Search Results - "BARON, Gerald S"

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  1. 1

    High-resolution structure and strain comparison of infectious mammalian prions by Kraus, Allison, Hoyt, Forrest, Schwartz, Cindi L., Hansen, Bryan, Artikis, Efrosini, Hughson, Andrew G., Raymond, Gregory J., Race, Brent, Baron, Gerald S., Caughey, Byron

    Published in Molecular cell (04-11-2021)
    “…Within the extensive range of self-propagating pathologic protein aggregates of mammals, prions are the most clearly infectious (e.g., ∼109 lethal doses per…”
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  2. 2

    Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions by Caughey, Byron, Baron, Gerald S, Chesebro, Bruce, Jeffrey, Martin

    Published in Annual review of biochemistry (01-01-2009)
    “…The prion (infectious protein) concept has evolved with the discovery of new self-propagating protein states in organisms as diverse as mammals and fungi. The…”
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  3. 3

    Cryo-EM structure of anchorless RML prion reveals variations in shared motifs between distinct strains by Hoyt, Forrest, Standke, Heidi G., Artikis, Efrosini, Schwartz, Cindi L., Hansen, Bryan, Li, Kunpeng, Hughson, Andrew G., Manca, Matteo, Thomas, Olivia R., Raymond, Gregory J., Race, Brent, Baron, Gerald S., Caughey, Byron, Kraus, Allison

    Published in Nature communications (13-07-2022)
    “…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 infectious…”
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  4. 4

    Cryo-EM of prion strains from the same genotype of host identifies conformational determinants by Hoyt, Forrest, Alam, Parvez, Artikis, Efrosini, Schwartz, Cindi L, Hughson, Andrew G, Race, Brent, Baune, Chase, Raymond, Gregory J, Baron, Gerald S, Kraus, Allison, Caughey, Byron

    Published in PLoS pathogens (07-11-2022)
    “…Prion strains in a given type of mammalian host are distinguished by differences in clinical presentation, neuropathological lesions, survival time, and…”
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  5. 5

    Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange by Surewicz, Witold K, Smirnovas, Vytautas, Baron, Gerald S, Offerdahl, Danielle K, Raymond, Gregory J, Caughey, Byron

    Published in Nature structural & molecular biology (01-04-2011)
    “…One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrPSc. Here we used mass spectrometry analysis of…”
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  6. 6

    PrP Knockout Cells Expressing Transmembrane PrP Resist Prion Infection by Marshall, Karen E, Hughson, Andrew, Vascellari, Sarah, Priola, Suzette A, Sakudo, Akikazu, Onodera, Takashi, Baron, Gerald S

    Published in Journal of virology (15-01-2017)
    “…Glycosylphosphatidylinositol (GPI) anchoring of the prion protein (PrP ) influences PrP misfolding into the disease-associated isoform, PrP , as well as prion…”
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  7. 7

    Effect of Glycans and the Glycophosphatidylinositol Anchor on Strain Dependent Conformations of Scrapie Prion Protein: Improved Purifications and Infrared Spectra by Baron, Gerald S, Hughson, Andrew G, Raymond, Gregory J, Offerdahl, Danielle K, Barton, Kelly A, Raymond, Lynne D, Dorward, David W, Caughey, Byron

    Published in Biochemistry (Easton) (31-05-2011)
    “…Mammalian prion diseases involve conversion of normal prion protein, PrPC, to a pathological aggregated state (PrPres). The three-dimensional structure of…”
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  8. 8

    Characterization of intracellular dynamics of inoculated PrP-res and newly generated PrPSc during early stage prion infection in Neuro2a cells by Yamasaki, Takeshi, Baron, Gerald S, Suzuki, Akio, Hasebe, Rie, Horiuchi, Motohiro

    Published in Virology (New York, N.Y.) (01-02-2014)
    “…Abstract To clarify the cellular mechanisms for the establishment of prion infection, we analyzed the intracellular dynamics of inoculated and newly generated…”
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  9. 9

    Efficient uptake and dissemination of scrapie prion protein by astrocytes and fibroblasts from adult hamster brain by Hollister, Jason R, Lee, Kil Sun, Dorward, David W, Baron, Gerald S

    Published in PloS one (30-01-2015)
    “…Prion infections target neurons and lead to neuronal loss. However, the role of non-neuronal cells in the initiation and spread of infection throughout the…”
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  10. 10

    Prion seeding activities of mouse scrapie strains with divergent PrPSc protease sensitivities and amyloid plaque content using RT-QuIC and eQuIC by Vascellari, Sarah, Orrù, Christina D, Hughson, Andrew G, King, Declan, Barron, Rona, Wilham, Jason M, Baron, Gerald S, Race, Brent, Pani, Alessandra, Caughey, Byron

    Published in PloS one (05-11-2012)
    “…Different transmissible spongiform encephalopathy (TSE)-associated forms of prion protein (e.g. PrP(Sc)) can vary markedly in ultrastructure and biochemical…”
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  11. 11

    Isolation of Novel Synthetic Prion Strains by Amplification in Transgenic Mice Coexpressing Wild-Type and Anchorless Prion Proteins by RAYMOND, Gregory J, RACE, Brent, DORWARD, David W, BARON, Gerald S, HOLLISTER, Jason R, OFFERDAHL, Danielle K, MOORE, Roger A, KODALI, Ravindra, RAYMOND, Lynne D, HUGHSON, Andrew G, ROSENKE, Rebecca, DAN LONG

    Published in Journal of Virology (01-11-2012)
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  12. 12

    Effect of Glycosylphosphatidylinositol Anchor-dependent and -independent Prion Protein Association with Model Raft Membranes on Conversion to the Protease-resistant Isoform by Baron, Gerald S., Caughey, Byron

    Published in The Journal of biological chemistry (25-04-2003)
    “…Prion protein (PrP) is usually bound to membranes by a glycosylphosphatidylinositol (GPI) anchor that associates with detergent-resistant membranes, or rafts…”
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  13. 13

    Specific biarsenical labeling of cell surface proteins allows fluorescent- and biotin-tagging of amyloid precursor protein and prion proteins by Taguchi, Yuzuru, Shi, Zhen-Dan, Ruddy, Brian, Dorward, David W, Greene, Lois, Baron, Gerald S

    Published in Molecular biology of the cell (01-01-2009)
    “…Fluorescent tagging is a powerful tool for imaging proteins in living cells. However, the steric effects imposed by fluorescent tags impair the behavior of…”
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  14. 14

    GPI anchoring facilitates propagation and spread of misfolded Sup35 aggregates in mammalian cells by Speare, Jonathan O, Offerdahl, Danielle K, Hasenkrug, Aaron, Carmody, Aaron B, Baron, Gerald S

    Published in The EMBO journal (17-02-2010)
    “…Prion diseases differ from other amyloid‐associated protein misfolding diseases (e.g. Alzheimer's) because they are naturally transmitted between individuals…”
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  15. 15

    Prions and their partners in crime by Caughey, Byron, Baron, Gerald S

    Published in Nature (19-10-2006)
    “…Prions, the infectious agents of transmissible spongiform encephalopathies (TSEs), have defied full characterization for decades. The dogma has been that…”
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  16. 16

    Mouse-Adapted Scrapie Infection of SN56 Cells: Greater Efficiency with Microsome-Associated versus Purified PrP-res by BARON, Gerald S, MAGALHAES, Ana C, PRADO, Marco A. M, CAUGHEY, Byron

    Published in Journal of Virology (01-03-2006)
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  17. 17
  18. 18

    Inhibition of Protease-Resistant Prion Protein Accumulation In Vitro by Curcumin by Caughey, Byron, Raymond, Lynne D, Raymond, Gregory J, Maxson, Laura, Silveira, Jay, Baron, Gerald S

    Published in Journal of Virology (01-05-2003)
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  19. 19

    Effects of FlAsH/Tetracysteine (TC) Tag on PrP Proteolysis and PrPres Formation by TC-Scanning by Taguchi, Yuzuru, Hohsfield, Lindsay A., Hollister, Jason R., Baron, Gerald S.

    “…Protein–protein interactions associated with proteolytic processing and aggregation are integral to normal and pathological aspects of prion protein (PrP)…”
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  20. 20

    Hemin Interactions and Alterations of the Subcellular Localization of Prion Protein by Lee, Kil S., Raymond, Lynne D., Schoen, Brianna, Raymond, Gregory J., Kett, Lauren, Moore, Roger A., Johnson, Lisa M., Taubner, Lara, Speare, Jonathan O., Onwubiko, Henry A., Baron, Gerald S., Caughey, Winslow S., Caughey, Byron

    Published in The Journal of biological chemistry (14-12-2007)
    “…Hemin (iron protoporphyrin IX) is a crucial component of many physiological processes acting either as a prosthetic group or as an intracellular messenger…”
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