postdoctoral research on prions and transmissible spongiform encephalopathies (TSEs) in the laboratory of Dr. Byron Caughey at the Rocky Mountain Laboratories. In 2005, he established an independent laboratory as a tenure-track investigator.
James “Mac” McGuire
Baron GS, Hughson AG, Raymond GJ, Offerdahl DK, Barton KA, Raymond LD, Dorward DW, Caughey B. Effect of glycans and the glycophosphatidylinositol anchor on strain dependent conformations of scrapie prion protein: improved purifications and infrared spectra. Biochemistry. 2011 May 31;50(21):4479-90.
Smirnovas V, Baron GS, Offerdahl DK, Raymond GJ, Caughey B, Surewicz WK. Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange. Nat Struct Mol Biol. 2011 Apr;18(4):504-6.
Speare JO, Offerdahl DK, Hasenkrug A, Carmody AB, Baron GS. GPI anchoring facilitates propagation and spread of misfolded Sup35 aggregates in mammalian cells. EMBO J. 2010 Feb 17;29(4):782-94.
Taguchi Y, Shi ZD, Ruddy B, Dorward DW, Greene L, Baron GS. Specific biarsenical labeling of cell surface proteins allows fluorescent- and biotin-tagging of amyloid precursor protein and prion proteins. Mol Biol Cell. 2009 Jan;20(1):233-44.
Baron GS, Magalhães AC, Prado MA, Caughey B. Mouse-adapted scrapie infection of SN56 cells: greater efficiency with microsome-associated versus purified PrP-res. J Virol. 2006 Mar;80(5):2106-17.
Magalhães AC, Baron GS, Lee KS, Steele-Mortimer O, Dorward D, Prado MA, Caughey B. Uptake and neuritic transport of scrapie prion protein coincident with infection of neuronal cells. J Neurosci. 2005 May 25;25(21):5207-16.
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Last Updated September 11, 2012
Last Reviewed September 11, 2012